CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023096
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 G patch domain-containing protein 8 
Protein Synonyms/Alias
  
Gene Name
 GPATCH8 
Gene Synonyms/Alias
 GPATC8; KIAA0553 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1096TAKLLLEKIQSRKVEacetylation[1]
1142LPPSLGNKPVLPLIGacetylation[1, 2]
1322EEMEKYSKLQQAAQQubiquitination[3, 4, 5, 6]
1338IQQQLLAKQVKAFPAubiquitination[3, 4, 5, 6, 7]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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] 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] 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]
 [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
  
Sequence Annotation
 DOMAIN 40 86 G-patch.
 ZN_FING 136 160 C2H2-type.
 MOD_RES 653 653 Phosphoserine.
 MOD_RES 738 738 Phosphoserine.
 MOD_RES 740 740 Phosphoserine.
 MOD_RES 758 758 Phosphoserine.
 MOD_RES 981 981 Phosphoserine.
 MOD_RES 1014 1014 Phosphoserine.
 MOD_RES 1033 1033 Phosphoserine.
 MOD_RES 1035 1035 Phosphoserine.
 MOD_RES 1081 1081 Phosphoserine.
 MOD_RES 1107 1107 Phosphoserine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1502 AA 
Protein Sequence
MADRFSRFNE DRDFQGNHFD QYEEGHLEIE QASLDKPIES DNIGHRLLQK HGWKLGQGLG 60
KSLQGRTDPI PIVVKYDVMG MGRMEMELDY AEDATERRRV LEVEKEDTEE LRQKYKDYVD 120
KEKAIAKALE DLRANFYCEL CDKQYQKHQE FDNHINSYDH AHKQRLKDLK QREFARNVSS 180
RSRKDEKKQE KALRRLHELA EQRKQAECAP GSGPMFKPTT VAVDEEGGED DKDESATNSG 240
TGATASCGLG SEFSTDKGGP FTAVQITNTT GLAQAPGLAS QGISFGIKNN LGTPLQKLGV 300
SFSFAKKAPV KLESIASVFK DHAEEGTSED GTKPDEKSSD QGLQKVGDSD GSSNLDGKKE 360
DEDPQDGGSL ASTLSKLKRM KREEGAGATE PEYYHYIPPA HCKVKPNFPF LLFMRASEQM 420
DGDNTTHPKN APESKKGSSP KPKSCIKAAA SQGAEKTVSE VSEQPKETSM TEPSEPGSKA 480
EAKKALGGDV SDQSLESHSQ KVSETQMCES NSSKETSLAT PAGKESQEGP KHPTGPFFPV 540
LSKDESTALQ WPSELLIFTK AEPSISYSCN PLYFDFKLSR NKDARTKGTE KPKDIGSSSK 600
DHLQGLDPGE PNKSKEVGGE KIVRSSGGRM DAPASGSACS GLNKQEPGGS HGSETEDTGR 660
SLPSKKERSG KSHRHKKKKK HKKSSKHKRK HKADTEEKSS KAESGEKSKK RKKRKRKKNK 720
SSAPADSERG PKPEPPGSGS PAPPRRRRRA QDDSQRRSLP AEEGSSGKKD EGGGGSSSQD 780
HGGRKHKGEL PPSSCQRRAG TKRSSRSSHR SQPSSGDEDS DDASSHRLHQ KSPSQYSEEE 840
EEEDSGSEHS RSRSRSGRRH SSHRSSRRSY SSSSDASSDQ SCYSRQRSYS DDSYSDYSDR 900
SRRHSKRSHD SDDSDYASSK HRSKRHKYSS SDDDYSLSCS QSRSRSRSHT RERSRSRGRS 960
RSSSCSRSRS KRRSRSTTAH SWQRSRSYSR DRSRSTRSPS QRSGSRKRSW GHESPEERHS 1020
GRRDFIRSKI YRSQSPHYFR SGRGEGPGKK DDGRGDDSKA TGPPSQNSNI GTGRGSEGDC 1080
SPEDKNSVTA KLLLEKIQSR KVERKPSVSE EVQATPNKAG PKLKDPPQGY FGPKLPPSLG 1140
NKPVLPLIGK LPATRKPNKK CEESGLERGE EQEQSETEEG PPGSSDALFG HQFPSEETTG 1200
PLLDPPPEES KSGEATADHP VAPLGTPAHS DCYPGDPTIS HNYLPDPSDG DTLESLDSSS 1260
QPGPVESSLL PIAPDLEHFP SYAPPSGDPS IESTDGAEDA SLAPLESQPI TFTPEEMEKY 1320
SKLQQAAQQH IQQQLLAKQV KAFPASAALA PATPALQPIH IQQPATASAT SITTVQHAIL 1380
QHHAAAAAAA IGIHPHPHPQ PLAQVHHIPQ PHLTPISLSH LTHSIIPGHP ATFLASHPIH 1440
IIPASAIHPG PFTFHPVPHA ALYPTLLAPR PAAAAATALH LHPLLHPIFS GQDLQHPPSH 1500
GT 1502 
Gene Ontology
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR000467; G_patch_dom.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR022755; Znf_C2H2_jaz. 
Pfam
 PF01585; G-patch
 PF12171; zf-C2H2_jaz 
SMART
 SM00443; G_patch
 SM00355; ZnF_C2H2 
PROSITE
 PS50174; G_PATCH
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS