ID ASB12_HUMAN Reviewed; 309 AA.
AC Q8WXK4; J3KP57; Q2M3D5; Q52LK4; Q6ISF9; Q8N8F5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Ankyrin repeat and SOCS box protein 12;
DE Short=ASB-12;
GN Name=ASB12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-308 (ISOFORM 1).
RA Kile B.T., Nicola N.A.;
RT "SOCS box proteins.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL5 AND
RP RNF7.
RX PubMed=16325183; DOI=10.1016/j.febslet.2005.11.016;
RA Kohroki J., Nishiyama T., Nakamura T., Masuho Y.;
RT "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin ligase
RT complexes.";
RL FEBS Lett. 579:6796-6802(2005).
CC -!- FUNCTION: Probable substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250,
CC ECO:0000269|PubMed:16325183}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL5 and RNF7. {ECO:0000269|PubMed:16325183}.
CC -!- INTERACTION:
CC Q8WXK4-2; O15197-2: EPHB6; NbExp=3; IntAct=EBI-18394052, EBI-10182490;
CC Q8WXK4-2; O14964: HGS; NbExp=3; IntAct=EBI-18394052, EBI-740220;
CC Q8WXK4-2; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-18394052, EBI-3918847;
CC Q8WXK4-2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-18394052, EBI-6426443;
CC Q8WXK4-2; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-18394052, EBI-726510;
CC Q8WXK4-2; O43711: TLX3; NbExp=3; IntAct=EBI-18394052, EBI-3939165;
CC Q8WXK4-2; Q8WW01: TSEN15; NbExp=3; IntAct=EBI-18394052, EBI-372432;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WXK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXK4-2; Sequence=VSP_044865;
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
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DR EMBL; AF403030; AAL57349.1; -; mRNA.
DR EMBL; AK096896; BAC04888.1; -; mRNA.
DR EMBL; AL356317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05414.1; -; Genomic_DNA.
DR EMBL; BC069436; AAH69436.1; -; mRNA.
DR EMBL; BC069555; AAH69555.1; -; mRNA.
DR EMBL; BC093883; AAH93883.1; -; mRNA.
DR EMBL; BC104946; AAI04947.1; -; mRNA.
DR CCDS; CCDS14378.2; -. [Q8WXK4-2]
DR RefSeq; NP_569059.3; NM_130388.3. [Q8WXK4-2]
DR AlphaFoldDB; Q8WXK4; -.
DR SMR; Q8WXK4; -.
DR BioGRID; 126776; 37.
DR CORUM; Q8WXK4; -.
DR IntAct; Q8WXK4; 11.
DR MINT; Q8WXK4; -.
DR STRING; 9606.ENSP00000355195; -.
DR iPTMnet; Q8WXK4; -.
DR PhosphoSitePlus; Q8WXK4; -.
DR BioMuta; ASB12; -.
DR DMDM; 62512181; -.
DR PaxDb; 9606-ENSP00000355195; -.
DR PeptideAtlas; Q8WXK4; -.
DR ProteomicsDB; 75075; -. [Q8WXK4-1]
DR Antibodypedia; 27045; 59 antibodies from 14 providers.
DR DNASU; 142689; -.
DR Ensembl; ENST00000362002.3; ENSP00000355195.2; ENSG00000198881.10. [Q8WXK4-2]
DR GeneID; 142689; -.
DR KEGG; hsa:142689; -.
DR MANE-Select; ENST00000362002.3; ENSP00000355195.2; NM_130388.4; NP_569059.3. [Q8WXK4-2]
DR UCSC; uc004dvr.3; human. [Q8WXK4-1]
DR AGR; HGNC:19763; -.
DR CTD; 142689; -.
DR DisGeNET; 142689; -.
DR GeneCards; ASB12; -.
DR HGNC; HGNC:19763; ASB12.
DR HPA; ENSG00000198881; Group enriched (skeletal muscle, tongue).
DR MIM; 300891; gene.
DR neXtProt; NX_Q8WXK4; -.
DR OpenTargets; ENSG00000198881; -.
DR PharmGKB; PA134937084; -.
DR VEuPathDB; HostDB:ENSG00000198881; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000153902; -.
DR HOGENOM; CLU_053981_1_0_1; -.
DR InParanoid; Q8WXK4; -.
DR OMA; DYNCTDR; -.
DR OrthoDB; 5475985at2759; -.
DR PhylomeDB; Q8WXK4; -.
DR TreeFam; TF331945; -.
DR PathwayCommons; Q8WXK4; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8WXK4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 142689; 13 hits in 810 CRISPR screens.
DR GenomeRNAi; 142689; -.
DR Pharos; Q8WXK4; Tdark.
DR PRO; PR:Q8WXK4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WXK4; Protein.
DR Bgee; ENSG00000198881; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 133 other cell types or tissues.
DR Genevisible; Q8WXK4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001496; SOCS_box.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF165; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..309
FT /note="Ankyrin repeat and SOCS box protein 12"
FT /id="PRO_0000066947"
FT REPEAT 63..92
FT /note="ANK 1"
FT REPEAT 96..125
FT /note="ANK 2"
FT REPEAT 129..158
FT /note="ANK 3"
FT REPEAT 171..200
FT /note="ANK 4"
FT REPEAT 213..243
FT /note="ANK 5"
FT DOMAIN 268..308
FT /note="SOCS box"
FT VAR_SEQ 1
FT /note="M -> MRIVLQLAKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044865"
FT CONFLICT 149
FT /note="L -> P (in Ref. 2; BAC04888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 33943 MW; 8280C47C544D03D8 CRC64;
MNLMDITKIF SLLQPDKEEE DTDTEEKQAL NQAVYDNDSY TLDQLLRQER YKRFINSRSG
WGVPGTPLRL AASYGHLSCL QVLLAHGADV DSLDVKAQTP LFTAVSHGHL DCVRVLLEAG
ASPGGSIYNN CSPVLTAARD GAVAILQELL DHGAEANVKA KLPVWASNIA SCSGPLYLAA
VYGHLDCFRL LLLHGADPDY NCTDQGLLAR VPRPRTLLEI CLHHNCEPEY IQLLIDFGAN
IYLPSLSLDL TSQDDKGIAL LLQARATPRS LLSQVRLVVR RALCQAGQPQ AINQLDIPPM
LISYLKHQL
//
