ASAP3_HUMAN - dbPTM
ASAP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASAP3_HUMAN
UniProt AC Q8TDY4
Protein Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3
Gene Name ASAP3
Organism Homo sapiens (Human).
Sequence Length 903
Subcellular Localization Cytoplasm .
Protein Description Promotes cell proliferation..
Protein Sequence MPEQFSVAEFLAVTAEDLSSPAGAAAFAAKMPRYRGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGIPGEVAQDMQRERRIFQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKLAASVHALHQAQEDELQKLTQLRDSLRGTLQLESREEHLSRKNSGCGYSIHQHQGNKQFGTEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTYHFQAEDEHECEAWVSVLQNSKDEALSSAFLGEPSAGPGSWGSAGHDGEPHDLTKLLIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLPSHGGPKPSAESDMGTRRDYIMAKYVEHRFARRCTPEPQRLWTAICNRDLLSVLEAFANGQDFGQPLPGPDAQAPEELVLHLAVKVANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELLEQAQAGTFAFPLHVDYSWVISTEPGSDSEEDEEEKRCLLKLPAQAHWASGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDRSEVSSLSSEAPETPESLGSPASSSSLMSPLEPGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSYRRGARSPEDGPSARQPLPRRNVPVGITEGDGSRTGSLPASSVQLLQD
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
34PhosphorylationFAAKMPRYRGAALAR
HHHHCCCCHHCHHHH		13.92-
76PhosphorylationHVENEEQYREAVESL
CCCCHHHHHHHHHHH		17.44-
143 (in isoform 3)Phosphorylation-33.1528348404
145UbiquitinationDGRQDSKKQLEKAWK
CCCCCHHHHHHHHHH		65.16-
152AcetylationKQLEKAWKDYEAKMA
HHHHHHHHHHHHHHH		56.1219815663
152UbiquitinationKQLEKAWKDYEAKMA
HHHHHHHHHHHHHHH		56.12-
157AcetylationAWKDYEAKMAKLEKE
HHHHHHHHHHHHHHH		27.7019815671
214PhosphorylationQGPDFLQSLIKFFHA
HCHHHHHHHHHHHHH		33.9224719451
260UbiquitinationAQEDELQKLTQLRDS
HCHHHHHHHHHHHHH		67.15-
286PhosphorylationEHLSRKNSGCGYSIH
HHHHHCCCCCCCCCE		38.2025159151
290PhosphorylationRKNSGCGYSIHQHQG
HCCCCCCCCCEECCC		14.4528152594
291PhosphorylationKNSGCGYSIHQHQGN
CCCCCCCCCEECCCC		10.0128152594
530PhosphorylationDMGTRRDYIMAKYVE
CCCCCHHHHHHHHHH		7.2625884760
534UbiquitinationRRDYIMAKYVEHRFA
CHHHHHHHHHHHHHH		32.23-
535PhosphorylationRDYIMAKYVEHRFAR
HHHHHHHHHHHHHHH		11.0925884760
545PhosphorylationHRFARRCTPEPQRLW
HHHHHHCCCCHHHHH		28.95-
639UbiquitinationYNQPDCLKLLLKGRA
HCCCCHHHHHHHCCC		43.34-
643UbiquitinationDCLKLLLKGRALVGT
CHHHHHHHCCCEEEE		46.44-
700PhosphorylationVISTEPGSDSEEDEE
EEECCCCCCCCCCHH		48.9927251275
723PhosphorylationPAQAHWASGRLDISN
HHHHHHHCCCCCCCC		21.1822210691
729PhosphorylationASGRLDISNKTYETV
HCCCCCCCCCCHHHH		31.7622210691
732PhosphorylationRLDISNKTYETVASL
CCCCCCCCHHHHHHC		30.7328796482
733PhosphorylationLDISNKTYETVASLG
CCCCCCCHHHHHHCC		15.9425884760
735PhosphorylationISNKTYETVASLGAA
CCCCCHHHHHHCCCC		15.8028796482
738PhosphorylationKTYETVASLGAATPQ
CCHHHHHHCCCCCCC		24.0128152594
743PhosphorylationVASLGAATPQGESED
HHHCCCCCCCCCCCC		18.6627251275
828PhosphorylationGLREPPGTSRPSLTS
CCCCCCCCCCCCCCC		27.6023312004
829PhosphorylationLREPPGTSRPSLTSG
CCCCCCCCCCCCCCC		48.3823312004
832PhosphorylationPPGTSRPSLTSGTTP
CCCCCCCCCCCCCCC		43.0723312004
834PhosphorylationGTSRPSLTSGTTPSE
CCCCCCCCCCCCCHH		29.4623312004
835PhosphorylationTSRPSLTSGTTPSEM
CCCCCCCCCCCCHHH		39.1623312004
837PhosphorylationRPSLTSGTTPSEMYL
CCCCCCCCCCHHHEE		34.9923312004
838PhosphorylationPSLTSGTTPSEMYLP
CCCCCCCCCHHHEEC		28.4823312004
840PhosphorylationLTSGTTPSEMYLPVR
CCCCCCCHHHEECEE		32.6723312004
843PhosphorylationGTTPSEMYLPVRFSS
CCCCHHHEECEEECC		12.1025884760
852PhosphorylationPVRFSSESTRSYRRG
CEEECCCCCCCCCCC		30.9424719451
862PhosphorylationSYRRGARSPEDGPSA
CCCCCCCCCCCCCCC		31.9125849741
868PhosphorylationRSPEDGPSARQPLPR
CCCCCCCCCCCCCCC		41.4327794612
890PhosphorylationTEGDGSRTGSLPASS
ECCCCCCCCCCCHHH		32.5928348404
892PhosphorylationGDGSRTGSLPASSVQ
CCCCCCCCCCHHHHH		30.4828348404
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
34YPhosphorylationKinaseEGFRP00533
PSP
545TPhosphorylationKinaseMST4Q9P289
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASAP3_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 ASAP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF4_HUMANPDZD3physical
25416956
RFIP3_HUMANRAB11FIP3physical
18685082
ASAP1_HUMANASAP1physical
28514442
ASAP2_HUMANASAP2physical
28514442
ACD11_HUMANACAD11physical
28514442
ELP2_HUMANELP2physical
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 ASAP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-733, AND MASSSPECTROMETRY.

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