AN13D_HUMAN - dbPTM
AN13D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AN13D_HUMAN
UniProt AC Q6ZTN6
Protein Name Ankyrin repeat domain-containing protein 13D
Gene Name ANKRD13D
Organism Homo sapiens (Human).
Sequence Length 518
Subcellular Localization Cell membrane . Late endosome . Interaction with EGFR may enhance association with the cell membrane.
Protein Description Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Does not bind 'Lys-48'-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane..
Protein Sequence MVQLVLQYRDYQRATQRLAGIPELLNKLRQAPDFYVEMKWEFTSWVPLVSKMCPSDVYRVWKRGESLRVDTSLLGFEHMTWQRGRRSFIFKGQEAGALVMEVDHDRQVVHVETLGLTLQEPETLLAAMRPSEEHVASRLTSPIVSTHLDTRNVAFERNKCGIWGWRSEKMETVSGYEAKVYSATNVELVTRTRTEHLSDQDKSRSKAGKTPFQSFLGMAQQHSSHTGAPVQQAASPTNPTAISPEEYFDPNFSLESRNIGRPIEMSSKVQRFKATLWLSEEHPLSLGDQVTPIIDLMAISNAHFAKLRDFITLRLPPGFPVKIEIPLFHVLNARITFSNLCGCDEPLSSVWVPAPSSAVAASGNPFPCEVDPTVFEVPNGYSVLGMERNEPLRDEDDDLLQFAIQQSLLEAGTEAEQVTVWEALTNTRPGARPPPQATVYEEQLQLERALQESLQLSTEPRGPGSPPRTPPAPGPPSFEEQLRLALELSSREQEERERRGQQEEEDLQRILQLSLTEH
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
8PhosphorylationMVQLVLQYRDYQRAT
CCEEEEHHHHHHHHH		10.9924043423
11PhosphorylationLVLQYRDYQRATQRL
EEEHHHHHHHHHHHH		7.3024043423
27UbiquitinationGIPELLNKLRQAPDF
CHHHHHHHHHCCCCE		45.04-
51UbiquitinationSWVPLVSKMCPSDVY
CHHHHHHHHCHHHHH		36.72-
87PhosphorylationTWQRGRRSFIFKGQE
EECCCCCEEEECCCE		22.7224719451
113PhosphorylationRQVVHVETLGLTLQE
CCEEEEEECEEECCC		25.6624043423
114UbiquitinationQVVHVETLGLTLQEP
CEEEEEECEEECCCH		3.15-
114 (in isoform 3)Ubiquitination-3.15-
117PhosphorylationHVETLGLTLQEPETL
EEEECEEECCCHHHH		25.2924043423
123PhosphorylationLTLQEPETLLAAMRP
EECCCHHHHHHHCCC		37.4724043423
138UbiquitinationSEEHVASRLTSPIVS
CHHHHHHHCCCCCEE		32.04-
138 (in isoform 3)Ubiquitination-32.04-
150PhosphorylationIVSTHLDTRNVAFER
CEECCCCCCCCCCCC		30.4246163843
159UbiquitinationNVAFERNKCGIWGWR
CCCCCCCCCCCCEEE		39.812189047
159 (in isoform 1)Ubiquitination-39.8121890473
169UbiquitinationIWGWRSEKMETVSGY
CCEEECCEEEEECCC		43.19-
169AcetylationIWGWRSEKMETVSGY
CCEEECCEEEEECCC		43.1919807423
172PhosphorylationWRSEKMETVSGYEAK
EECCEEEEECCCEEE		19.2450565353
174PhosphorylationSEKMETVSGYEAKVY
CCEEEEECCCEEEEE		42.9811758341
174 (in isoform 3)Phosphorylation-42.9824719451
176PhosphorylationKMETVSGYEAKVYSA
EEEEECCCEEEEEEE		12.7650565359
181PhosphorylationSGYEAKVYSATNVEL
CCCEEEEEEECCEEE		7.5925219547
182PhosphorylationGYEAKVYSATNVELV
CCEEEEEEECCEEEE		31.4425219547
184PhosphorylationEAKVYSATNVELVTR
EEEEEEECCEEEEEE		33.5825219547
190PhosphorylationATNVELVTRTRTEHL
ECCEEEEEEECHHHC		38.6625219547
209UbiquitinationKSRSKAGKTPFQSFL
HHHHCCCCCCHHHHH		58.86-
246UbiquitinationPTAISPEEYFDPNFS
CCCCCHHHHCCCCCC		55.6821890473
246 (in isoform 3)Ubiquitination-55.68-
246 (in isoform 2)Ubiquitination-55.6821890473
246UbiquitinationPTAISPEEYFDPNFS
CCCCCHHHHCCCCCC		55.68-
256 (in isoform 3)Ubiquitination-35.60-
256UbiquitinationDPNFSLESRNIGRPI
CCCCCCCCCCCCCCC		35.60-
268UbiquitinationRPIEMSSKVQRFKAT
CCCCCHHHHHHHEEE		34.77-
322UbiquitinationLPPGFPVKIEIPLFH
CCCCCCEEEEEEEEE		34.55-
355 (in isoform 3)Ubiquitination-23.81-
355UbiquitinationSSVWVPAPSSAVAAS
CCCEEECCCCCCCCC		23.81-
409 (in isoform 3)Ubiquitination-5.26-
409UbiquitinationFAIQQSLLEAGTEAE
HHHHHHHHHHCCCHH		5.26-
438PhosphorylationARPPPQATVYEEQLQ
CCCCCCCCHHHHHHH		20.5528796482
440PhosphorylationPPPQATVYEEQLQLE
CCCCCCHHHHHHHHH		14.9228796482
453PhosphorylationLERALQESLQLSTEP
HHHHHHHHHCCCCCC		14.4146163831
457PhosphorylationLQESLQLSTEPRGPG
HHHHHCCCCCCCCCC		20.1226074081
458PhosphorylationQESLQLSTEPRGPGS
HHHHCCCCCCCCCCC		59.6126074081
465PhosphorylationTEPRGPGSPPRTPPA
CCCCCCCCCCCCCCC		34.5629255136
469PhosphorylationGPGSPPRTPPAPGPP
CCCCCCCCCCCCCCC		39.1229255136
477PhosphorylationPPAPGPPSFEEQLRL
CCCCCCCCHHHHHHH		48.7220363803
489PhosphorylationLRLALELSSREQEER
HHHHHHHHHHHHHHH		20.2728555341
514PhosphorylationLQRILQLSLTEH---
HHHHHHHHHCCC---		21.93113323003
516PhosphorylationRILQLSLTEH-----
HHHHHHHCCC-----		28.7428348404
527 (in isoform 3)Phosphorylation-27642862
552 (in isoform 3)Phosphorylation-24719451
552Phosphorylation-----------------------------------------
-----------------------------------------		19651622
556 (in isoform 3)Phosphorylation-24719451
556Phosphorylation---------------------------------------------
---------------------------------------------		19651622
564 (in isoform 3)Phosphorylation-27251275
564Phosphorylation-----------------------------------------------------
-----------------------------------------------------		-
601 (in isoform 3)Phosphorylation-27251275
601Phosphorylation------------------------------------------------------------------------------------------
------------------------------------------------------------------------------------------		-
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AN13D_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 AN13D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
UBC_HUMANUBCphysical
22298428
TERA_HUMANVCPphysical
26797118
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 AN13D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND THR-469, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND THR-469, ANDMASS SPECTROMETRY.
"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-465 AND THR-469, ANDMASS SPECTROMETRY.

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