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P50502 (F10A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Hsc70-interacting protein
PRO_0000190811

Regions

Repeat114 – 14734TPR 1
Repeat148 – 18134TPR 2
Repeat182 – 21534TPR 3
Domain319 – 35840STI1
Compositional bias279 – 31234Gly/Met/Pro-rich

Amino acid modifications

Modified residue3461Phosphoserine; by GRK5 Ref.12
Modified residue3531N6-acetyllysine By similarity
Modified residue3601N6-acetyllysine By similarity

Natural variations

Natural variant2971M → I.
Corresponds to variant rs710193 [ dbSNP | Ensembl ].
VAR_011900

Experimental info

Sequence conflict241H → Y in AAB38382. Ref.1
Sequence conflict381M → I in AAB38382. Ref.1
Sequence conflict501K → I in AAB38382. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P50502 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 98FCC65BEE14CDD7

FASTA36941,332
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.
CCDSCCDS14006.1.
RefSeqNP_003923.2. NM_003932.4.
UniGeneHs.712713.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UZSmodel-A98-244[»]
ProteinModelPortalP50502.
SMRP50502. Positions 1-44, 78-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112644. 34 interactions.
IntActP50502. 21 interactions.
MINTMINT-4999606.
STRING9606.ENSP00000216218.

PTM databases

PhosphoSiteP50502.

Polymorphism databases

DMDM6686278.

2D gel databases

OGPP50502.
REPRODUCTION-2DPAGEIPI00032826.

Proteomic databases

MaxQBP50502.
PaxDbP50502.
PeptideAtlasP50502.
PRIDEP50502.

Protocols and materials databases

DNASU6767.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216218; ENSP00000216218; ENSG00000100380.
GeneID6767.
KEGGhsa:6767.
UCSCuc003aze.3. human.

Organism-specific databases

CTD6767.
GeneCardsGC22M041220.
HGNCHGNC:11343. ST13.
HPAHPA043233.
HPA046412.
HPA047114.
HPA047116.
MIM606796. gene.
neXtProtNX_P50502.
PharmGKBPA36167.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260098.
HOGENOMHOG000001586.
HOVERGENHBG002482.
InParanoidP50502.
KOK09560.
OMAQANEKKM.
OrthoDBEOG77M8P3.
PhylomeDBP50502.
TreeFamTF313244.

Gene expression databases

ArrayExpressP50502.
BgeeP50502.
CleanExHS_ST13.
GenevestigatorP50502.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 1 hit.
PF07719. TPR_2. 2 hits.
[Graphical view]
SMARTSM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSST13. human.
GeneWikiST13.
GenomeRNAi6767.
NextBio26408.
PMAP-CutDBP50502.
PROP50502.
SOURCESearch...

Entry information

Entry nameF10A1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM