DEFI6_HUMAN - dbPTM
DEFI6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEFI6_HUMAN
UniProt AC Q9H4E7
Protein Name Differentially expressed in FDCP 6 homolog
Gene Name DEF6
Organism Homo sapiens (Human).
Sequence Length 631
Subcellular Localization Cytoplasm . Cell membrane . Nucleus . Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell projection, filopodium . Recruited to the plasma membrane upon binding phosphatidylinositol 3,4,5-trisphosphate (PubMed:15023524). Binds to actin fil
Protein Description Phosphatidylinositol 3,4,5-trisphosphate-dependent guanine nucleotide exchange factor (GEF) which plays a role in the activation of Rho GTPases RAC1, RhoA and CDC42. Can regulate cell morphology in cooperation with activated RAC1. Plays a role in Th2 (T helper cells) development and/or activation, perhaps by interfering with ZAP70 signaling (By similarity)..
Protein Sequence MALRKELLKSIWYAFTALDVEKSGKVSKSQLKVLSHNLYTVLHIPHDPVALEEHFRDDDDGPVSSQGYMPYLNKYILDKVEEGAFVKEHFDELCWTLTAKKNYRADSNGNSMLSNQDAFRLWCLFNFLSEDKYPLIMVPDEVEYLLKKVLSSMSLEVSLGELEELLAQEAQVAQTTGGLSVWQFLELFNSGRCLRGVGRDTLSMAIHEVYQELIQDVLKQGYLWKRGHLRRNWAERWFQLQPSCLCYFGSEECKEKRGIIPLDAHCCVEVLPDRDGKRCMFCVKTANRTYEMSASDTRQRQEWTAAIQMAIRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQQLQEEKERKLQELELLQEAQRQAERLLQEEEERRRSQHRELQQALEGQLREAEQARASMQAEMELKEEEAARQRQRIKELEEMQQRLQEALQLEVKARRDEESVRIAQTRLLEEEEEKLKQLMQLKEEQERYIERAQQEKEELQQEMAQQSRSLQQAQQQLEEVRQNRQRADEDVEAAQRKLRQASTNVKHWNVQMNRLMHPIEPGDKRPVTSSSFSGFQPPLLAHRDSSLKRLTRWGSQGNRTPSPNSNEQQKSLNGGDEAPAPASTPQEDKLDPAPEN
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
27PhosphorylationVEKSGKVSKSQLKVL
HHHCCCCCHHHHHHH		30.0324275569
28UbiquitinationEKSGKVSKSQLKVLS
HHCCCCCHHHHHHHH		45.25-
79UbiquitinationLNKYILDKVEEGAFV
HHHHHHHHHHCCCCH		48.3729967540
87UbiquitinationVEEGAFVKEHFDELC
HHCCCCHHHHHHHHH		38.7329967540
100UbiquitinationLCWTLTAKKNYRADS
HHHEEECCCCCCCCC		35.9929967540
107PhosphorylationKKNYRADSNGNSMLS
CCCCCCCCCCCCCCC		45.7322210691
111PhosphorylationRADSNGNSMLSNQDA
CCCCCCCCCCCHHHH		23.6222210691
144PhosphorylationMVPDEVEYLLKKVLS
ECCHHHHHHHHHHHH		23.6222817900
151PhosphorylationYLLKKVLSSMSLEVS
HHHHHHHHHCCCEEE		27.2926074081
152PhosphorylationLLKKVLSSMSLEVSL
HHHHHHHHCCCEEEH		14.2926074081
154PhosphorylationKKVLSSMSLEVSLGE
HHHHHHCCCEEEHHH		24.2726074081
158PhosphorylationSSMSLEVSLGELEEL
HHCCCEEEHHHHHHH		22.6826074081
210PhosphorylationSMAIHEVYQELIQDV
HHHHHHHHHHHHHHH		8.0319060867
222PhosphorylationQDVLKQGYLWKRGHL
HHHHHCCCCHHCCCC		13.59-
225AcetylationLKQGYLWKRGHLRRN
HHCCCCHHCCCCCCC		46.0019608861
256UbiquitinationGSEECKEKRGIIPLD
CCHHHHHHCCCCCCC		41.23-
318UbiquitinationIRLQAEGKTSLHKDL
HHHHHCCCCCHHHHH		26.8429967540
320PhosphorylationLQAEGKTSLHKDLKQ
HHHCCCCCHHHHHHH		31.7827067055
323UbiquitinationEGKTSLHKDLKQKRR
CCCCCHHHHHHHHHH		70.7829967540
343UbiquitinationRERRRAAKEEELLRL
HHHHHHHHHHHHHHH		65.75-
357UbiquitinationLQQLQEEKERKLQEL
HHHHHHHHHHHHHHH		63.1724816145
360UbiquitinationLQEEKERKLQELELL
HHHHHHHHHHHHHHH		56.4624816145
387PhosphorylationEEEERRRSQHRELQQ
HHHHHHHHHHHHHHH		28.6428464451
410SulfoxidationAEQARASMQAEMELK
HHHHHHHHHHHHHHH		4.2321406390
417UbiquitinationMQAEMELKEEEAARQ
HHHHHHHHHHHHHHH		50.1824816145
429UbiquitinationARQRQRIKELEEMQQ
HHHHHHHHHHHHHHH		59.4424816145
434SulfoxidationRIKELEEMQQRLQEA
HHHHHHHHHHHHHHH		2.7621406390
491UbiquitinationIERAQQEKEELQQEM
HHHHHHHHHHHHHHH		52.7529967540
498SulfoxidationKEELQQEMAQQSRSL
HHHHHHHHHHHHHHH		3.3821406390
504PhosphorylationEMAQQSRSLQQAQQQ
HHHHHHHHHHHHHHH		35.4624043423
537PhosphorylationQRKLRQASTNVKHWN
HHHHHHHHHCCCHHH		16.51-
538PhosphorylationRKLRQASTNVKHWNV
HHHHHHHHCCCHHHH		47.23-
563PhosphorylationPGDKRPVTSSSFSGF
CCCCCCCCCCCCCCC		26.1030576142
564PhosphorylationGDKRPVTSSSFSGFQ
CCCCCCCCCCCCCCC		24.9926074081
565PhosphorylationDKRPVTSSSFSGFQP
CCCCCCCCCCCCCCC		26.4930576142
566PhosphorylationKRPVTSSSFSGFQPP
CCCCCCCCCCCCCCC		24.1730576142
568PhosphorylationPVTSSSFSGFQPPLL
CCCCCCCCCCCCCCC		40.4230576142
580PhosphorylationPLLAHRDSSLKRLTR
CCCCCCCCHHHHHHH		37.2128993769
581PhosphorylationLLAHRDSSLKRLTRW
CCCCCCCHHHHHHHH		42.0528993769
586PhosphorylationDSSLKRLTRWGSQGN
CCHHHHHHHHCCCCC		28.5426074081
590PhosphorylationKRLTRWGSQGNRTPS
HHHHHHCCCCCCCCC		28.1423401153
595PhosphorylationWGSQGNRTPSPNSNE
HCCCCCCCCCCCCHH		31.9223401153
597PhosphorylationSQGNRTPSPNSNEQQ
CCCCCCCCCCCHHHH		35.7823401153
600PhosphorylationNRTPSPNSNEQQKSL
CCCCCCCCHHHHHHC		45.1623927012
606PhosphorylationNSNEQQKSLNGGDEA
CCHHHHHHCCCCCCC		23.8028450419
618PhosphorylationDEAPAPASTPQEDKL
CCCCCCCCCCCHHCC		39.2928450419
619PhosphorylationEAPAPASTPQEDKLD
CCCCCCCCCCHHCCC		30.9728450419
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
210YPhosphorylationKinaseITKQ08881
PSP
222YPhosphorylationKinaseITKQ08881
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEFI6_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 DEFI6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BEGIN_HUMANBEGAINphysical
16189514
RAC2_HUMANRAC2physical
15023524
RAC1_HUMANRAC1physical
15023524
RHOA_HUMANRHOAphysical
15023524
CDC42_HUMANCDC42physical
15023524
A4_HUMANAPPphysical
21832049
4ET_HUMANEIF4ENIF1physical
25416956
PBIP1_HUMANPBXIP1physical
25416956
HOMEZ_HUMANHOMEZphysical
25416956
DCXR_HUMANDCXRphysical
26186194
CHAP1_HUMANCHAMP1physical
26186194
ADDB_HUMANADD2physical
26186194
RHG42_HUMANARHGAP42physical
26186194
RBM45_HUMANRBM45physical
26186194
MYCB2_HUMANMYCBP2physical
26186194
SMCA1_HUMANSMARCA1physical
26186194
BABA1_HUMANBABAM1physical
26186194
BRCC3_HUMANBRCC3physical
26186194
ABRX2_HUMANFAM175Bphysical
26186194
BABA2_HUMANBREphysical
26186194
ANS1A_HUMANANKS1Aphysical
26186194
NFKB2_HUMANNFKB2physical
26186194
KBTB6_HUMANKBTBD6physical
26186194
KPCT_HUMANPRKCQphysical
26186194
HOMEZ_HUMANHOMEZphysical
26186194
GRID1_HUMANGRID1physical
26186194
CA052_HUMANC1orf52physical
26186194
DCA16_HUMANDCAF16physical
26186194
RHG42_HUMANARHGAP42physical
28514442
GRID1_HUMANGRID1physical
28514442
ABRX2_HUMANFAM175Bphysical
28514442
HOMEZ_HUMANHOMEZphysical
28514442
BABA2_HUMANBREphysical
28514442
KPCT_HUMANPRKCQphysical
28514442
RBM45_HUMANRBM45physical
28514442
BABA1_HUMANBABAM1physical
28514442
ANS1A_HUMANANKS1Aphysical
28514442
NFKB2_HUMANNFKB2physical
28514442
SMCA1_HUMANSMARCA1physical
28514442
DCXR_HUMANDCXRphysical
28514442
CHAP1_HUMANCHAMP1physical
28514442
ADDB_HUMANADD2physical
28514442
BRCC3_HUMANBRCC3physical
28514442
CA052_HUMANC1orf52physical
28514442
TNR6C_HUMANTNRC6Cphysical
28514442
RCC2_HUMANRCC2physical
28514442
DCA16_HUMANDCAF16physical
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 DEFI6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-225, AND MASS SPECTROMETRY.
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-590 AND SER-597, ANDMASS SPECTROMETRY.

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