CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014104
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 318 
Protein Synonyms/Alias
 Endocrine regulatory protein 
Gene Name
 ZNF318 
Gene Synonyms/Alias
 HRIHFB2436 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
591ETNPEYAKIHDLLKTubiquitination[1, 2]
1275PTSSSFGKFSWKKPEacetylation[3]
1866ACSFTKAKLDSFLSEacetylation[2]
1866ACSFTKAKLDSFLSEubiquitination[4, 5]
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] 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]
 [3] 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]
 [4] 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]
 [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
Functional Description
 Repressed AR-mediated transcriptional activation. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division (By similarity). 
Sequence Annotation
 ZN_FING 1063 1097 Matrin-type 1.
 ZN_FING 1136 1166 Matrin-type 2.
 MOD_RES 79 79 Phosphoserine.
 MOD_RES 81 81 Phosphoserine.
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 173 173 Phosphoserine.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 464 464 Phosphoserine.
 MOD_RES 527 527 Phosphoserine.
 MOD_RES 550 550 Phosphoserine (By similarity).
 MOD_RES 1037 1037 Phosphoserine.
 MOD_RES 1243 1243 Phosphoserine.
 MOD_RES 1420 1420 Phosphoserine.
 MOD_RES 1713 1713 Phosphoserine.
 MOD_RES 1896 1896 Phosphoserine.
 MOD_RES 2101 2101 Phosphoserine.
 MOD_RES 2189 2189 Phosphoserine.
 MOD_RES 2192 2192 Phosphoserine.
 MOD_RES 2243 2243 Phosphoserine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Meiosis; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2279 AA 
Protein Sequence
MYRSSARSSV SSHRPKDDGG GGPRSGRSSG SSSGPARRSS PPPPPSGSSS RTPARRPRSP 60
SGHRGRRASP SPPRGRRVSP SPPRARRGSP SPPRGRRLFP PGPAGFRGSS RGESRADYAR 120
DGRGDHPGDS GSRRRSPGLC SDSLEKSLRI TVGNDHFCVS TPERRRLSDR LGSPVDNLED 180
MDRDDLTDDS VFTRSSQCSR GLERYISQEE GPLSPFLGQL DEDYRTKETF LHRSDYSPHI 240
SCHDELLRGT ERNREKLKGY SIRSEERSRE AKRPRYDDTV KINSMGGDHP SFTSGTRNYR 300
QRRRSPSPRF LDPEFRELDL ARRKREEEEE RSRSLSQELV GVDGGGTGCS IPGLSGVLTA 360
SEPGYSLHRP EEVSVMPKKS ILKKRIEVDI MEPSMQLESF SSSTSSSQDH PLYSGHPSLP 420
LSGAIAAFAS EIENKGTMVE TALKEPQGNL YQWGPLPGIP KDNSPLREKF GSFLCHKDNL 480
DLKAEGPERH TDFLLPHERA SQDGSGFSRI LSMLADSTST QEKRRRSFPD IEDEEKFLYG 540
DEEEDLKAES VPKPLGSSES EVMRQKASSL PSSAPAVKLE SLEETNPEYA KIHDLLKTIG 600
LDIGVAEISQ LAARTQERLH GKKPSLRSSA DRRSSVDRYF SADHCSSVDH RFSADRCSSV 660
DHCFSADRRS SDPHRLESRE AHHSNTHSPE VSHPHPPSPV DPYLLTKNSP PFLKSDHPVG 720
HISGPEVVGS GFQSSVAVRC MLPSAPSAPI RLPHTAALSQ FHMPRASQFA AARIPPNYQG 780
PAIPPASFDA YRHYMAYAAS RWPMYPTSQP SNHPVPEPHR IMPITKQATR SRPNLRVIPT 840
VTPDKPKQKE SLRGSIPAAQ VPVQVSIPSL IRYNPEKISD EKNRASQKQK VIEEREKLKN 900
DREARQKKMY YLRTELERLH KQQGEMLRKK RREKDGHKDP LLVEVSRLQD NIMKDIAELR 960
QEAEEAEKKQ SELDKVAQIL GINIFDKSQK SLSDSREPTE KPGKAEKSKS PEKVSSFSNS 1020
SSNKESKVNN EKFRTKSPKP AESPQSATKQ LDQPTAAYEY YDAGNHWCKD CNTICGTMFD 1080
FFTHMHNKKH TQTLDPYNRP WASKTQSEAK QDAIKRTDKI TVPAKGSEFL VPISGFYCQL 1140
CEEFLGDPIS GEQHVKGHQH NEKYKKYVDE NPLYEERRNL DRQAGLAVVL ETERRRQSEL 1200
KRKLSEKPKE EKKEKKAKAV KEVKEDDKVS EKLEDQLSEG RNSPEKAENK RNTGIKLQLK 1260
EEVKKESPTS SSFGKFSWKK PEKEEEKSSL VTPSISKEEI LESSKDKEDG KTEAGKAKPI 1320
KIKLSGKTVV AHTSPWMPVV TTSTQTKIRP NLPIPSTVLR KSCSATMSKP APLNTFLSIK 1380
SSGTTAKPLP VVKESSADLL LPPDIISKAF GGEEVILKGS PEEKVVLAEK SEPSHLPEQI 1440
LPPPPPPPPP PPPPPPVIPH PAAPSAAQAN AILAPVKSNP VVSQTLSPGF VGPNILNPVL 1500
PVAIMASAQP AAIPSDETAP GVSESDRDQT LFSVLVRPPP PLSSVFSEQA KKLEKRNSCL 1560
ATANAKDLYD IFYSSGGKGA PETKGAPETK LSGGPLANGE NSNLSRTKSS DTSSTSPLNS 1620
SASQEELHQD EGLVAAPIVS NSEKPIAKTL VALGKWSVVE HVGPKSTGST YGFLQPLTRL 1680
CQSRPYETIT PKTDTLAIWT SSSFQSDTSR DISPEKSELD LGEPGPPGVE PPPQLLDIQC 1740
KESQKLVEIH LRESVNQDKE SQELRKSEDC RESEIETNTE LKERVKELSE GIVDEGVSTS 1800
IGPHSIDDSN LNHGNRYMWE GEVKQPNLLM IDKEAEQSNK LMTGSETPSK VVIKLSPQAC 1860
SFTKAKLDSF LSEARSLLNP QDTPVKISAP ELLLHSPARS AMCLTGSPQE QGVSVVSEEG 1920
LENSAPESAS RTSRYRSLKL KRERSKDFQV KKIYELAVWD ENKKRPETWE SPEKPKTEAL 1980
ELQDVHPELT VTIESKALED FEATDLKVEE LTALGNLGDM PVDFCTTRVS PAHRSPTVLC 2040
QKVCEENSVS PIGCNSSDPA DFEPIPSFSG FPLDSPKTLV LDFETEGERN SPNPRSVRIP 2100
SPNILKTGLT ENVDRGLGGL EGTHQALDLL AGGMMPEEVK ESSQLDKQES LGLELKTINS 2160
AGLGPSPCLP DLVDFVTRTS GVQKDKLCSP LSEPGDPSKC SSLELGPLQL EISNASTTEV 2220
AILQVDDDSG DPLNLVKAPV SRSPPREQVI EDNMVPQGMP EQETTVGAIQ DHTESSVHN 2279 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007126; P:meiosis; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR015880; Znf_C2H2-like.
 IPR003604; Znf_U1. 
Pfam
  
SMART
 SM00355; ZnF_C2H2
 SM00451; ZnF_U1 
PROSITE
 PS50171; ZF_MATRIN 
PRINTS