CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 638 
Protein Synonyms/Alias
 Nuclear protein 220; Zinc finger matrin-like protein 
Gene Name
 Znf638 
Gene Synonyms/Alias
 Np220; Zfml 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
740ETMPLVIKGKSVKVCubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Early regulator of adipogenesis that works as a transcription cofactor of CEBPs, controlling the expression of PPARG and probably of other proadipogenic genes, such as SREBF1. Binds to cytidine clusters in double-stranded DNA. 
Sequence Annotation
 DOMAIN 676 751 RRM 1.
 DOMAIN 902 976 RRM 2.
 ZN_FING 1876 1906 Matrin-type.
 MOD_RES 128 128 Phosphoserine (By similarity).
 MOD_RES 381 381 Phosphoserine (By similarity).
 MOD_RES 418 418 Phosphoserine (By similarity).
 MOD_RES 554 554 Phosphoserine (By similarity).
 MOD_RES 606 606 Phosphoserine (By similarity).
 MOD_RES 615 615 Phosphoserine (By similarity).
 MOD_RES 1099 1099 Phosphoserine (By similarity).
 MOD_RES 1400 1400 Phosphoserine (By similarity).
 MOD_RES 1661 1661 Phosphoserine (By similarity).
 MOD_RES 1864 1864 Phosphoserine (By similarity).  
Keyword
 Activator; Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1960 AA 
Protein Sequence
MSRPRFNPRG TFPLQRPRAP NPPGMRPPGP FVRPGSMGLP RFYPAGRARG IPHRFPGHGS 60
YQNMGPQRMN VQVTQHRTDP RLTKEKLDFP EAQQKKGKPH GSRWDDESHI TPPVEVKQSS 120
VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR 180
KMSRRLPNLP SHSRNKETLS NETVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVKN 240
EFQPQQSISA TVSTPNVICN SVFPGGDMFR QMDFPGESSS QSFFPVESGT KMSGLHISGQ 300
SVLEPVKSIS QSISQTVSQT TSQSLNPPSM NQVPFTFELD AVLRQQERIS QKSVISSADA 360
HGGPTESKKD YQSEADLPIR SPFGIVKASW LPKFTQAGAQ KMKRLPTPSM MNDYYAASPR 420
IFPHLCSLCN VECSHLKDWI QHQNTSTHIE SCRQLRQQYP DWNPEILPSR RNESNRKENE 480
TPRRRSHSPS PRHSRRSSSG HRIRRSRSPV RYIYRPRSRS PRICHRFISK YRSRSRSRSR 540
SRSPYRSRNL LRRSPKSYRS ASPERTSRKS VRSDRKKALE DGGQRSVHGT EVTKQKHTET 600
VDKGLSPAQK PKLASGTKPS AKSLSSVKSD SHLGAYSAHK SENLEDDTLP EGKQESGKSA 660
LAQRKPQKDQ SLSSNSILLV SELPEDGFTE EDIRKAFLPF GKISDVLLVP CRNEAYLEME 720
LRKAVTSIMK YIETMPLVIK GKSVKVCVPG KKKPQNKEMK KKPSDIKKSS ASALKKETDA 780
SKTMETVSSS SSAKSGQIKS STVKVNKCAG KSAGSVKSVV TVAAKGKASI KTAKSGKKSL 840
EAKKSGNIKN KDSNKPVTVP ANSEIKASSE DKATGKSAEE SPSGTLEATE KEPVNKESEE 900
MSVVFISNLP NKGYSTEEIY NLAKPFGALK DILVLSSHKK AYIEINKKSA DSMVKFYTCF 960
PISMDGNQLS ISMAPEHVDL KDEEALFTTL IQENDPEANI DKIYNRFVHL DNLPEDGLQC 1020
VLCVGHQFGK VDRYMFMSNK NKVILQLESP ESALSMYNFL KQNPQNIGEH VLTCTLSPKT 1080
DSEVQRKNDL ELGKGSTFSP DLKNSPVDES EVQTAADSSS VKPSEVEEET TSNIGTETSV 1140
HQEELGKEEP KQALCESDFA IQTLELEAQG AEVSIEIPLV ASTPANIELF SENIDESALN 1200
QQMYTSDFEK EEAEVTNPET ELAVSDSVFI EERNIKGIIE DSPSETEDIF SGIVQPMVDA 1260
IAEVDKHETV SEVLPSACNV TQAPGSYIED EKVVSKKDIA EKVILDEKEE DEFNVKETRM 1320
DLQVKTEKAE KNEAIIFKEK LEKIIAAIRE KPIESSVIKA DPTKGLDQTS KPDETGKSSV 1380
LTVSNVYSSK SSIKATVVSS PKAKSTPSKT ESHSTFPKPV LREQIKADKK VSAKEFGLLK 1440
NTRSGLAESN SKSKPTQIGV NRGCSGRISA LQCKDSKVDY KDITKQSQET ETKPPIMKRD 1500
DSNNKALALQ NTKNSKSTTD RSSKSKEEPL FTFNLDEFVT VDEVIEEVNP SQAKQNPLKG 1560
KRKEALKISP SPELNLKKKK GKTSVPHSVE GELSFVTLDE IGEEEDATVQ ALVTVDEVID 1620
EEELNMEEMV KNSNSLLTLD ELIDQDDCIP HSGPKDVTVL SMAEEQDLQQ ERLVTVDEIG 1680
EVEESADITF ATLNAKRDKR DSIGFISSQM PEDPSTLVTV DEIQDDSSDF HLMTLDEVTE 1740
EDENSLADFN NLKEELNFVT VDEVGDEEDG DNDSKVELAR GKIEHHTDKK GNRKRRAVDP 1800
KKSKLDSFSQ VGPGSETVTQ KDLKTMPERH LAAKTPMKRV RLGKSSPSQK VAEPTKGEEA 1860
FQMSEGVDDA ELKDSEPDEK RRKTQDSSVG KSMTSDVPGD LDFLVPKAGF FCPICSLFYS 1920
GEKAMANHCK STRHKQNTEK FMAKQRKEKE QNETEERSSR 1960 
Gene Ontology
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR000690; Znf_C2H2_matrin.
 IPR003604; Znf_U1. 
Pfam
  
SMART
 SM00360; RRM
 SM00355; ZnF_C2H2
 SM00451; ZnF_U1 
PROSITE
 PS50102; RRM
 PS50171; ZF_MATRIN 
PRINTS