F10A1_MOUSE
ID F10A1_MOUSE Reviewed; 371 AA.
AC Q99L47; Q4FJT4;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Hsc70-interacting protein;
DE Short=Hip;
DE AltName: Full=Protein FAM10A1;
DE AltName: Full=Protein ST13 homolog;
GN Name=St13; Synonyms=Fam10a1, Hip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-355 AND LYS-362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least two
CC HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40.
CC Stabilizes the ADP state of HSC70 that has a high affinity for
CC substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of HSC70 with various target proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Interacts with HSC70 as well as DNAJ homologs
CC and HSP90 (By similarity). Interacts (via the C-terminus 302- 318 AA)
CC with GRK5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000305}.
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DR EMBL; CT010318; CAJ18526.1; -; mRNA.
DR EMBL; AK146528; BAE27237.1; -; mRNA.
DR EMBL; AK147169; BAE27733.1; -; mRNA.
DR EMBL; AK159149; BAE34856.1; -; mRNA.
DR EMBL; BC003843; AAH03843.1; -; mRNA.
DR CCDS; CCDS27667.1; -.
DR RefSeq; NP_598487.1; NM_133726.2.
DR AlphaFoldDB; Q99L47; -.
DR SMR; Q99L47; -.
DR BioGRID; 213997; 14.
DR IntAct; Q99L47; 3.
DR MINT; Q99L47; -.
DR STRING; 10090.ENSMUSP00000130195; -.
DR iPTMnet; Q99L47; -.
DR PhosphoSitePlus; Q99L47; -.
DR SwissPalm; Q99L47; -.
DR REPRODUCTION-2DPAGE; Q99L47; -.
DR EPD; Q99L47; -.
DR jPOST; Q99L47; -.
DR MaxQB; Q99L47; -.
DR PaxDb; Q99L47; -.
DR PeptideAtlas; Q99L47; -.
DR PRIDE; Q99L47; -.
DR ProteomicsDB; 275491; -.
DR Antibodypedia; 3378; 387 antibodies from 34 providers.
DR DNASU; 70356; -.
DR Ensembl; ENSMUST00000172107; ENSMUSP00000130195; ENSMUSG00000022403.
DR GeneID; 70356; -.
DR KEGG; mmu:70356; -.
DR UCSC; uc007wwl.1; mouse.
DR CTD; 6767; -.
DR MGI; MGI:1917606; St13.
DR VEuPathDB; HostDB:ENSMUSG00000022403; -.
DR eggNOG; KOG1308; Eukaryota.
DR GeneTree; ENSGT00390000001347; -.
DR InParanoid; Q99L47; -.
DR OMA; TVLNMPQ; -.
DR OrthoDB; 1282821at2759; -.
DR PhylomeDB; Q99L47; -.
DR TreeFam; TF313244; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 70356; 1 hit in 73 CRISPR screens.
DR ChiTaRS; St13; mouse.
DR PRO; PR:Q99L47; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99L47; protein.
DR Bgee; ENSMUSG00000022403; Expressed in pineal body and 251 other tissues.
DR ExpressionAtlas; Q99L47; baseline and differential.
DR Genevisible; Q99L47; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0032564; F:dATP binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:MGI.
DR GO; GO:0061084; P:negative regulation of protein refolding; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18253; HipN; 1.
DR Pfam; PF17830; STI1; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..371
FT /note="Hsc70-interacting protein"
FT /id="PRO_0000190812"
FT REPEAT 113..146
FT /note="TPR 1"
FT REPEAT 147..180
FT /note="TPR 2"
FT REPEAT 181..214
FT /note="TPR 3"
FT DOMAIN 321..360
FT /note="STI1"
FT REGION 38..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 348
FT /note="Phosphoserine; by GRK5"
FT /evidence="ECO:0000250|UniProtKB:P50502"
FT MOD_RES 355
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 371 AA; 41656 MW; 7F9417F251B99F4C CRC64;
MDPRKVSELR AFVKMCRQDP SVLHTEEMRF LREWVESMGG KVPPATHKAK SEENTKEEKR
DKTTEENIKT EELSSEESDL EIDNEGVIEP DTDAPQEMGD ENAEITEEMM DEANEKKGAA
IEALNDGELQ KAIDLFTDAI KLNPRLAILY AKRASVFVKL QKPNAAIRDC DRAIEINPDS
AQPYKWRGKA HRLLGHWEEA AHDLALACKL DYDEDASAML REVQPRAQKI AEHRRKYERK
REEREIKERI ERVKKAREEH ERAQREEEAR RQSGSQYGSF PGGFPGGMPG NFPGGMPGMG
GAMPGMAGMA GMPGLNEILS DPEVLAAMQD PEVMVAFQDV AQNPSNMSKY QSNPKVMNLI
SKLSAKFGGQ S
