TRI47_HUMAN - dbPTM
TRI47_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI47_HUMAN
UniProt AC Q96LD4
Protein Name Tripartite motif-containing protein 47
Gene Name TRIM47
Organism Homo sapiens (Human).
Sequence Length 638
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MDGSGPFSCPICLEPLREPVTLPCGHNFCLACLGALWPHRGASGAGGPGGAARCPLCQEPFPDGLQLRKNHTLSELLQLRQGSGPGSGPGPAPALAPEPSAPSALPSVPEPSAPCAPEPWPAGEEPVRCDACPEGAALPAALSCLSCLASFCPAHLGPHERSPALRGHRLVPPLRRLEESLCPRHLRPLERYCRAERVCLCEACAAQEHRGHELVPLEQERALQEAEQSKVLSAVEDRMDELGAGIAQSRRTVALIKSAAVAERERVSRLFADAAAALQGFQTQVLGFIEEGEAAMLGRSQGDLRRQEEQRSRLSRARQNLSQVPEADSVSFLQELLALRLALEDGCGPGPGPPRELSFTKSSQAVRAVRDMLAVACVNQWEQLRGPGGNEDGPQKLDSEADAEPQDLESTNLLESEAPRDYFLKFAYIVDLDSDTADKFLQLFGTKGVKRVLCPINYPLSPTRFTHCEQVLGEGALDRGTYYWEVEIIEGWVSMGVMAEDFSPQEPYDRGRLGRNAHSCCLQWNGRSFSVWFHGLEAPLPHPFSPTVGVCLEYADRALAFYAVRDGKMSLLRRLKASRPRRGGIPASPIDPFQSRLDSHFAGLFTHRLKPAFFLESVDAHLQIGPLKKSCISVLKRR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1 (in isoform 2)Acetylation-13.7022814378
19UbiquitinationCLEPLREPVTLPCGH
CCCCCCCCEEECCCC		20.2621963094
72PhosphorylationLQLRKNHTLSELLQL
CHHCCCCCHHHHHHH		41.1826657352
74PhosphorylationLRKNHTLSELLQLRQ
HCCCCCHHHHHHHHC		27.6128555341
123UbiquitinationAPEPWPAGEEPVRCD
CCCCCCCCCCCCCCC		35.40-
123UbiquitinationAPEPWPAGEEPVRCD
CCCCCCCCCCCCCCC		35.4027667366
158UbiquitinationFCPAHLGPHERSPAL
HCCHHHCCCCCCHHH		32.31-
158UbiquitinationFCPAHLGPHERSPAL
HCCHHHCCCCCCHHH		32.3121963094
162PhosphorylationHLGPHERSPALRGHR
HHCCCCCCHHHCCCC		16.1328348404
180PhosphorylationPLRRLEESLCPRHLR
CHHHHHHHHCHHHCH		26.3728857561
209UbiquitinationEACAAQEHRGHELVP
HHHHCCCCCCCCCCC		29.01-
209UbiquitinationEACAAQEHRGHELVP
HHHHCCCCCCCCCCC		29.0122817900
212UbiquitinationAAQEHRGHELVPLEQ
HCCCCCCCCCCCHHH		25.7722817900
230UbiquitinationLQEAEQSKVLSAVED
HHHHHHHHHHHHHHH		47.0621906983
233PhosphorylationAEQSKVLSAVEDRMD
HHHHHHHHHHHHHHH		33.0020068231
257UbiquitinationRRTVALIKSAAVAER
HHHHHHHHHHHHHHH		34.5921906983
258PhosphorylationRTVALIKSAAVAERE
HHHHHHHHHHHHHHH		17.9228176443
329PhosphorylationSQVPEADSVSFLQEL
HCCCCHHHHHHHHHH		27.06-
330UbiquitinationQVPEADSVSFLQELL
CCCCHHHHHHHHHHH		4.89-
330UbiquitinationQVPEADSVSFLQELL
CCCCHHHHHHHHHHH		4.8921963094
331PhosphorylationVPEADSVSFLQELLA
CCCHHHHHHHHHHHH		24.9627251275
358PhosphorylationPGPPRELSFTKSSQA
CCCCCCCCCCCHHHH		26.5624719451
360PhosphorylationPPRELSFTKSSQAVR
CCCCCCCCCHHHHHH		27.0027251275
361UbiquitinationPRELSFTKSSQAVRA
CCCCCCCCHHHHHHH		46.2121906983
372UbiquitinationAVRAVRDMLAVACVN
HHHHHHHHHHHHHHH		1.49-
372UbiquitinationAVRAVRDMLAVACVN
HHHHHHHHHHHHHHH		1.4921963094
390UbiquitinationQLRGPGGNEDGPQKL
HHCCCCCCCCCCCCC		50.53-
390UbiquitinationQLRGPGGNEDGPQKL
HHCCCCCCCCCCCCC		50.5323503661
391UbiquitinationLRGPGGNEDGPQKLD
HCCCCCCCCCCCCCC		68.56-
391UbiquitinationLRGPGGNEDGPQKLD
HCCCCCCCCCCCCCC		68.5623503661
396SumoylationGNEDGPQKLDSEADA
CCCCCCCCCCCCCCC		58.35-
396UbiquitinationGNEDGPQKLDSEADA
CCCCCCCCCCCCCCC		58.3521906983
398UbiquitinationEDGPQKLDSEADAEP
CCCCCCCCCCCCCCC		52.01-
398UbiquitinationEDGPQKLDSEADAEP
CCCCCCCCCCCCCCC		52.0121963094
399PhosphorylationDGPQKLDSEADAEPQ
CCCCCCCCCCCCCCC		45.16-
410PhosphorylationAEPQDLESTNLLESE
CCCCCHHHCCCCCCC		29.8728555341
447AcetylationFLQLFGTKGVKRVLC
HHHHHCCCCCCEEEE		63.1820167786
447UbiquitinationFLQLFGTKGVKRVLC
HHHHHCCCCCCEEEE		63.1822817900
450UbiquitinationLFGTKGVKRVLCPIN
HHCCCCCCEEEECCC		45.5222817900
458PhosphorylationRVLCPINYPLSPTRF
EEEECCCCCCCCCCC		13.2824732914
461PhosphorylationCPINYPLSPTRFTHC
ECCCCCCCCCCCCCH		21.5228731282
463PhosphorylationINYPLSPTRFTHCEQ
CCCCCCCCCCCCHHH		34.7321815630
568UbiquitinationFYAVRDGKMSLLRRL
HHHHHCCCHHHHHHH		29.6121963094
582MethylationLKASRPRRGGIPASP
HHHCCCCCCCCCCCC		50.8224129315
588PhosphorylationRRGGIPASPIDPFQS
CCCCCCCCCCCHHHH		19.6229255136
595PhosphorylationSPIDPFQSRLDSHFA
CCCCHHHHHHHHHHH		34.8823403867
599PhosphorylationPFQSRLDSHFAGLFT
HHHHHHHHHHHHHHH		25.7020873877
610UbiquitinationGLFTHRLKPAFFLES
HHHHCCCCHHHHHHH		33.9721963094
628UbiquitinationHLQIGPLKKSCISVL
HHCCCCCHHHHHHHH		45.8623503661
629UbiquitinationLQIGPLKKSCISVLK
HCCCCCHHHHHHHHH		59.2423503661
630PhosphorylationQIGPLKKSCISVLKR
CCCCCHHHHHHHHHC		18.3327251275
633PhosphorylationPLKKSCISVLKRR--
CCHHHHHHHHHCC--		26.2324719451
636UbiquitinationKSCISVLKRR-----
HHHHHHHHCC-----		43.9321906983
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TRI47_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI47_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TRI47_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TRIM8_HUMANTRIM8physical
22493164
ANS1A_HUMANANKS1Aphysical
22863883
DNPEP_HUMANDNPEPphysical
22863883
GANAB_HUMANGANABphysical
22863883
PTN12_HUMANPTPN12physical
22863883
TENS3_HUMANTNS3physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRI47_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASSSPECTROMETRY.

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