CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022867
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger MYM-type protein 2 
Protein Synonyms/Alias
 Fused in myeloproliferative disorders protein; Rearranged in atypical myeloproliferative disorder protein; Zinc finger protein 198 
Gene Name
 ZMYM2 
Gene Synonyms/Alias
 FIM; RAMP; ZNF198 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88TITFTSSKNEELQGNubiquitination[1, 2, 3]
104SKITPSSKELASQKGubiquitination[3]
297ASFPRNQKQPGVDSLubiquitination[3]
441IRHEVSFKNMTHKLCubiquitination[3]
503QSCVSEYKQVGSHPSubiquitination[3]
513GSHPSFLKEVRDHMQubiquitination[3, 4]
529SFLMQPEKYGKLTTCubiquitination[3]
532MQPEKYGKLTTCTGCubiquitination[3]
603QATMPDGKLYNFCNSubiquitination[3]
638APSDIQLKCNYCKNSubiquitination[3]
649CKNSFCSKPEILEWEubiquitination[3]
700TVNFSGVKRPFCSEGubiquitination[3]
713EGCKLLYKQDFARRLubiquitination[2, 3]
735NYCSQLCKKGATKELubiquitination[3]
740LCKKGATKELDGVVRubiquitination[3]
757CSEDCCKKFQDWYYKubiquitination[3]
812EPNMTTQKGPENLHYubiquitination[3]
938PAAIEELKSKVSSDAubiquitination[3]
963MMSEDEGKTETTNINsumoylation[5]
1080TYGVNAWKHWVKTRQubiquitination[3]
1099LLVLDELKSSKSVKLubiquitination[2, 3]
1102LDELKSSKSVKLKEDubiquitination[3]
1105LKSSKSVKLKEDLLSubiquitination[3]
1159YLCGSNRKDNIFIDPubiquitination[3]
1177TFEQELNKILRSWQPubiquitination[3]
1230NTKYFGLKTVEQHLRubiquitination[3]
1249TVFRHWKKNPLTMENubiquitination[3]
1257NPLTMENKACLRYQVubiquitination[3]
1275CGTDNEDKITTGKRKubiquitination[3]
1280EDKITTGKRKHEDDEubiquitination[3]
1282KITTGKRKHEDDEPVubiquitination[3]
1305NPSRCPVKMFECYLSubiquitination[3]
1313MFECYLSKSPQNLNQubiquitination[2, 3]
1362LVRVLLVKDIYDKDNubiquitination[3]
1367LVKDIYDKDNYELDEubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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] 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]
 [4] 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]
 [5] ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML.
 Kunapuli P, Kasyapa CS, Chin SF, Caldas C, Cowell JK.
 Exp Cell Res. 2006 Nov 15;312(19):3739-51. [PMID: 17027752
Functional Description
 May function as a transcription factor. 
Sequence Annotation
 ZN_FING 352 386 MYM-type 1.
 ZN_FING 398 436 MYM-type 2.
 ZN_FING 445 480 MYM-type 3.
 ZN_FING 491 549 MYM-type 4.
 ZN_FING 559 597 MYM-type 5.
 ZN_FING 605 652 MYM-type 6.
 ZN_FING 660 694 MYM-type 7.
 ZN_FING 701 740 MYM-type 8.
 ZN_FING 747 781 MYM-type 9.
 MOD_RES 303 303 Phosphoserine.
 MOD_RES 305 305 Phosphoserine.
 MOD_RES 838 838 Phosphoserine.
 MOD_RES 958 958 Phosphoserine.
 MOD_RES 1376 1376 Phosphothreonine.  
Keyword
 Alternative splicing; Chromosomal rearrangement; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1377 AA 
Protein Sequence
MDTSSVGGLE LTDQTPVLLG STAMATSLTN VGNSFSGPAN PLVSRSNKFQ NSSVEDDDDV 60
VFIEPVQPPP PSVPVVADQR TITFTSSKNE ELQGNDSKIT PSSKELASQK GSVSETIVID 120
DEEDMETNQG QEKNSSNFIE RRPPETKNRT NDVDFSTSSF SRSKVNAGMG NSGITTEPDS 180
EIQIANVTTL ETGVSSVNDG QLENTDGRDM NLMITHVTSL QNTNLGDVSN GLQSSNFGVN 240
IQTYTPSLTS QTKTGVGPFN PGRMNVAGDV FQNGESATHH NPDSWISQSA SFPRNQKQPG 300
VDSLSPVASL PKQIFQPSVQ QQPTKPVKVT CANCKKPLQK GQTAYQRKGS AHLFCSTTCL 360
SSFSHKPAPK KLCVMCKKDI TTMKGTIVAQ VDSSESFQEF CSTSCLSLYE DKQNPTKGAL 420
NKSRCTICGK LTEIRHEVSF KNMTHKLCSD HCFNRYRMAN GLIMNCCEQC GEYLPSKGAG 480
NNVLVIDGQQ KRFCCQSCVS EYKQVGSHPS FLKEVRDHMQ DSFLMQPEKY GKLTTCTGCR 540
TQCRFFDMTQ CIGPNGYMEP YCSTACMNSH KTKYAKSQSL GIICHFCKRN SLPQYQATMP 600
DGKLYNFCNS SCVAKFQALS MQSSPNGQFV APSDIQLKCN YCKNSFCSKP EILEWENKVH 660
QFCSKTCSDD YKKLHCIVTY CEYCQEEKTL HETVNFSGVK RPFCSEGCKL LYKQDFARRL 720
GLRCVTCNYC SQLCKKGATK ELDGVVRDFC SEDCCKKFQD WYYKAARCDC CKSQGTLKER 780
VQWRGEMKHF CDQHCLLRFY CQQNEPNMTT QKGPENLHYD QGCQTSRTKM TGSAPPPSPT 840
PNKEMKNKAV LCKPLTMTKA TYCKPHMQTK SCQTDDTWRT EYVPVPIPVP VYIPVPMHMY 900
SQNIPVPTTV PVPVPVPVFL PAPLDSSEKI PAAIEELKSK VSSDALDTEL LTMTDMMSED 960
EGKTETTNIN SVIIETDIIG SDLLKNSDPE TQSSMPDVPY EPDLDIEIDF PRAAEELDME 1020
NEFLLPPVFG EEYEEQPRPR SKKKGAKRKA VSGYQSHDDS SDNSECSFPF KYTYGVNAWK 1080
HWVKTRQLDE DLLVLDELKS SKSVKLKEDL LSHTTAELNY GLAHFVNEIR RPNGENYAPD 1140
SIYYLCLGIQ EYLCGSNRKD NIFIDPGYQT FEQELNKILR SWQPSILPDG SIFSRVEEDY 1200
LWRIKQLGSH SPVALLNTLF YFNTKYFGLK TVEQHLRLSF GTVFRHWKKN PLTMENKACL 1260
RYQVSSLCGT DNEDKITTGK RKHEDDEPVF EQIENTANPS RCPVKMFECY LSKSPQNLNQ 1320
RMDVFYLQPE CSSSTDSPVW YTSTSLDRNT LENMLVRVLL VKDIYDKDNY ELDEDTD 1377 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR021893; DUF3504.
 IPR011017; TRASH_dom.
 IPR010507; Znf_MYM. 
Pfam
 PF12012; DUF3504
 PF06467; zf-FCS 
SMART
 SM00746; TRASH 
PROSITE
  
PRINTS