P50502 (F10A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hsc70-interacting protein
Short name=Hip

Alternative name(s):
Progesterone receptor-associated p48 protein
Protein FAM10A1
Putative tumor suppressor ST13
Renal carcinoma antigen NY-REN-33
Suppression of tumorigenicity 13 protein

Gene names

Name:	ST13
Synonyms:	FAM10A1, HIP, SNC6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins By similarity.
Subunit structure	Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 By similarity. Interacts (via the C-terminus 303- 319 AA) with GRK5. Ref.12
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the FAM10 family. Contains 1 STI1 domain. Contains 3 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	protein binding, bridging Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APOE	P02649	3	EBI-357285,EBI-1222467
NOS3	P29474	3	EBI-357285,EBI-1391623
PSEN1	P49768	3	EBI-357285,EBI-297277

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Hsc70-interacting protein		PRO_0000190811
Regions
	Repeat	114 – 147	34	TPR 1
	Repeat	148 – 181	34	TPR 2
	Repeat	182 – 215	34	TPR 3
	Domain	319 – 358	40	STI1
	Compositional bias	279 – 312	34	Gly/Met/Pro-rich
Amino acid modifications
	Modified residue	75	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14 Ref.15
	Modified residue	76	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	79	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
	Modified residue	181	1	Phosphoserine Ref.14
	Modified residue	346	1	Phosphoserine; by GRK5 Ref.12
Natural variations
	Natural variant	297	1	M → I. Corresponds to variant rs710193 [ dbSNP | Ensembl ].		VAR_011900
Experimental info
	Sequence conflict	24	1	H → Y in AAB38382. Ref.1
	Sequence conflict	38	1	M → I in AAB38382. Ref.1
	Sequence conflict	50	1	K → I in AAB38382. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P50502 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 98FCC65BEE14CDD7	FASTA	369	41,332
	10 20 30 40 50 60 MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP 70 80 90 100 110 120 DSKKVEEDLK ADEPSSEESD LEIDKEGVIE PDTDAPQEMG DENAEITEEM MDQANDKKVA 130 140 150 160 170 180 AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD 190 200 210 220 230 240 SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER 250 260 270 280 290 300 KREEREIKER IERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM 310 320 330 340 350 360 GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein." Prapapanich V., Chen S., Nair S.C., Rimerman R.A., Smith D.F. Mol. Endocrinol. 10:420-431(1996) [PubMed: 8721986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa." Mo Y., Zheng S., Shen D. Zhonghua Zhong Liu Za Zhi 18:241-243(1996) [PubMed: 9387309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon mucosa.
[3]	"Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening." Cao J., Cai X., Zheng L., Geng L., Shi Z., Pao C.C., Zheng S. J. Cancer Res. Clin. Oncol. 123:447-451(1997) [PubMed: 9292708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon mucosa.
[4]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin and Testis.
[7]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 119-142; 147-153; 174-186 AND 211-222, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[8]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Pituitary.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"G protein-coupled receptor kinase 5 phosphorylation of Hip regulates internalization of the chemokine receptor CXCR4." Barker B.L., Benovic J.L. Biochemistry 50:6933-6941(2011) [PubMed: 21728385] [Abstract] Cited for: PHOSPHORYLATION AT SER-346, INTERACTION WITH GRK5.
[13]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76; SER-79 AND SER-181, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-79, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28918 mRNA. Translation: AAB38382.1.
U17714 mRNA. Translation: AAC97526.1.
CR456586 mRNA. Translation: CAG30472.1.
Z98048 Genomic DNA. Translation: CAB10844.1.
BC052982 mRNA. Translation: AAH52982.1.
BC071629 mRNA. Translation: AAH71629.1.

IPI

IPI00032826.

RefSeq

NP_003923.2. NM_003932.3.

UniGene

Hs.712713.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UZS	model	-	A	98-244	[»]

ProteinModelPortal

P50502.

SMR

P50502. Positions 111-217.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50502. 16 interactions.

MINT

MINT-4999606.

STRING

P50502.

PTM databases

PhosphoSite

P50502.

Polymorphism databases

DMDM

6686278.

2D gel databases

OGP

P50502.

REPRODUCTION-2DPAGE

IPI00032826.

Proteomic databases

PeptideAtlas

P50502.

PRIDE

P50502.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216218; ENSP00000216218; ENSG00000100380.

GeneID

6767.

KEGG

hsa:6767.

UCSC

uc003aze.1. human.

Organism-specific databases

CTD

6767.

GeneCards

GC22M041220.

H-InvDB

HIX0016508.

HGNC

HGNC:11343. ST13.

HPA

CAB017443.

MIM

606796. gene.

neXtProt

NX_P50502.

PharmGKB

PA36167.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10570.

HOGENOM

HBG607553.

HOVERGEN

HBG002482.

InParanoid

P50502.

OMA

AKRASVY.

OrthoDB

EOG447FV0.

PhylomeDB

P50502.

Gene expression databases

ArrayExpress

P50502.

Bgee

P50502.

CleanEx

HS_ST13.

Genevestigator

P50502.

GermOnline

ENSG00000100380. Homo sapiens.

Family and domain databases

InterPro

IPR006636. STI1_HS-bd.
IPR001440. TPR-1.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 1 hit.

KO

K09560.

Pfam

PF00515. TPR_1. 1 hit.
[Graphical view]

SMART

SM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]

PROSITE

PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

26408.

PMAP-CutDB

P50502.

SOURCE

Search...

Entry information

Entry name

F10A1_HUMAN

Accession

Primary (citable) accession number: P50502
Secondary accession number(s): O14999

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.