NGEF_HUMAN - dbPTM
NGEF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NGEF_HUMAN
UniProt AC Q8N5V2
Protein Name Ephexin-1
Gene Name NGEF
Organism Homo sapiens (Human).
Sequence Length 710
Subcellular Localization Cytoplasm. Membrane. Cell projection, growth cone. Associated with membranes. Localizes to axonal growth cones (By similarity)..
Protein Description Acts as a guanine nucleotide exchange factor (GEF) which differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a role in axon guidance regulating ephrin-induced growth cone collapse and dendritic spine morphogenesis. Upon activation by ephrin through EPHA4, the GEF activity switches toward RHOA resulting in its activation. Activated RHOA promotes cone retraction at the expense of RAC1- and CDC42-stimulated growth cone extension (By similarity)..
Protein Sequence METRESEDLEKTRRKSASDQWNTDNEPAKVKPELLPEKEETSQADQDIQDKEPHCHIPIKRNSIFNRSIRRKSKAKARDNPERNASCLADSQDNGKSVNEPLTLNIPWSRMPPCRTAMQTDPGAQEMSESSSTPGNGATPEEWPALADSPTTLTEALRMIHPIPADSWRNLIEQIGLLYQEYRDKSTLQEIETRRQQDAEIEDNTNGSPASEDTPEEEEEEEEEEEPASPPERKTLPQICLLSNPHSRFNLWQDLPEIRSSGVLEILQPEEIKLQEAMFELVTSEASYYKSLNLLVSHFMENERIRKILHPSEAHILFSNVLDVLAVSERFLLELEHRMEENIVISDVCDIVYRYAADHFSVYITYVSNQTYQERTYKQLLQEKAAFRELIAQLELDPKCRGLPFSSFLILPFQRITRLKLLVQNILKRVEERSERECTALDAHKELEMVVKACNEGVRKMSRTEQMISIQKKMEFKIKSVPIISHSRWLLKQGELQQMSGPKTSRTLRTKKLFHEIYLFLFNDLLVICRQIPGDKYQVFDSAPRGLLRVEELEDQGQTLANVFILRLLENADDREATYMLKASSQSEMKRWMTSLAPNRRTKFVSFTSRLLDCPQVQCVHPYVAQQPDELTLELADILNILDKTDDGWIFGERLHDQERGWFPSSMTEEILNPKIRSQNLKECFRVHKMDDPQRSQNKDRRKLGSRNRQ
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
9 (in isoform 3)Phosphorylation-6.8028348404
9 (in isoform 2)Phosphorylation-6.8028348404
16PhosphorylationLEKTRRKSASDQWNT
HHHHHHHCHHHHCCC
31.0626657352
18PhosphorylationKTRRKSASDQWNTDN
HHHHHCHHHHCCCCC
37.1126657352
18 (in isoform 3)Phosphorylation-37.1128348404
18 (in isoform 2)Phosphorylation-37.1128348404
19 (in isoform 2)Phosphorylation-58.1724719451
19 (in isoform 3)Phosphorylation-58.1724719451
20 (in isoform 3)Phosphorylation-32.5928348404
20 (in isoform 2)Phosphorylation-32.5928348404
21 (in isoform 3)Phosphorylation-18.0628348404
21 (in isoform 2)Phosphorylation-18.0628348404
41 (in isoform 3)Phosphorylation-27.51-
41 (in isoform 2)Phosphorylation-27.51-
57 (in isoform 3)Phosphorylation-4.6124076635
57 (in isoform 2)Phosphorylation-4.6124076635
63PhosphorylationHIPIKRNSIFNRSIR
CCCCCCCCCCCHHHH
32.3723312004
149PhosphorylationEWPALADSPTTLTEA
HCCHHCCCCCCHHHH
20.66-
155 (in isoform 3)Phosphorylation-49.1424719451
179PhosphorylationIEQIGLLYQEYRDKS
HHHHHHHHHHHCCHH
12.35-
185UbiquitinationLYQEYRDKSTLQEIE
HHHHHCCHHHHHHHH
36.02-
186PhosphorylationYQEYRDKSTLQEIET
HHHHCCHHHHHHHHH
38.3429083192
187PhosphorylationQEYRDKSTLQEIETR
HHHCCHHHHHHHHHH
37.9029083192
193PhosphorylationSTLQEIETRRQQDAE
HHHHHHHHHHHHHHC
36.4929083192
234UbiquitinationPASPPERKTLPQICL
CCCCCCCCCCCHHHH
53.39-
247PhosphorylationCLLSNPHSRFNLWQD
HHCCCCCCCCCCCCC
39.5624719451
283PhosphorylationEAMFELVTSEASYYK
HHHHHHHHCCHHHHH
33.2125850435
284PhosphorylationAMFELVTSEASYYKS
HHHHHHHCCHHHHHH
24.5625850435
287PhosphorylationELVTSEASYYKSLNL
HHHHCCHHHHHHHHH
25.5825850435
288PhosphorylationLVTSEASYYKSLNLL
HHHCCHHHHHHHHHH
23.2025850435
289PhosphorylationVTSEASYYKSLNLLV
HHCCHHHHHHHHHHH
7.5125850435
291PhosphorylationSEASYYKSLNLLVSH
CCHHHHHHHHHHHHH
13.3324719451
297PhosphorylationKSLNLLVSHFMENER
HHHHHHHHHHHCCHH
15.8124719451
372 (in isoform 3)Phosphorylation-9.9024719451
464PhosphorylationGVRKMSRTEQMISIQ
HHHHCCHHHHHHHHH
24.2224719451
492UbiquitinationSHSRWLLKQGELQQM
ECHHHHHHHCCHHHH
54.83-
514 (in isoform 3)Phosphorylation-7.1624719451
537PhosphorylationRQIPGDKYQVFDSAP
HCCCCCCCEEECCCC
18.04-
578PhosphorylationNADDREATYMLKASS
CCCHHHHHHHHHCCC
12.5229083192
579PhosphorylationADDREATYMLKASSQ
CCHHHHHHHHHCCCH
13.9029083192
584PhosphorylationATYMLKASSQSEMKR
HHHHHHCCCHHHHHH
27.5929083192
585PhosphorylationTYMLKASSQSEMKRW
HHHHHCCCHHHHHHH
42.4529083192
587PhosphorylationMLKASSQSEMKRWMT
HHHCCCHHHHHHHHH
41.4229083192
594PhosphorylationSEMKRWMTSLAPNRR
HHHHHHHHHHCCCCC
17.4030622161
595PhosphorylationEMKRWMTSLAPNRRT
HHHHHHHHHCCCCCH
13.3630622161
602PhosphorylationSLAPNRRTKFVSFTS
HHCCCCCHHEEEHHH
26.1223312004
606PhosphorylationNRRTKFVSFTSRLLD
CCCHHEEEHHHHHHC
26.4130266825
608PhosphorylationRTKFVSFTSRLLDCP
CHHEEEHHHHHHCCC
12.8730266825
609PhosphorylationTKFVSFTSRLLDCPQ
HHEEEHHHHHHCCCC
20.9430266825
678PhosphorylationILNPKIRSQNLKECF
HHCHHHHCCCHHHHH
27.2222798277
696PhosphorylationKMDDPQRSQNKDRRK
CCCCHHHHCCHHHHH
32.6222798277

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 NGEF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NGEF_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 NGEF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPHA4_HUMANEPHA4physical
11336673
KPCD_HUMANPRKCDphysical
28514442
KPCI_HUMANPRKCIphysical
28514442
MRS2_HUMANMRS2physical
28514442
ACTY_HUMANACTR1Bphysical
28514442
ARP10_HUMANACTR10physical
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 NGEF_HUMAN

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Related Literatures of Post-Translational Modification

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