TP4AP_HUMAN - dbPTM
TP4AP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TP4AP_HUMAN
UniProt AC Q8TEL6
Protein Name Short transient receptor potential channel 4-associated protein
Gene Name TRPC4AP
Organism Homo sapiens (Human).
Sequence Length 797
Subcellular Localization
Protein Description Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC. Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca(2+) storage reduction in response to CHRM1..
Protein Sequence MAAAPVAAGSGAGRGRRSAATVAAWGGWGGRPRPGNILLQLRQGQLTGRGLVRAVQFTETFLTERDKQSKWSGIPQLLLKLHTTSHLHSDFVECQNILKEISPLLSMEAMAFVTEERKLTQETTYPNTYIFDLFGGVDLLVEILMRPTISIRGQKLKISDEMSKDCLSILYNTCVCTEGVTKRLAEKNDFVIFLFTLMTSKKTFLQTATLIEDILGVKKEMIRLDEVPNLSSLVSNFDQQQLANFCRILAVTISEMDTGNDDKHTLLAKNAQQKKSLSLGPSAAEINQAALLSIPGFVERLCKLATRKVSESTGTASFLQELEEWYTWLDNALVLDALMRVANEESEHNQASIVFPPPGASEENGLPHTSARTQLPQSMKIMHEIMYKLEVLYVLCVLLMGRQRNQVHRMIAEFKLIPGLNNLFDKLIWRKHSASALVLHGHNQNCDCSPDITLKIQFLRLLQSFSDHHENKYLLLNNQELNELSAISLKANIPEVEAVLNTDRSLVCDGKRGLLTRLLQVMKKEPAESSFRFWQARAVESFLRGTTSYADQMFLLKRGLLEHILYCIVDSECKSRDVLQSYFDLLGELMKFNVDAFKRFNKYINTDAKFQVFLKQINSSLVDSNMLVRCVTLSLDRFENQVDMKVAEVLSECRLLAYISQVPTQMSFLFRLINIIHVQTLTQENVSCLNTSLVILMLARRKERLPLYLRLLQRMEHSKKYPGFLLNNFHNLLRFWQQHYLHKDKDSTCLENSSCISFSYWKETVSILLNPDRQSPSALVSYIEEPYMDIDRDFTEE
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
2Acetylation------MAAAPVAAG
------CCCCCCCCC
16.6022814378
10PhosphorylationAAPVAAGSGAGRGRR
CCCCCCCCCCCCCCC
22.2723532336
14MethylationAAGSGAGRGRRSAAT
CCCCCCCCCCCCCHH
34.61115368459
16MethylationGSGAGRGRRSAATVA
CCCCCCCCCCCHHHH
28.20115387821
18PhosphorylationGAGRGRRSAATVAAW
CCCCCCCCCHHHHHC
22.3928348404
67AcetylationTFLTERDKQSKWSGI
HHCCHHHHHCCCCCC
63.797925387
70UbiquitinationTERDKQSKWSGIPQL
CHHHHHCCCCCCCHH
42.7721890473
70 (in isoform 2)Ubiquitination-42.7721890473
70 (in isoform 1)Ubiquitination-42.7721890473
150PhosphorylationILMRPTISIRGQKLK
HHHCCCEEECCEECC
14.5424719451
157 (in isoform 2)Ubiquitination-47.3921890473
157UbiquitinationSIRGQKLKISDEMSK
EECCEECCCCHHHCH
47.3921906983
157AcetylationSIRGQKLKISDEMSK
EECCEECCCCHHHCH
47.397380731
157 (in isoform 1)Ubiquitination-47.3921890473
157UbiquitinationSIRGQKLKISDEMSK
EECCEECCCCHHHCH
47.3921906983
164AcetylationKISDEMSKDCLSILY
CCCHHHCHHHHHHHH
51.677380741
182UbiquitinationVCTEGVTKRLAEKND
HCCCCHHHHHHHHCC
42.90-
203PhosphorylationTLMTSKKTFLQTATL
EHHHCCCHHHHHHHH
33.06-
218 (in isoform 2)Ubiquitination-41.0121890473
218UbiquitinationIEDILGVKKEMIRLD
HHHHHCCCHHHHCHH
41.0121890473
218 (in isoform 1)Ubiquitination-41.0121890473
218UbiquitinationIEDILGVKKEMIRLD
HHHHHCCCHHHHCHH
41.0121906983
219UbiquitinationEDILGVKKEMIRLDE
HHHHCCCHHHHCHHC
50.54-
263UbiquitinationMDTGNDDKHTLLAKN
CCCCCCCHHHHHHHC
41.16-
265PhosphorylationTGNDDKHTLLAKNAQ
CCCCCHHHHHHHCHH
29.25-
269UbiquitinationDKHTLLAKNAQQKKS
CHHHHHHHCHHHHHC
53.4321906983
269 (in isoform 2)Ubiquitination-53.4321890473
269UbiquitinationDKHTLLAKNAQQKKS
CHHHHHHHCHHHHHC
53.4321906983
269 (in isoform 1)Ubiquitination-53.4321890473
275 (in isoform 2)Ubiquitination-52.9021890473
275UbiquitinationAKNAQQKKSLSLGPS
HHCHHHHHCCCCCCC
52.9021890473
275UbiquitinationAKNAQQKKSLSLGPS
HHCHHHHHCCCCCCC
52.9021906983
275 (in isoform 1)Ubiquitination-52.9021890473
303 (in isoform 2)Ubiquitination-45.8321890473
303UbiquitinationGFVERLCKLATRKVS
HHHHHHHHHHCCCCH
45.8321906983
303UbiquitinationGFVERLCKLATRKVS
HHHHHHHHHHCCCCH
45.8321906983
303 (in isoform 1)Ubiquitination-45.8321890473
407UbiquitinationMGRQRNQVHRMIAEF
HHCCHHHHHHHHHHH
3.3621906983
415UbiquitinationHRMIAEFKLIPGLNN
HHHHHHHCCCCCHHH
36.6921906983
415 (in isoform 1)Ubiquitination-36.6921890473
415 (in isoform 2)Ubiquitination-36.6921890473
472 (in isoform 2)Ubiquitination-34.0021890473
472UbiquitinationFSDHHENKYLLLNNQ
CCCCCCCCEEEECHH
34.0021890473
472 (in isoform 1)Ubiquitination-34.0021890473
490UbiquitinationELSAISLKANIPEVE
HHHHHHHHCCCCHHH
32.37-
511UbiquitinationRSLVCDGKRGLLTRL
CCHHCCCHHHHHHHH
30.00-
523 (in isoform 2)Ubiquitination-55.9421890473
523UbiquitinationTRLLQVMKKEPAESS
HHHHHHHHHCCCCCC
55.9421890473
523 (in isoform 1)Ubiquitination-55.9421890473
524UbiquitinationRLLQVMKKEPAESSF
HHHHHHHHCCCCCCH
51.32-
549UbiquitinationFLRGTTSYADQMFLL
HHHCCCCHHHHHHHH
16.4721906983
557UbiquitinationADQMFLLKRGLLEHI
HHHHHHHHHCHHHHH
46.7121890473
557 (in isoform 1)Ubiquitination-46.7121890473
582PhosphorylationSRDVLQSYFDLLGEL
CHHHHHHHHHHHHHH
6.5326657352
590UbiquitinationFDLLGELMKFNVDAF
HHHHHHHHHCCHHHH
3.9721906983
594UbiquitinationGELMKFNVDAFKRFN
HHHHHCCHHHHHHHH
6.7221906983
598 (in isoform 1)Ubiquitination-58.7721890473
598UbiquitinationKFNVDAFKRFNKYIN
HCCHHHHHHHHHHCC
58.7721890473
602 (in isoform 1)Ubiquitination-44.8121890473
602UbiquitinationDAFKRFNKYINTDAK
HHHHHHHHHCCCCHH
44.8121906983
719UbiquitinationLQRMEHSKKYPGFLL
HHHHHHHCCCCCCHH
59.23-
720 (in isoform 1)Ubiquitination-60.7421890473
720UbiquitinationQRMEHSKKYPGFLLN
HHHHHHCCCCCCHHH
60.7421890473
764PhosphorylationSFSYWKETVSILLNP
EEEEHHHHEEEHHCC
18.8030576142
775PhosphorylationLLNPDRQSPSALVSY
HHCCCCCCCHHHHHH
23.0122210691
777PhosphorylationNPDRQSPSALVSYIE
CCCCCCCHHHHHHHH
39.2122210691
781PhosphorylationQSPSALVSYIEEPYM
CCCHHHHHHHHCCCC
22.6530576142
795PhosphorylationMDIDRDFTEE-----
CCCCCCCCCC-----
43.4222210691

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 TP4AP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TP4AP_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 TP4AP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRADD_HUMANTRADDphysical
14585990
IKKB_HUMANIKBKBphysical
14585990
NEMO_HUMANIKBKGphysical
14585990
IKKA_HUMANCHUKphysical
14585990
TRAF2_HUMANTRAF2physical
14585990
RIPK1_HUMANRIPK1physical
14585990
DDB1_HUMANDDB1physical
20551172
CUL4A_HUMANCUL4Aphysical
20551172
DDA1_HUMANDDA1physical
20551172
RBX1_HUMANRBX1physical
20551172
TRPC1_HUMANTRPC1physical
20458742
TRPC4_HUMANTRPC4physical
20458742
TRPC5_HUMANTRPC5physical
20458742
TNR1A_HUMANTNFRSF1Aphysical
20458742
SKP2_HUMANSKP2physical
26038816
MYC_HUMANMYCphysical
26038816
DDB1_HUMANDDB1physical
26038816
SMHD1_HUMANSMCHD1physical
28514442
CCDC6_HUMANCCDC6physical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
NCOA1_HUMANNCOA1physical
28514442
DDB1_HUMANDDB1physical
28514442
HERC1_HUMANHERC1physical
28514442
RBBP6_HUMANRBBP6physical
28514442
SCAFB_HUMANSCAF11physical
28514442
E41L5_HUMANEPB41L5physical
28514442
MCES_HUMANRNMTphysical
28514442
KLC1_HUMANKLC1physical
28514442
SULF2_HUMANSULF2physical
28514442
KDM4D_HUMANKDM4Dphysical
28514442
DDA1_HUMANDDA1physical
28514442
MPZL1_HUMANMPZL1physical
28514442
IQGA1_HUMANIQGAP1physical
28514442
INT14_HUMANVWA9physical
28514442
PRC2C_HUMANPRRC2Cphysical
28514442
SETD2_HUMANSETD2physical
28514442
PRC2A_HUMANPRRC2Aphysical
28514442
CAPON_HUMANNOS1APphysical
28514442
S23IP_HUMANSEC23IPphysical
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 TP4AP_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP