ID H0Y394_HUMAN Unreviewed; 973 AA.
AC H0Y394;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=High density lipoprotein binding protein {ECO:0000313|Ensembl:ENSP00000362389.4};
DE Flags: Fragment;
GN Name=HDLBP {ECO:0000313|Ensembl:ENSP00000362389.4};
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 {ECO:0000313|Ensembl:ENSP00000362389.4, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0007829|PubMed:15592455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [2] {ECO:0000313|Ensembl:ENSP00000362389.4, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4] {ECO:0007829|PubMed:21269460}
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., Burckstummer T.,
RA 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 [5] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6] {ECO:0007829|PubMed:25944712}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7] {ECO:0000313|Ensembl:ENSP00000362389.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AC104841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MassIVE; H0Y394; -.
DR MaxQB; H0Y394; -.
DR PeptideAtlas; H0Y394; -.
DR ProteomicsDB; 34463; -.
DR Antibodypedia; 1371; 355 antibodies from 29 providers.
DR Ensembl; ENST00000373292.8; ENSP00000362389.4; ENSG00000115677.18.
DR UCSC; uc061umt.1; human.
DR HGNC; HGNC:4857; HDLBP.
DR VEuPathDB; HostDB:ENSG00000115677; -.
DR GeneTree; ENSGT00900000141059; -.
DR HOGENOM; CLU_008532_0_0_1; -.
DR ChiTaRS; HDLBP; human.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000115677; Expressed in stromal cell of endometrium and 207 other cell types or tissues.
DR ExpressionAtlas; H0Y394; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd22413; KH-I_Vigilin_rpt10; 1.
DR CDD; cd22414; KH-I_Vigilin_rpt11; 1.
DR CDD; cd22415; KH-I_Vigilin_rpt12; 1.
DR CDD; cd22416; KH-I_Vigilin_rpt13; 1.
DR CDD; cd22406; KH-I_Vigilin_rpt2; 1.
DR CDD; cd22407; KH-I_Vigilin_rpt3; 1.
DR CDD; cd22409; KH-I_Vigilin_rpt5; 1.
DR CDD; cd02394; KH-I_Vigilin_rpt6; 1.
DR CDD; cd22410; KH-I_Vigilin_rpt7; 1.
DR CDD; cd22411; KH-I_Vigilin_rpt8; 1.
DR CDD; cd22412; KH-I_Vigilin_rpt9; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 12.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627; SCP160; 1.
DR PANTHER; PTHR10627:SF34; VIGILIN; 1.
DR Pfam; PF00013; KH_1; 12.
DR SMART; SM00322; KH; 12.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 10.
DR PROSITE; PS50084; KH_TYPE_1; 12.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|EPD:H0Y394,
KW ECO:0007829|MaxQB:H0Y394};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 27..95
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 99..167
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 172..238
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 243..311
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 315..384
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 389..457
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 461..530
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 535..604
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 608..677
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 681..781
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 782..848
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 860..933
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 726..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..612
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 943..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000362389.4"
SQ SEQUENCE 973 AA; 108845 MW; A6E300E3E38E8EF4 CRC64;
XGLSIMVSGK LDAVMKARKD IVARLQTQAS ATVAIPKEHH RFVIGKNGEK LQDLELKTAT
KIQIPRPDDP SNQIKITGTK EGIEKARHEV LLISAEQDKR AVERLEVEKA FHPFIAGPYN
RLVGEIMQET GTRINIPPPS VNRTEIVFTG EKEQLAQAVA RIKKIYEEKA NSFTVSSVAA
PSWLHRFIIG KKGQNLAKIT QQMPKVHIEF TEGEDKITLE GPTEDVNVAQ EQIEGMVKDL
INRMDYVEIN IDHKFHRHLI GKSGANINRI KDQYKVSVRI PPDSEKSNLI RIEGDPQGVQ
QAKRELLELA SRMENERTKD LIIEQRFHRT IIGQKGERIR EIRDKFPEVI INFPDPAQKS
DIVQLRGPKN EVEKCTKYMQ KMVADLVENS YSISVPIFKQ FHKNIIGKGG ANIKKIREES
NTKIDLPAEN SNSETIIITG KRANCEAARS RILSIQKDLA NIAEVEVSIP AKLHNSLIGT
KGRLIRSIME ECGGVHIHFP VEGSGSDTVV IRGPSSDVEK AKKQLLHLAE EKQTKSFTVD
IRAKPEYHKF LIGKGGGKIR KVRDSTGARV IFPAAEDKDQ DLITIIGKED AVREAQKELE
ALIQNLDNVV EDSMLVDPKH HRHFVIRRGQ VLREIAEEYG GVMVSFPRSG TQSDKVTLKG
AKDCVEAAKK RIQEIIEDLE AQVTLECAIP QKFHRSVMGP KGSRIQQITR DFSVQIKFPD
REENAVHSTE PVVQENGDEA GEGREAKDCD PGSPRRCDII IISGRKEKCE AAKEALEALV
PVTIEVEVPF DLHRYVIGQK GSGIRKMMDE FEVNIHVPAP ELQSDIIAIT GLAANLDRAK
AGLLERVKEL QAEQEDRALR SFKLSVTVDP KYHPKIIGRK GAVITQIRLE HDVNILNLEE
EYLADVVDSE ALQVYMKPPA HEEAKAPSRG FVVRDAPWTA SSSEKAPDMS SSEEFPSFGA
QVAPKTLPWG PKR
//
