AFTIN_HUMAN - dbPTM
AFTIN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AFTIN_HUMAN
UniProt AC Q6ULP2
Protein Name Aftiphilin
Gene Name AFTPH
Organism Homo sapiens (Human).
Sequence Length 936
Subcellular Localization Cytoplasm . Colocalizes with AP1G1 and clathrin.
Protein Description May play a role in membrane trafficking..
Protein Sequence MEPDIIRMYSSSPPPLDNGAEDDDDDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEEFVPSNHFMPIHEFSENVDSLTSFKSIKNGNDKDITAELSAPVKGQSDVLLSTTSKEIISSEMLATSIDGMERPGNLNKVVEQRQNVGTLESFSPGDFRTNMNVVHQNKQLESCNGEKPPCLEILTNGFAVLETVNPQGTDDLDNVADSKGRKPLSTHSTEYNLDSVPSPAEEFADFATFSKKERIQLEEIECAVLNDREALTIRENNKINRVNELNSVKEVALGRSLDNKGDTDGEDQVCVSEISIVTNRGFSVEKQGLPTLQQDEFLQSGVQSKAWSLVDSADNSEAIRREQCKTEEKLDLLTSKCAHLCMDSVKTSDDEVGSPKEESRKFTNFQSPNIDPTEENDLDDSLSVKNGDSSNDFVTCNDINEDDFGDFGDFGSASGSTPPFVTGTQDSMSDATFEESSEHFPHFSEPGDDFGEFGDINAVSCQEETILTKSDLKQTSDNLSEECQLARKSSGTGTEPVAKLKNGQEGEIGHFDSVPNIQDDCNGFQDSDDFADFSSAGPSQVVDWNAFEDEQKDSCSWAAFGDQQATESHHRKEAWQSHRTDENIDTPGTPKTHSVPSATSKGAVASGHLQESATSVQTALLNRLERIFEACFPSILVPDAEEEVTSLKHLLETSTLPIKTREALPESGELLDVWTELQDIHDAHGLRYQWGGSHSNKKLLSSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTATMSPDMNTCTSDQFQESLPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTTIPGVDPELYELTTSKLEISTSSLKVTDAFARLMSTVEKTSTSTRKPKREEHLSEEAIKVIAGLPDLTFMHAKVLMFPATLTPSTSSQEKADG
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
11PhosphorylationDIIRMYSSSPPPLDN
CCEEECCCCCCCCCC
29.4028348404
12PhosphorylationIIRMYSSSPPPLDNG
CEEECCCCCCCCCCC
35.1726074081
38PhosphorylationFGGFSEVSPSGVGFV
CCCCCCCCCCCCCEE
14.8622468782
52PhosphorylationVDFDTPDYTRPKEEF
EECCCCCCCCCHHHC
13.07138789
77PhosphorylationEFSENVDSLTSFKSI
HCCCCCCHHHHCCCC
29.30113322191
82AcetylationVDSLTSFKSIKNGND
CCHHHHCCCCCCCCC
51.5525953088
93PhosphorylationNGNDKDITAELSAPV
CCCCCCCEEEECCCC
24.9828555341
109PhosphorylationGQSDVLLSTTSKEII
CCCCEEEECCCHHHH
26.0228348404
110PhosphorylationQSDVLLSTTSKEIIS
CCCEEEECCCHHHHC
34.7521586687
111PhosphorylationSDVLLSTTSKEIISS
CCEEEECCCHHHHCH
34.1321586697
112PhosphorylationDVLLSTTSKEIISSE
CEEEECCCHHHHCHH
28.5128348404
117PhosphorylationTTSKEIISSEMLATS
CCCHHHHCHHHHHHH
26.3829900121
118PhosphorylationTSKEIISSEMLATSI
CCHHHHCHHHHHHHC
19.3329900121
123PhosphorylationISSEMLATSIDGMER
HCHHHHHHHCCCCCC
23.4324719451
124PhosphorylationSSEMLATSIDGMERP
CHHHHHHHCCCCCCC
17.0528348404
130MethylationTSIDGMERPGNLNKV
HHCCCCCCCCCHHHH
35.22-
146PhosphorylationEQRQNVGTLESFSPG
HHHCCCCCCCCCCCC
24.0625850435
149PhosphorylationQNVGTLESFSPGDFR
CCCCCCCCCCCCCCH
33.8525850435
151PhosphorylationVGTLESFSPGDFRTN
CCCCCCCCCCCCHHC
36.9325159151
213PhosphorylationSKGRKPLSTHSTEYN
CCCCCCCCCCCCEEC
32.3827080861
214PhosphorylationKGRKPLSTHSTEYNL
CCCCCCCCCCCEECC
27.7727080861
216PhosphorylationRKPLSTHSTEYNLDS
CCCCCCCCCEECCCC
24.0327080861
217PhosphorylationKPLSTHSTEYNLDSV
CCCCCCCCEECCCCC
34.5827080861
219PhosphorylationLSTHSTEYNLDSVPS
CCCCCCEECCCCCCC
22.5527080861
223PhosphorylationSTEYNLDSVPSPAEE
CCEECCCCCCCCHHH
38.8129496963
226PhosphorylationYNLDSVPSPAEEFAD
ECCCCCCCCHHHHHH
34.2925159151
236PhosphorylationEEFADFATFSKKERI
HHHHHHHCCCHHHCC
28.5628270605
238PhosphorylationFADFATFSKKERIQL
HHHHHCCCHHHCCCH
38.1623312004
275PhosphorylationNRVNELNSVKEVALG
CCHHHCCCCCHHHHC
47.38113322199
284PhosphorylationKEVALGRSLDNKGDT
CHHHHCCCCCCCCCC
37.9746349001
291PhosphorylationSLDNKGDTDGEDQVC
CCCCCCCCCCCCCEE
55.3530266825
311PhosphorylationIVTNRGFSVEKQGLP
EEECCCCCHHHCCCC
31.9924719451
336PhosphorylationGVQSKAWSLVDSADN
CCCHHHHHHHHCCCC
24.3130624053
340PhosphorylationKAWSLVDSADNSEAI
HHHHHHHCCCCHHHH
30.00113322207
357AcetylationEQCKTEEKLDLLTSK
HHCCCHHHHHHHHHH
40.8620167786
362PhosphorylationEEKLDLLTSKCAHLC
HHHHHHHHHHHHHHH
33.1829396449
363PhosphorylationEKLDLLTSKCAHLCM
HHHHHHHHHHHHHHH
26.2129396449
372PhosphorylationCAHLCMDSVKTSDDE
HHHHHHHHCCCCCCC
9.9123663014
375PhosphorylationLCMDSVKTSDDEVGS
HHHHHCCCCCCCCCC
34.9223927012
376PhosphorylationCMDSVKTSDDEVGSP
HHHHCCCCCCCCCCC
37.0325159151
382PhosphorylationTSDDEVGSPKEESRK
CCCCCCCCCHHHHHC
37.6623401153
387PhosphorylationVGSPKEESRKFTNFQ
CCCCHHHHHCCCCCC
41.6923927012
391PhosphorylationKEESRKFTNFQSPNI
HHHHHCCCCCCCCCC
37.8521712546
395PhosphorylationRKFTNFQSPNIDPTE
HCCCCCCCCCCCCCC
18.7725159151
401PhosphorylationQSPNIDPTEENDLDD
CCCCCCCCCCCCCCC
52.7830266825
409PhosphorylationEENDLDDSLSVKNGD
CCCCCCCCCEECCCC
23.3930266825
411PhosphorylationNDLDDSLSVKNGDSS
CCCCCCCEECCCCCC
34.6930266825
450O-linked_GlycosylationGSTPPFVTGTQDSMS
CCCCCCCCCCCCCCC
34.5923301498
452O-linked_GlycosylationTPPFVTGTQDSMSDA
CCCCCCCCCCCCCCC
21.6023301498
503PhosphorylationTKSDLKQTSDNLSEE
CHHHHHHHCCCHHHH
36.1423882029
504PhosphorylationKSDLKQTSDNLSEEC
HHHHHHHCCCHHHHH
23.2323882029
508PhosphorylationKQTSDNLSEECQLAR
HHHCCCHHHHHHHHH
37.2921815630
517PhosphorylationECQLARKSSGTGTEP
HHHHHHHCCCCCCCC
28.5711603737
518PhosphorylationCQLARKSSGTGTEPV
HHHHHHCCCCCCCCC
43.3327273156
520PhosphorylationLARKSSGTGTEPVAK
HHHHCCCCCCCCCEE
42.7623927012
522PhosphorylationRKSSGTGTEPVAKLK
HHCCCCCCCCCEECC
36.6323927012
584PhosphorylationDEQKDSCSWAAFGDQ
CCCCCCCCCHHHCCH
24.5727251275
605PhosphorylationHRKEAWQSHRTDENI
HHHHHHHHHCCCCCC
12.3028985074
608PhosphorylationEAWQSHRTDENIDTP
HHHHHHCCCCCCCCC
42.0923312004
614PhosphorylationRTDENIDTPGTPKTH
CCCCCCCCCCCCCCC
21.5930266825
617PhosphorylationENIDTPGTPKTHSVP
CCCCCCCCCCCCCCC
23.8623401153
620PhosphorylationDTPGTPKTHSVPSAT
CCCCCCCCCCCCCCC
22.1623312004
622PhosphorylationPGTPKTHSVPSATSK
CCCCCCCCCCCCCCC
40.7423312004
625PhosphorylationPKTHSVPSATSKGAV
CCCCCCCCCCCCCCH
41.8623312004
627PhosphorylationTHSVPSATSKGAVAS
CCCCCCCCCCCCHHC
35.0023312004
628PhosphorylationHSVPSATSKGAVASG
CCCCCCCCCCCHHCC
28.8923312004
640PhosphorylationASGHLQESATSVQTA
HCCCHHHHHHHHHHH
24.7228122231
642PhosphorylationGHLQESATSVQTALL
CCHHHHHHHHHHHHH
38.4228122231
643PhosphorylationHLQESATSVQTALLN
CHHHHHHHHHHHHHH
16.3728122231
646PhosphorylationESATSVQTALLNRLE
HHHHHHHHHHHHHHH
19.6728122231
687UbiquitinationETSTLPIKTREALPE
HHCCCCCCCHHHCCC
39.32-
729PhosphorylationHSNKKLLSSLGIDTR
CCCHHHHHHCCCCCC
33.6723403867
730PhosphorylationSNKKLLSSLGIDTRN
CCHHHHHHCCCCCCC
30.5023403867
735PhosphorylationLSSLGIDTRNILFTG
HHHCCCCCCCEEECC
24.5623403867
745AcetylationILFTGNKKQPVIVPM
EEECCCCCCCEEEEE
64.9319413330
753PhosphorylationQPVIVPMYAAGLGML
CCEEEEECCCCCCCC
6.2921945579
763PhosphorylationGLGMLEPTKEPLKPL
CCCCCCCCCCCCCCC
38.3721945579
850 (in isoform 5)Phosphorylation-30.96118409
851 (in isoform 5)Phosphorylation-60.5629083192
855 (in isoform 5)Phosphorylation-3.9029083192
856 (in isoform 5)Phosphorylation-19.6529083192
857 (in isoform 5)Phosphorylation-36.1729083192
858 (in isoform 5)Phosphorylation-29.9729083192
859 (in isoform 5)Phosphorylation-48.3129083192
863PhosphorylationTTSKLEISTSSLKVT
CCCEEEEECCHHHHH
16.9226657352
864PhosphorylationTSKLEISTSSLKVTD
CCEEEEECCHHHHHH
28.1726437602
865PhosphorylationSKLEISTSSLKVTDA
CEEEEECCHHHHHHH
27.2125159151
866PhosphorylationKLEISTSSLKVTDAF
EEEEECCHHHHHHHH
32.0926437602
870PhosphorylationSTSSLKVTDAFARLM
ECCHHHHHHHHHHHH
21.7430301811
878PhosphorylationDAFARLMSTVEKTST
HHHHHHHHHHHHCCC
33.6130576142
878 (in isoform 4)Phosphorylation-33.61118409
879PhosphorylationAFARLMSTVEKTSTS
HHHHHHHHHHHCCCC
20.7930301811
879 (in isoform 4)Phosphorylation-20.7929083192
883 (in isoform 4)Phosphorylation-24.5929083192
884 (in isoform 4)Phosphorylation-31.2829083192
885 (in isoform 4)Phosphorylation-41.0529083192
886PhosphorylationTVEKTSTSTRKPKRE
HHHHCCCCCCCCCCH
24.9330576142
886 (in isoform 4)Phosphorylation-24.9329083192
887 (in isoform 4)Phosphorylation-32.4129083192
924PhosphorylationVLMFPATLTPSTSSQ
EEEEECCCCCCCCCC
31.2528348404
925PhosphorylationLMFPATLTPSTSSQE
EEEECCCCCCCCCCC
7.8227251275
926PhosphorylationMFPATLTPSTSSQEK
EEECCCCCCCCCCCC
15.7327050516
928PhosphorylationPATLTPSTSSQEKAD
ECCCCCCCCCCCCCC
35.3728348404
929PhosphorylationATLTPSTSSQEKADG
CCCCCCCCCCCCCCC
33.3325850435
930PhosphorylationTLTPSTSSQEKADG-
CCCCCCCCCCCCCC-
34.0725850435
931PhosphorylationLTPSTSSQEKADG--
CCCCCCCCCCCCC--
42.3125850435

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 AFTIN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AFTIN_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 AFTIN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STA5B_HUMANSTAT5Bphysical
21988832

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 AFTIN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 AND THR-522, ANDMASS SPECTROMETRY.
"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 THR-617, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-617, AND MASSSPECTROMETRY.

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