CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008292
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serpin H1 
Protein Synonyms/Alias
 47 kDa heat shock protein; Arsenic-transactivated protein 3; AsTP3; Cell proliferation-inducing gene 14 protein; Collagen-binding protein; Colligin; Rheumatoid arthritis-related antigen RA-A47 
Gene Name
 SERPINH1 
Gene Synonyms/Alias
 CBP1; CBP2; HSP47; SERPINH2; PIG14 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
39TAEKLSPKAATLAERubiquitination[1, 2, 3]
94ATTASQAKAVLSAEQubiquitination[1, 3, 4, 5]
129TARNVTWKLGSRLYGubiquitination[4]
184AAQTTDGKLPEVTKDubiquitination[5, 6]
190GKLPEVTKDVERTDGubiquitination[4]
207LVNAMFFKPHWDEKFubiquitination[5, 6]
250YNYYDDEKEKLQIVEubiquitination[5, 6]
252YYDDEKEKLQIVEMPubiquitination[2, 4]
283EPLERLEKLLTKEQLubiquitination[2]
287RLEKLLTKEQLKIWMubiquitination[4]
319EVTHDLQKHLAGLGLubiquitination[1, 3]
334TEAIDKNKADLSRMSubiquitination[4]
380REELRSPKLFYADHPubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] 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] 
Functional Description
 Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen. 
Sequence Annotation
 MOTIF 415 418 Prevents secretion from ER (Potential).
 CARBOHYD 120 120 N-linked (GlcNAc...) (Potential).
 CARBOHYD 125 125 N-linked (GlcNAc...) (Potential).  
Keyword
 Chaperone; Complete proteome; Endoplasmic reticulum; Glycoprotein; Osteogenesis imperfecta; Polymorphism; Reference proteome; Signal; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 418 AA 
Protein Sequence
MRSLLLLSAF CLLEAALAAE VKKPAAAAAP GTAEKLSPKA ATLAERSAGL AFSLYQAMAK 60
DQAVENILVS PVVVASSLGL VSLGGKATTA SQAKAVLSAE QLRDEEVHAG LGELLRSLSN 120
STARNVTWKL GSRLYGPSSV SFADDFVRSS KQHYNCEHSK INFRDKRSAL QSINEWAAQT 180
TDGKLPEVTK DVERTDGALL VNAMFFKPHW DEKFHHKMVD NRGFMVTRSY TVGVMMMHRT 240
GLYNYYDDEK EKLQIVEMPL AHKLSSLIIL MPHHVEPLER LEKLLTKEQL KIWMGKMQKK 300
AVAISLPKGV VEVTHDLQKH LAGLGLTEAI DKNKADLSRM SGKKDLYLAS VFHATAFELD 360
TDGNPFDQDI YGREELRSPK LFYADHPFIF LVRDTQSGSL LFIGRLVRPK GDKMRDEL 418 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
 GO:0005518; F:collagen binding; NAS:UniProtKB.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:RefGenome.
 GO:0032964; P:collagen biosynthetic process; IEA:Compara.
 GO:0030199; P:collagen fibril organization; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0051604; P:protein maturation; IEA:Compara.
 GO:0030162; P:regulation of proteolysis; IBA:RefGenome.
 GO:0006986; P:response to unfolded protein; TAS:ProtInc. 
Interpro
 IPR023795; Protease_inhib_I4_serpin_CS.
 IPR023796; Serpin_dom.
 IPR000215; Serpin_fam. 
Pfam
 PF00079; Serpin 
SMART
 SM00093; SERPIN 
PROSITE
 PS00014; ER_TARGET
 PS00284; SERPIN 
PRINTS