CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001510
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM37 
Protein Synonyms/Alias
 Mulibrey nanism protein; Tripartite motif-containing protein 37 
Gene Name
 TRIM37 
Gene Synonyms/Alias
 KIAA0898; MUL; POB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
234HQLRSCSKSELISKSubiquitination[1]
411RSPTFFQKSRDQHWYubiquitination[1]
474ALETRAKKSACSDMLubiquitination[1]
673WRVPSDLKMLKRLKTubiquitination[1]
693RCMKTDVKNTLSEIKubiquitination[2]
742LGMELLAKSSVANCYubiquitination[1]
787PGENSRSKGDCQTLSubiquitination[1]
824SIGDILPKTEDRQCKubiquitination[2]
854PAVEKRRKMVTLGANubiquitination[1]
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] 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] 
Functional Description
 E3 ubiquitin-protein ligase. 
Sequence Annotation
 DOMAIN 276 403 MATH.
 ZN_FING 15 55 RING-type; degenerate.
 ZN_FING 90 132 B box-type.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Peroxisome; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 964 AA 
Protein Sequence
MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL 60
RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW 120
GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR 180
EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK 240
SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP 300
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII 360
REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR FQVRSPTFFQ KSRDQHWYIT 420
QLEAAQTSYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDALET RAKKSACSDM 480
LLEGGPTTAS VREAKEDEED EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS 540
TATSNTEEND IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR 600
THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA SYSRKDKDQR 660
KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK SSSAASGDMQ TSLFSADQAA 720
LAACGTENSG RLQDLGMELL AKSSVANCYI RNSTNKKSNS PKPARSSVAG SLSLRRAVDP 780
GENSRSKGDC QTLSEGSPGS SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV 840
AVFSGLPAVE KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM 900
SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG PEDLSFNTDE 960
NSGR 964 
Gene Ontology
 GO:0016235; C:aggresome; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0070842; P:aggresome assembly; IDA:UniProtKB.
 GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. 
Interpro
 IPR003649; Bbox_C.
 IPR002083; MATH.
 IPR008974; TRAF-like.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00917; MATH
 PF00643; zf-B_box 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00061; MATH
 SM00184; RING 
PROSITE
 PS50144; MATH
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS