Reviewed, UniProtKB/Swiss-Prot P31948 (STIP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Stress-induced-phosphoprotein 1
      Short name=STI1
Alternative name(s):
    Hsc70/Hsp90-organizing protein
      Short name=Hop
    Transformation-sensitive protein IEF SSP 3521
    NY-REN-11 antigen

Gene names

Name:

STIP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.10
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 component	Cytoplasm Nucleus
Domain	Repeat TPR repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to stress Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Ref.1 Traceable author statement. Source: ProtInc nucleus Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NME2	P22392	1	EBI-1054052,EBI-713693
WDR8	Q9P2S5	1	EBI-1054052,EBI-1054904

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 543

543

Stress-induced-phosphoprotein 1

PRO_0000106372

Regions

Repeat

4 – 37

34

TPR 1

Repeat

38 – 71

34

TPR 2

Repeat

72 – 105

34

TPR 3

Domain

130 – 169

40

STI1 1

Repeat

225 – 258

34

TPR 4

Repeat

259 – 292

34

TPR 5

Repeat

300 – 333

34

TPR 6

Repeat

360 – 393

34

TPR 7

Repeat

394 – 427

34

TPR 8

Repeat

428 – 461

34

TPR 9

Domain

492 – 531

40

STI1 2

Motif

222 – 239

18

Bipartite nuclear localization signal Potential

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6

Modified residue

8

1

N6-acetyllysine Ref.18

Modified residue

16

1

Phosphoserine Ref.15

Modified residue

68

1

N6-acetyllysine Ref.18

Modified residue

73

1

N6-acetyllysine Ref.18

Modified residue

100

1

N6-acetyllysine Ref.18

Modified residue

198

1

Phosphothreonine Ref.14

Modified residue

246

1

N6-acetyllysine Ref.13

Modified residue

301

1

N6-acetyllysine Ref.18

Modified residue

312

1

N6-acetyllysine Ref.18

Modified residue

325

1

N6-acetyllysine Ref.18

Modified residue

344

1

N6-acetyllysine Ref.18

Modified residue

354

1

Phosphotyrosine Ref.11 Ref.17

Modified residue

388

1

N6-acetyllysine Ref.18

Modified residue

446

1

N6-acetyllysine Ref.18

Modified residue

481

1

Phosphoserine Ref.15 Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

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.

.

.

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.

.

.

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.

.

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543

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

20 – 33

14

Helix

38 – 51

14

Helix

54 – 67

14

Helix

72 – 84

13

Helix

88 – 99

12

Helix

106 – 117

12

Helix

223 – 237

15

Helix

241 – 254

14

Helix

259 – 272

14

Helix

275 – 291

17

Helix

296 – 312

17

Helix

316 – 329

14

Helix

333 – 348

16

Sequences

	Sequence		Length	Mass (Da)
	P31948-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 8E58ECA13825CB0E	FASTA	543	62,639
	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

References

	« Hide 'large scale' referencesShow '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: 1569099] [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. , 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: 15489334] [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, 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, 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: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 101-109; 352-364 AND 374-381. Tissue: Keratinocyte.
[9]	"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.
[10]	"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: 14532270] [Abstract] Cited for: INTERACTION WITH PACRG.
[11]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, MASS SPECTROMETRY.
[12]	"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-481, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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 THR-198, MASS SPECTROMETRY.
[15]	"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-16 AND SER-481, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-68; LYS-73; LYS-100; LYS-301; LYS-312; LYS-325; LYS-344; LYS-388 AND LYS-446, MASS SPECTROMETRY.
[19]	"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: 10786835] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 223-349.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00013894.

PIR

A38093.

RefSeq

NP_006810.1.

UniGene

Hs.337295

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ELR	X-ray	1.90	A	223-352	[»]
1ELW	X-ray	1.60	A/B	1-118	[»]
3ESK	X-ray	2.05	A	223-350	[»]
3FWV	X-ray	2.20	A/B	223-349	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P31948. 6 interactions.

STRING

P31948.

PTM databases

PhosphoSite

P31948.

2-D gel databases

Aarhus/Ghent-2DPAGE

2410. IEF.

REPRODUCTION-2DPAGE

IPI00013894.

Proteomic databases

PRIDE

P31948.

Genome annotation databases

Ensembl

ENST00000305218; ENSP00000305958; ENSG00000168439; Homo sapiens. [Genome view]
ENST00000358794; ENSP00000351646; ENSG00000168439; Homo sapiens. [Genome view]

GeneID

10963.

KEGG

hsa:10963.

UCSC

uc001nyk.1. human.

Organism-specific databases

CTD

10963.

GeneCards

GC11P063709.

H-InvDB

HIX0019658.

HGNC

HGNC:11387. STIP1.

MIM

605063. gene.

PharmGKB

PA36196.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P31948.

Gene expression databases

ArrayExpress

P31948.

Bgee

P31948.

CleanEx

HS_STIP1.

Genevestigator

P31948.

GermOnline

ENSG00000168439. Homo sapiens.

Family and domain databases

InterPro

IPR006636. STI1_HS_bd.
IPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
IPR019734. TPR_repeat.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 2 hits.

Pfam

PF00515. TPR_1. 9 hits.
[Graphical view]

SMART

SM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]

PROSITE

PS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

41662.

SOURCE

Search...

Entry information

Entry name

STIP1_HUMAN

Accession

Primary (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:	November 3, 2009
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.