CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012315
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Caprin-1 
Protein Synonyms/Alias
 Cell cycle-associated protein 1; Cytoplasmic activation- and proliferation-associated protein 1; GPI-anchored membrane protein 1; GPI-anchored protein p137; GPI-p137; p137GPI; Membrane component chromosome 11 surface marker 1; RNA granule protein 105 
Gene Name
 CAPRIN1 
Gene Synonyms/Alias
 GPIAP1; GPIP137; M11S1; RNG105 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55AVQTEAMKQILGVIDubiquitination[1]
64ILGVIDKKLRNLEKKubiquitination[1]
74NLEKKKGKLDDYQERacetylation[2]
74NLEKKKGKLDDYQERubiquitination[1, 3, 4, 5]
98DQLDAVSKYQEVTNNubiquitination[1]
110TNNLEFAKELQRSFMubiquitination[1, 3, 4, 5]
125ALSQDIQKTIKKTARubiquitination[1, 3, 4, 5, 6, 7]
129DIQKTIKKTARREQLubiquitination[1]
158ELQYVLDKLGDDEVRubiquitination[6]
223DLLEGKEKPVCGTTYubiquitination[1]
234GTTYKVLKEIVERVFubiquitination[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]
 [2] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [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] 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]
 [5] 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]
 [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]
 [7] 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
Functional Description
 May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types (By similarity). 
Sequence Annotation
 REGION 360 381 G3BP1-binding.
 MOD_RES 2 2 N-acetylproline.
 MOD_RES 10 10 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Differentiation; Direct protein sequencing; Glycoprotein; Phosphoprotein; Polymorphism; Protein synthesis inhibitor; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 709 AA 
Protein Sequence
MPSATSHSGS GSKSSGPPPP SGSSGSEAAA GAGAAAPASQ HPATGTGAVQ TEAMKQILGV 60
IDKKLRNLEK KKGKLDDYQE RMNKGERLNQ DQLDAVSKYQ EVTNNLEFAK ELQRSFMALS 120
QDIQKTIKKT ARREQLMREE AEQKRLKTVL ELQYVLDKLG DDEVRTDLKQ GLNGVPILSE 180
EELSLLDEFY KLVDPERDMS LRLNEQYEHA SIHLWDLLEG KEKPVCGTTY KVLKEIVERV 240
FQSNYFDSTH NHQNGLCEEE EAASAPAVED QVPEAEPEPA EEYTEQSEVE STEYVNRQFM 300
AETQFTSGEK EQVDEWTVET VEVVNSLQQQ PQAASPSVPE PHSLTPVAQA DPLVRRQRVQ 360
DLMAQMQGPY NFIQDSMLDF ENQTLDPAIV SAQPMNPTQN MDMPQLVCPP VHSESRLAQP 420
NQVPVQPEAT QVPLVSSTSE GYTASQPLYQ PSHATEQRPQ KEPIDQIQAT ISLNTDQTTA 480
SSSLPAASQP QVFQAGTSKP LHSSGINVNA APFQSMQTVF NMNAPVPPVN EPETLKQQNQ 540
YQASYNQSFS SQPHQVEQTE LQQEQLQTVV GTYHGSPDQS HQVTGNHQQP PQQNTGFPRS 600
NQPYYNSRGV SRGGSRGARG LMNGYRGPAN GFRGGYDGYR PSFSNTPNSG YTQSQFSAPR 660
DYSGYQRDGY QQNFKRGSGQ SGPRGAPRGR GGPPRPNRGM PQMNTQQVN 709 
Gene Ontology
 GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
 GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0003723; F:RNA binding; ISS:UniProtKB.
 GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
 GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:UniProtKB.
 GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:UniProtKB. 
Interpro
 IPR022070; Caprin-1_C. 
Pfam
 PF12287; Caprin-1_C 
SMART
  
PROSITE
  
PRINTS