DEN1C_HUMAN - dbPTM
DEN1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEN1C_HUMAN
UniProt AC Q8IV53
Protein Name DENN domain-containing protein 1C
Gene Name DENND1C
Organism Homo sapiens (Human).
Sequence Length 801
Subcellular Localization Cytoplasm, cytosol . Cytoplasmic vesicle, clathrin-coated vesicle .
Protein Description Guanine nucleotide exchange factor (GEF) which may activate RAB8A, RAB13 and RAB35. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form..
Protein Sequence MESRAEGGSPAVFDWFFEAACPASLQEDPPILRQFPPDFRDQEAMQMVPKFCFPFDVEREPPSPAVQHFTFALTDLAGNRRFGFCRLRAGTQSCLCILSHLPWFEVFYKLLNTVGDLLAQDQVTEAEELLQNLFQQSLSGPQASVGLELGSGVTVSSGQGIPPPTRGNSKPLSCFVAPDSGRLPSIPENRNLTELVVAVTDENIVGLFAALLAERRVLLTASKLSTLTSCVHASCALLYPMRWEHVLIPTLPPHLLDYCCAPMPYLIGVHASLAERVREKALEDVVVLNVDANTLETTFNDVQALPPDVVSLLRLRLRKVALAPGEGVSRLFLKAQALLFGGYRDALVCSPGQPVTFSEEVFLAQKPGAPLQAFHRRAVHLQLFKQFIEARLEKLNKGEGFSDQFEQEITGCGASSGALRSYQLWADNLKKGGGALLHSVKAKTQPAVKNMYRSAKSGLKGVQSLLMYKDGDSVLQRGGSLRAPALPSRSDRLQQRLPITQHFGKNRPLRPSRRRQLEEGTSEPPGAGTPPLSPEDEGCPWAEEALDSSFLGSGEELDLLSEILDSLSMGAKSAGSLRPSQSLDCCHRGDLDSCFSLPNIPRWQPDDKKLPEPEPQPLSLPSLQNASSLDATSSSKDSRSQLIPSESDQEVTSPSQSSTASADPSIWGDPKPSPLTEPLILHLTPSHKAAEDSTAQENPTPWLSTAPTEPSPPESPQILAPTKPNFDIAWTSQPLDPSSDPSSLEDPRARPPKALLAERAHLQPREEPGALNSPATPTSNCQKSQPSSRPRVADLKKCFEG
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
50UbiquitinationEAMQMVPKFCFPFDV
HHHHHCCCCCCCCCC		43.27-
169PhosphorylationPPPTRGNSKPLSCFV
CCCCCCCCCCCEEEE		38.1724719451
170UbiquitinationPPTRGNSKPLSCFVA
CCCCCCCCCCEEEEC		54.71-
180PhosphorylationSCFVAPDSGRLPSIP
EEEECCCCCCCCCCC		25.42-
275UbiquitinationGVHASLAERVREKAL
HHHHHHHHHHHHHHH		57.9329967540
319UbiquitinationLLRLRLRKVALAPGE
HHHHHHHHHHCCCCC		36.1329967540
353UbiquitinationALVCSPGQPVTFSEE
EEEECCCCCCCCCCC		32.4529967540
366UbiquitinationEEVFLAQKPGAPLQA
CCCHHCCCCCCCHHH		39.55-
385UbiquitinationAVHLQLFKQFIEARL
HHHHHHHHHHHHHHH		53.55-
386UbiquitinationVHLQLFKQFIEARLE
HHHHHHHHHHHHHHH		36.9029967540
387UbiquitinationHLQLFKQFIEARLEK
HHHHHHHHHHHHHHH		5.8529967540
394UbiquitinationFIEARLEKLNKGEGF
HHHHHHHHHHCCCCC		63.05-
397UbiquitinationARLEKLNKGEGFSDQ
HHHHHHHCCCCCHHH		69.6329967540
405UbiquitinationGEGFSDQFEQEITGC
CCCCHHHHHHHHHCC		14.5429967540
410PhosphorylationDQFEQEITGCGASSG
HHHHHHHHCCCCCCH		26.1830576142
415PhosphorylationEITGCGASSGALRSY
HHHCCCCCCHHHHHH		18.0030576142
416UbiquitinationITGCGASSGALRSYQ
HHCCCCCCHHHHHHH		27.7929967540
416PhosphorylationITGCGASSGALRSYQ
HHCCCCCCHHHHHHH		27.7930576142
425UbiquitinationALRSYQLWADNLKKG
HHHHHHHHHHHHHHC		6.0029967540
430UbiquitinationQLWADNLKKGGGALL
HHHHHHHHHCCCHHH		56.4829967540
431UbiquitinationLWADNLKKGGGALLH
HHHHHHHHCCCHHHH		66.9929967540
439PhosphorylationGGGALLHSVKAKTQP
CCCHHHHHHHHCCCH		25.8623401153
441UbiquitinationGALLHSVKAKTQPAV
CHHHHHHHHCCCHHH		47.3729967540
449UbiquitinationAKTQPAVKNMYRSAK
HCCCHHHHHHHHHHH		37.8029967540
460UbiquitinationRSAKSGLKGVQSLLM
HHHHHHCCHHHHHEE		61.6429967540
464PhosphorylationSGLKGVQSLLMYKDG
HHCCHHHHHEEEECC		22.5123401153
468PhosphorylationGVQSLLMYKDGDSVL
HHHHHEEEECCCCHH		13.0928111955
469UbiquitinationVQSLLMYKDGDSVLQ
HHHHEEEECCCCHHH		41.0729967540
473PhosphorylationLMYKDGDSVLQRGGS
EEEECCCCHHHCCCC		30.2026074081
477MethylationDGDSVLQRGGSLRAP
CCCCHHHCCCCCCCC		47.48-
480PhosphorylationSVLQRGGSLRAPALP
CHHHCCCCCCCCCCC		19.9423401153
512PhosphorylationKNRPLRPSRRRQLEE
CCCCCCHHHHHHHHC		31.8024719451
553PhosphorylationLDSSFLGSGEELDLL
HCCCCCCCHHHHHHH		45.2214702039
564UbiquitinationLDLLSEILDSLSMGA
HHHHHHHHHHHCCCC		3.0029967540
565UbiquitinationDLLSEILDSLSMGAK
HHHHHHHHHHCCCCC		53.8729967540
573PhosphorylationSLSMGAKSAGSLRPS
HHCCCCCCCCCCCCC		37.0123684312
576PhosphorylationMGAKSAGSLRPSQSL
CCCCCCCCCCCCCCC		22.4128450419
580PhosphorylationSAGSLRPSQSLDCCH
CCCCCCCCCCCCCCC		26.4328450419
582PhosphorylationGSLRPSQSLDCCHRG
CCCCCCCCCCCCCCC		30.4323401153
593PhosphorylationCHRGDLDSCFSLPNI
CCCCCHHHHCCCCCC		25.1023401153
596PhosphorylationGDLDSCFSLPNIPRW
CCHHHHCCCCCCCCC		47.4423401153
608UbiquitinationPRWQPDDKKLPEPEP
CCCCCCCCCCCCCCC		64.6929967540
609UbiquitinationRWQPDDKKLPEPEPQ
CCCCCCCCCCCCCCC		76.0329967540
619PhosphorylationEPEPQPLSLPSLQNA
CCCCCCCCCCCCCCC		44.9426657352
622PhosphorylationPQPLSLPSLQNASSL
CCCCCCCCCCCCCCC		48.1328450419
627PhosphorylationLPSLQNASSLDATSS
CCCCCCCCCCCCCCC		38.7027080861
628PhosphorylationPSLQNASSLDATSSS
CCCCCCCCCCCCCCC		28.0527080861
640PhosphorylationSSSKDSRSQLIPSES
CCCCCHHHHCCCCCC		33.0326434776
645PhosphorylationSRSQLIPSESDQEVT
HHHHCCCCCCCCCCC		42.6226434776
647PhosphorylationSQLIPSESDQEVTSP
HHCCCCCCCCCCCCC		49.2726434776
652PhosphorylationSESDQEVTSPSQSST
CCCCCCCCCCCCCCC		33.8826434776
653PhosphorylationESDQEVTSPSQSSTA
CCCCCCCCCCCCCCC		27.9426434776
655PhosphorylationDQEVTSPSQSSTASA
CCCCCCCCCCCCCCC		42.3226434776
657PhosphorylationEVTSPSQSSTASADP
CCCCCCCCCCCCCCH		33.7126434776
658PhosphorylationVTSPSQSSTASADPS
CCCCCCCCCCCCCHH		21.9826434776
659PhosphorylationTSPSQSSTASADPSI
CCCCCCCCCCCCHHH		29.8526434776
661PhosphorylationPSQSSTASADPSIWG
CCCCCCCCCCHHHCC		33.0426434776
665PhosphorylationSTASADPSIWGDPKP
CCCCCCHHHCCCCCC		31.3626434776
700PhosphorylationSTAQENPTPWLSTAP
CCCCCCCCCCCCCCC		38.3826074081
704PhosphorylationENPTPWLSTAPTEPS
CCCCCCCCCCCCCCC		20.7526074081
705PhosphorylationNPTPWLSTAPTEPSP
CCCCCCCCCCCCCCC		34.1926074081
708PhosphorylationPWLSTAPTEPSPPES
CCCCCCCCCCCCCCC		59.0526074081
711PhosphorylationSTAPTEPSPPESPQI
CCCCCCCCCCCCCCC		47.0226074081
715PhosphorylationTEPSPPESPQILAPT
CCCCCCCCCCCCCCC		28.0726074081
722PhosphorylationSPQILAPTKPNFDIA
CCCCCCCCCCCCEEE		54.2326074081
784PhosphorylationPTSNCQKSQPSSRPR
CCCCCCCCCCCCCCC		22.8027174698
787PhosphorylationNCQKSQPSSRPRVAD
CCCCCCCCCCCCHHH		31.2027174698
788PhosphorylationCQKSQPSSRPRVADL
CCCCCCCCCCCHHHH		53.6527174698
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 DEN1C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEN1C_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 DEN1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 DEN1C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.

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