AN13A_HUMAN - dbPTM
AN13A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AN13A_HUMAN
UniProt AC Q8IZ07
Protein Name Ankyrin repeat domain-containing protein 13A
Gene Name ANKRD13A
Organism Homo sapiens (Human).
Sequence Length 590
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 MSSACDAGDHYPLHLLVWKNDYRQLEKELQGQNVEAVDPRGRTLLHLAVSLGHLESARVLLRHKADVTKENRQGWTVLHEAVSTGDPEMVYTVLQHRDYHNTSMALEGVPELLQKILEAPDFYVQMKWEFTSWVPLVSRICPNDVCRIWKSGAKLRVDITLLGFENMSWIRGRRSFIFKGEDNWAELMEVNHDDKVVTTERFDLSQEMERLTLDLMKPKSREVERRLTSPVINTSLDTKNIAFERTKSGFWGWRTDKAEVVNGYEAKVYTVNNVNVITKIRTEHLTEEEKKRYKADRNPLESLLGTVEHQFGAQGDLTTECATANNPTAITPDEYFNEEFDLKDRDIGRPKELTIRTQKFKAMLWMCEEFPLSLVEQVIPIIDLMARTSAHFARLRDFIKLEFPPGFPVKIEIPLFHVLNARITFGNVNGCSTAEESVSQNVEGTQADSASHITNFEVDQSVFEIPESYYVQDNGRNVHLQDEDYEIMQFAIQQSLLESSRSQELSGPASNGGISQTNTYDAQYERAIQESLLTSTEGLCPSALSETSRFDNDLQLAMELSAKELEEWELRLQEEEAELQQVLQLSLTDK
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
2Phosphorylation------MSSACDAGD
------CCCCCCCCC
27.0028857561
3Phosphorylation-----MSSACDAGDH
-----CCCCCCCCCC
31.4528857561
19UbiquitinationPLHLLVWKNDYRQLE
CEEEEEEECHHHHHH
32.2521890473
27UbiquitinationNDYRQLEKELQGQNV
CHHHHHHHHHCCCCC
72.7721906983
91PhosphorylationTGDPEMVYTVLQHRD
CCCHHHHEEEEHHCC
6.9975317
99PhosphorylationTVLQHRDYHNTSMAL
EEEHHCCCCCHHHHH
9.2722199227
102PhosphorylationQHRDYHNTSMALEGV
HHCCCCCHHHHHCCH
13.4328857561
103PhosphorylationHRDYHNTSMALEGVP
HCCCCCHHHHHCCHH
13.8422199227
175PhosphorylationSWIRGRRSFIFKGED
CEECCCCEEEEECCC
22.7224719451
188SulfoxidationEDNWAELMEVNHDDK
CCCHHHHCCCCCCCC
3.9830846556
195UbiquitinationMEVNHDDKVVTTERF
CCCCCCCCEEEECCC
44.6621906983
205PhosphorylationTTERFDLSQEMERLT
EECCCCHHHHHHHHH
26.4121082442
208SulfoxidationRFDLSQEMERLTLDL
CCCHHHHHHHHHHHH
2.5521406390
217UbiquitinationRLTLDLMKPKSREVE
HHHHHHHCCCCHHHH
57.5021906983
217AcetylationRLTLDLMKPKSREVE
HHHHHHHCCCCHHHH
57.507825331
219UbiquitinationTLDLMKPKSREVERR
HHHHHCCCCHHHHHH
57.54-
219AcetylationTLDLMKPKSREVERR
HHHHHCCCCHHHHHH
57.547825341
228PhosphorylationREVERRLTSPVINTS
HHHHHHHCCCCCCCC
29.2228857561
229PhosphorylationEVERRLTSPVINTSL
HHHHHHCCCCCCCCC
23.0528857561
239UbiquitinationINTSLDTKNIAFERT
CCCCCCCCCCEEEEC
46.1321906983
247UbiquitinationNIAFERTKSGFWGWR
CCEEEECCCCCCCEE
55.6021906983
248PhosphorylationIAFERTKSGFWGWRT
CEEEECCCCCCCEEC
38.3128857561
257UbiquitinationFWGWRTDKAEVVNGY
CCCEECCCEEEECCE
45.9221906983
269PhosphorylationNGYEAKVYTVNNVNV
CCEEEEEEEECCEEE
12.3128064214
270PhosphorylationGYEAKVYTVNNVNVI
CEEEEEEEECCEEEE
21.5330301811
279UbiquitinationNNVNVITKIRTEHLT
CCEEEEEEEEHHHCC
21.0421906983
281MethylationVNVITKIRTEHLTEE
EEEEEEEEHHHCCHH
35.30-
290UbiquitinationEHLTEEEKKRYKADR
HHCCHHHHHHHHCCC
45.92-
291UbiquitinationHLTEEEKKRYKADRN
HCCHHHHHHHHCCCC
65.33-
351UbiquitinationDRDIGRPKELTIRTQ
CCCCCCCCCCEEHHH
65.09-
400UbiquitinationARLRDFIKLEFPPGF
HHHHHHHCCCCCCCC
41.7921906983
410UbiquitinationFPPGFPVKIEIPLFH
CCCCCCEEEEEEEEE
34.5521906983
470PhosphorylationFEIPESYYVQDNGRN
EECCCCEEEEECCEE
10.8322817900
485PhosphorylationVHLQDEDYEIMQFAI
EEECCCCHHHHHHHH
12.81119633
506PhosphorylationSSRSQELSGPASNGG
HCCCCCCCCCCCCCC
41.8128857561
510PhosphorylationQELSGPASNGGISQT
CCCCCCCCCCCCCCC
38.86113326403
515PhosphorylationPASNGGISQTNTYDA
CCCCCCCCCCCCHHH
33.9428555341
519PhosphorylationGGISQTNTYDAQYER
CCCCCCCCHHHHHHH
26.6021552520
520PhosphorylationGISQTNTYDAQYERA
CCCCCCCHHHHHHHH
16.0222817900
524PhosphorylationTNTYDAQYERAIQES
CCCHHHHHHHHHHHH
14.7622817900
534PhosphorylationAIQESLLTSTEGLCP
HHHHHHHHCCCCCCH
38.6128857561
535PhosphorylationIQESLLTSTEGLCPS
HHHHHHHCCCCCCHH
25.1628857561
536PhosphorylationQESLLTSTEGLCPSA
HHHHHHCCCCCCHHH
28.9228857561
563UbiquitinationLAMELSAKELEEWEL
HHHHHCHHHHHHHHH
60.5021906983
586PhosphorylationLQQVLQLSLTDK---
HHHHHHHHHCCC---
19.0922298428

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 AN13A_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 AN13A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
22298428
TERA_HUMANVCPphysical
26797118
CAV1_HUMANCAV1physical
26797118
GDIR1_HUMANARHGDIAphysical
27173435
STOM_HUMANSTOMphysical
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 AN13A_HUMAN

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Related Literatures of Post-Translational Modification

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