CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029143
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Tripartite motif-containing protein 5 
Protein Synonyms/Alias
  
Gene Name
 TRIM5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45CLTANHKKSMLDKGEubiquitination[1, 2]
50HKKSMLDKGESSCPVubiquitination[1, 2]
79HVANIVEKLREVKLSubiquitination[1, 3]
84VEKLREVKLSPEGQKubiquitination[1, 2]
91KLSPEGQKVDHCARHubiquitination[1, 2]
152ALEMLRQKQQEAEELubiquitination[1]
171REEKASWKTQIQYDKubiquitination[1, 4]
178KTQIQYDKTNVLADFubiquitination[1, 2, 4, 5]
212KEEEDILKSLTNSETubiquitination[5]
263RTENVTLKKPETFPKubiquitination[1]
264TENVTLKKPETFPKNubiquitination[1]
270KKPETFPKNQRRVFRubiquitination[1]
282VFRAPDLKGMLEVFRubiquitination[1, 2, 3, 4, 5, 6, 7]
324KRQVSSPKPQIIYGAubiquitination[1, 8]
368WEVDVSKKTAWILGVubiquitination[1]
481FPYLNPRKCGVPMTLubiquitination[1, 7]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 493 AA 
Protein Sequence
MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK GESSCPVCRI 60
SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE KLLLFCQEDG KVICWLCERS 120
QEHRGHHTFL TEEVAREYQV KLQAALEMLR QKQQEAEELE ADIREEKASW KTQIQYDKTN 180
VLADFEQLRD ILDWEESNEL QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ 240
GSVMELLQKV SGKILRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD 300
VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG SQSITSGKHY 360
WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW VIGLEEGVKC SAFQDSSFHT 420
PSVPFIVPLS VIICPDRVGV FLDYEACTVS FFNITNHGFL IYKFSHCSFS QPVFPYLNPR 480
KCGVPMTLCS PSS 493 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box 
SMART
 SM00336; BBOX
 SM00184; RING 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.