MIPT3_HUMAN - dbPTM
MIPT3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MIPT3_HUMAN
UniProt AC Q8TDR0
Protein Name TRAF3-interacting protein 1
Gene Name TRAF3IP1
Organism Homo sapiens (Human).
Sequence Length 691
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, cilium . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm, cytoskeleton, cilium basal body . Microtubules (PubMed:12935900). In the cilium, it is observed at the ciliary base, ciliary transition zone and
Protein Description Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules. Involved in kidney development and epithelial morphogenesis. Involved in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels. [PubMed: 26487268 Involved in ciliogenesis (By similarity]
Protein Sequence MNAAVVRRTQEALGKVIRRPPLTEKLLSKPPFRYLHDIITEVIRMTGFMKGLYTDAEMKSDNVKDKDAKISFLQKAIDVVVMVSGEPLLAKPARIVAGHEPERTNELLQIIGKCCLNKLSSDDAVRRVLAGEKGEVKGRASLTSRSQELDNKNVREEESRVHKNTEDRGDAEIKERSTSRDRKQKEELKEDRKPREKDKDKEKAKENGGNRHREGERERAKARARPDNERQKDRGNRERDRDSERKKETERKSEGGKEKERLRDRDRERDRDKGKDRDRRRVKNGEHSWDLDREKNREHDKPEKKSASSGEMSKKLSDGTFKDSKAETETEISTRASKSLTTKTSKRRSKNSVEGRKEDNISAKSLDSIVSGINNEPNQETTTSEIGTKEANINSTSISDDNSASLRCENIQPNPTEKQKGDSTSDAEGDAGPAGQDKSEVPETPEIPNELSSNIRRIPRPGSARPAPPRVKRQDSMEALQMDRSGSGKTVSNVITESHNSDNEEDDQFVVEAAPQLSEMSEIEMVTAVELEEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDVDAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSINLTSRR
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
40PhosphorylationRYLHDIITEVIRMTG
HHHHHHHHHHHHHHC		25.2426356563
46PhosphorylationITEVIRMTGFMKGLY
HHHHHHHHCHHHHCC		19.8826356563
69AcetylationNVKDKDAKISFLQKA
CCCCHHHHHHHHHHH		49.367666333
75AcetylationAKISFLQKAIDVVVM
HHHHHHHHHCCEEEE		49.837666343
84PhosphorylationIDVVVMVSGEPLLAK
CCEEEEECCCCCCCC		21.24-
141PhosphorylationGEVKGRASLTSRSQE
CCCCCCHHHCCCCHH		30.7126699800
143PhosphorylationVKGRASLTSRSQELD
CCCCHHHCCCCHHHH		21.4329214152
144PhosphorylationKGRASLTSRSQELDN
CCCHHHCCCCHHHHC		34.9221712546
146PhosphorylationRASLTSRSQELDNKN
CHHHCCCCHHHHCCC		27.9827966365
252AcetylationRKKETERKSEGGKEK
HHHHHHHHCCCHHHH		46.7712650503
288PhosphorylationRVKNGEHSWDLDREK
HHHCCCCCCCCCHHH		20.2728985074
306PhosphorylationHDKPEKKSASSGEMS
CCCCCHHCCCCCHHH		44.4429759185
308PhosphorylationKPEKKSASSGEMSKK
CCCHHCCCCCHHHHH		46.06-
309PhosphorylationPEKKSASSGEMSKKL
CCHHCCCCCHHHHHH		38.19-
313PhosphorylationSASSGEMSKKLSDGT
CCCCCHHHHHHCCCC		23.4929759185
317PhosphorylationGEMSKKLSDGTFKDS
CHHHHHHCCCCCCCC		42.7623312004
320PhosphorylationSKKLSDGTFKDSKAE
HHHHCCCCCCCCCCC		32.2823312004
324PhosphorylationSDGTFKDSKAETETE
CCCCCCCCCCCHHHH		34.06-
341PhosphorylationTRASKSLTTKTSKRR
HHHHHCCCCCCCCCC		33.0822210691
342PhosphorylationRASKSLTTKTSKRRS
HHHHCCCCCCCCCCC		37.3022210691
352 (in isoform 2)Phosphorylation-25.8625850435
357 (in isoform 2)Phosphorylation-79.0523663014
357UbiquitinationKNSVEGRKEDNISAK
CCCCCCCCCCCCCHH		79.05-
358 (in isoform 2)Phosphorylation-55.7323663014
359 (in isoform 2)Phosphorylation-61.8828355574
364UbiquitinationKEDNISAKSLDSIVS
CCCCCCHHHHHHHHH		44.77-
373 (in isoform 2)Phosphorylation-3.7926471730
381PhosphorylationNNEPNQETTTSEIGT
CCCCCCCCCHHHHCC		26.1318452278
383PhosphorylationEPNQETTTSEIGTKE
CCCCCCCHHHHCCCE		31.6118452278
384PhosphorylationPNQETTTSEIGTKEA
CCCCCCHHHHCCCEE		25.7318452278
403PhosphorylationTSISDDNSASLRCEN
CCCCCCCCCCEEEEC		26.6524905233
405PhosphorylationISDDNSASLRCENIQ
CCCCCCCCEEEECCC		19.0324905233
410PhosphorylationSASLRCENIQPNPTE
CCCEEEECCCCCCCC		41.6532645325
410 (in isoform 2)Phosphorylation-41.6521406692
444PhosphorylationDKSEVPETPEIPNEL
CCCCCCCCCCCCCHH		21.8328555341
463PhosphorylationRRIPRPGSARPAPPR
CCCCCCCCCCCCCCC		24.6428555341
476PhosphorylationPRVKRQDSMEALQMD
CCCCCCCHHHHHHCC		15.3523927012
496PhosphorylationKTVSNVITESHNSDN
CCHHHHHHCCCCCCC		27.4427251275
498PhosphorylationVSNVITESHNSDNEE
HHHHHHCCCCCCCHH		21.2227251275
501PhosphorylationVITESHNSDNEEDDQ
HHHCCCCCCCHHHHH		36.0722468782
547PhosphorylationLVKKILETKKDYEKL
HHHHHHHCHHHHHHH		39.6929116813
551PhosphorylationILETKKDYEKLQQSP
HHHCHHHHHHHHHCC		24.6829116813
557PhosphorylationDYEKLQQSPKPGEKE
HHHHHHHCCCCCHHH		23.1725849741
574UbiquitinationLFESAWKKEKDIVSK
HHHHHHHHHHHHHHH		60.33-
581UbiquitinationKEKDIVSKEIEKLRT
HHHHHHHHHHHHHHH		52.39-
585UbiquitinationIVSKEIEKLRTSIQT
HHHHHHHHHHHHHHH		49.26-
588PhosphorylationKEIEKLRTSIQTLCK
HHHHHHHHHHHHHHH		40.3922210691
589PhosphorylationEIEKLRTSIQTLCKS
HHHHHHHHHHHHHHH		13.2822210691
639PhosphorylationLQQEQRITDCAVEPL
HHHHHCHHHHCHHHH		27.4928348404
683PhosphorylationEKIQKMVYSINLTSR
HHHHHHHHHHCCCCC		10.5930257219
688PhosphorylationMVYSINLTSRR----
HHHHHCCCCCC----		18.7230257219
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 MIPT3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MIPT3_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 MIPT3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF3_HUMANTRAF3physical
10791955
TRAF6_HUMANTRAF6physical
10791955
DMD_HUMANDMDphysical
17043677
CDC5L_HUMANCDC5Lphysical
17043677
DYST_HUMANDSTphysical
17043677
TAB2_HUMANTAB2physical
17043677
AP180_HUMANSNAP91physical
17043677
NOE1_HUMANOLFM1physical
17043677
SMC2_HUMANSMC2physical
17043677
SFR1_HUMANSFR1physical
17043677
SMC3_HUMANSMC3physical
17043677
FRM4A_HUMANFRMD4Aphysical
17043677
WAC_HUMANWACphysical
17043677
ABI2_HUMANABI2physical
17043677
CCD93_HUMANCCDC93physical
17043677
MIC60_HUMANIMMTphysical
17043677
SPTB2_HUMANSPTBN1physical
17043677
MACF1_HUMANMACF1physical
17043677
GOGA4_HUMANGOLGA4physical
17043677
TRAK1_HUMANTRAK1physical
17043677
SMC4_HUMANSMC4physical
17043677
CCNA2_HUMANCCNA2physical
17043677
EXOC1_HUMANEXOC1physical
17043677
A4_HUMANAPPphysical
21832049
ACTS_HUMANACTA1physical
20391533
ACTB_HUMANACTBphysical
20391533
ACTC_HUMANACTC1physical
20391533
ACTG_HUMANACTG1physical
20391533
ACTN1_HUMANACTN1physical
20391533
ACTN4_HUMANACTN4physical
20391533
SAHH_HUMANAHCYphysical
20391533
KCRB_HUMANCKBphysical
20391533
EF1A1_HUMANEEF1A1physical
20391533
HS90A_HUMANHSP90AA1physical
20391533
HS90B_HUMANHSP90AB1physical
20391533
HS71L_HUMANHSPA1Lphysical
20391533
HSP76_HUMANHSPA6physical
20391533
HSP7C_HUMANHSPA8physical
20391533
GRP75_HUMANHSPA9physical
20391533
K1C10_HUMANKRT10physical
20391533
K1C9_HUMANKRT9physical
20391533
MAP1A_HUMANMAP1Aphysical
20391533
MAP4_HUMANMAP4physical
20391533
MARE2_HUMANMAPRE2physical
20391533
MYH9_HUMANMYH9physical
20391533
PGK1_HUMANPGK1physical
20391533
PHB_HUMANPHBphysical
20391533
SERA_HUMANPHGDHphysical
20391533
KPYM_HUMANPKMphysical
20391533
RL24_HUMANRPL24physical
20391533
RL7_HUMANRPL7physical
20391533
S10A8_HUMANS100A8physical
20391533
TRAP1_HUMANTRAP1physical
20391533
TBB5_HUMANTUBBphysical
20391533
TBB2A_HUMANTUBB2Aphysical
20391533
TBB2B_HUMANTUBB2Bphysical
20391533
UBX10_HUMANUBXN10physical
26389662
IFT20_HUMANIFT20physical
27173435
DTBP1_HUMANDTNBP1physical
27173435
IF172_HUMANIFT172physical
27173435
IFT57_HUMANIFT57physical
27173435
IFT74_HUMANIFT74physical
27173435
SSNA1_HUMANSSNA1physical
27173435
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 MIPT3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-476, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory