TRI35_HUMAN - dbPTM
TRI35_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRI35_HUMAN
UniProt AC Q9UPQ4
Protein Name Tripartite motif-containing protein 35
Gene Name TRIM35
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Cytoplasm . Nucleus. Found predominantly in cytoplasm with a granular distribution. Found in punctuate nuclear bodies (By similarity)..
Protein Description Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth. [PubMed: 25263439 Involved in the cell death mechanism (By similarity]
Protein Sequence MERSPDVSPGPSRSFKEELLCAVCYDPFRDAVTLRCGHNFCRGCVSRCWEVQVSPTCPVCKDRASPADLRTNHTLNNLVEKLLREEAEGARWTSYRFSRVCRLHRGQLSLFCLEDKELLCCSCQADPRHQGHRVQPVKDTAHDFRAKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGRIRQEFDKLREFLRVEEQAILDAMAEETRQKQLLADEKMKQLTEETEVLAHEIERLQMEMKEDDVSFLMKHKSRKRRLFCTMEPEPVQPGMLIDVCKYLGSLQYRVWKKMLASVESVPFSFDPNTAAGWLSVSDDLTSVTNHGYRVQVENPERFSSAPCLLGSRVFSQGSHAWEVALGGLQSWRVGVVRVRQDSGAEGHSHSCYHDTRSGFWYVCRTQGVEGDHCVTSDPATSPLVLAIPRRLRVELECEEGELSFYDAERHCHLYTFHARFGEVRPYFYLGGARGAGPPEPLRICPLHISVKEELDG
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
1Acetylation-------MERSPDVS
-------CCCCCCCC		9.7221406692
4Phosphorylation----MERSPDVSPGP
----CCCCCCCCCCC		16.4929255136
8PhosphorylationMERSPDVSPGPSRSF
CCCCCCCCCCCCCCH		31.3629255136
12PhosphorylationPDVSPGPSRSFKEEL
CCCCCCCCCCHHHHH		46.6129255136
14PhosphorylationVSPGPSRSFKEELLC
CCCCCCCCHHHHHHH		45.0321955146
61UbiquitinationSPTCPVCKDRASPAD
CCCCCCCCCCCCHHH		50.94-
65PhosphorylationPVCKDRASPADLRTN
CCCCCCCCHHHHHHH		22.8630266825
71PhosphorylationASPADLRTNHTLNNL
CCHHHHHHHHHHHHH		38.3524076635
74PhosphorylationADLRTNHTLNNLVEK
HHHHHHHHHHHHHHH		33.0024076635
138TrimethylationGHRVQPVKDTAHDFR
CCCCCCCCCCHHHHH		56.92-
138UbiquitinationGHRVQPVKDTAHDFR
CCCCCCCCCCHHHHH		56.92-
138MethylationGHRVQPVKDTAHDFR
CCCCCCCCCCHHHHH		56.9223644510
160UbiquitinationHALREKAKAFWAMRR
HHHHHHHHHHHHHHH		56.00-
168PhosphorylationAFWAMRRSYEAIAKH
HHHHHHHHHHHHHHH		19.5722817900
169PhosphorylationFWAMRRSYEAIAKHN
HHHHHHHHHHHHHHC		13.9422817900
174UbiquitinationRSYEAIAKHNQVEAA
HHHHHHHHHCHHHHH		36.65-
174 (in isoform 2)Phosphorylation-36.6525159151
193UbiquitinationRIRQEFDKLREFLRV
HHHHHHHHHHHHHHH		55.56-
216UbiquitinationMAEETRQKQLLADEK
HHHHHHHHHHHCHHH		39.35-
223UbiquitinationKQLLADEKMKQLTEE
HHHHCHHHHHHHHHH		52.52-
225UbiquitinationLLADEKMKQLTEETE
HHCHHHHHHHHHHHH		53.90-
246UbiquitinationERLQMEMKEDDVSFL
HHHHHHCCCCHHHHH		44.69-
255UbiquitinationDDVSFLMKHKSRKRR
CHHHHHHHCCCCCCE		50.45-
257UbiquitinationVSFLMKHKSRKRRLF
HHHHHHCCCCCCEEE		46.57-
257AcetylationVSFLMKHKSRKRRLF
HHHHHHCCCCCCEEE		46.577407745
258O-linked_GlycosylationSFLMKHKSRKRRLFC
HHHHHCCCCCCEEEE		42.6330379171
260AcetylationLMKHKSRKRRLFCTM
HHHCCCCCCEEEEEC		49.307407755
379PhosphorylationVVRVRQDSGAEGHSH
EEEEECCCCCCCCCC		31.4024043423
385PhosphorylationDSGAEGHSHSCYHDT
CCCCCCCCCCCEEEC		28.1424043423
387PhosphorylationGAEGHSHSCYHDTRS
CCCCCCCCCEEECCC		21.2724043423
389PhosphorylationEGHSHSCYHDTRSGF
CCCCCCCEEECCCCE		13.0224043423
392PhosphorylationSHSCYHDTRSGFWYV
CCCCEEECCCCEEEE		17.2724043423
417PhosphorylationCVTSDPATSPLVLAI
EECCCCCCCCEEEEE		35.9423312004
418PhosphorylationVTSDPATSPLVLAIP
ECCCCCCCCEEEEEE		20.5323312004
488UbiquitinationCPLHISVKEELDG--
CCEEEEEEHHHCC--		38.39-
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 TRI35_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRI35_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 TRI35_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM5_HUMANTRIM5physical
16775307
KPYM_HUMANPKMphysical
25263439
AKTIP_HUMANAKTIPphysical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
OTUD5_HUMANOTUD5physical
28514442
KDM5C_HUMANKDM5Cphysical
28514442
KLH11_HUMANKLHL11physical
28514442
WDR20_HUMANWDR20physical
28514442
LIMD1_HUMANLIMD1physical
28514442
2AAB_HUMANPPP2R1Bphysical
28514442
MYO1F_HUMANMYO1Fphysical
28514442
MTA2_HUMANMTA2physical
28514442
HSP7E_HUMANHSPA14physical
28514442
LIMK2_HUMANLIMK2physical
28514442
ZMYM2_HUMANZMYM2physical
28514442
KIF1A_HUMANKIF1Aphysical
28514442
PIAS1_HUMANPIAS1physical
28514442
MKS1_HUMANMKS1physical
28514442
UBP7_HUMANUSP7physical
28514442
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 TRI35_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-8, AND MASSSPECTROMETRY.

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