ARFP1_HUMAN - dbPTM
ARFP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARFP1_HUMAN
UniProt AC P53367
Protein Name Arfaptin-1
Gene Name ARFIP1
Organism Homo sapiens (Human).
Sequence Length 373
Subcellular Localization
Protein Description Putative target protein of ADP-ribosylation factor..
Protein Sequence MAQESPKNSAAEIPVTSNGEVDDSREHSFNRDLKHSLPSGLGLSETQITSHGFDNTKEGVIEAGAFQGSPAPPLPSVMSPSRVAASRLAQQGSDLIVPAGGQRTQTKSGPVILADEIKNPAMEKLELVRKWSLNTYKCTRQIISEKLGRGSRTVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQRQLGDAFADLSLKSLELHEEFGYNADTQKLLAKNGETLLGAINFFIASVNTLVNKTIEDTLMTVKQYESARIEYDAYRTDLEELNLGPRDANTLPKIEQSQHLFQAHKEKYDKMRNDVSVKLKFLEENKVKVLHNQLVLFHNAIAAYFAGNQKQLEQTLKQFHIKLKTPGVDAPSWLEEQ
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------MAQESPKNS
------CCCCCCCCC
23.1121406692
5 (in isoform 2)Phosphorylation-29.15-
5Phosphorylation---MAQESPKNSAAE
---CCCCCCCCCCCC
29.1523401153
9PhosphorylationAQESPKNSAAEIPVT
CCCCCCCCCCCCCCC
34.6722617229
16PhosphorylationSAAEIPVTSNGEVDD
CCCCCCCCCCCCCCC
15.8923401153
17PhosphorylationAAEIPVTSNGEVDDS
CCCCCCCCCCCCCCC
42.9723663014
24 (in isoform 2)Phosphorylation-34.80-
24PhosphorylationSNGEVDDSREHSFNR
CCCCCCCCHHHCCCH
34.8025159151
28 (in isoform 2)Phosphorylation-21.33-
28PhosphorylationVDDSREHSFNRDLKH
CCCCHHHCCCHHHHH
21.3325159151
34UbiquitinationHSFNRDLKHSLPSGL
HCCCHHHHHCCCCCC
35.12-
36PhosphorylationFNRDLKHSLPSGLGL
CCHHHHHCCCCCCCC
40.1522617229
36 (in isoform 2)Phosphorylation-40.15-
39PhosphorylationDLKHSLPSGLGLSET
HHHHCCCCCCCCCCH
52.5223401153
39 (in isoform 2)Phosphorylation-52.52-
44PhosphorylationLPSGLGLSETQITSH
CCCCCCCCCHHHEEC
36.4822617229
46PhosphorylationSGLGLSETQITSHGF
CCCCCCCHHHEECCC
23.1525693802
49PhosphorylationGLSETQITSHGFDNT
CCCCHHHEECCCCCC
12.5923403867
50PhosphorylationLSETQITSHGFDNTK
CCCHHHEECCCCCCC
24.2023403867
56PhosphorylationTSHGFDNTKEGVIEA
EECCCCCCCCCEEEE
32.1123403867
69PhosphorylationEAGAFQGSPAPPLPS
EECCCCCCCCCCCCC
13.7029255136
76PhosphorylationSPAPPLPSVMSPSRV
CCCCCCCCCCCHHHH
37.8329255136
76 (in isoform 2)Phosphorylation-37.8325159151
78SulfoxidationAPPLPSVMSPSRVAA
CCCCCCCCCHHHHHH
5.9830846556
79PhosphorylationPPLPSVMSPSRVAAS
CCCCCCCCHHHHHHH
19.9829255136
81PhosphorylationLPSVMSPSRVAASRL
CCCCCCHHHHHHHHH
31.8929255136
86 (in isoform 2)Ubiquitination-20.3521890473
86PhosphorylationSPSRVAASRLAQQGS
CHHHHHHHHHHHCCC
20.3523090842
93PhosphorylationSRLAQQGSDLIVPAG
HHHHHCCCCEEECCC
25.5525693802
100 (in isoform 2)Phosphorylation-27.05-
104PhosphorylationVPAGGQRTQTKSGPV
ECCCCCCCCCCCCCE
32.4728555341
107UbiquitinationGGQRTQTKSGPVILA
CCCCCCCCCCCEEEE
43.53-
108PhosphorylationGQRTQTKSGPVILAD
CCCCCCCCCCEEEEH
52.2821815630
118UbiquitinationVILADEIKNPAMEKL
EEEEHHCCCHHHHHH
55.6321906983
118 (in isoform 1)Ubiquitination-55.6321890473
124UbiquitinationIKNPAMEKLELVRKW
CCCHHHHHHHHHHHH
33.89-
1242-HydroxyisobutyrylationIKNPAMEKLELVRKW
CCCHHHHHHHHHHHH
33.89-
132PhosphorylationLELVRKWSLNTYKCT
HHHHHHHCCCHHHHH
18.1222167270
135PhosphorylationVRKWSLNTYKCTRQI
HHHHCCCHHHHHHHH
29.6522167270
136PhosphorylationRKWSLNTYKCTRQII
HHHCCCHHHHHHHHH
11.7323403867
144PhosphorylationKCTRQIISEKLGRGS
HHHHHHHHHHHCCCC
30.2424719451
146AcetylationTRQIISEKLGRGSRT
HHHHHHHHHCCCCCE
49.8325953088
1462-HydroxyisobutyrylationTRQIISEKLGRGSRT
HHHHHHHHHCCCCCE
49.83-
146UbiquitinationTRQIISEKLGRGSRT
HHHHHHHHHCCCCCE
49.83-
172PhosphorylationLRDNKKKYENILKLA
HHCCHHHHHHHHHHH
24.0822210691
173UbiquitinationRDNKKKYENILKLAQ
HCCHHHHHHHHHHHH
46.8321890473
180UbiquitinationENILKLAQTLSTQLF
HHHHHHHHHHHHHHH
54.10-
192PhosphorylationQLFQMVHTQRQLGDA
HHHHHHHHHHHHHHH
17.6522210691
221 (in isoform 2)Phosphorylation-34.64-
222UbiquitinationGYNADTQKLLAKNGE
CCCHHHHHHHHHCCC
47.78-
249PhosphorylationVNTLVNKTIEDTLMT
HHHHHCHHHHHHHHH
25.1322210691
253PhosphorylationVNKTIEDTLMTVKQY
HCHHHHHHHHHHHHH
12.9720068231
255SulfoxidationKTIEDTLMTVKQYES
HHHHHHHHHHHHHHH
4.3721406390
256PhosphorylationTIEDTLMTVKQYESA
HHHHHHHHHHHHHHC
27.8822210691
258UbiquitinationEDTLMTVKQYESARI
HHHHHHHHHHHHCCC
37.69-
272PhosphorylationIEYDAYRTDLEELNL
CEECEECCCHHHCCC
32.0619060867
289UbiquitinationRDANTLPKIEQSQHL
CCCCCCHHHHHHHHH
63.09-
293PhosphorylationTLPKIEQSQHLFQAH
CCHHHHHHHHHHHHH
13.5330622161
301UbiquitinationQHLFQAHKEKYDKMR
HHHHHHHHHHHHHHH
59.94-
304PhosphorylationFQAHKEKYDKMRNDV
HHHHHHHHHHHHCCH
23.14-
316UbiquitinationNDVSVKLKFLEENKV
CCHHHHHHHHHHCCC
42.03-
321 (in isoform 2)Ubiquitination-45.0721890473
321UbiquitinationKLKFLEENKVKVLHN
HHHHHHHCCCCEEHH
45.0721890473
322UbiquitinationLKFLEENKVKVLHNQ
HHHHHHCCCCEEHHH
46.87-
3222-HydroxyisobutyrylationLKFLEENKVKVLHNQ
HHHHHHCCCCEEHHH
46.87-
353 (in isoform 1)Ubiquitination-55.0621890473
353UbiquitinationKQLEQTLKQFHIKLK
HHHHHHHHHHCHHCC
55.0621890473
360UbiquitinationKQFHIKLKTPGVDAP
HHHCHHCCCCCCCCC
47.90-
361PhosphorylationQFHIKLKTPGVDAPS
HHCHHCCCCCCCCCH
35.3928355574
368PhosphorylationTPGVDAPSWLEEQ--
CCCCCCCHHHHCC--
46.1126552605

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
100SPhosphorylationKinasePRKD1Q15139
GPS
100SPhosphorylationKinasePRKD2Q9BZL6
PSP
132SPhosphorylationKinasePRKD1Q15139
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARFP1_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 ARFP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF3_HUMANARF3physical
10413101
DNM1L_HUMANDNM1Lphysical
22863883
IDE_HUMANIDEphysical
22863883
LC7L2_HUMANLUC7L2physical
22863883
ANM3_HUMANPRMT3physical
22863883
PSMG3_HUMANPSMG3physical
22863883
SC24A_HUMANSEC24Aphysical
22863883
GLYM_HUMANSHMT2physical
22863883
STAT3_HUMANSTAT3physical
22863883
AACS_HUMANAACSphysical
26344197
AK1A1_HUMANAKR1A1physical
26344197
ATOX1_HUMANATOX1physical
26344197
ECH1_HUMANECH1physical
26344197
FLNB_HUMANFLNBphysical
26344197
LYPA1_HUMANLYPLA1physical
26344197
PA1B2_HUMANPAFAH1B2physical
26344197
PDCD6_HUMANPDCD6physical
26344197
PGM2L_HUMANPGM2L1physical
26344197
DHPR_HUMANQDPRphysical
26344197
STIP1_HUMANSTIP1physical
26344197
TBCA_HUMANTBCAphysical
26344197

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 ARFP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY.
"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-69; SER-79 AND SER-132,AND MASS 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-272 AND THR-361, ANDMASS SPECTROMETRY.

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