CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019172
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CAP-Gly domain-containing linker protein 3 
Protein Synonyms/Alias
 Cytoplasmic linker protein 170-related 59 kDa protein; CLIP-170-related 59 kDa protein; CLIPR-59 
Gene Name
 CLIP3 
Gene Synonyms/Alias
 CLIPR59 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
127TLLHYACKAGAHGVGubiquitination[1]
306RVLLDGQKTGTLRFCubiquitination[1]
428QVLVAGQKQGIVRFYubiquitination[1]
456ELDQPTGKHDGSVFGubiquitination[1]
499PGDSVGAKKVHQVTMubiquitination[2]
500GDSVGAKKVHQVTMTubiquitination[1]
520FTTVRTPKDIASENSubiquitination[1, 3]
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] 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]
 [3] 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
 Functions as a cytoplasmic linker protein. Involved in TGN-endosome dynamics. 
Sequence Annotation
 REPEAT 117 158 ANK 1.
 REPEAT 160 191 ANK 2.
 REPEAT 197 229 ANK 3.
 DOMAIN 314 356 CAP-Gly 1.
 DOMAIN 436 478 CAP-Gly 2.
 REGION 488 547 GoLD.  
Keyword
 3D-structure; ANK repeat; Complete proteome; Cytoplasm; Golgi apparatus; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 547 AA 
Protein Sequence
MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP LPKDYAFTFF 60
DPNDPACQEI LFDPQTTIPE LFAIVRQWVP QVQHKIDVIG NEILRRGCHV NDRDGLTDMT 120
LLHYACKAGA HGVGDPAAAV RLSQQLLALG ADVTLRSRWT NMNALHYAAY FDVPDLVRVL 180
LKGARPRVVN STCSDFNHGS ALHIAASSLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD 240
PMDMSLDKAE AALVAKELRT LLEEAVPLSC ALPKVTLPNY DNVPGNLMLS ALGLRLGDRV 300
LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK QGLFASVSKI 360
SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKTP SSPSLGSLQQ RDGAKAEVGD 420
QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCP PRHGVFAPAS 480
RIQRIGGSTD SPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM 540
LRAEMQS 547 
Gene Ontology
 GO:0031901; C:early endosome membrane; IDA:UniProtKB.
 GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
 GO:0045121; C:membrane raft; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
 GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
 GO:0035594; F:ganglioside binding; IDA:UniProtKB.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0072321; P:chaperone-mediated protein transport; IMP:UniProtKB.
 GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
 GO:0044091; P:membrane biogenesis; IMP:UniProtKB.
 GO:0031115; P:negative regulation of microtubule polymerization; IMP:UniProtKB.
 GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
 GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:UniProtKB.
 GO:0010828; P:positive regulation of glucose transport; ISS:UniProtKB.
 GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR000938; CAP-Gly_domain. 
Pfam
 PF12796; Ank_2
 PF01302; CAP_GLY 
SMART
 SM00248; ANK
 SM01052; CAP_GLY 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS00845; CAP_GLY_1
 PS50245; CAP_GLY_2 
PRINTS