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Q9NZL4 (HPBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hsp70-binding protein 1

Short name=HspBP1
Alternative name(s):
Heat shock protein-binding protein 1
Hsp70-binding protein 2
Short name=HspBP2
Hsp70-interacting protein 1
Hsp70-interacting protein 2
Gene names
Name:HSPBP1
Synonyms:HSPBP
ORF Names:PP1845
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.1 Ref.2 Ref.9 Ref.10

Subunit structure

Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Ref.1 Ref.9 Ref.10

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Contains 4 ARM repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA2P546523EBI-356763,EBI-356991

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZL4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NZL4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     207-309: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NZL4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGGRRAPLKRRLLSRPSRIDPSGRQSCFSGDHLLPLTHSSLLHKRPM
     25-28: GGGG → V
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Hsp70-binding protein 1
PRO_0000084035

Regions

Repeat135 – 17743ARM 1
Repeat180 – 22041ARM 2
Repeat223 – 26240ARM 3
Repeat265 – 30440ARM 4
Compositional bias21 – 4020Gly-rich

Amino acid modifications

Modified residue3541Phosphoserine Ref.11
Modified residue3591Phosphoserine Ref.11 Ref.12 Ref.14

Natural variations

Alternative sequence11M → MGGRRAPLKRRLLSRPSRID PSGRQSCFSGDHLLPLTHSS LLHKRPM in isoform 3.
VSP_053681
Alternative sequence25 – 284GGGG → V in isoform 3.
VSP_053682
Alternative sequence207 – 309103Missing in isoform 2.
VSP_015945
Natural variant25 – 273Missing.
VAR_023645

Experimental info

Sequence conflict2761M → V in BAG57622. Ref.5

Secondary structure

........................................ 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2B6AAB4161D5A326

FASTA36239,474
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 50A959E12693AF09
Show »

FASTA25928,024
Isoform 3 [UniParc].

Checksum: AF3566553A8B3EB3
Show »

FASTA40544,516

References

« Hide 'large scale' references
[1]"Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein."
Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 273:32883-32888(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL, FUNCTION, INTERACTION WITH HSPA1A, TISSUE SPECIFICITY.
Tissue: Heart.
[2]"Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70."
Guerriero V. Jr., Raynes D.A.
Biochim. Biophys. Acta 1490:203-207(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, POLYMORPHISM OF POLY-GLY REGION.
Tissue: Heart.
[3]Tanimura S., Tsujimoto M., Kohno M.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
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. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Amygdala and Spleen.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL.
[7]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"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] (ISOFORM 1), VARIANT 25-GLY--GLY-27 DEL.
Tissue: Lung and Placenta.
[9]"HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain."
McLellan C.A., Raynes D.A., Guerriero V. Jr.
J. Biol. Chem. 278:19017-19022(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSPA1A.
[10]"The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator."
Alberti S., Boehse K., Arndt V., Schmitz A., Hoehfeld J.
Mol. Biol. Cell 15:4003-4010(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HSPA1A AND STUB1.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange."
Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C., Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.
Mol. Cell 17:367-379(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-362 IN COMPLEX WITH HSPA1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF093420 mRNA. Translation: AAC79703.1.
AF187859 mRNA. Translation: AAF35833.1.
AB020592 mRNA. Translation: BAB18742.1.
AF217996 mRNA. Translation: AAG17238.1.
AK130636 mRNA. Translation: BAC85399.1.
AK294358 mRNA. Translation: BAG57622.1.
CR457118 mRNA. Translation: CAG33399.1.
AK075293 mRNA. Translation: BAG52102.1.
BC001236 mRNA. Translation: AAH01236.1.
BC002373 mRNA. Translation: AAH02373.1.
RefSeqNP_001123578.1. NM_001130106.1.
NP_036399.3. NM_012267.4.
UniGeneHs.53066.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XQRX-ray2.10A/B87-362[»]
1XQSX-ray2.90A/B87-362[»]
ProteinModelPortalQ9NZL4.
SMRQ9NZL4. Positions 87-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117168. 37 interactions.
IntActQ9NZL4. 8 interactions.
MINTMINT-1158196.
STRING9606.ENSP00000255631.

PTM databases

PhosphoSiteQ9NZL4.

Polymorphism databases

DMDM74734730.

Proteomic databases

MaxQBQ9NZL4.
PaxDbQ9NZL4.
PRIDEQ9NZL4.

Protocols and materials databases

DNASU23640.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255631; ENSP00000255631; ENSG00000133265.
ENST00000433386; ENSP00000398244; ENSG00000133265.
ENST00000587922; ENSP00000467574; ENSG00000133265.
GeneID23640.
KEGGhsa:23640.
UCSCuc002qkc.3. human. [Q9NZL4-1]

Organism-specific databases

CTD23640.
GeneCardsGC19M055773.
H-InvDBHIX0015460.
HGNCHGNC:24989. HSPBP1.
HPACAB005865.
MIM612939. gene.
neXtProtNX_Q9NZL4.
PharmGKBPA164720725.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235694.
HOVERGENHBG053282.
InParanoidQ9NZL4.
KOK09562.
OrthoDBEOG7N37D8.
PhylomeDBQ9NZL4.
TreeFamTF324307.

Gene expression databases

ArrayExpressQ9NZL4.
BgeeQ9NZL4.
GenevestigatorQ9NZL4.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSHSPBP1. human.
EvolutionaryTraceQ9NZL4.
GeneWikiHSPBP1.
GenomeRNAi23640.
NextBio35471637.
PROQ9NZL4.
SOURCESearch...

Entry information

Entry nameHPBP1_HUMAN
AccessionPrimary (citable) accession number: Q9NZL4
Secondary accession number(s): B3KQP0 expand/collapse secondary AC list , B4DG11, O95351, Q6ZNU5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM