TGFA1_HUMAN - dbPTM
TGFA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGFA1_HUMAN
UniProt AC Q8WUH2
Protein Name Transforming growth factor-beta receptor-associated protein 1
Gene Name TGFBRAP1
Organism Homo sapiens (Human).
Sequence Length 860
Subcellular Localization Cytoplasm . Early endosome . Colocalizes with TGF-beta receptors in the absence of signaling.
Protein Description Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2.; Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. [PubMed: 25266290 Functions predominantly in APPL1-containing endosomes and in degradative but not recycling trafficking of endocytosed cargo]
Protein Sequence MMSIKAFTLVSAVERELLMGDKERVNIECVECCGRDLYVGTNDCFVYHFLLEERPVPAGPATFTATKQLQRHLGFKKPVNELRAASALNRLLVLCDNSISLVNMLNLEPVPSGARIKGAATFALNENPVSGDPFCVEVCIISVKRRTIQMFLVYEDRVQIVKEVSTAEQPLAVAVDGHFLCLALTTQYIIHNYSTGVSQDLFPYCSEERPPIVKRIGRQEFLLAGPGGLGMFATVAGISQRAPVHWSENVIGAAVSFPYVIALDDEFITVHSMLDQQQKQTLPFKEGHILQDFEGRVIVATSKGVYILVPLPLEKQIQDLLASRRVEEALVLAKGARRNIPKEKFQVMYRRILQQAGFIQFAQLQFLEAKELFRSGQLDVRELISLYPFLLPTSSSFTRSHPPLHEYADLNQLTQGDQEKMAKCKRFLMSYLNEVRSTEVANGYKEDIDTALLKLYAEADHDSLLDLLVTENFCLLTDSAAWLEKHKKYFALGLLYHYNNQDAAAVQLWVNIVNGDVQDSTRSDLYEYIVDFLTYCLDEELVWAYADWVLQKSEEVGVQVFTKRPLDEQQKNSFNPDDIINCLKKYPKALVKYLEHLVIDKRLQKEEYHTHLAVLYLEEVLLQRASASGKGAEATETQAKLRRLLQKSDLYRVHFLLERLQGAGLPMESAILHGKLGEHEKALHILVHELQDFAAAEDYCLWCSEGRDPPHRQQLFHTLLAIYLHAGPTAHELAVAAVDLLNRHATEFDAAQVLQMLPDTWSVQLLCPFLMGAMRDSIHARRTMQVALGLARSENLIYTYDKMKLKGSSIQLSDKKLCQICQNPFCEPVFVRYPNGGLVHTHCAASRHTNPSSSSPGTRT
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
3Phosphorylation-----MMSIKAFTLV
-----CCCHHHHHHH		21.4624043423
8PhosphorylationMMSIKAFTLVSAVER
CCCHHHHHHHHHHHH		30.9824043423
11PhosphorylationIKAFTLVSAVERELL
HHHHHHHHHHHHHHH		29.7024043423
76UbiquitinationLQRHLGFKKPVNELR
HHHHCCCCCCHHHHH		55.13-
77UbiquitinationQRHLGFKKPVNELRA
HHHCCCCCCHHHHHH		52.5229967540
112PhosphorylationLNLEPVPSGARIKGA
CCCCCCCCCCEEECE		45.37-
210UbiquitinationPYCSEERPPIVKRIG
HHCCCCCCCCHHHHC		26.6722817900
220UbiquitinationVKRIGRQEFLLAGPG
HHHHCCCEEEECCCC		36.5824816145
234PhosphorylationGGLGMFATVAGISQR
CCCHHHHHHHCCCCC		10.3024043423
239PhosphorylationFATVAGISQRAPVHW
HHHHHCCCCCCCCCC		16.8224043423
281PhosphorylationLDQQQKQTLPFKEGH
CHHHHHCCCCCCCCC		43.3528060719
285UbiquitinationQKQTLPFKEGHILQD
HHCCCCCCCCCEEEC		61.93-
334UbiquitinationEEALVLAKGARRNIP
HHHHHHHHHHHCCCC		49.2827667366
344UbiquitinationRRNIPKEKFQVMYRR
HCCCCHHHHHHHHHH		47.42-
370UbiquitinationQLQFLEAKELFRSGQ
HHHHHHHHHHHHCCC		45.6430230243
385PhosphorylationLDVRELISLYPFLLP
CCHHHHHHHHCHHCC		34.18-
393PhosphorylationLYPFLLPTSSSFTRS
HHCHHCCCCCCCCCC		41.0128348404
394PhosphorylationYPFLLPTSSSFTRSH
HCHHCCCCCCCCCCC		23.2628348404
395PhosphorylationPFLLPTSSSFTRSHP
CHHCCCCCCCCCCCC		31.7627251275
396PhosphorylationFLLPTSSSFTRSHPP
HHCCCCCCCCCCCCC		30.3328348404
398PhosphorylationLPTSSSFTRSHPPLH
CCCCCCCCCCCCCHH		32.9628348404
407PhosphorylationSHPPLHEYADLNQLT
CCCCHHHHCCHHHCC		8.4827642862
437PhosphorylationSYLNEVRSTEVANGY
HHHHHHHCHHHHCCC		33.81-
438PhosphorylationYLNEVRSTEVANGYK
HHHHHHCHHHHCCCH		24.74-
444PhosphorylationSTEVANGYKEDIDTA
CHHHHCCCHHCHHHH		15.83-
445UbiquitinationTEVANGYKEDIDTAL
HHHHCCCHHCHHHHH		50.7629967540
563UbiquitinationVGVQVFTKRPLDEQQ
HCCEEEECCCCCHHH		40.3229967540
571UbiquitinationRPLDEQQKNSFNPDD
CCCCHHHHHCCCHHH		55.0129967540
584UbiquitinationDDIINCLKKYPKALV
HHHHHHHHHCHHHHH		53.0829967540
593PhosphorylationYPKALVKYLEHLVID
CHHHHHHHHHHHHHC		15.16-
601UbiquitinationLEHLVIDKRLQKEEY
HHHHHHCHHHCCHHH		43.83-
630AcetylationQRASASGKGAEATET
HHHHHCCCCHHHHHH		53.0726051181
630UbiquitinationQRASASGKGAEATET
HHHHHCCCCHHHHHH		53.0722817900
640UbiquitinationEATETQAKLRRLLQK
HHHHHHHHHHHHHHH		32.4824816145
647UbiquitinationKLRRLLQKSDLYRVH
HHHHHHHHCCHHHHH		46.00-
783PhosphorylationDSIHARRTMQVALGL
HHHHHHHHHHHHHHH		13.3524719451
793PhosphorylationVALGLARSENLIYTY
HHHHHHCCCCEEEEE		25.8124719451
798PhosphorylationARSENLIYTYDKMKL
HCCCCEEEEEECCCC		11.4727762562
799PhosphorylationRSENLIYTYDKMKLK
CCCCEEEEEECCCCC		20.4624719451
800PhosphorylationSENLIYTYDKMKLKG
CCCEEEEEECCCCCC		9.1527762562
802UbiquitinationNLIYTYDKMKLKGSS
CEEEEEECCCCCCCC		27.76-
806UbiquitinationTYDKMKLKGSSIQLS
EEECCCCCCCCCCCC		51.7529967540
808PhosphorylationDKMKLKGSSIQLSDK
ECCCCCCCCCCCCCH		23.7625690035
815UbiquitinationSSIQLSDKKLCQICQ
CCCCCCCHHHHHHCC		44.2429967540
816UbiquitinationSIQLSDKKLCQICQN
CCCCCCHHHHHHCCC		60.53-
846PhosphorylationVHTHCAASRHTNPSS
EEEEECCCCCCCCCC		13.18-
849PhosphorylationHCAASRHTNPSSSSP
EECCCCCCCCCCCCC		47.9528450419
852PhosphorylationASRHTNPSSSSPGTR
CCCCCCCCCCCCCCC		44.9421955146
853PhosphorylationSRHTNPSSSSPGTRT
CCCCCCCCCCCCCCC		35.7721955146
854PhosphorylationRHTNPSSSSPGTRT-
CCCCCCCCCCCCCC-		44.9125159151
855PhosphorylationHTNPSSSSPGTRT--
CCCCCCCCCCCCC--		29.3325159151
858PhosphorylationPSSSSPGTRT-----
CCCCCCCCCC-----		34.2228450419
860PhosphorylationSSSPGTRT-------
CCCCCCCC-------		42.6828450419
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 TGFA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGFA1_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 TGFA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD4_HUMANSMAD4physical
11278302
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 TGFA1_HUMAN

loading...

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-855, AND MASSSPECTROMETRY.

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