Full text data of HSPBP1
HSPBP1
(HSPBP)
[Confidence: low (only semi-automatic identification from reviews)]
Hsp70-binding protein 1; HspBP1 (Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Hsp70-binding protein 1; HspBP1 (Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NZL4
ID HPBP1_HUMAN Reviewed; 362 AA.
AC Q9NZL4; B3KQP0; O95351; Q6ZNU5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Hsp70-binding protein 1;
DE Short=HspBP1;
DE AltName: Full=Heat shock protein-binding protein 1;
DE AltName: Full=Hsp70-binding protein 2;
DE Short=HspBP2;
DE AltName: Full=Hsp70-interacting protein 1;
DE AltName: Full=Hsp70-interacting protein 2;
GN Name=HSPBP1; Synonyms=HSPBP; ORFNames=PP1845;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL,
RP FUNCTION, INTERACTION WITH HSPA1A, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9830037; DOI=10.1074/jbc.273.49.32883;
RA Raynes D.A., Guerriero V. Jr.;
RT "Inhibition of Hsp70 ATPase activity and protein renaturation by a
RT novel Hsp70-binding protein.";
RL J. Biol. Chem. 273:32883-32888(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND POLYMORPHISM OF
RP POLY-GLY REGION.
RC TISSUE=Heart;
RX PubMed=10786638; DOI=10.1016/S0167-4781(99)00238-9;
RA Guerriero V. Jr., Raynes D.A.;
RT "Isolation and characterization of isoforms of HspBP1, inhibitors of
RT Hsp70.";
RL Biochim. Biophys. Acta 1490:203-207(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 25-GLY--GLY-27
RP DEL.
RA Tanimura S., Tsujimoto M., Kohno M.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP 25-GLY--GLY-27 DEL.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP 25-GLY--GLY-27 DEL.
RC TISSUE=Lung, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH HSPA1A.
RX PubMed=12651857; DOI=10.1074/jbc.M301109200;
RA McLellan C.A., Raynes D.A., Guerriero V. Jr.;
RT "HspBP1, an Hsp70 cochaperone, has two structural domains and is
RT capable of altering the conformation of the Hsp70 ATPase domain.";
RL J. Biol. Chem. 278:19017-19022(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH HSPA1A AND STUB1.
RX PubMed=15215316; DOI=10.1091/mbc.E04-04-0293;
RA Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
RT "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and
RT stimulates the maturation of the cystic fibrosis transmembrane
RT conductance regulator.";
RL Mol. Biol. Cell 15:4003-4010(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH
RP HSPA1A.
RX PubMed=15694338; DOI=10.1016/j.molcel.2004.12.023;
RA Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C.,
RA Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.;
RT "Regulation of Hsp70 function by HspBP1: structural analysis reveals
RT an alternate mechanism for Hsp70 nucleotide exchange.";
RL Mol. Cell 17:367-379(2005).
CC -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC conformation of the ATP-binding domain of HSPA1A and interfering
CC with ATP binding. Interferes with ubiquitination mediated by STUB1
CC and inhibits chaperone-assisted degradation of immature CFTR.
CC -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected
CC in a ternary complex containing STUB1, HSPA1A and HSPBP1.
CC -!- INTERACTION:
CC P54652:HSPA2; NbExp=3; IntAct=EBI-356763, EBI-356991;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZL4-2; Sequence=VSP_015945;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 4 ARM repeats.
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DR EMBL; AF093420; AAC79703.1; -; mRNA.
DR EMBL; AF187859; AAF35833.1; -; mRNA.
DR EMBL; AB020592; BAB18742.1; -; mRNA.
DR EMBL; AF217996; AAG17238.1; -; mRNA.
DR EMBL; AK130636; BAC85399.1; -; mRNA.
DR EMBL; CR457118; CAG33399.1; -; mRNA.
DR EMBL; AK075293; BAG52102.1; -; mRNA.
DR EMBL; BC001236; AAH01236.1; -; mRNA.
DR EMBL; BC002373; AAH02373.1; -; mRNA.
DR RefSeq; NP_001123578.1; NM_001130106.1.
DR RefSeq; NP_036399.3; NM_012267.4.
DR UniGene; Hs.53066; -.
DR PDB; 1XQR; X-ray; 2.10 A; A/B=87-362.
DR PDB; 1XQS; X-ray; 2.90 A; A/B=87-362.
DR PDBsum; 1XQR; -.
DR PDBsum; 1XQS; -.
DR ProteinModelPortal; Q9NZL4; -.
DR SMR; Q9NZL4; 87-353.
DR IntAct; Q9NZL4; 8.
DR MINT; MINT-1158196; -.
DR STRING; 9606.ENSP00000255631; -.
DR PhosphoSite; Q9NZL4; -.
DR DMDM; 74734730; -.
DR PaxDb; Q9NZL4; -.
DR PRIDE; Q9NZL4; -.
DR DNASU; 23640; -.
DR Ensembl; ENST00000255631; ENSP00000255631; ENSG00000133265.
DR Ensembl; ENST00000433386; ENSP00000398244; ENSG00000133265.
DR Ensembl; ENST00000587922; ENSP00000467574; ENSG00000133265.
DR GeneID; 23640; -.
DR KEGG; hsa:23640; -.
DR UCSC; uc002qkc.3; human.
DR CTD; 23640; -.
DR GeneCards; GC19M055773; -.
DR H-InvDB; HIX0015460; -.
DR HGNC; HGNC:24989; HSPBP1.
DR HPA; CAB005865; -.
DR MIM; 612939; gene.
DR neXtProt; NX_Q9NZL4; -.
DR PharmGKB; PA164720725; -.
DR eggNOG; NOG235694; -.
DR HOVERGEN; HBG053282; -.
DR InParanoid; Q9NZL4; -.
DR KO; K09562; -.
DR OrthoDB; EOG7N37D8; -.
DR ChiTaRS; HSPBP1; human.
DR EvolutionaryTrace; Q9NZL4; -.
DR GeneWiki; HSPBP1; -.
DR GenomeRNAi; 23640; -.
DR NextBio; 46437; -.
DR PRO; PR:Q9NZL4; -.
DR ArrayExpress; Q9NZL4; -.
DR Bgee; Q9NZL4; -.
DR Genevestigator; Q9NZL4; -.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 362 Hsp70-binding protein 1.
FT /FTId=PRO_0000084035.
FT REPEAT 135 177 ARM 1.
FT REPEAT 180 220 ARM 2.
FT REPEAT 223 262 ARM 3.
FT REPEAT 265 304 ARM 4.
FT COMPBIAS 21 40 Gly-rich.
FT MOD_RES 354 354 Phosphoserine.
FT MOD_RES 359 359 Phosphoserine.
FT VAR_SEQ 207 309 Missing (in isoform 2).
FT /FTId=VSP_015945.
FT VARIANT 25 27 Missing.
FT /FTId=VAR_023645.
FT HELIX 90 104
FT HELIX 113 134
FT HELIX 137 145
FT HELIX 148 154
FT TURN 155 158
FT HELIX 162 176
FT HELIX 180 188
FT HELIX 191 201
FT HELIX 205 219
FT HELIX 223 231
FT HELIX 234 243
FT HELIX 247 263
FT HELIX 265 267
FT HELIX 268 273
FT HELIX 276 284
FT HELIX 291 303
FT HELIX 307 314
FT HELIX 316 318
FT HELIX 320 331
FT HELIX 335 337
FT HELIX 338 351
SQ SEQUENCE 362 AA; 39474 MW; 2B6AAB4161D5A326 CRC64;
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS
EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ
QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA
AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR
AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM
DR
//
ID HPBP1_HUMAN Reviewed; 362 AA.
AC Q9NZL4; B3KQP0; O95351; Q6ZNU5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Hsp70-binding protein 1;
DE Short=HspBP1;
DE AltName: Full=Heat shock protein-binding protein 1;
DE AltName: Full=Hsp70-binding protein 2;
DE Short=HspBP2;
DE AltName: Full=Hsp70-interacting protein 1;
DE AltName: Full=Hsp70-interacting protein 2;
GN Name=HSPBP1; Synonyms=HSPBP; ORFNames=PP1845;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL,
RP FUNCTION, INTERACTION WITH HSPA1A, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9830037; DOI=10.1074/jbc.273.49.32883;
RA Raynes D.A., Guerriero V. Jr.;
RT "Inhibition of Hsp70 ATPase activity and protein renaturation by a
RT novel Hsp70-binding protein.";
RL J. Biol. Chem. 273:32883-32888(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND POLYMORPHISM OF
RP POLY-GLY REGION.
RC TISSUE=Heart;
RX PubMed=10786638; DOI=10.1016/S0167-4781(99)00238-9;
RA Guerriero V. Jr., Raynes D.A.;
RT "Isolation and characterization of isoforms of HspBP1, inhibitors of
RT Hsp70.";
RL Biochim. Biophys. Acta 1490:203-207(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 25-GLY--GLY-27
RP DEL.
RA Tanimura S., Tsujimoto M., Kohno M.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP 25-GLY--GLY-27 DEL.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP 25-GLY--GLY-27 DEL.
RC TISSUE=Lung, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH HSPA1A.
RX PubMed=12651857; DOI=10.1074/jbc.M301109200;
RA McLellan C.A., Raynes D.A., Guerriero V. Jr.;
RT "HspBP1, an Hsp70 cochaperone, has two structural domains and is
RT capable of altering the conformation of the Hsp70 ATPase domain.";
RL J. Biol. Chem. 278:19017-19022(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH HSPA1A AND STUB1.
RX PubMed=15215316; DOI=10.1091/mbc.E04-04-0293;
RA Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
RT "The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and
RT stimulates the maturation of the cystic fibrosis transmembrane
RT conductance regulator.";
RL Mol. Biol. Cell 15:4003-4010(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH
RP HSPA1A.
RX PubMed=15694338; DOI=10.1016/j.molcel.2004.12.023;
RA Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C.,
RA Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.;
RT "Regulation of Hsp70 function by HspBP1: structural analysis reveals
RT an alternate mechanism for Hsp70 nucleotide exchange.";
RL Mol. Cell 17:367-379(2005).
CC -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC conformation of the ATP-binding domain of HSPA1A and interfering
CC with ATP binding. Interferes with ubiquitination mediated by STUB1
CC and inhibits chaperone-assisted degradation of immature CFTR.
CC -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected
CC in a ternary complex containing STUB1, HSPA1A and HSPBP1.
CC -!- INTERACTION:
CC P54652:HSPA2; NbExp=3; IntAct=EBI-356763, EBI-356991;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZL4-2; Sequence=VSP_015945;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 4 ARM repeats.
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DR EMBL; AF093420; AAC79703.1; -; mRNA.
DR EMBL; AF187859; AAF35833.1; -; mRNA.
DR EMBL; AB020592; BAB18742.1; -; mRNA.
DR EMBL; AF217996; AAG17238.1; -; mRNA.
DR EMBL; AK130636; BAC85399.1; -; mRNA.
DR EMBL; CR457118; CAG33399.1; -; mRNA.
DR EMBL; AK075293; BAG52102.1; -; mRNA.
DR EMBL; BC001236; AAH01236.1; -; mRNA.
DR EMBL; BC002373; AAH02373.1; -; mRNA.
DR RefSeq; NP_001123578.1; NM_001130106.1.
DR RefSeq; NP_036399.3; NM_012267.4.
DR UniGene; Hs.53066; -.
DR PDB; 1XQR; X-ray; 2.10 A; A/B=87-362.
DR PDB; 1XQS; X-ray; 2.90 A; A/B=87-362.
DR PDBsum; 1XQR; -.
DR PDBsum; 1XQS; -.
DR ProteinModelPortal; Q9NZL4; -.
DR SMR; Q9NZL4; 87-353.
DR IntAct; Q9NZL4; 8.
DR MINT; MINT-1158196; -.
DR STRING; 9606.ENSP00000255631; -.
DR PhosphoSite; Q9NZL4; -.
DR DMDM; 74734730; -.
DR PaxDb; Q9NZL4; -.
DR PRIDE; Q9NZL4; -.
DR DNASU; 23640; -.
DR Ensembl; ENST00000255631; ENSP00000255631; ENSG00000133265.
DR Ensembl; ENST00000433386; ENSP00000398244; ENSG00000133265.
DR Ensembl; ENST00000587922; ENSP00000467574; ENSG00000133265.
DR GeneID; 23640; -.
DR KEGG; hsa:23640; -.
DR UCSC; uc002qkc.3; human.
DR CTD; 23640; -.
DR GeneCards; GC19M055773; -.
DR H-InvDB; HIX0015460; -.
DR HGNC; HGNC:24989; HSPBP1.
DR HPA; CAB005865; -.
DR MIM; 612939; gene.
DR neXtProt; NX_Q9NZL4; -.
DR PharmGKB; PA164720725; -.
DR eggNOG; NOG235694; -.
DR HOVERGEN; HBG053282; -.
DR InParanoid; Q9NZL4; -.
DR KO; K09562; -.
DR OrthoDB; EOG7N37D8; -.
DR ChiTaRS; HSPBP1; human.
DR EvolutionaryTrace; Q9NZL4; -.
DR GeneWiki; HSPBP1; -.
DR GenomeRNAi; 23640; -.
DR NextBio; 46437; -.
DR PRO; PR:Q9NZL4; -.
DR ArrayExpress; Q9NZL4; -.
DR Bgee; Q9NZL4; -.
DR Genevestigator; Q9NZL4; -.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 362 Hsp70-binding protein 1.
FT /FTId=PRO_0000084035.
FT REPEAT 135 177 ARM 1.
FT REPEAT 180 220 ARM 2.
FT REPEAT 223 262 ARM 3.
FT REPEAT 265 304 ARM 4.
FT COMPBIAS 21 40 Gly-rich.
FT MOD_RES 354 354 Phosphoserine.
FT MOD_RES 359 359 Phosphoserine.
FT VAR_SEQ 207 309 Missing (in isoform 2).
FT /FTId=VSP_015945.
FT VARIANT 25 27 Missing.
FT /FTId=VAR_023645.
FT HELIX 90 104
FT HELIX 113 134
FT HELIX 137 145
FT HELIX 148 154
FT TURN 155 158
FT HELIX 162 176
FT HELIX 180 188
FT HELIX 191 201
FT HELIX 205 219
FT HELIX 223 231
FT HELIX 234 243
FT HELIX 247 263
FT HELIX 265 267
FT HELIX 268 273
FT HELIX 276 284
FT HELIX 291 303
FT HELIX 307 314
FT HELIX 316 318
FT HELIX 320 331
FT HELIX 335 337
FT HELIX 338 351
SQ SEQUENCE 362 AA; 39474 MW; 2B6AAB4161D5A326 CRC64;
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS
EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ
QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA
AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR
AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM
DR
//
MIM
612939
*RECORD*
*FIELD* NO
612939
*FIELD* TI
*612939 HEAT-SHOCK 70-KD PROTEIN-BINDING PROTEIN 1; HSPBP1
;;HSPA-BINDING PROTEIN 1;;
read moreHSP70-BINDING PROTEIN 1
*FIELD* TX
CLONING
Using the ATPase domain of human HSP70 (see HSPA1A; 140550) as bait in a
yeast 2-hybrid screen of a human heart cDNA library, Raynes and
Guerriero (1998) cloned HSPBP1. The deduced 459-amino acid protein has a
calculated molecular mass of 39.3 kD and contains 6 consecutive glycines
near its N terminus. Northern blot analysis detected a 1.7-kb HSPBP1
transcript in all tissues examined, with highest expression in heart and
skeletal muscle. Raynes and Guerriero (1998) also identified an HSPBP1
variant that they called HSPBP2, which has 2 polyadenylation signals
rather than the single polyadenylation signal of HSPBP1. The deduced
HSPBP2 protein is identical to HSPBP1 except that it has 9 consecutive
glycines near the N terminus.
Using Northern blot analysis, Raynes and Guerriero (2000) found that the
expression pattern of Hspbp1 in rat tissues was distinct from that in
human. In rat, highest expression was in testis and lowest expression
was in heart and skeletal muscle.
GENE FUNCTION
Raynes and Guerriero (1998) showed that human HSPBP1 coprecipitated with
Hsp70 and Hsc70 (HSPA8; 600816) from bovine heart lysate. Recombinant
HSPBP1 inhibited HSP40 (DNAJB1; 604572)-mediated stimulation of HSP70
ATPase activity in a dose-dependent manner, resulting in reduced ability
of HSP70 to renature heat-denatured firefly luciferase. HSPBP1
specifically bound the ATPase domain of HSP70 and inhibited ATP binding.
Kabani et al. (2002) showed that human HSPBP1 functioned as a nucleotide
exchange factor for HSP70, bovine Hsc70, and the yeast HSP70 ortholog
Ssa1. HSPBP1 inhibited ATP binding and induced nucleotide dissociation.
It inhibited refolding of luciferase by rabbit reticulocyte lysates,
which contain factors required for protein refolding.
Raynes and Guerriero (2000) showed that the HSPBP1 and HSPBP2 isoforms
had comparable inhibitory activities in luciferase refolding by rabbit
reticulocyte lysates.
Alberti et al. (2004) found that epitope-tagged HSPBP1
immunoprecipitated HSC70 and the HSC70 cochaperone CHIP (STUB1; 607207)
from HeLa cell lysates. In the absence of HSC70, HSPBP1 and CHIP bound
each other with low affinity. In the presence of ubiquitin-activating
and -conjugating enzymes, CHIP mediated ubiquitination of test proteins
when bound to HSC70. Addition of HSPBP1 inhibited CHIP-mediated
ubiquitination of test proteins as well as CHIP-mediated ubiquitination
of HSC70. Complex formation between HSPBP1, HSC70, and CHIP was
necessary for HSPBP1 to inhibit CHIP. Alberti et al. (2004) concluded
that HSPBP1 regulates CHIP ubiquitin ligase activity.
MAPPING
Hartz (2009) mapped the HSPBP1 gene to chromosome 19q13.42 based on an
alignment of the HSPBP1 sequence (GenBank GENBANK AF093420) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Alberti, S.; Bohse, K.; Arndt, V.; Schmitz, A.; Hohfeld, J.: The
cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates
the maturation of the cystic fibrosis transmembrane conductance regulator. Molec.
Biol. Cell 15: 4003-4010, 2004.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/17/2009.
3. Kabani, M.; McLellan, C.; Raynes, D. A.; Guerriero, V.; Brodsky,
J. L.: HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is
an Hsc70 nucleotide exchange factor. FEBS Lett. 531: 339-342, 2002.
4. Raynes, D. A.; Guerriero, V.: Isolation and characterization of
isoforms of HspBP1, inhibitors of Hsp70. Biochim. Biophys. Acta 1490:
203-207, 2000.
5. Raynes, D. A.; Guerriero, V., Jr.: Inhibition of Hsp70 ATPase
activity and protein renaturation by a novel Hsp70-binding protein. J.
Biol. Chem. 273: 32883-32888, 1998.
*FIELD* CD
Patricia A. Hartz: 7/28/2009
*FIELD* ED
mgross: 07/28/2009
*RECORD*
*FIELD* NO
612939
*FIELD* TI
*612939 HEAT-SHOCK 70-KD PROTEIN-BINDING PROTEIN 1; HSPBP1
;;HSPA-BINDING PROTEIN 1;;
read moreHSP70-BINDING PROTEIN 1
*FIELD* TX
CLONING
Using the ATPase domain of human HSP70 (see HSPA1A; 140550) as bait in a
yeast 2-hybrid screen of a human heart cDNA library, Raynes and
Guerriero (1998) cloned HSPBP1. The deduced 459-amino acid protein has a
calculated molecular mass of 39.3 kD and contains 6 consecutive glycines
near its N terminus. Northern blot analysis detected a 1.7-kb HSPBP1
transcript in all tissues examined, with highest expression in heart and
skeletal muscle. Raynes and Guerriero (1998) also identified an HSPBP1
variant that they called HSPBP2, which has 2 polyadenylation signals
rather than the single polyadenylation signal of HSPBP1. The deduced
HSPBP2 protein is identical to HSPBP1 except that it has 9 consecutive
glycines near the N terminus.
Using Northern blot analysis, Raynes and Guerriero (2000) found that the
expression pattern of Hspbp1 in rat tissues was distinct from that in
human. In rat, highest expression was in testis and lowest expression
was in heart and skeletal muscle.
GENE FUNCTION
Raynes and Guerriero (1998) showed that human HSPBP1 coprecipitated with
Hsp70 and Hsc70 (HSPA8; 600816) from bovine heart lysate. Recombinant
HSPBP1 inhibited HSP40 (DNAJB1; 604572)-mediated stimulation of HSP70
ATPase activity in a dose-dependent manner, resulting in reduced ability
of HSP70 to renature heat-denatured firefly luciferase. HSPBP1
specifically bound the ATPase domain of HSP70 and inhibited ATP binding.
Kabani et al. (2002) showed that human HSPBP1 functioned as a nucleotide
exchange factor for HSP70, bovine Hsc70, and the yeast HSP70 ortholog
Ssa1. HSPBP1 inhibited ATP binding and induced nucleotide dissociation.
It inhibited refolding of luciferase by rabbit reticulocyte lysates,
which contain factors required for protein refolding.
Raynes and Guerriero (2000) showed that the HSPBP1 and HSPBP2 isoforms
had comparable inhibitory activities in luciferase refolding by rabbit
reticulocyte lysates.
Alberti et al. (2004) found that epitope-tagged HSPBP1
immunoprecipitated HSC70 and the HSC70 cochaperone CHIP (STUB1; 607207)
from HeLa cell lysates. In the absence of HSC70, HSPBP1 and CHIP bound
each other with low affinity. In the presence of ubiquitin-activating
and -conjugating enzymes, CHIP mediated ubiquitination of test proteins
when bound to HSC70. Addition of HSPBP1 inhibited CHIP-mediated
ubiquitination of test proteins as well as CHIP-mediated ubiquitination
of HSC70. Complex formation between HSPBP1, HSC70, and CHIP was
necessary for HSPBP1 to inhibit CHIP. Alberti et al. (2004) concluded
that HSPBP1 regulates CHIP ubiquitin ligase activity.
MAPPING
Hartz (2009) mapped the HSPBP1 gene to chromosome 19q13.42 based on an
alignment of the HSPBP1 sequence (GenBank GENBANK AF093420) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Alberti, S.; Bohse, K.; Arndt, V.; Schmitz, A.; Hohfeld, J.: The
cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates
the maturation of the cystic fibrosis transmembrane conductance regulator. Molec.
Biol. Cell 15: 4003-4010, 2004.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 7/17/2009.
3. Kabani, M.; McLellan, C.; Raynes, D. A.; Guerriero, V.; Brodsky,
J. L.: HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is
an Hsc70 nucleotide exchange factor. FEBS Lett. 531: 339-342, 2002.
4. Raynes, D. A.; Guerriero, V.: Isolation and characterization of
isoforms of HspBP1, inhibitors of Hsp70. Biochim. Biophys. Acta 1490:
203-207, 2000.
5. Raynes, D. A.; Guerriero, V., Jr.: Inhibition of Hsp70 ATPase
activity and protein renaturation by a novel Hsp70-binding protein. J.
Biol. Chem. 273: 32883-32888, 1998.
*FIELD* CD
Patricia A. Hartz: 7/28/2009
*FIELD* ED
mgross: 07/28/2009