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Protein

Hsc70-interacting protein

Gene

St13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Hsc70-interacting protein
Short name:
Hip
Alternative name(s):
Protein FAM10A1
Protein ST13 homolog
Gene namesi
Name:St13
Synonyms:Fam10a1, Hip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1917606. St13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Hsc70-interacting proteinPRO_0000190812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei348 – 3481Phosphoserine; by GRK5By similarity
Modified residuei355 – 3551N6-acetyllysineCombined sources
Modified residuei362 – 3621N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99L47.
MaxQBiQ99L47.
PaxDbiQ99L47.
PeptideAtlasiQ99L47.
PRIDEiQ99L47.

2D gel databases

REPRODUCTION-2DPAGEQ99L47.

PTM databases

iPTMnetiQ99L47.
PhosphoSiteiQ99L47.

Expressioni

Gene expression databases

BgeeiQ99L47.
CleanExiMM_ST13.
ExpressionAtlasiQ99L47. baseline and differential.
GenevisibleiQ99L47. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90 (By similarity). Interacts (via the C-terminus 302- 318 AA) with GRK5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi213997. 1 interaction.
IntActiQ99L47. 5 interactions.
MINTiMINT-1869549.
STRINGi10090.ENSMUSP00000130195.

Structurei

3D structure databases

ProteinModelPortaliQ99L47.
SMRiQ99L47. Positions 1-44, 77-274.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati113 – 14634TPR 1Add
BLAST
Repeati147 – 18034TPR 2Add
BLAST
Repeati181 – 21434TPR 3Add
BLAST
Domaini321 – 36040STI1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi278 – 31437Gly/Met/Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the FAM10 family.Curated
Contains 1 STI1 domain.Curated
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1308. Eukaryota.
ENOG410XR19. LUCA.
GeneTreeiENSGT00390000001347.
HOGENOMiHOG000001586.
HOVERGENiHBG002482.
InParanoidiQ99L47.
KOiK09560.
OMAiVQPKANK.
OrthoDBiEOG77M8P3.
TreeFamiTF313244.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99L47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPRKVSELR AFVKMCRQDP SVLHTEEMRF LREWVESMGG KVPPATHKAK
60 70 80 90 100
SEENTKEEKR DKTTEENIKT EELSSEESDL EIDNEGVIEP DTDAPQEMGD
110 120 130 140 150
ENAEITEEMM DEANEKKGAA IEALNDGELQ KAIDLFTDAI KLNPRLAILY
160 170 180 190 200
AKRASVFVKL QKPNAAIRDC DRAIEINPDS AQPYKWRGKA HRLLGHWEEA
210 220 230 240 250
AHDLALACKL DYDEDASAML REVQPRAQKI AEHRRKYERK REEREIKERI
260 270 280 290 300
ERVKKAREEH ERAQREEEAR RQSGSQYGSF PGGFPGGMPG NFPGGMPGMG
310 320 330 340 350
GAMPGMAGMA GMPGLNEILS DPEVLAAMQD PEVMVAFQDV AQNPSNMSKY
360 370
QSNPKVMNLI SKLSAKFGGQ S
Length:371
Mass (Da):41,656
Last modified:June 1, 2001 - v1
Checksum:i7F9417F251B99F4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT010318 mRNA. Translation: CAJ18526.1.
AK146528 mRNA. Translation: BAE27237.1.
AK147169 mRNA. Translation: BAE27733.1.
AK159149 mRNA. Translation: BAE34856.1.
BC003843 mRNA. Translation: AAH03843.1.
CCDSiCCDS27667.1.
RefSeqiNP_598487.1. NM_133726.2.
UniGeneiMm.180337.
Mm.389440.

Genome annotation databases

EnsembliENSMUST00000172107; ENSMUSP00000130195; ENSMUSG00000022403.
GeneIDi70356.
KEGGimmu:70356.
UCSCiuc007wwl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT010318 mRNA. Translation: CAJ18526.1.
AK146528 mRNA. Translation: BAE27237.1.
AK147169 mRNA. Translation: BAE27733.1.
AK159149 mRNA. Translation: BAE34856.1.
BC003843 mRNA. Translation: AAH03843.1.
CCDSiCCDS27667.1.
RefSeqiNP_598487.1. NM_133726.2.
UniGeneiMm.180337.
Mm.389440.

3D structure databases

ProteinModelPortaliQ99L47.
SMRiQ99L47. Positions 1-44, 77-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213997. 1 interaction.
IntActiQ99L47. 5 interactions.
MINTiMINT-1869549.
STRINGi10090.ENSMUSP00000130195.

PTM databases

iPTMnetiQ99L47.
PhosphoSiteiQ99L47.

2D gel databases

REPRODUCTION-2DPAGEQ99L47.

Proteomic databases

EPDiQ99L47.
MaxQBiQ99L47.
PaxDbiQ99L47.
PeptideAtlasiQ99L47.
PRIDEiQ99L47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000172107; ENSMUSP00000130195; ENSMUSG00000022403.
GeneIDi70356.
KEGGimmu:70356.
UCSCiuc007wwl.1. mouse.

Organism-specific databases

CTDi6767.
MGIiMGI:1917606. St13.

Phylogenomic databases

eggNOGiKOG1308. Eukaryota.
ENOG410XR19. LUCA.
GeneTreeiENSGT00390000001347.
HOGENOMiHOG000001586.
HOVERGENiHBG002482.
InParanoidiQ99L47.
KOiK09560.
OMAiVQPKANK.
OrthoDBiEOG77M8P3.
TreeFamiTF313244.

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiSt13. mouse.
PROiQ99L47.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L47.
CleanExiMM_ST13.
ExpressionAtlasiQ99L47. baseline and differential.
GenevisibleiQ99L47. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006636. STI1_HS-bd.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00727. STI1. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
  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].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "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-355 AND LYS-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiF10A1_MOUSE
AccessioniPrimary (citable) accession number: Q99L47
Secondary accession number(s): Q4FJT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 121 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, 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.