C2TA_HUMAN - dbPTM
C2TA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C2TA_HUMAN
UniProt AC P33076
Protein Name MHC class II transactivator
Gene Name CIITA
Organism Homo sapiens (Human).
Sequence Length 1130
Subcellular Localization Nucleus . Nucleus, PML body . Recruited to PML body by PML.
Protein Description Essential for transcriptional activity of the HLA class II promoter; activation is via the proximal promoter. No DNA binding of in vitro translated CIITA was detected. May act in a coactivator-like fashion through protein-protein interactions by contacting factors binding to the proximal MHC class II promoter, to elements of the transcription machinery, or both. Alternatively it may activate HLA class II transcription by modifying proteins that bind to the MHC class II promoter. Also mediates enhanced MHC class I transcription; the promoter element requirements for CIITA-mediated transcription are distinct from those of constitutive MHC class I transcription, and CIITA can functionally replace TAF1 at these genes. Exhibits intrinsic GTP-stimulated acetyltransferase activity. Exhibits serine/threonine protein kinase activity: can phosphorylate the TFIID component TAF7, the RAP74 subunit of the general transcription factor TFIIF, histone H2B at 'Ser-37' and other histones (in vitro)..
Protein Sequence MRCLAPRPAGSYLSEPQGSSQCATMELGPLEGGYLELLNSDADPLCLYHFYDQMDLAGEEEIELYSEPDTDTINCDQFSRLLCDMEGDEETREAYANIAELDQYVFQDSQLEGLSKDIFKHIGPDEVIGESMEMPAEVGQKSQKRPFPEELPADLKHWKPAEPPTVVTGSLLVRPVSDCSTLPCLPLPALFNQEPASGQMRLEKTDQIPMPFSSSSLSCLNLPEGPIQFVPTISTLPHGLWQISEAGTGVSSIFIYHGEVPQASQVPPPSGFTVHGLPTSPDRPGSTSPFAPSATDLPSMPEPALTSRANMTEHKTSPTQCPAAGEVSNKLPKWPEPVEQFYRSLQDTYGAEPAGPDGILVEVDLVQARLERSSSKSLERELATPDWAERQLAQGGLAEVLLAAKEHRRPRETRVIAVLGKAGQGKSYWAGAVSRAWACGRLPQYDFVFSVPCHCLNRPGDAYGLQDLLFSLGPQPLVAADEVFSHILKRPDRVLLILDGFEELEAQDGFLHSTCGPAPAEPCSLRGLLAGLFQKKLLRGCTLLLTARPRGRLVQSLSKADALFELSGFSMEQAQAYVMRYFESSGMTEHQDRALTLLRDRPLLLSHSHSPTLCRAVCQLSEALLELGEDAKLPSTLTGLYVGLLGRAALDSPPGALAELAKLAWELGRRHQSTLQEDQFPSADVRTWAMAKGLVQHPPRAAESELAFPSFLLQCFLGALWLALSGEIKDKELPQYLALTPRKKRPYDNWLEGVPRFLAGLIFQPPARCLGALLGPSAAASVDRKQKVLARYLKRLQPGTLRARQLLELLHCAHEAEEAGIWQHVVQELPGRLSFLGTRLTPPDAHVLGKALEAAGQDFSLDLRSTGICPSGLGSLVGLSCVTRFRAALSDTVALWESLQQHGETKLLQAAEEKFTIEPFKAKSLKDVEDLGKLVQTQRTRSSSEDTAGELPAVRDLKKLEFALGPVSGPQAFPKLVRILTAFSSLQHLDLDALSENKIGDEGVSQLSATFPQLKSLETLNLSQNNITDLGAYKLAEALPSLAASLLRLSLYNNCICDVGAESLARVLPDMVSLRVMDVQYNKFTAAGAQQLAASLRRCPHVETLAMWTPTIPFSVQEHLQQQDSRISLR
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
95PhosphorylationDEETREAYANIAELD
CHHHHHHHHHHHHHH
8.7422210691
104PhosphorylationNIAELDQYVFQDSQL
HHHHHHHHHHCCHHH
11.6922210691
109PhosphorylationDQYVFQDSQLEGLSK
HHHHHCCHHHCCCCH
26.3622210691
141AcetylationMPAEVGQKSQKRPFP
CCHHHCCCCCCCCCC
49.2611046145
144AcetylationEVGQKSQKRPFPEEL
HHCCCCCCCCCCCCC
69.9511514574
280PhosphorylationTVHGLPTSPDRPGST
EEECCCCCCCCCCCC
23.9020538595
286PhosphorylationTSPDRPGSTSPFAPS
CCCCCCCCCCCCCCC
28.5215210796
287PhosphorylationSPDRPGSTSPFAPSA
CCCCCCCCCCCCCCC
46.4629449344
288PhosphorylationPDRPGSTSPFAPSAT
CCCCCCCCCCCCCCC
21.5123663014
293PhosphorylationSTSPFAPSATDLPSM
CCCCCCCCCCCCCCC
40.1315210796
315UbiquitinationRANMTEHKTSPTQCP
CCCCCCCCCCCCCCC
44.4520538595
330UbiquitinationAAGEVSNKLPKWPEP
CCHHHCCCCCCCCCH
59.6720538595
333UbiquitinationEVSNKLPKWPEPVEQ
HHCCCCCCCCCHHHH
82.742053859
373PhosphorylationVQARLERSSSKSLER
HHHHHHHCCCHHHHH
29.5917991736
427PhosphorylationGKAGQGKSYWAGAVS
ECCCCCHHHHHHHHH
32.50-
428PhosphorylationKAGQGKSYWAGAVSR
CCCCCHHHHHHHHHH
11.63-
434PhosphorylationSYWAGAVSRAWACGR
HHHHHHHHHHHHCCC
18.75-
536UbiquitinationLAGLFQKKLLRGCTL
HHHHHHHHHHCCCEE
41.81-
546PhosphorylationRGCTLLLTARPRGRL
CCCEEEEEECCCCHH
22.16-
740PhosphorylationLPQYLALTPRKKRPY
CCHHHHCCCCCCCCC
18.5524719451
834PhosphorylationQELPGRLSFLGTRLT
HHCCCCCEECCCCCC
19.6421712546
838PhosphorylationGRLSFLGTRLTPPDA
CCCEECCCCCCCCCH
25.3421712546
916O-linked_GlycosylationQAAEEKFTIEPFKAK
HHHHHCCCCCCCCCC
35.1830379171
942PhosphorylationVQTQRTRSSSEDTAG
HHHHHHCCCCCCCCC
37.2925002506
943PhosphorylationQTQRTRSSSEDTAGE
HHHHHCCCCCCCCCC
34.1625002506
944PhosphorylationTQRTRSSSEDTAGEL
HHHHCCCCCCCCCCC
40.5126670566
947PhosphorylationTRSSSEDTAGELPAV
HCCCCCCCCCCCCCH
32.2925002506
959AcetylationPAVRDLKKLEFALGP
CCHHHHHHCCHHCCC
61.62156323
1016PhosphorylationATFPQLKSLETLNLS
CCCHHHCCCCCCCCC
39.7829083192
1019PhosphorylationPQLKSLETLNLSQNN
HHHCCCCCCCCCCCC
26.6629083192
1023PhosphorylationSLETLNLSQNNITDL
CCCCCCCCCCCCCHH
29.7729116813
1028PhosphorylationNLSQNNITDLGAYKL
CCCCCCCCHHHHHHH
27.5629083192
1033PhosphorylationNITDLGAYKLAEALP
CCCHHHHHHHHHHHH
12.5329083192
1045PhosphorylationALPSLAASLLRLSLY
HHHHHHHHHHHHHHH
23.4824719451
1050PhosphorylationAASLLRLSLYNNCIC
HHHHHHHHHHCCCCC
23.5211416140
1073O-linked_GlycosylationRVLPDMVSLRVMDVQ
HHCCCCCEEEEEECC
12.1030379171
1073PhosphorylationRVLPDMVSLRVMDVQ
HHCCCCCEEEEEECC
12.10-

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
280SPhosphorylationKinaseMAPK1P28482
GPS
280SPhosphorylationKinaseMAPK3P27361
GPS
288SPhosphorylationKinaseMAPK1P28482
GPS
288SPhosphorylationKinaseMAPK3P27361
GPS
373SPhosphorylationKinaseGSK3BP49841
PSP
834SPhosphorylationKinasePRKACAP17612
GPS
834SPhosphorylationKinasePKA-FAMILY-GPS
834SPhosphorylationKinasePKA_GROUP-PhosphoELM
1050SPhosphorylationKinasePRKACAP17612
GPS
1050SPhosphorylationKinasePKA-FAMILY-GPS
1050SPhosphorylationKinasePKA_GROUP-PhosphoELM
1128SPhosphorylationKinasePRKACAP17252
GPS
-KUbiquitinationE3 ubiquitin ligaseMARCHF8Q5T0T0
PMID:19566897
-KUbiquitinationE3 ubiquitin ligaseMARCHF1Q8TCQ1
PMID:19880452
-KUbiquitinationE3 ubiquitin ligaseMARCHF5Q9NX47
PMID:18389477

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C2TA_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 C2TA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA1_HUMANNCOA1physical
12933903
RFX5_HUMANRFX5physical
11003667
RFXK_HUMANRFXANKphysical
11003667
MK03_HUMANMAPK3physical
18245089
MK01_HUMANMAPK1physical
18245089
HDAC2_HUMANHDAC2physical
19041327
SMCA4_HUMANSMARCA4physical
12077331
HDAC4_HUMANHDAC4physical
15964851
HDAC2_HUMANHDAC2physical
17991736
SIN3B_HUMANSIN3Bphysical
17991736
TF2B_HUMANGTF2Bphysical
9177216
TAF9_HUMANTAF9physical
9177216
PRS8_HUMANPSMC5physical
18215421
PPARG_HUMANPPARGphysical
17611194
EP300_HUMANEP300physical
26871568
EP400_HUMANEP400physical
26871568
TBP_HUMANTBPphysical
26871568
RFX5_HUMANRFX5physical
26871568
PRS8_HUMANPSMC5physical
26871568
PML_HUMANPMLphysical
28555140
CCNT1_HUMANCCNT1physical
28555140

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
209920Bare lymphocyte syndrome 2 (BLS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C2TA_HUMAN

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Related Literatures of Post-Translational Modification

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