CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017020
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GRIP and coiled-coil domain-containing protein 2 
Protein Synonyms/Alias
 185 kDa Golgi coiled-coil protein; GCC185; CLL-associated antigen KW-11; CTCL tumor antigen se1-1; Ran-binding protein 2-like 4; RanBP2L4; Renal carcinoma antigen NY-REN-53 
Gene Name
 GCC2 
Gene Synonyms/Alias
 KIAA0336; RANBP2L4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32LPKEDLIKFAKKQMMubiquitination[1, 2]
36DLIKFAKKQMMLIQKubiquitination[3]
72EGTGDIIKALTERLDubiquitination[1, 2]
500ELGESAGKISQEFESubiquitination[3]
807LAFQRDEKVLELEKEubiquitination[3]
813EKVLELEKEIKCLQEubiquitination[3]
952SVKELEEKIENLEKEacetylation[4]
958EKIENLEKECKEKEEacetylation[4]
1456HLQEEHRKTVETLQQubiquitination[3]
1492VSSQQSLKNLRERRNubiquitination[5]
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] 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]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] 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] 
Functional Description
 Golgin which probably tethers transport vesicles to the trans-Golgi network (TGN) and regulates vesicular transport between the endosomes and the Golgi. As a RAB9A effector it is involved in recycling of the mannose 6-phosphate receptor from the late endosomes to the TGN. May also play a role in transport between the recycling endosomes and the Golgi. Required for maintenance of the Golgi structure, it is involved in the biogenesis of noncentrosomal, Golgi-associated microtubules through recruitment of CLASP1 and CLASP2. 
Sequence Annotation
 DOMAIN 1609 1659 GRIP.
 REGION 1574 1684 Mediates interaction with RAB9A.
 REGION 1574 1613 Mediates interaction with RAB6A.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 14 14 Phosphothreonine.
 MOD_RES 236 236 Phosphoserine.
 MOD_RES 1483 1483 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1684 AA 
Protein Sequence
MEDLVQDGVA SPATPGTGKS KLETLPKEDL IKFAKKQMML IQKAKSRCTE LEKEIEELRS 60
KPVTEGTGDI IKALTERLDA LLLEKAETEQ QCLSLKKENI KMKQEVEDSV TKMGDAHKEL 120
EQSHINYVKE IENLKNELMA VRSKYSEDKA NLQKQLEEAM NTQLELSEQL KFQNNSEDNV 180
KKLQEEIEKI RPGFEEQILY LQKQLDATTD EKKETVTQLQ NIIEANSQHY QKNINSLQEE 240
LLQLKAIHQE EVKELMCQIE ASAKEHEAEI NKLNELKENL VKQCEASEKN IQKKYECELE 300
NLRKATSNAN QDNQICSILL QENTFVEQVV NEKVKHLEDT LKELESQHSI LKDEVTYMNN 360
LKLKLEMDAQ HIKDEFFHER EDLEFKINEL LLAKEEQGCV IEKLKSELAG LNKQFCYTVE 420
QHNREVQSLK EQHQKEISEL NETFLSDSEK EKLTLMFEIQ GLKEQCENLQ QEKQEAILNY 480
ESLREIMEIL QTELGESAGK ISQEFESMKQ QQASDVHELQ QKLRTAFTEK DALLETVNRL 540
QGENEKLLSQ QELVPELENT IKNLQEKNGV YLLSLSQRDT MLKELEGKIN SLTEEKDDFI 600
NKLKNSHEEM DNFHKKCERE ERLILELGKK VEQTIQYNSE LEQKVNELTG GLEETLKEKD 660
QNDQKLEKLM VQMKVLSEDK EVLSAEVKSL YEENNKLSSE KKQLSRDLEV FLSQKEDVIL 720
KEHITQLEKK LQLMVEEQDN LNKLLENEQV QKLFVKTQLY GFLKEMGSEV SEDSEEKDVV 780
NVLQAVGESL AKINEEKCNL AFQRDEKVLE LEKEIKCLQE ESVVQCEELK SLLRDYEQEK 840
VLLRKELEEI QSEKEALQSD LLEMKNANEK TRLENQNLLI QVEEVSQTCS KSEIHNEKEK 900
CFIKEHENLK PLLEQKELRD RRAELILLKD SLAKSPSVKN DPLSSVKELE EKIENLEKEC 960
KEKEEKINKI KLVAVKAKKE LDSSRKETQT VKEELESLRS EKDQLSASMR DLIQGAESYK 1020
NLLLEYEKQS EQLDVEKERA NNFEHRIEDL TRQLRNSTLQ CETINSDNED LLARIETLQS 1080
NAKLLEVQIL EVQRAKAMVD KELEAEKLQK EQKIKEHATT VNELEELQVQ LQKQKKQLQK 1140
TMQELELVKK DAQQTTLMNM EIADYERLMK ELNQKLTNKN NKIEDLEQEI KIQKQKQETL 1200
QEEITSLQSS VQQYEEKNTK IKQLLVKTKK ELADSKQAET DHLILQASLK GELEASQQQV 1260
EVYKIQLAEI TSEKHKIHEH LKTSAEQHQR TLSAYQQRVT ALQEECRAAK AEQATVTSEF 1320
ESYKVRVHNV LKQQKNKSMS QAETEGAKQE REHLEMLIDQ LKIKLQDSQN NLQINVSELQ 1380
TLQSEHDTLL ERHNKMLQET VSKEAELREK LCSIQSENMM MKSEHTQTVS QLTSQNEVLR 1440
NSFRDQVRHL QEEHRKTVET LQQQLSKMEA QLFQLKNEPT TRSPVSSQQS LKNLRERRNT 1500
DLPLLDMHTV TREEGEGMET TDTESVSSAS TYTQSLEQLL NSPETKLEPP LWHAEFTKEE 1560
LVQKLSSTTK SADHLNGLLR ETEATNAILM EQIKLLKSEI RRLERNQERE KSAANLEYLK 1620
NVLLQFIFLK PGSERERLLP VINTMLQLSP EEKGKLAAVA QGEEENASRS SGWASYLHSW 1680
SGLR 1684 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
 GO:0034499; P:late endosome to Golgi transport; IMP:UniProtKB.
 GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
 GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
 GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
 GO:0000042; P:protein targeting to Golgi; IEA:InterPro.
 GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
 GO:0071955; P:recycling endosome to Golgi transport; IMP:UniProtKB.
 GO:0070861; P:regulation of protein exit from endoplasmic reticulum; IMP:UniProtKB. 
Interpro
 IPR000237; GRIP. 
Pfam
 PF01465; GRIP 
SMART
 SM00755; Grip 
PROSITE
 PS50913; GRIP 
PRINTS