CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017644
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytosolic carboxypeptidase-like protein 5 
Protein Synonyms/Alias
 ATP/GTP-binding protein-like 5 
Gene Name
 AGBL5 
Gene Synonyms/Alias
 CCP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
317NLNRQYLKPDAVLHPubiquitination[1]
Reference
 [1] 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
Functional Description
 Metallocarboxypeptidase that mediates tubulin deglutamylation. Specifically catalyzes the deglutamylation of the branching point glutamate side chains generated by post- translational glutamylation in proteins such as tubulins. In contrast, it is not able to act as a long-chain deglutamylase that shortens long polyglutamate chains, a process catalyzed by AGTPBP1/ CCP1, AGBL1/CCP4 and AGBL4/CCP6 (By similarity). 
Sequence Annotation
 ACT_SITE 303 303 Nucleophile (By similarity).
 METAL 252 252 Zinc (By similarity).
 METAL 255 255 Zinc (By similarity).
 METAL 434 434 Zinc (By similarity).  
Keyword
 Alternative splicing; Carboxypeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Polymorphism; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 886 AA 
Protein Sequence
MELRCGGLLF SSRFDSGNLA HVEKVESLSS DGEGVGGGAS ALTSGIASSP DYEFNVWTRP 60
DCAETEFENG NRSWFYFSVR GGMPGKLIKI NIMNMNKQSK LYSQGMAPFV RTLPTRPRWE 120
RIRDRPTFEM TETQFVLSFV HRFVEGRGAT TFFAFCYPFS YSDCQELLNQ LDQRFPENHP 180
THSSPLDTIY YHRELLCYSL DGLRVDLLTI TSCHGLREDR EPRLEQLFPD TSTPRPFRFA 240
GKRIFFLSSR VHPGETPSSF VFNGFLDFIL RPDDPRAQTL RRLFVFKLIP MLNPDGVVRG 300
HYRTDSRGVN LNRQYLKPDA VLHPAIYGAK AVLLYHHVHS RLNSQSSSEH QPSSCLPPDA 360
PVSDLEKANN LQNEAQCGHS ADRHNAEAWK QTEPAEQKLN SVWIMPQQSA GLEESAPDTI 420
PPKESGVAYY VDLHGHASKR GCFMYGNSFS DESTQVENML YPKLISLNSA HFDFQGCNFS 480
EKNMYARDRR DGQSKEGSGR VAIYKASGII HSYTLECNYN TGRSVNSIPA ACHDNGRASP 540
PPPPAFPSRY TVELFEQVGR AMAIAALDMA ECNPWPRIVL SEHSSLTNLR AWMLKHVRNS 600
RGLSSTLNVG VNKKRGLRTP PKSHNGLPVS CSENTLSRAR SFSTGTSAGG SSSSQQNSPQ 660
MKNSPSFPFH GSRPAGLPGL GSSTQKVTHR VLGPVREPRS QDRRRQQQPL NHRPAGSLAP 720
SPAPTSSGPA SSHKLGSCLL PDSFNIPGSS CSLLSSGDKP EAVMVIGKGL LGTGARMPCI 780
KTRLQARPRL GRGSPPTRRG MKGSSGPTSP TPRTRESSEL ELGSCSATPG LPQARPPRPR 840
SAPAFSPISC SLSDSPSWNC YSRGPLGQPE VCFVPKSPPL TVSPRV 886 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0004181; F:metallocarboxypeptidase activity; ISS:UniProtKB.
 GO:0015631; F:tubulin binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0035611; P:protein branching point deglutamylation; ISS:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000834; Peptidase_M14. 
Pfam
 PF00246; Peptidase_M14 
SMART
  
PROSITE
 PS00132; CARBOXYPEPT_ZN_1
 PS00133; CARBOXYPEPT_ZN_2 
PRINTS