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Q9NZL4

- HPBP1_HUMAN

UniProt

Q9NZL4 - HPBP1_HUMAN

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Protein

Hsp70-binding protein 1

Gene
HSPBP1, HSPBP, PP1845
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. enzyme inhibitor activity Source: ProtInc
  2. protein binding Source: IntAct

GO - Biological processi

  1. negative regulation of catalytic activity Source: GOC
  2. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  3. positive regulation of protein ubiquitination Source: BHF-UCL
  4. protein folding Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HSPBP1
Synonyms:HSPBP
ORF Names:PP1845
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:24989. HSPBP1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 362362Hsp70-binding protein 1PRO_0000084035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei359 – 3591Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NZL4.
PaxDbiQ9NZL4.
PRIDEiQ9NZL4.

PTM databases

PhosphoSiteiQ9NZL4.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiQ9NZL4.
BgeeiQ9NZL4.
GenevestigatoriQ9NZL4.

Organism-specific databases

HPAiCAB005865.

Interactioni

Subunit structurei

Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPA2P546523EBI-356763,EBI-356991

Protein-protein interaction databases

BioGridi117168. 37 interactions.
IntActiQ9NZL4. 8 interactions.
MINTiMINT-1158196.
STRINGi9606.ENSP00000255631.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 10415
Helixi113 – 13422
Helixi137 – 1459
Helixi148 – 1547
Turni155 – 1584
Helixi162 – 17615
Helixi180 – 1889
Helixi191 – 20111
Helixi205 – 21915
Helixi223 – 2319
Helixi234 – 24310
Helixi247 – 26317
Helixi265 – 2673
Helixi268 – 2736
Helixi276 – 2849
Helixi291 – 30313
Helixi307 – 3148
Helixi316 – 3183
Helixi320 – 33112
Helixi335 – 3373
Helixi338 – 35114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XQRX-ray2.10A/B87-362[»]
1XQSX-ray2.90A/B87-362[»]
ProteinModelPortaliQ9NZL4.
SMRiQ9NZL4. Positions 87-353.

Miscellaneous databases

EvolutionaryTraceiQ9NZL4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati135 – 17743ARM 1Add
BLAST
Repeati180 – 22041ARM 2Add
BLAST
Repeati223 – 26240ARM 3Add
BLAST
Repeati265 – 30440ARM 4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 4020Gly-richAdd
BLAST

Sequence similaritiesi

Contains 4 ARM repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG235694.
HOVERGENiHBG053282.
InParanoidiQ9NZL4.
KOiK09562.
OrthoDBiEOG7N37D8.
PhylomeDBiQ9NZL4.
TreeFamiTF324307.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NZL4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG    50
LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL 100
RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH 150
LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD 200
RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK 250
VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC 300
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT 350
CFSSPADDSM DR 362
Length:362
Mass (Da):39,474
Last modified:October 1, 2000 - v1
Checksum:i2B6AAB4161D5A326
GO
Isoform 2 (identifier: Q9NZL4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-309: Missing.

Note: No experimental confirmation available.

Show »
Length:259
Mass (Da):28,024
Checksum:i50A959E12693AF09
GO
Isoform 3 (identifier: Q9NZL4-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:405
Mass (Da):44,516
Checksum:iAF3566553A8B3EB3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 273Missing.
VAR_023645

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGGRRAPLKRRLLSRPSRID PSGRQSCFSGDHLLPLTHSS LLHKRPM in isoform 3. VSP_053681
Alternative sequencei25 – 284GGGG → V in isoform 3. VSP_053682
Alternative sequencei207 – 309103Missing in isoform 2. VSP_015945Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti276 – 2761M → V in BAG57622. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_001123578.1. NM_001130106.1.
NP_036399.3. NM_012267.4.
UniGeneiHs.53066.

Genome annotation databases

EnsembliENST00000255631; ENSP00000255631; ENSG00000133265.
ENST00000433386; ENSP00000398244; ENSG00000133265.
ENST00000587922; ENSP00000467574; ENSG00000133265.
GeneIDi23640.
KEGGihsa:23640.
UCSCiuc002qkc.3. human. [Q9NZL4-1]

Polymorphism databases

DMDMi74734730.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_001123578.1. NM_001130106.1.
NP_036399.3. NM_012267.4.
UniGenei Hs.53066.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XQR X-ray 2.10 A/B 87-362 [» ]
1XQS X-ray 2.90 A/B 87-362 [» ]
ProteinModelPortali Q9NZL4.
SMRi Q9NZL4. Positions 87-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117168. 37 interactions.
IntActi Q9NZL4. 8 interactions.
MINTi MINT-1158196.
STRINGi 9606.ENSP00000255631.

PTM databases

PhosphoSitei Q9NZL4.

Polymorphism databases

DMDMi 74734730.

Proteomic databases

MaxQBi Q9NZL4.
PaxDbi Q9NZL4.
PRIDEi Q9NZL4.

Protocols and materials databases

DNASUi 23640.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255631 ; ENSP00000255631 ; ENSG00000133265 .
ENST00000433386 ; ENSP00000398244 ; ENSG00000133265 .
ENST00000587922 ; ENSP00000467574 ; ENSG00000133265 .
GeneIDi 23640.
KEGGi hsa:23640.
UCSCi uc002qkc.3. human. [Q9NZL4-1 ]

Organism-specific databases

CTDi 23640.
GeneCardsi GC19M055773.
H-InvDB HIX0015460.
HGNCi HGNC:24989. HSPBP1.
HPAi CAB005865.
MIMi 612939. gene.
neXtProti NX_Q9NZL4.
PharmGKBi PA164720725.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235694.
HOVERGENi HBG053282.
InParanoidi Q9NZL4.
KOi K09562.
OrthoDBi EOG7N37D8.
PhylomeDBi Q9NZL4.
TreeFami TF324307.

Miscellaneous databases

ChiTaRSi HSPBP1. human.
EvolutionaryTracei Q9NZL4.
GeneWikii HSPBP1.
GenomeRNAii 23640.
NextBioi 35471637.
PROi Q9NZL4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NZL4.
Bgeei Q9NZL4.
Genevestigatori Q9NZL4.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiHPBP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZL4
Secondary accession number(s): B3KQP0
, B4DG11, O95351, Q6ZNU5
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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