ICEF1_HUMAN - dbPTM
ICEF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ICEF1_HUMAN
UniProt AC Q8WWN9
Protein Name Interactor protein for cytohesin exchange factors 1
Gene Name IPCEF1
Organism Homo sapiens (Human).
Sequence Length 437
Subcellular Localization Cytoplasm. Cell membrane. Translocated with PSCD2 to the plasma membrane upon epidermal growth factor (EGF) stimulation..
Protein Description Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner..
Protein Sequence MTSYMAIDGSALVPLRQKPRRKTQGFLTMSRRRISCKDLGHADCQGWLYKKKEKGSFLSNKWKKFWVILKGSSLYWYSNQMAEKADGFVNLPDFTVERASECKKKHAFKISHPQIKTFYFAAENVQEMNVWLNKLGSAVIHQESTTKDEECYSESEQEDPEIAAETPPPPHASQTQSLTAQQASSSSPSLSGTSYSFSSLENTVKTPSSFPSSLSKERQSLPDTVNSLSAAEDEGQPITFAVQVHSPVPSEAGIHKALENSFVTSESGFLNSLSSDDTSSLSSNHDHLTVPDKPAGSKIMDKEETKVSEDDEMEKLYKSLEQASLSPLGDRRPSTKKELRKSFVKRCKNPSINEKLHKIRTLNSTLKCKEHDLAMINQLLDDPKLTARKYREWKVMNTLLIQDIYQQQRASPAPDDTDDTPQELKKSPSSPSVENSI
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------MTSYMAIDG
------CCCEEEECC
28.6824043423
3Phosphorylation-----MTSYMAIDGS
-----CCCEEEECCC
16.1824043423
4Phosphorylation----MTSYMAIDGSA
----CCCEEEECCCE
4.9629759185
10PhosphorylationSYMAIDGSALVPLRQ
CEEEECCCEEEECCC
18.0624043423
23PhosphorylationRQKPRRKTQGFLTMS
CCCCCCCCCCEEEEE
31.92-
28PhosphorylationRKTQGFLTMSRRRIS
CCCCCEEEEECCCEE
15.73-
30PhosphorylationTQGFLTMSRRRISCK
CCCEEEEECCCEEHH
19.8730631047
56PhosphorylationYKKKEKGSFLSNKWK
EEECCCCCCCCCCCC
33.8030108239
75PhosphorylationILKGSSLYWYSNQMA
EEECCCEEEECHHHH
12.30-
206PhosphorylationSLENTVKTPSSFPSS
CCCCCCCCCCCCCCC
24.8623312004
208PhosphorylationENTVKTPSSFPSSLS
CCCCCCCCCCCCCCC
50.2530108239
209PhosphorylationNTVKTPSSFPSSLSK
CCCCCCCCCCCCCCH
42.2428450419
210PhosphorylationTVKTPSSFPSSLSKE
CCCCCCCCCCCCCHH
8.8027251275
212PhosphorylationKTPSSFPSSLSKERQ
CCCCCCCCCCCHHHH
41.7328450419
213PhosphorylationTPSSFPSSLSKERQS
CCCCCCCCCCHHHHC
36.5828450419
215PhosphorylationSSFPSSLSKERQSLP
CCCCCCCCHHHHCCC
34.1228450419
220PhosphorylationSLSKERQSLPDTVNS
CCCHHHHCCCCHHHH
48.3628348404
224PhosphorylationERQSLPDTVNSLSAA
HHHCCCCHHHHCHHH
21.4628348404
225PhosphorylationRQSLPDTVNSLSAAE
HHCCCCHHHHCHHHH
6.2927251275
227PhosphorylationSLPDTVNSLSAAEDE
CCCCHHHHCHHHHHC
21.2628348404
229PhosphorylationPDTVNSLSAAEDEGQ
CCHHHHCHHHHHCCC
25.8327251275
239PhosphorylationEDEGQPITFAVQVHS
HHCCCCCEEEEEECC
16.5430108239
246PhosphorylationTFAVQVHSPVPSEAG
EEEEEECCCCCCCCC
28.8330108239
247PhosphorylationFAVQVHSPVPSEAGI
EEEEECCCCCCCCCH
27.4527251275
250PhosphorylationQVHSPVPSEAGIHKA
EECCCCCCCCCHHHH
40.0730108239
305PhosphorylationKIMDKEETKVSEDDE
CCCCHHHHCCCCHHH
37.5330108239
306PhosphorylationIMDKEETKVSEDDEM
CCCHHHHCCCCHHHH
47.2227251275
308PhosphorylationDKEETKVSEDDEMEK
CHHHHCCCCHHHHHH
36.5430108239
317PhosphorylationDDEMEKLYKSLEQAS
HHHHHHHHHHHHHHC
15.0329978859
319PhosphorylationEMEKLYKSLEQASLS
HHHHHHHHHHHHCCC
24.4725278378
324PhosphorylationYKSLEQASLSPLGDR
HHHHHHHCCCCCCCC
29.1328450419
326PhosphorylationSLEQASLSPLGDRRP
HHHHHCCCCCCCCCC
18.6423401153
334PhosphorylationPLGDRRPSTKKELRK
CCCCCCCCCHHHHHH
51.5523882029
335PhosphorylationLGDRRPSTKKELRKS
CCCCCCCCHHHHHHH
49.1430576142
336PhosphorylationGDRRPSTKKELRKSF
CCCCCCCHHHHHHHH
48.8924719451
342PhosphorylationTKKELRKSFVKRCKN
CHHHHHHHHHHHCCC
28.9223401153
398PhosphorylationREWKVMNTLLIQDIY
HHHHHHHHHHHHHHH
12.5822617229
405PhosphorylationTLLIQDIYQQQRASP
HHHHHHHHHHHCCCC
14.4628450419
411PhosphorylationIYQQQRASPAPDDTD
HHHHHCCCCCCCCCC
24.6323401153
412PhosphorylationYQQQRASPAPDDTDD
HHHHCCCCCCCCCCC
46.9924719451
417PhosphorylationASPAPDDTDDTPQEL
CCCCCCCCCCCHHHH
43.0623684312
420PhosphorylationAPDDTDDTPQELKKS
CCCCCCCCHHHHHHC
29.6723684312
427PhosphorylationTPQELKKSPSSPSVE
CHHHHHHCCCCCCCC
28.5520164059
429PhosphorylationQELKKSPSSPSVENS
HHHHHCCCCCCCCCC
63.0720164059
430PhosphorylationELKKSPSSPSVENSI
HHHHCCCCCCCCCCC
25.2823401153
431PhosphorylationLKKSPSSPSVENSI-
HHHCCCCCCCCCCC-
46.8927251275
432PhosphorylationKKSPSSPSVENSI--
HHCCCCCCCCCCC--
43.9728450419
436PhosphorylationSSPSVENSI------
CCCCCCCCC------
19.0328450419

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 ICEF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ICEF1_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 ICEF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYH2_HUMANCYTH2physical
12920129
CYH1_HUMANCYTH1physical
12920129
CYH3_HUMANCYTH3physical
12920129
CYH4_HUMANCYTH4physical
12920129
CYH1_HUMANCYTH1physical
28514442
CYH2_HUMANCYTH2physical
28514442
CYH3_HUMANCYTH3physical
28514442
TRI11_HUMANTRIM11physical
28514442

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 ICEF1_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-411, AND MASSSPECTROMETRY.

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