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P31948 (STIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Stress-induced-phosphoprotein 1

Short name=STI1
Alternative name(s):
Hsc70/Hsp90-organizing protein
Short name=Hop
Renal carcinoma antigen NY-REN-11
Transformation-sensitive protein IEF SSP 3521
Gene names
Name:STIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB).

Subunit structure

Forms a complex with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84. Interacts with PACRG. Interacts with METTL21B. Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction. Ref.9 Ref.11 Ref.20

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Domain

The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.

Sequence similarities

Contains 2 STI1 domains.

Contains 9 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
TPR repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stress

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Traceable author statement Ref.1. Source: ProtInc

nucleus

Traceable author statement PubMed 16130169. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFRP005332EBI-1054052,EBI-297353

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543Stress-induced-phosphoprotein 1
PRO_0000106372

Regions

Repeat4 – 3734TPR 1
Repeat38 – 7134TPR 2
Repeat72 – 10534TPR 3
Domain130 – 16940STI1 1
Repeat225 – 25834TPR 4
Repeat259 – 29234TPR 5
Repeat300 – 33334TPR 6
Repeat360 – 39334TPR 7
Repeat394 – 42734TPR 8
Repeat428 – 46134TPR 9
Domain492 – 53140STI1 2
Motif222 – 23918Bipartite nuclear localization signal Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.14 Ref.15 Ref.19
Modified residue81N6-acetyllysine Ref.15
Modified residue161Phosphoserine Ref.13
Modified residue3011N6-acetyllysine Ref.15
Modified residue3121N6-acetyllysine Ref.15
Modified residue3251N6-acetyllysine Ref.15
Modified residue3441N6-acetyllysine Ref.15
Modified residue3541Phosphotyrosine Ref.12
Modified residue4461N6-acetyllysine Ref.15
Modified residue4811Phosphoserine Ref.16 Ref.18

Secondary structure

............................................. 543
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31948 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 8E58ECA13825CB0E

FASTA54362,639
        10         20         30         40         50         60 
MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED 

        70         80         90        100        110        120 
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA 

       130        140        150        160        170        180 
ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLR NKPSDLGTKL QDPRIMTTLS 

       190        200        210        220        230        240 
VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD 

       250        260        270        280        290        300 
FDTALKHYDK AKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA 

       310        320        330        340        350        360 
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA 

       370        380        390        400        410        420 
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC 

       430        440        450        460        470        480 
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD 

       490        500        510        520        530        540 
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI 


AIR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1."
Honore B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.
J. Biol. Chem. 267:8485-8491(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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].
[5]"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: Lung.
[6]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-10; 110-118; 345-364; 382-389; 479-486 AND 534-543, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[7]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-44; 64-73; 79-87; 154-160; 253-272; 306-312; 352-364; 407-429; 454-462; 489-513 AND 534-543, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381.
Tissue: Keratinocyte.
[9]"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSP90AA1.
[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]"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACRG.
[12]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-8; LYS-301; LYS-312; LYS-325; LYS-344 AND LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH METTL21B.
[21]"Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine."
Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I.
Cell 101:199-210(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86752 mRNA. Translation: AAA58682.1.
BT020010 mRNA. Translation: AAV38813.1.
BT020011 mRNA. Translation: AAV38814.1.
CR536512 mRNA. Translation: CAG38750.1.
CH471076 Genomic DNA. Translation: EAW74196.1.
BC002987 mRNA. Translation: AAH02987.1.
PIRA38093.
RefSeqNP_006810.1. NM_006819.2.
UniGeneHs.337295.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELRX-ray1.90A223-352[»]
1ELWX-ray1.60A/B1-118[»]
2LNINMR-A356-477[»]
3ESKX-ray2.05A223-350[»]
3FWVX-ray2.20A/B223-349[»]
ProteinModelPortalP31948.
SMRP31948. Positions 2-118, 223-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116162. 58 interactions.
DIPDIP-41085N.
IntActP31948. 25 interactions.
MINTMINT-132047.
STRING9606.ENSP00000305958.

PTM databases

PhosphoSiteP31948.

Polymorphism databases

DMDM400042.

2D gel databases

REPRODUCTION-2DPAGEIPI00013894.
UCD-2DPAGEP31948.

Proteomic databases

PaxDbP31948.
PRIDEP31948.

Protocols and materials databases

DNASU10963.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305218; ENSP00000305958; ENSG00000168439.
GeneID10963.
KEGGhsa:10963.
UCSCuc001nyk.1. human.

Organism-specific databases

CTD10963.
GeneCardsGC11P063953.
HGNCHGNC:11387. STIP1.
HPACAB017448.
HPA039291.
HPA044062.
MIM605063. gene.
neXtProtNX_P31948.
PharmGKBPA36196.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000186562.
HOVERGENHBG057820.
KOK09553.
PhylomeDBP31948.
TreeFamTF300478.

Gene expression databases

ArrayExpressP31948.
BgeeP31948.
CleanExHS_STIP1.
GenevestigatorP31948.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 8 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
PROSITEPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTIP1. human.
EvolutionaryTraceP31948.
GeneWikiHop_(protein).
GenomeRNAi10963.
NextBio41662.
PROP31948.
SOURCESearch...

Entry information

Entry nameSTIP1_HUMAN
AccessionPrimary (citable) accession number: P31948
Secondary accession number(s): Q5TZU9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 153 of the entry and version 1 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 chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM