ANFY1_HUMAN - dbPTM
ANFY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANFY1_HUMAN
UniProt AC Q9P2R3
Protein Name Rabankyrin-5 {ECO:0000303|PubMed:15328530}
Gene Name ANKFY1
Organism Homo sapiens (Human).
Sequence Length 1169
Subcellular Localization Cytoplasm . Endosome membrane
Peripheral membrane protein . Early endosome . Also associated with endosomal membranes. Localizes to macropinosomes.
Protein Description Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI(3)P). Involved in homotypic early endosome fusion and to a lesser extent in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Involved in macropinocytosis; the function is dependent on Rab5-GTP. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the subcellular localization of the retromer complex in a EHD1-dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport..
Protein Sequence MAEEEVAKLEKHLMLLRQEYVKLQKKLAETEKRCALLAAQANKESSSESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGAQETPLHLVALYSSKKHSADVMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLELKDHEGSTALWLAVQHITVSSDQSVNPFEDVPVVNGTSFDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEALPLPKEAASLTSLADSVHLQTPLHMAIAYNHPDVVSVILEQKANALHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPRQPGANGEGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLHILGQYGKENAAAIFDLFLECMPGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGVNIFNYQVATKQLLFRLLDMLSKEPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVLTLGGVS
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------MAEEEVAKL
------CCHHHHHHH		44.18-
8AcetylationMAEEEVAKLEKHLML
CCHHHHHHHHHHHHH		63.4525953088
8UbiquitinationMAEEEVAKLEKHLML
CCHHHHHHHHHHHHH		63.45-
11UbiquitinationEEVAKLEKHLMLLRQ
HHHHHHHHHHHHHHH		53.10-
43UbiquitinationLLAAQANKESSSESF
HHHHHHCCCCCCHHH		63.09-
52PhosphorylationSSSESFISRLLAIVA
CCCHHHHHHHHHHHH		18.1824719451
85UbiquitinationHISAHKFVLAARSDS
EEHHHHEEEEEECCC		4.19-
90PhosphorylationKFVLAARSDSWSLAN
HEEEEEECCCCCCCC		31.1328857561
92PhosphorylationVLAARSDSWSLANLS
EEEEECCCCCCCCCC		21.5828857561
94PhosphorylationAARSDSWSLANLSST
EEECCCCCCCCCCCC		22.8928348404
100PhosphorylationWSLANLSSTKELDLS
CCCCCCCCCCCCCCC		46.8228961369
144UbiquitinationELMKLANRFQLQLLR
HHHHHHHHHHHHHHH		18.32-
173PhosphorylationNCIRFYQTAEELNAS
HHHHHHHCHHHCCHH		25.3422210691
181PhosphorylationAEELNASTLMNYCAE
HHHCCHHHHHHHHHH		27.8422210691
185PhosphorylationNASTLMNYCAEIIAS
CHHHHHHHHHHHHHH		4.5022210691
203PhosphorylationDLRKEDFSSMSAQLL
HHCHHCHHHHHHHHH		37.1429978859
204PhosphorylationLRKEDFSSMSAQLLY
HCHHCHHHHHHHHHH		19.4220068231
206PhosphorylationKEDFSSMSAQLLYKM
HHCHHHHHHHHHHHH		18.1420068231
211PhosphorylationSMSAQLLYKMIKSKT
HHHHHHHHHHHHCCC		13.7026604765
216PhosphorylationLLYKMIKSKTEYPLH
HHHHHHHCCCCCCHH		33.6129978859
245PhosphorylationLIEMDSQLPGKLNEA
EEECCCCCCCCCCCC		7.5620068231
246PhosphorylationIEMDSQLPGKLNEAD
EECCCCCCCCCCCCC		30.1820068231
253PhosphorylationPGKLNEADHNGDLAL
CCCCCCCCCCCCHHH		29.6118452278
259UbiquitinationADHNGDLALDLALSR
CCCCCCHHHHHHHHH		12.08-
265PhosphorylationLALDLALSRRLESIA
HHHHHHHHHHHHHHH		15.1124719451
266UbiquitinationALDLALSRRLESIAT
HHHHHHHHHHHHHHH		48.32-
270PhosphorylationALSRRLESIATTLVS
HHHHHHHHHHHHHHH		23.3210574462
277PhosphorylationSIATTLVSHKADVDM
HHHHHHHHCCCCHHH		23.5320068231
279UbiquitinationATTLVSHKADVDMVD
HHHHHHCCCCHHHCC		38.48-
312PhosphorylationATFLIKNGAFVNAAT
EEEEECCCCEEEHHH		18.52-
321UbiquitinationFVNAATLGAQETPLH
EEEHHHCCCCCCCHH		22.36-
329UbiquitinationAQETPLHLVALYSSK
CCCCCHHHHHHHCCC		2.96-
339PhosphorylationLYSSKKHSADVMSEM
HHCCCCCCHHHHHHH		34.7428258704
344PhosphorylationKHSADVMSEMAQIAE
CCCHHHHHHHHHHHH		24.8628258704
446MethylationFAARLIQRGSHTDAP
HHHHHHHCCCCCCCC		41.40-
448PhosphorylationARLIQRGSHTDAPDT
HHHHHCCCCCCCCCC		25.9621406692
450PhosphorylationLIQRGSHTDAPDTAT
HHHCCCCCCCCCCHH		35.2418669648
460GlutathionylationPDTATGNCLLQRAAG
CCCHHHCHHHHHHCC		4.2022555962
488MethylationGAHVNHRNKWGETPL
CCCCCCCCCCCCCCH		36.56-
489UbiquitinationAHVNHRNKWGETPLH
CCCCCCCCCCCCCHH		57.44-
531UbiquitinationALPLPKEAASLTSLA
CCCCCHHHHHHHHHH		14.42-
533PhosphorylationPLPKEAASLTSLADS
CCCHHHHHHHHHHHH		38.9527251275
535PhosphorylationPKEAASLTSLADSVH
CHHHHHHHHHHHHHC		21.1427251275
536PhosphorylationKEAASLTSLADSVHL
HHHHHHHHHHHHHCC		27.1827251275
540PhosphorylationSLTSLADSVHLQTPL
HHHHHHHHHCCCCHH		13.0627251275
545PhosphorylationADSVHLQTPLHMAIA
HHHHCCCCHHHHHHH		33.8927251275
577 (in isoform 4)Phosphorylation-33.4227251275
585UbiquitinationIIPDFSLKDSRDQTV
ECCCCCCCCCCCCHH		53.08-
591PhosphorylationLKDSRDQTVLGLALW
CCCCCCCHHHHHHHH		23.2224043423
599PhosphorylationVLGLALWTGMHTIAA
HHHHHHHHCHHHHHH		26.0224043423
603PhosphorylationALWTGMHTIAAQLLG
HHHHCHHHHHHHHHC		11.9224043423
611PhosphorylationIAAQLLGSGAAINDT
HHHHHHCCCCCCCCC		25.8124043423
618PhosphorylationSGAAINDTMSDGQTL
CCCCCCCCCCCHHHH		17.6824043423
620PhosphorylationAAINDTMSDGQTLLH
CCCCCCCCCHHHHHH		40.4524043423
624PhosphorylationDTMSDGQTLLHMAIQ
CCCCCHHHHHHHHHH		36.5024043423
627UbiquitinationSDGQTLLHMAIQRQD
CCHHHHHHHHHHCCC		13.52-
636UbiquitinationAIQRQDSKSALFLLE
HHHCCCCHHHHHHHH		48.3022053931
657PhosphorylationVRTQDGETALQLAIR
EECCCHHHHHHHHHH		37.8922468782
675GlutathionylationPLVVDAICTRGADMS
CHHEEEEECCCCCCC		1.9722555962
676PhosphorylationLVVDAICTRGADMSV
HHEEEEECCCCCCCC		26.4822468782
678UbiquitinationVDAICTRGADMSVPD
EEEEECCCCCCCCCC		14.05-
681SulfoxidationICTRGADMSVPDEKG
EECCCCCCCCCCCCC		4.2830846556
851UbiquitinationAMTFKNNKSAEAILK
EEEECCCCCHHHHHH		61.51-
858UbiquitinationKSAEAILKRESGAAE
CCHHHHHHCCCCCHH		48.2621890473
859 (in isoform 2)Ubiquitination-39.6121890473
861PhosphorylationEAILKRESGAAEQVD
HHHHHCCCCCHHHCC		37.4529255136
870UbiquitinationAAEQVDNKGRNFLHV
CHHHCCCCCCCEEEE		55.58-
893UbiquitinationSVLFLISVHANVNSR
HEEEEEEHHCCCCCC		3.81-
900 (in isoform 1)Ubiquitination-25.5521890473
900UbiquitinationVHANVNSRVQDASKL
HHCCCCCCCCCHHHC		25.55-
900 (in isoform 4)Ubiquitination-25.55-
903 (in isoform 4)Phosphorylation-50.3727251275
903PhosphorylationNVNSRVQDASKLTPL
CCCCCCCCHHHCCHH		50.37-
912UbiquitinationSKLTPLHLAVQAGSE
HHCCHHHHHHHCCCH		7.04-
931UbiquitinationNLLLAGAKVNELTKH
HHHHCCCCHHHHHHH		44.68-
937AcetylationAKVNELTKHRQTALH
CCHHHHHHHHHHHHH		49.7925953088
948UbiquitinationTALHLAAQQDLPTIC
HHHHHHHCCCHHHHH		31.54-
973UbiquitinationAAVDENGNNALHLAV
EEECCCCCCHHHHHH		42.03-
979UbiquitinationGNNALHLAVMHGRLN
CCCHHHHHHHCCCCC		5.95-
1052PhosphorylationSTVLLLAYMKGNANL
CEEEEEHHHHCCHHH		10.1818083107
1083PhosphorylationQGVNIFNYQVATKQL
CCCCEECHHHHHHHH		8.1346163573
1088UbiquitinationFNYQVATKQLLFRLL
ECHHHHHHHHHHHHH		29.25-
1130UbiquitinationKHHCRHCGRLLCHKC
CHHCCCCCCEEECCC		19.69-
1138PhosphorylationRLLCHKCSTKEIPII
CEEECCCCCCCCCEE		47.52113334309
1146UbiquitinationTKEIPIIKFDLNKPV
CCCCCEEEEECCCCC		33.28-
1151UbiquitinationIIKFDLNKPVRVCNI
EEEEECCCCCCHHCC		52.792189047
1152 (in isoform 2)Ubiquitination-20.3421890473
1180 (in isoform 4)Phosphorylation-27251275
1180Phosphorylation------------------
------------------		-
1188Ubiquitination--------------------------
--------------------------		-
1193 (in isoform 1)Ubiquitination-21890473
1193Ubiquitination-------------------------------
-------------------------------		-
1193 (in isoform 4)Ubiquitination--
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 ANFY1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANFY1_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 ANFY1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHD1_HUMANEHD1physical
22284051
MILK1_HUMANMICALL1physical
22284051
VPS35_HUMANVPS35physical
22284051
VP26A_HUMANVPS26Aphysical
22284051
WASC4_HUMANKIAA1033physical
22863883
RHOD_HUMANRHODphysical
24102721
RHOF_HUMANRHOFphysical
24102721
RAB5A_HUMANRAB5Aphysical
24102721
ERAL1_HUMANERAL1physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
CUL3_HUMANCUL3physical
29038302
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 ANFY1_HUMAN

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Related Literatures of Post-Translational Modification

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