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Protein

Stress-induced-phosphoprotein 1

Gene

Stip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-447041. CHL1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Stress-induced-phosphoprotein 1
Short name:
STI1
Short name:
mSTI1
Alternative name(s):
Hsc70/Hsp90-organizing protein
Short name:
Hop
Gene namesi
Name:Stip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:109130. Stip1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • myelin sheath Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Stress-induced-phosphoprotein 1PRO_0000106373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity
Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei198 – 1981PhosphothreonineBy similarity
Modified residuei301 – 3011N6-acetyllysineBy similarity
Modified residuei312 – 3121N6-acetyllysineBy similarity
Modified residuei325 – 3251N6-acetyllysineCombined sources
Modified residuei344 – 3441N6-acetyllysineBy similarity
Modified residuei354 – 3541PhosphotyrosineBy similarity
Modified residuei446 – 4461N6-acetyllysineBy similarity
Modified residuei481 – 4811PhosphoserineBy similarity

Post-translational modificationi

In vitro kinase assay failed to detect phosphorylation by MAPKAPK2.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ60864.
MaxQBiQ60864.
PaxDbiQ60864.
PRIDEiQ60864.

2D gel databases

REPRODUCTION-2DPAGEIPI00121514.
Q60864.
UCD-2DPAGEQ60864.

PTM databases

iPTMnetiQ60864.
PhosphoSiteiQ60864.
SwissPalmiQ60864.

Expressioni

Gene expression databases

BgeeiQ60864.
CleanExiMM_STIP1.
GenevisibleiQ60864. MM.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi203539. 4 interactions.
IntActiQ60864. 4 interactions.
MINTiMINT-1869468.
STRINGi10090.ENSMUSP00000025918.

Structurei

3D structure databases

ProteinModelPortaliQ60864.
SMRiQ60864. Positions 2-118, 223-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati4 – 3734TPR 1Add
BLAST
Repeati39 – 7133TPR 2Add
BLAST
Repeati73 – 10533TPR 3Add
BLAST
Domaini130 – 16940STI1 1Add
BLAST
Repeati225 – 25834TPR 4Add
BLAST
Repeati260 – 29233TPR 5Add
BLAST
Repeati300 – 33334TPR 6Add
BLAST
Repeati360 – 39334TPR 7Add
BLAST
Repeati395 – 42733TPR 8Add
BLAST
Repeati428 – 46134TPR 9Add
BLAST
Domaini492 – 53140STI1 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi222 – 23918Bipartite nuclear localization signalSequence analysisAdd
BLAST

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Contains 2 STI1 domains.Curated
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0548. Eukaryota.
ENOG410XTCJ. LUCA.
GeneTreeiENSGT00840000129761.
HOGENOMiHOG000186562.
HOVERGENiHBG057820.
InParanoidiQ60864.
KOiK09553.
OMAiSKCRELC.
OrthoDBiEOG7BGHM5.
PhylomeDBiQ60864.
TreeFamiTF300478.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
PF13414. TPR_11. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60864-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK
60 70 80 90 100
KGDYQKAYED GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK
110 120 130 140 150
HEANNLQLKE GLQNMEARLA ERKFMNPFNL PNLYQKLEND PRTRSLLSDP
160 170 180 190 200
TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS VLLGVDLGSM DEEEEAATPP
210 220 230 240 250
PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDKALKHYDR
260 270 280 290 300
AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
310 320 330 340 350
KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE
360 370 380 390 400
RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR
410 420 430 440 450
AACYTKLLEF QLALKDCEEC IQLEPTFIKG YTRKAAALEA MKDYTKAMDV
460 470 480 490 500
YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS
510 520 530 540
DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR
Length:543
Mass (Da):62,582
Last modified:November 1, 1996 - v1
Checksum:iB737FBA92B198D6C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151L → P in BAC36100 (PubMed:16141072).Curated
Sequence conflicti106 – 1061L → V in AAH03794 (PubMed:15489334).Curated
Sequence conflicti274 – 2796DYNKCR → RLYKCT in BAC36100 (PubMed:16141072).Curated
Sequence conflicti288 – 2881V → S in BAC36100 (PubMed:16141072).Curated
Sequence conflicti305 – 3106RIGNSY → PNWQFL in BAC36100 (PubMed:16141072).Curated
Sequence conflicti316 – 3172YK → VQ in BAC36100 (PubMed:16141072).Curated
Sequence conflicti333 – 34715PDVLK…EKILK → QMCSRSASSQRNSE in BAC36100 (PubMed:16141072).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27830 mRNA. Translation: AAC53267.1.
AK075988 mRNA. Translation: BAC36100.1.
AK088494 mRNA. Translation: BAC40389.1.
AK149493 mRNA. Translation: BAE28916.1.
AK161645 mRNA. Translation: BAE36509.1.
AK167273 mRNA. Translation: BAE39385.1.
BC003794 mRNA. Translation: AAH03794.1.
CCDSiCCDS37901.1.
RefSeqiNP_058017.1. NM_016737.2.
UniGeneiMm.258633.

Genome annotation databases

EnsembliENSMUST00000025918; ENSMUSP00000025918; ENSMUSG00000024966.
GeneIDi20867.
KEGGimmu:20867.
UCSCiuc008gke.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27830 mRNA. Translation: AAC53267.1.
AK075988 mRNA. Translation: BAC36100.1.
AK088494 mRNA. Translation: BAC40389.1.
AK149493 mRNA. Translation: BAE28916.1.
AK161645 mRNA. Translation: BAE36509.1.
AK167273 mRNA. Translation: BAE39385.1.
BC003794 mRNA. Translation: AAH03794.1.
CCDSiCCDS37901.1.
RefSeqiNP_058017.1. NM_016737.2.
UniGeneiMm.258633.

3D structure databases

ProteinModelPortaliQ60864.
SMRiQ60864. Positions 2-118, 223-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203539. 4 interactions.
IntActiQ60864. 4 interactions.
MINTiMINT-1869468.
STRINGi10090.ENSMUSP00000025918.

PTM databases

iPTMnetiQ60864.
PhosphoSiteiQ60864.
SwissPalmiQ60864.

2D gel databases

REPRODUCTION-2DPAGEIPI00121514.
Q60864.
UCD-2DPAGEQ60864.

Proteomic databases

EPDiQ60864.
MaxQBiQ60864.
PaxDbiQ60864.
PRIDEiQ60864.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025918; ENSMUSP00000025918; ENSMUSG00000024966.
GeneIDi20867.
KEGGimmu:20867.
UCSCiuc008gke.2. mouse.

Organism-specific databases

CTDi10963.
MGIiMGI:109130. Stip1.

Phylogenomic databases

eggNOGiKOG0548. Eukaryota.
ENOG410XTCJ. LUCA.
GeneTreeiENSGT00840000129761.
HOGENOMiHOG000186562.
HOVERGENiHBG057820.
InParanoidiQ60864.
KOiK09553.
OMAiSKCRELC.
OrthoDBiEOG7BGHM5.
PhylomeDBiQ60864.
TreeFamiTF300478.

Enzyme and pathway databases

ReactomeiR-MMU-447041. CHL1 interactions.

Miscellaneous databases

ChiTaRSiStip1. mouse.
PROiQ60864.
SOURCEiSearch...

Gene expression databases

BgeeiQ60864.
CleanExiMM_STIP1.
GenevisibleiQ60864. MM.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
PF13414. TPR_11. 2 hits.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00028. TPR. 9 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 9 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif."
    Blatch G.L., Laessle M., Zetter B.R., Kundra V.
    Gene 194:277-282(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung carcinoma.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Liver and Thymus.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. Bienvenut W.V., Frezza C., Gottlieb E.
    Submitted (MAY-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-10; 94-109; 124-136; 145-169; 306-315; 352-364; 435-446; 506-513 AND 534-543, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Kidney.
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 14-44, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases."
    Laessle M., Blatch G.L., Kundra V., Takatori T., Zetter B.R.
    J. Biol. Chem. 272:1876-1884(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HSC70; HSPCA AND HSPCB.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-325, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSTIP1_MOUSE
AccessioniPrimary (citable) accession number: Q60864
Secondary accession number(s): Q3TT16, Q8BPH3, Q99L66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.