DEN1B_HUMAN - dbPTM
DEN1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEN1B_HUMAN
UniProt AC Q6P3S1
Protein Name DENN domain-containing protein 1B {ECO:0000312|HGNC:HGNC:28404}
Gene Name DENND1B {ECO:0000312|HGNC:HGNC:28404}
Organism Homo sapiens (Human).
Sequence Length 775
Subcellular Localization Cytoplasm, cytosol . Cytoplasmic vesicle, clathrin-coated vesicle .
Protein Description Guanine nucleotide exchange factor (GEF) for RAB35 that acts as a regulator of T-cell receptor (TCR) internalization in TH2 cells. [PubMed: 20154091]
Protein Sequence MDCRTKANPDRTFDLVLKVKCHASENEDPVVLWKFPEDFGDQEILQSVPKFCFPFDVERVSQNQVGQHFTFVLTDIESKQRFGFCRLTSGGTICLCILSYLPWFEVYYKLLNTLADYLAKELENDLNETLRSLYNHPVPKANTPVNLSVNQEIFIACEQVLKDQPALVPHSYFIAPDVTGLPTIPESRNLTEYFVAVDVNNMLQLYASMLHERRIVIISSKLSTLTACIHGSAALLYPMYWQHIYIPVLPPHLLDYCCAPMPYLIGIHSSLIERVKNKSLEDVVMLNVDTNTLESPFSDLNNLPSDVVSALKNKLKKQSTATGDGVARAFLRAQAALFGSYRDALRYKPGEPITFCEESFVKHRSSVMKQFLETAINLQLFKQFIDGRLAKLNAGRGFSDVFEEEITSGGFCGGNPRSYQQWVHTVKKGGALFNTAMTKATPAVRTAYKFAKNHAKLGLKEVKSKLKHKENEEDYGTCSSSVQYTPVYKLHNEKGGNSEKRKLAQARLKRPLKSLDGALYDDEDDDDIERASKLSSEDGEEASAYLYESDDSVETRVKTPYSGEMDLLGEILDTLSTHSSDQGKLAAAKSLDFFRSMDDIDYKPTNKSNAPSENNLAFLCGGSGDQAEWNLGQDDSALHGKHLPPSPRKRVSSSGLTDSLFILKEENSNKHLGADNVSDPTSGLDFQLTSPEVSQTDKGKTEKRETLSQISDDLLIPGLGRHSSTFVPWEKEGKEAKETSEDIGLLHEVVSLCHMTSDFQQSLNISDKNTNGNQT
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
78PhosphorylationFVLTDIESKQRFGFC
EEEEECCCCCCEEEE		34.1322798277
134 (in isoform 5)Phosphorylation-16.81-
134PhosphorylationNETLRSLYNHPVPKA
HHHHHHHHCCCCCCC		16.8121060948
362 (in isoform 5)"N6,N6-dimethyllysine"-31.15-
362MethylationFCEESFVKHRSSVMK
CCHHHHHHHHHHHHH		31.15-
369MethylationKHRSSVMKQFLETAI
HHHHHHHHHHHHHHH		35.42-
369 (in isoform 5)"N6,N6-dimethyllysine"-35.42-
391UbiquitinationFIDGRLAKLNAGRGF
HHHHHHHHCCCCCCC		47.03-
399PhosphorylationLNAGRGFSDVFEEEI
CCCCCCCHHHHHHHH		35.37-
456UbiquitinationKFAKNHAKLGLKEVK
HHHHHHHHHCHHHHH		-
475PhosphorylationHKENEEDYGTCSSSV
CCCCCCCCCCCCCCC		25884760
475 (in isoform 5)Phosphorylation--
477PhosphorylationENEEDYGTCSSSVQY
CCCCCCCCCCCCCEE		28796482
479PhosphorylationEEDYGTCSSSVQYTP
CCCCCCCCCCCEECC		29978859
480 (in isoform 5)Phosphorylation--
480PhosphorylationEDYGTCSSSVQYTPV
CCCCCCCCCCEECCC		29978859
481 (in isoform 5)Phosphorylation--
481PhosphorylationDYGTCSSSVQYTPVY
CCCCCCCCCEECCCE		29978859
484 (in isoform 5)Phosphorylation--
484PhosphorylationTCSSSVQYTPVYKLH
CCCCCCEECCCEECC		25884760
485PhosphorylationCSSSVQYTPVYKLHN
CCCCCEECCCEECCC		28796482
485 (in isoform 5)Phosphorylation--
488 (in isoform 5)Phosphorylation--
488PhosphorylationSVQYTPVYKLHNEKG
CCEECCCEECCCCCC		28796482
514 (in isoform 5)Phosphorylation-27251275
514PhosphorylationRLKRPLKSLDGALYD
HHHCCHHHCCCCCCC		29507054
520PhosphorylationKSLDGALYDDEDDDD
HHCCCCCCCCCCCHH		28796482
520 (in isoform 5)Phosphorylation--
532 (in isoform 5)Phosphorylation-24719451
532PhosphorylationDDDIERASKLSSEDG
CHHHHHHHHHCCCCC		24719451
535 (in isoform 5)Phosphorylation--
535PhosphorylationIERASKLSSEDGEEA
HHHHHHHCCCCCHHH		28348404
536PhosphorylationERASKLSSEDGEEAS
HHHHHHCCCCCHHHH		28348404
536 (in isoform 5)Phosphorylation--
547 (in isoform 5)Phosphorylation-27251275
547PhosphorylationEEASAYLYESDDSVE
HHHHHHEEECCCCCE		27251275
549PhosphorylationASAYLYESDDSVETR
HHHHEEECCCCCEEE		27251275
549 (in isoform 5)Phosphorylation-27251275
552PhosphorylationYLYESDDSVETRVKT
HEEECCCCCEEEECC		27251275
552 (in isoform 5)Phosphorylation--
559PhosphorylationSVETRVKTPYSGEMD
CCEEEECCCCCCCCH		28450419
559 (in isoform 5)Phosphorylation--
561PhosphorylationETRVKTPYSGEMDLL
EEEECCCCCCCCHHH		27251275
562PhosphorylationTRVKTPYSGEMDLLG
EEECCCCCCCCHHHH		22115753
574PhosphorylationLLGEILDTLSTHSSD
HHHHHHHHHHHCCCH		28450419
574 (in isoform 5)Phosphorylation-27251275
576 (in isoform 5)Phosphorylation--
576PhosphorylationGEILDTLSTHSSDQG
HHHHHHHHHCCCHHH		28450419
577PhosphorylationEILDTLSTHSSDQGK
HHHHHHHHCCCHHHH		28450419
579PhosphorylationLDTLSTHSSDQGKLA
HHHHHHCCCHHHHHH		28450419
579 (in isoform 5)Phosphorylation--
580PhosphorylationDTLSTHSSDQGKLAA
HHHHHCCCHHHHHHH		28450419
590PhosphorylationGKLAAAKSLDFFRSM
HHHHHHHHHHHHHCC		22617229
590 (in isoform 5)Phosphorylation-24719451
596PhosphorylationKSLDFFRSMDDIDYK
HHHHHHHCCCCCCCC		22617229
596 (in isoform 5)Phosphorylation-24719451
602PhosphorylationRSMDDIDYKPTNKSN
HCCCCCCCCCCCCCC		29978859
605 (in isoform 5)Phosphorylation--
605PhosphorylationDDIDYKPTNKSNAPS
CCCCCCCCCCCCCCC		29978859
608PhosphorylationDYKPTNKSNAPSENN
CCCCCCCCCCCCCCC		28348404
608 (in isoform 5)Phosphorylation-27251275
612PhosphorylationTNKSNAPSENNLAFL
CCCCCCCCCCCEEEC		28857561
612 (in isoform 5)Phosphorylation-24719451
646PhosphorylationHGKHLPPSPRKRVSS
CCCCCCCCCCCCCCC		23312004
646 (in isoform 5)Phosphorylation-24719451
652PhosphorylationPSPRKRVSSSGLTDS
CCCCCCCCCCCCCCE		30266825
652 (in isoform 5)Phosphorylation--
653 (in isoform 5)Phosphorylation-20736484
653PhosphorylationSPRKRVSSSGLTDSL
CCCCCCCCCCCCCEE		30266825
654 (in isoform 5)Phosphorylation-24719451
654PhosphorylationPRKRVSSSGLTDSLF
CCCCCCCCCCCCEEE		30266825
657PhosphorylationRVSSSGLTDSLFILK
CCCCCCCCCEEEEEE		28450419
659PhosphorylationSSSGLTDSLFILKEE
CCCCCCCEEEEEECC		30576142
689PhosphorylationSGLDFQLTSPEVSQT
CCCCEEECCCCCHHC		22199227
690 (in isoform 5)Phosphorylation--
690PhosphorylationGLDFQLTSPEVSQTD
CCCEEECCCCCHHCC		30576142
694PhosphorylationQLTSPEVSQTDKGKT
EECCCCCHHCCCCCC		22199227
706PhosphorylationGKTEKRETLSQISDD
CCCCCHHHHHHHCCC		28634120
708PhosphorylationTEKRETLSQISDDLL
CCCHHHHHHHCCCCC		28634120
711PhosphorylationRETLSQISDDLLIPG
HHHHHHHCCCCCCCC		22199227
711 (in isoform 5)Phosphorylation-24719451
723PhosphorylationIPGLGRHSSTFVPWE
CCCCCCCCCCCCCHH		25159151
723 (in isoform 5)Phosphorylation--
724PhosphorylationPGLGRHSSTFVPWEK
CCCCCCCCCCCCHHH		28857561
724 (in isoform 5)Phosphorylation-24719451
725PhosphorylationGLGRHSSTFVPWEKE
CCCCCCCCCCCHHHC		28348404
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 DEN1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEN1B_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 DEN1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPA12_HUMANSERPINA12physical
26186194
SPA12_HUMANSERPINA12physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DEN1B_HUMAN

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Related Literatures of Post-Translational Modification

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