P50502 (F10A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hsc70-interacting protein
Short name=Hip

Alternative name(s):
Aging-associated protein 2
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:	AAG2, FAM10A1, HIP, SNC6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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)
Biological_process	chaperone cofactor-dependent protein refolding Inferred from electronic annotation. Source: Compara negative regulation of protein refolding Inferred from electronic annotation. Source: Compara protein folding Traceable author statement Ref.1. Source: ProtInc protein homooligomerization Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc cytosol Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	dATP binding Inferred from electronic annotation. Source: Compara protein binding, bridging Traceable author statement Ref.1. 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	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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon mucosa.
[4]	"Identification of human aging-associated gene." Kim J.W. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin and Testis.
[9]	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.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-346, INTERACTION WITH GRK5.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28918 mRNA. Translation: AAB38382.1.
U17714 mRNA. Translation: AAC97526.1.
AY513286 mRNA. Translation: AAT08039.1.
CR456586 mRNA. Translation: CAG30472.1.
Z98048 Genomic DNA. Translation: CAB10844.1.
CH471095 Genomic DNA. Translation: EAW60394.1.
BC052982 mRNA. Translation: AAH52982.1.
BC071629 mRNA. Translation: AAH71629.1.
BC139724 mRNA. Translation: AAI39725.1.

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.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50502. 19 interactions.

MINT

MINT-4999606.

STRING

9606.ENSP00000216218.

PTM databases

PhosphoSite

P50502.

Polymorphism databases

DMDM

6686278.

2D gel databases

OGP

P50502.

REPRODUCTION-2DPAGE

IPI00032826.

Proteomic databases

PaxDb

P50502.

PeptideAtlas

P50502.

PRIDE

P50502.

Protocols and materials databases

DNASU

6767.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216218; ENSP00000216218; ENSG00000100380.

GeneID

6767.

KEGG

hsa:6767.

UCSC

uc003aze.3. human.

Organism-specific databases

CTD

6767.

GeneCards

GC22M041220.

HGNC

HGNC:11343. ST13.

HPA

HPA043233.
HPA046412.
HPA047114.
HPA047116.

MIM

606796. gene.

neXtProt

NX_P50502.

PharmGKB

PA36167.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260098.

HOGENOM

HOG000001586.

HOVERGEN

HBG002482.

InParanoid

P50502.

KO

K09560.

OMA

PPATHKT.

OrthoDB

EOG447FV0.

PhylomeDB

P50502.

Gene expression databases

ArrayExpress

P50502.

Bgee

P50502.

CleanEx

HS_ST13.

Genevestigator

P50502.

GermOnline

ENSG00000100380. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 1 hit.

InterPro

IPR006636. STI1_HS-bd.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF00515. TPR_1. 1 hit.
PF07719. TPR_2. 2 hits.
[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

ChiTaRS

ST13. human.

GenomeRNAi

6767.

NextBio

26408.

PMAP-CutDB

P50502.

SOURCE

Search...

Entry information

Entry name

F10A1_HUMAN

Accession

Primary (citable) accession number: P50502
Secondary accession number(s): O14999, Q2TU77

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 143 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.