HPBP1_MOUSE
ID HPBP1_MOUSE Reviewed; 357 AA.
AC Q99P31; Q9CYV8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Hsp70-binding protein 1;
DE Short=HspBP1;
DE AltName: Full=Heat shock protein-binding protein 1;
DE AltName: Full=Hsp70-interacting protein 1;
GN Name=Hspbp1; Synonyms=Hspbp;
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 [MRNA].
RC TISSUE=Mammary gland;
RA Guerriero V. Jr., Raynes D.A.;
RT "Mouse HspBP sequence.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Embryo, and Thymus;
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].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC conformation of the ATP-binding domain of HSPA1A and interfering with
CC ATP binding. Interferes with ubiquitination mediated by STUB1 and
CC inhibits chaperone-assisted degradation of target proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a
CC ternary complex containing STUB1, HSPA1A and HSPBP1 (By similarity).
CC Interacts with PGLYRP1; this interaction blocks the cytotoxic activity
CC of the PGLYRP1-HSPA1A complex (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF338351; AAK11657.1; -; mRNA.
DR EMBL; AK013263; BAB28756.1; ALT_FRAME; mRNA.
DR EMBL; AK088469; BAC40373.1; -; mRNA.
DR EMBL; BC014758; AAH14758.1; -; mRNA.
DR CCDS; CCDS20740.1; -.
DR RefSeq; NP_077134.1; NM_024172.3.
DR RefSeq; XP_006540351.1; XM_006540288.3.
DR AlphaFoldDB; Q99P31; -.
DR SMR; Q99P31; -.
DR BioGRID; 211323; 13.
DR IntAct; Q99P31; 1.
DR STRING; 10090.ENSMUSP00000078886; -.
DR iPTMnet; Q99P31; -.
DR PhosphoSitePlus; Q99P31; -.
DR EPD; Q99P31; -.
DR MaxQB; Q99P31; -.
DR PaxDb; Q99P31; -.
DR PeptideAtlas; Q99P31; -.
DR PRIDE; Q99P31; -.
DR ProteomicsDB; 273268; -.
DR Antibodypedia; 33053; 311 antibodies from 24 providers.
DR Ensembl; ENSMUST00000079970; ENSMUSP00000078886; ENSMUSG00000063802.
DR GeneID; 66245; -.
DR KEGG; mmu:66245; -.
DR UCSC; uc009eyc.1; mouse.
DR CTD; 23640; -.
DR MGI; MGI:1913495; Hspbp1.
DR VEuPathDB; HostDB:ENSMUSG00000063802; -.
DR eggNOG; KOG2160; Eukaryota.
DR GeneTree; ENSGT00940000153909; -.
DR HOGENOM; CLU_049387_0_1_1; -.
DR InParanoid; Q99P31; -.
DR OMA; CHVQSGL; -.
DR OrthoDB; 313400at2759; -.
DR PhylomeDB; Q99P31; -.
DR TreeFam; TF324307; -.
DR BioGRID-ORCS; 66245; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Hspbp1; mouse.
DR PRO; PR:Q99P31; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99P31; protein.
DR Bgee; ENSMUSG00000063802; Expressed in spermatid and 235 other tissues.
DR ExpressionAtlas; Q99P31; baseline and differential.
DR Genevisible; Q99P31; MM.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR Pfam; PF08609; Fes1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..357
FT /note="Hsp70-binding protein 1"
FT /id="PRO_0000084037"
FT REPEAT 130..172
FT /note="ARM 1"
FT REPEAT 175..215
FT /note="ARM 2"
FT REPEAT 218..257
FT /note="ARM 3"
FT REPEAT 260..299
FT /note="ARM 4"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL4"
FT CONFLICT 109
FT /note="A -> L (in Ref. 2; BAB28756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 39167 MW; 6D6BB583730E3474 CRC64;
MADKGSGGSR LPLALPPASQ GCSSGGSGSS AGGSGNPRPP RNLQGLLQMA ITAGSQEPDP
PPEPMSEERR QWLQEAMSAA FRGQREEVEQ MKNCLRVLSQ ATPAMAGEAE LATDQQEREG
ALELLADLCE NMDNAADFCQ LSGMHLLVGR YLEAGAAGLR WRAAQLIGTC SQNVAAIQEQ
VLGLGALRKL LRLLDRDSCD TVRVKALFAI SCLVREQEAG LLQFLRLDGF SVLMRAMQQQ
VQKLKVKSAF LLQNLLVGHP EHKGTLCSMG MVQQLVALVR TEHSPFHEHV LGALCSLVTD
FPQGVRECRE PELGLEELLR HRCQLLQQRE EYQEELEFCE KLLQTCFSSP TDDSMDR
