F10A1_HUMAN
ID F10A1_HUMAN Reviewed; 369 AA.
AC P50502; O14999; Q2TU77;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Hsc70-interacting protein;
DE Short=Hip;
DE AltName: Full=Aging-associated protein 2;
DE AltName: Full=Progesterone receptor-associated p48 protein;
DE AltName: Full=Protein FAM10A1;
DE AltName: Full=Putative tumor suppressor ST13;
DE AltName: Full=Renal carcinoma antigen NY-REN-33;
DE AltName: Full=Suppression of tumorigenicity 13 protein;
GN Name=ST13; Synonyms=AAG2, FAM10A1, HIP, SNC6;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8721986; DOI=10.1210/mend.10.4.8721986;
RA Prapapanich V., Chen S., Nair S.C., Rimerman R.A., Smith D.F.;
RT "Molecular cloning of human p48, a transient component of progesterone
RT receptor complexes and an Hsp70-binding protein.";
RL Mol. Endocrinol. 10:420-431(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9387309;
RA Mo Y., Zheng S., Shen D.;
RT "Differential expression of HSU17714 gene in colorectal cancer and normal
RT colonic mucosa.";
RL Zhonghua Zhong Liu Za Zhi 18:241-243(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon mucosa;
RX PubMed=9292708; DOI=10.1007/bf01372549;
RA Cao J., Cai X., Zheng L., Geng L., Shi Z., Pao C.C., Zheng S.;
RT "Characterization of colorectal-cancer-related cDNA clones obtained by
RT subtractive hybridization screening.";
RL J. Cancer Res. Clin. Oncol. 123:447-451(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim J.W.;
RT "Identification of human aging-associated gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Testis;
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 [9]
RP PROTEIN SEQUENCE OF 119-142; 147-153; 174-186 AND 211-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION AT SER-346, AND INTERACTION WITH GRK5.
RX PubMed=21728385; DOI=10.1021/bi2005202;
RA Barker B.L., Benovic J.L.;
RT "G protein-coupled receptor kinase 5 phosphorylation of Hip regulates
RT internalization of the chemokine receptor CXCR4.";
RL Biochemistry 50:6933-6941(2011).
RN [13]
RP 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., 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).
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least two
CC HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40.
CC Stabilizes the ADP state of HSC70 that has a high affinity for
CC substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of HSC70 with various target proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs
CC and HSP90 (By similarity). Interacts (via the C-terminus 303- 319 AA)
CC with GRK5. {ECO:0000250, ECO:0000269|PubMed:21728385}.
CC -!- INTERACTION:
CC P50502; P02649: APOE; NbExp=3; IntAct=EBI-357285, EBI-1222467;
CC P50502; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-357285, EBI-12300031;
CC P50502; P42858: HTT; NbExp=13; IntAct=EBI-357285, EBI-466029;
CC P50502; P29474: NOS3; NbExp=3; IntAct=EBI-357285, EBI-1391623;
CC P50502; P49768: PSEN1; NbExp=3; IntAct=EBI-357285, EBI-297277;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28918; AAB38382.1; -; mRNA.
DR EMBL; U17714; AAC97526.1; -; mRNA.
DR EMBL; AY513286; AAT08039.1; -; mRNA.
DR EMBL; CR456586; CAG30472.1; -; mRNA.
DR EMBL; Z98048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60394.1; -; Genomic_DNA.
DR EMBL; BC052982; AAH52982.1; -; mRNA.
DR EMBL; BC071629; AAH71629.1; -; mRNA.
DR EMBL; BC139724; AAI39725.1; -; mRNA.
DR CCDS; CCDS14006.1; -.
DR RefSeq; NP_003923.2; NM_003932.4.
DR AlphaFoldDB; P50502; -.
DR SMR; P50502; -.
DR BioGRID; 112644; 96.
DR CORUM; P50502; -.
DR IntAct; P50502; 43.
DR MINT; P50502; -.
DR STRING; 9606.ENSP00000216218; -.
DR GlyGen; P50502; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50502; -.
DR MetOSite; P50502; -.
DR PhosphoSitePlus; P50502; -.
DR SwissPalm; P50502; -.
DR BioMuta; ST13; -.
DR DMDM; 6686278; -.
DR OGP; P50502; -.
DR REPRODUCTION-2DPAGE; IPI00032826; -.
DR EPD; P50502; -.
DR jPOST; P50502; -.
DR MassIVE; P50502; -.
DR PaxDb; P50502; -.
DR PeptideAtlas; P50502; -.
DR PRIDE; P50502; -.
DR ProteomicsDB; 56234; -.
DR Antibodypedia; 3378; 387 antibodies from 34 providers.
DR DNASU; 6767; -.
DR Ensembl; ENST00000216218.8; ENSP00000216218.3; ENSG00000100380.15.
DR GeneID; 6767; -.
DR KEGG; hsa:6767; -.
DR MANE-Select; ENST00000216218.8; ENSP00000216218.3; NM_003932.5; NP_003923.2.
DR UCSC; uc003aze.5; human.
DR CTD; 6767; -.
DR DisGeNET; 6767; -.
DR GeneCards; ST13; -.
DR HGNC; HGNC:11343; ST13.
DR HPA; ENSG00000100380; Low tissue specificity.
DR MIM; 606796; gene.
DR neXtProt; NX_P50502; -.
DR OpenTargets; ENSG00000100380; -.
DR PharmGKB; PA36167; -.
DR VEuPathDB; HostDB:ENSG00000100380; -.
DR eggNOG; KOG1308; Eukaryota.
DR GeneTree; ENSGT00390000001347; -.
DR InParanoid; P50502; -.
DR OMA; TVLNMPQ; -.
DR OrthoDB; 1282821at2759; -.
DR PhylomeDB; P50502; -.
DR TreeFam; TF313244; -.
DR PathwayCommons; P50502; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; P50502; -.
DR SIGNOR; P50502; -.
DR BioGRID-ORCS; 6767; 36 hits in 1035 CRISPR screens.
DR ChiTaRS; ST13; human.
DR GeneWiki; ST13; -.
DR GenomeRNAi; 6767; -.
DR Pharos; P50502; Tbio.
DR PRO; PR:P50502; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P50502; protein.
DR Bgee; ENSG00000100380; Expressed in left ovary and 208 other tissues.
DR ExpressionAtlas; P50502; baseline and differential.
DR Genevisible; P50502; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:ProtInc.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18253; HipN; 1.
DR Pfam; PF17830; STI1; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..369
FT /note="Hsc70-interacting protein"
FT /id="PRO_0000190811"
FT REPEAT 114..147
FT /note="TPR 1"
FT REPEAT 148..181
FT /note="TPR 2"
FT REPEAT 182..215
FT /note="TPR 3"
FT DOMAIN 319..358
FT /note="STI1"
FT REGION 38..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 346
FT /note="Phosphoserine; by GRK5"
FT /evidence="ECO:0000269|PubMed:21728385"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L47"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99L47"
FT VARIANT 297
FT /note="M -> I (in dbSNP:rs710193)"
FT /id="VAR_011900"
FT CONFLICT 24
FT /note="H -> Y (in Ref. 1; AAB38382)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="M -> I (in Ref. 1; AAB38382)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="K -> I (in Ref. 1; AAB38382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41332 MW; 98FCC65BEE14CDD7 CRC64;
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP
DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA
AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD
SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER
KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM
GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK
LSAKFGGQA
