CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022448
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hsp70-binding protein 1 
Protein Synonyms/Alias
 HspBP1; Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2 
Gene Name
 HSPBP1 
Gene Synonyms/Alias
 HSPBP; PP1845 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97REEVEQMKSCLRVLSubiquitination[1, 2]
210ACDTVRVKALFAISCubiquitination[2]
248AMQQQVQKLKVKSAFubiquitination[2, 3, 4, 5]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 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. 
Sequence Annotation
 REPEAT 135 177 ARM 1.
 REPEAT 180 220 ARM 2.
 REPEAT 223 262 ARM 3.
 REPEAT 265 304 ARM 4.
 MOD_RES 354 354 Phosphoserine.
 MOD_RES 359 359 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 362 AA 
Protein Sequence
MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS 60
EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ 120
QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA 180
AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR 240
AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC 300
SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM 360
DR 362 
Gene Ontology
 GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
 GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
 GO:0006457; P:protein folding; TAS:ProtInc. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold. 
Pfam
  
SMART
  
PROSITE
 PS50176; ARM_REPEAT 
PRINTS