ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9NZL4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HPBP1_HUMAN
Primary accession number Q9NZL4
Secondary accession numbers O95351 Q6ZNU5
Integrated into Swiss-Prot on October 25, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 53)
Name and origin of the protein
Protein name Hsp70-binding protein 1
Synonyms Heat shock protein-binding protein 1
HspBP1
Hsp70-interacting protein 1
Hsp70-binding protein 2
HspBP2
Hsp70-interacting protein 2
Gene name
Name: HSPBP1
Synonyms: HSPBP
ORFNames: PP1845
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, AND TISSUE SPECIFICITY.
TISSUE=Heart;
DOI=10.1074/jbc.273.49.32883; PubMed=9830037 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND POLYMORPHISM OF POLY-GLY STRETCH.
TISSUE=Heart;
DOI=10.1016/S0167-4781(99)00238-9; PubMed=10786638 [NCBI, ExPASy, EBI, Israel, Japan]
Guerriero V. Jr., Raynes D.A.;
"Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70.";
Biochim. Biophys. Acta 1490:203-207(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT 25-GLY--GLY-27 DEL.
Tanimura S., Tsujimoto M., Kohno M.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1073/pnas.0404089101; PubMed=15498874 [NCBI, ExPASy, EBI, Israel, Japan]
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT 25-GLY--GLY-27 DEL.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT 25-GLY--GLY-27 DEL.
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND INTERACTION WITH HSPA1A.
DOI=10.1074/jbc.M301109200; PubMed=12651857 [NCBI, ExPASy, EBI, Israel, Japan]
McLellan C.A., Raynes D.A., Guerriero V. Jr.;
"HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain.";
J. Biol. Chem. 278:19017-19022(2003).
[9]
FUNCTION, AND INTERACTION WITH HSPA1A AND STUB1.
DOI=10.1091/mbc.E04-04-0293; PubMed=15215316 [NCBI, ExPASy, EBI, Israel, Japan]
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.;
"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.";
Mol. Biol. Cell 15:4003-4010(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH HSPA1A.
DOI=10.1016/j.molcel.2004.12.023; PubMed=15694338 [NCBI, ExPASy, EBI, Israel, Japan]
Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C., Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.;
"Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange.";
Mol. Cell 17:367-379(2005).
Comments
  • FUNCTION: Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
  • SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1.
  • INTERACTION:
    P11142:HSPA8; NbExp=2; IntAct=EBI-356763, EBI-351896;
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9NZL4-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9NZL4-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_015945.
  • TISSUE SPECIFICITY: Ubiquitous.
  • SIMILARITY: Contains 4 ARM repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF093420; AAC79703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF187859; AAF35833.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020592; BAB18742.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF217996; AAG17238.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK130636; BAC85399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457118; CAG33399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001236; AAH01236.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002373; AAH02373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001123578.1; -.
NP_036399.3; -.
UniGene Hs.53066
3D structure databases
PDB
1XQR; X-ray; 2.10 A; A/B=87-362.[ExPASy / RCSB / EBI]
1XQS; X-ray; 2.90 A; A/B=87-362.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XQR; -.
1XQS; -.
ModBase Q9NZL4.
Protein-protein interaction databases
IntAct Q9NZL4; -.
PTM databases
PhosphoSite Q9NZL4; -.
Organism-specific databases
H-InvDB HIX0015460; -.
HPA CAB005865; -.
GeneCards Q9NZL4.
Gene expression databases
ArrayExpress Q9NZL4; -.
GermOnline ENSG00000133265; Homo sapiens.
Ontologies
GO
GO:0004857; Molecular function: enzyme inhibitor activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR000225; Armadillo.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
PROSITE PS50176; ARM_REPEAT; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NZL4.
Genome annotation databases
Ensembl ENSG00000133265; Homo sapiens. [Contig view]
GeneID 23640; -.
KEGG hsa:23640; -.
Phylogenomic databases
HOGENOM Q9NZL4; -.
HOVERGEN Q9NZL4; -.
Other
NextBio 46437; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   362  362     Hsp70-binding protein 1. PRO_0000084035
REPEAT   135   177  43     ARM 1. 
REPEAT   180   220  41     ARM 2. 
REPEAT   223   262  40     ARM 3. 
REPEAT   265   304  40     ARM 4. 
COMPBIAS   21    40  20     Gly-rich. 
MOD_RES   354   354        Phosphoserine. 
MOD_RES   359   359        Phosphoserine. 
VAR_SEQ   207   309        Missing (in isoform 2). VSP_015945
VARIANT   25    27  3     Missing. VAR_023645
HELIX   90   104  15      
HELIX   113   134  22      
HELIX   137   145  9      
HELIX   148   154  7      
TURN   155   158  4      
HELIX   162   176  15      
HELIX   180   188  9      
HELIX   191   201  11      
HELIX   205   219  15      
HELIX   223   231  9      
HELIX   234   243  10      
HELIX   247   263  17      
HELIX   265   267  3      
HELIX   268   273  6      
HELIX   276   284  9      
HELIX   291   303  13      
HELIX   307   314  8      
HELIX   316   318  3      
HELIX   320   331  12      
HELIX   335   337  3      
HELIX   338   351  14      
Sequence information
Length: 362 AA [This is the length of the unprocessed precursor] Molecular weight: 39474 Da [This is the MW of the unprocessed precursor] CRC64: 2B6AAB4161D5A326 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS 

        70         80         90        100        110        120 
EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ 

       130        140        150        160        170        180 
QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA 

       190        200        210        220        230        240 
AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR 

       250        260        270        280        290        300 
AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC 

       310        320        330        340        350        360 
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM 


DR 

Q9NZL4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!