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Database: UniProt
Entry: Q9H3P7
LinkDB: Q9H3P7
Original site: Q9H3P7 
ID   GCP60_HUMAN             Reviewed;         528 AA.
AC   Q9H3P7; B2RB29; Q5VTJ0; Q6P9F1; Q8IZC5; Q8N4D6; Q9H6U3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-JUN-2016, entry version 131.
DE   RecName: Full=Golgi resident protein GCP60;
DE   AltName: Full=Acyl-CoA-binding domain-containing protein 3;
DE   AltName: Full=Golgi complex-associated protein 1;
DE            Short=GOCAP1;
DE   AltName: Full=Golgi phosphoprotein 1;
DE            Short=GOLPH1;
DE   AltName: Full=PBR- and PKA-associated protein 7;
DE   AltName: Full=Peripheral benzodiazepine receptor-associated protein PAP7;
DE   Contains:
DE     RecName: Full=Golgi resident protein GCP60, N-terminally processed;
GN   Name=ACBD3; Synonyms=GCP60, GOCAP1, GOLPH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   INTERACTION WITH GOLGB1, AND TISSUE SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=11590181; DOI=10.1074/jbc.M108961200;
RA   Sohda M., Misumi Y., Yamamoto A., Yano A., Nakamura N., Ikehara Y.;
RT   "Identification and characterization of a novel Golgi protein, GCP60,
RT   that interacts with the integral membrane protein giantin.";
RL   J. Biol. Chem. 276:45298-45306(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-187.
RC   TISSUE=Placenta;
RA   Liu J., Tobin D., Tasken K., Papadopoulos V.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-187.
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-188; 231-406 AND 467-528, CLEAVAGE OF INITATOR
RP   METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION, INTERACTION WITH
RP   PI4KB; TBC1D22A; TBC1D22B AND 3A PROTEINS FROM PICORNAVIRUSES,
RP   MUTAGENESIS OF LYS-243; GLN-244; GLN-245; ILE-246; GLN-253; THR-254;
RP   256-VAL--PHE-258; GLN-257; PHE-258; GLN-259; GLN-260; TYR-261;
RP   264-GLN--TYR-266; 267-PRO--ASN-269; ILE-275; LEU-276;
RP   282-GLU--TYR-285; HIS-284; TYR-285; GLN-286; GLN-287; TYR-288;
RP   344-SER-SER-345; 414-SER--LEU-416; 417-PHE--PHE-420; 433-PHE--TRP-435;
RP   494-GLY--HIS-496; SER-511 AND 511-SER--SER-513, AND MASS SPECTROMETRY.
RX   PubMed=23572552; DOI=10.1128/mBio.00098-13;
RA   Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
RA   DeRisi J.L.;
RT   "ACBD3 interaction with TBC1 domain 22 protein is differentially
RT   affected by enteroviral and kobuviral 3A protein binding.";
RL   MBio 4:E00098-E00098(2013).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-9, AND CLEAVAGE OF INITIATOR METHIONINE.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-20, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-43 AND SER-47,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Involved in the maintenance of Golgi structure by
CC       interacting with giantin, affecting protein transport between the
CC       endoplasmic reticulum and Golgi. Involved in hormone-induced
CC       steroid biosynthesis in testicular Leydig cells (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:11590181}.
CC   -!- SUBUNIT: Interacts with the C-terminal cytoplasmic domain of
CC       giantin/GOLGB1 (PubMed:11590181). Interacts with PBR and PKA
CC       regulatory subunit RI-alpha. Does not interact with PKA regulatory
CC       subunit RI-beta nor PKA regulatory subunit RII-alpha (By
CC       similarity). Interacts with PI4KB, TBC1D22A AND TBC1D22B;
CC       interactions with PI4KB and with TBC1D22A and TBC1D22B are
CC       mutually exclusive. Interacts with C10ORF76 and RAB11B
CC       (PubMed:23572552). {ECO:0000250|UniProtKB:Q8BMP6,
CC       ECO:0000269|PubMed:11590181, ECO:0000269|PubMed:23572552}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with 3A proteins from
CC       various picornaviruses, including hepatitis A virus, human
CC       parechovirus 1, and human klassevirus. Kobuviral (Aichi) 3A
CC       protein binding may compete the physiological interaction with
CC       TBC1D22A, while enteroviral (poliovirus) 3A protein does not seem
CC       to interfere. {ECO:0000269|PubMed:23572552}.
CC   -!- INTERACTION:
CC       O91464:- (xeno); NbExp=21; IntAct=EBI-1791792, EBI-7587528;
CC       Q9UBF8:PI4KB; NbExp=4; IntAct=EBI-1791792, EBI-1053214;
CC       Q8BHN0:Ppm1l (xeno); NbExp=3; IntAct=EBI-1791792, EBI-7970002;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Also
CC       mitochondrial (via its interaction with PBR). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in testis
CC       and ovary. {ECO:0000269|PubMed:11590181}.
CC   -!- DOMAIN: The GOLD domain is essential for giantin binding.
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00573}.
CC   -!- SIMILARITY: Contains 1 GOLD domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00096}.
DR   EMBL; AB043587; BAB20592.2; -; mRNA.
DR   EMBL; AY150218; AAN60219.1; -; mRNA.
DR   EMBL; AK025520; BAB15159.1; -; mRNA.
DR   EMBL; AK314468; BAG37076.1; -; mRNA.
DR   EMBL; AL592045; CAH71922.1; -; Genomic_DNA.
DR   EMBL; CH471098; EAW69775.1; -; Genomic_DNA.
DR   EMBL; BC034563; AAH34563.2; -; mRNA.
DR   EMBL; BC045533; AAH45533.1; -; mRNA.
DR   EMBL; BC060792; AAH60792.1; -; mRNA.
DR   CCDS; CCDS1551.1; -.
DR   RefSeq; NP_073572.2; NM_022735.3.
DR   UniGene; Hs.520207; -.
DR   ProteinModelPortal; Q9H3P7; -.
DR   SMR; Q9H3P7; 101-162, 385-524.
DR   BioGrid; 122262; 30.
DR   DIP; DIP-40673N; -.
DR   IntAct; Q9H3P7; 15.
DR   MINT; MINT-5003562; -.
DR   STRING; 9606.ENSP00000355777; -.
DR   BindingDB; Q9H3P7; -.
DR   iPTMnet; Q9H3P7; -.
DR   PhosphoSite; Q9H3P7; -.
DR   SwissPalm; Q9H3P7; -.
DR   BioMuta; ACBD3; -.
DR   DMDM; 51316096; -.
DR   EPD; Q9H3P7; -.
DR   MaxQB; Q9H3P7; -.
DR   PaxDb; Q9H3P7; -.
DR   PeptideAtlas; Q9H3P7; -.
DR   PRIDE; Q9H3P7; -.
DR   Ensembl; ENST00000366812; ENSP00000355777; ENSG00000182827.
DR   GeneID; 64746; -.
DR   KEGG; hsa:64746; -.
DR   UCSC; uc001hpy.4; human.
DR   CTD; 64746; -.
DR   GeneCards; ACBD3; -.
DR   H-InvDB; HIX0159664; -.
DR   HGNC; HGNC:15453; ACBD3.
DR   HPA; HPA015594; -.
DR   MIM; 606809; gene.
DR   neXtProt; NX_Q9H3P7; -.
DR   PharmGKB; PA28803; -.
DR   eggNOG; KOG3878; Eukaryota.
DR   eggNOG; ENOG410XS5V; LUCA.
DR   GeneTree; ENSGT00530000063651; -.
DR   HOVERGEN; HBG051712; -.
DR   InParanoid; Q9H3P7; -.
DR   OMA; FGVFFEW; -.
DR   OrthoDB; EOG7KDFB4; -.
DR   PhylomeDB; Q9H3P7; -.
DR   TreeFam; TF321667; -.
DR   ChiTaRS; ACBD3; human.
DR   GeneWiki; ACBD3; -.
DR   GenomeRNAi; 64746; -.
DR   PRO; PR:Q9H3P7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; Q9H3P7; -.
DR   CleanEx; HS_ACBD3; -.
DR   ExpressionAtlas; Q9H3P7; baseline and differential.
DR   Genevisible; Q9H3P7; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   Gene3D; 1.20.80.10; -; 1.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR009038; GOLD_dom.
DR   Pfam; PF00887; ACBP; 1.
DR   Pfam; PF13897; GOLD_2; 1.
DR   SUPFAM; SSF101576; SSF101576; 2.
DR   SUPFAM; SSF47027; SSF47027; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
DR   PROSITE; PS50866; GOLD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Complete proteome;
KW   Direct protein sequencing; Golgi apparatus; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Mitochondrion; Phosphoprotein;
KW   Polymorphism; Reference proteome; Steroid biosynthesis.
FT   CHAIN         1    528       Golgi resident protein GCP60.
FT                                /FTId=PRO_0000436449.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378,
FT                                ECO:0000269|PubMed:12665801}.
FT   CHAIN         2    528       Golgi resident protein GCP60, N-
FT                                terminally processed.
FT                                /FTId=PRO_0000214029.
FT   DOMAIN       83    174       ACB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00573}.
FT   DOMAIN      384    526       GOLD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00096}.
FT   COILED      174    257       {ECO:0000255}.
FT   COMPBIAS     21     60       Pro-rich.
FT   COMPBIAS    182    240       Glu-rich.
FT   COMPBIAS    196    238       Arg-rich.
FT   COMPBIAS    241    308       Gln-rich.
FT   MOD_RES       2      2       N-acetylalanine; in Golgi resident
FT                                protein GCP60, N-terminally processed.
FT                                {ECO:0000244|PubMed:22223895,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES      18     18       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES      20     20       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES      43     43       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES      47     47       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VARIANT     187    187       E -> D (in dbSNP:rs2306120).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|Ref.2}.
FT                                /FTId=VAR_019615.
FT   MUTAGEN     243    243       K->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     244    244       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     245    245       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     246    246       I->A: Partial loss of PI4KB- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     253    253       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     254    254       T->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     256    258       VQF->AAA: Loss of PI4KB-, TBC1D22A- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     257    257       Q->A: Partial loss of PI4KB- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     258    258       F->A: Differential effect on PI4KB- and
FT                                TBC1D22B-binding, with PI4KB-binding
FT                                being much more affected than TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     259    259       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     260    260       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     261    261       Y->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     264    266       QQY->AAA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     267    269       PGN->AAA: Loss of PI4KB-, TBC1D22A- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     275    275       I->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     276    276       L->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     282    285       EQHY->AAAA: Loss of PI4KB-, TBC1D22A- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     284    284       H->A: Almost complete loss of PI4KB- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     285    285       Y->A: Differential loss of PI4KB- and
FT                                TBC1D22B-binding, with PI4KB-binding
FT                                being much more affected than TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     286    286       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     287    287       Q->A: No effect on PI4KB- and TBC1D22B-
FT                                binding. {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     288    288       Y->A: Almost complete loss of PI4KB- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     344    345       SS->AA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     414    416       SYL->AAA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     417    420       FWEF->AAAA: No effect on PI4KB-,
FT                                TBC1D22A- and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     433    435       FEW->AAA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     494    496       GSH->AAA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     511    513       SYS->AAA: No effect on PI4KB-, TBC1D22A-
FT                                and TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   MUTAGEN     511    511       S->A: Partial loss of PI4KB- and
FT                                TBC1D22B-binding.
FT                                {ECO:0000269|PubMed:23572552}.
FT   CONFLICT     93     93       F -> L (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       R -> I (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    265    265       Q -> R (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    333    333       S -> P (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    384    397       KEKIQQDADSVITV -> QREDSAGCRFRDYS (in Ref.
FT                                2). {ECO:0000305}.
FT   CONFLICT    425    425       Y -> C (in Ref. 2; AAN60219).
FT                                {ECO:0000305}.
FT   CONFLICT    473    473       K -> R (in Ref. 6; AAH60792).
FT                                {ECO:0000305}.
SQ   SEQUENCE   528 AA;  60593 MW;  B36EC550F8268FC2 CRC64;
     MAAVLNAERL EVSVDGLTLS PDPEERPGAE GAPLLPPPLP PPSPPGSGRG PGASGEQPEP
     GEAAAGGAAE EARRLEQRWG FGLEELYGLA LRFFKEKDGK AFHPTYEEKL KLVALHKQVL
     MGPYNPDTCP EVGFFDVLGN DRRREWAALG NMSKEDAMVE FVKLLNRCCH LFSTYVASHK
     IEKEEQEKKR KEEEERRRRE EEERERLQKE EEKRRREEEE RLRREEEERR RIEEERLRLE
     QQKQQIMAAL NSQTAVQFQQ YAAQQYPGNY EQQQILIRQL QEQHYQQYMQ QLYQVQLAQQ
     QAALQKQQEV VVAGSSLPTS SKVNATVPSN MMSVNGQAKT HTDSSEKELE PEAAEEALEN
     GPKESLPVIA APSMWTRPQI KDFKEKIQQD ADSVITVGRG EVVTVRVPTH EEGSYLFWEF
     ATDNYDIGFG VYFEWTDSPN TAVSVHVSES SDDDEEEEEN IGCEEKAKKN ANKPLLDEIV
     PVYRRDCHEE VYAGSHQYPG RGVYLLKFDN SYSLWRSKSV YYRVYYTR
//
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