MCF2L_HUMAN - dbPTM
MCF2L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCF2L_HUMAN
UniProt AC O15068
Protein Name Guanine nucleotide exchange factor DBS
Gene Name MCF2L
Organism Homo sapiens (Human).
Sequence Length 1137
Subcellular Localization Isoform 5: Cytoplasm . Cell membrane
Peripheral membrane protein
Cytoplasmic side .
Isoform 3: Cytoplasm . Endomembrane system . Interaction with membranes enriched in phosphoinositides is mediated by the CRAL-TRIO domain.
Cytoplasm . Cell memb
Protein Description Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity). Isoform 5 activates CDC42. [PubMed: 15157669; Isoform 3: Does not catalyze guanine nucleotide exchange on CDC42]
Protein Sequence MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEATAMATDEIMHQDIVPLCAADIQDQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRRDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDDFKMKVPVIMLSSVPDLHGYIDKSQLTEDLGGTLDYCHSRWLCQRTAIESFALMVKQTAQMLQSFGTELAETELPNDVQSTSSVLCAHTEKKDKAKEDLRLALKEGHSVLESLRELQAEGSEPSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGFREVKAILDAASQKIATFTDIGNSLAHVEHLLRDLASFEEKSGVAVERARALSLDGEQLIGNKHYAVDSIRPKCQELRHLCDQFSAEIARRRGLLSKSLELHRRLETSMKWCDEGIYLLASQPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNAIYKEYESILNQDLMEHVRKVFQKQASMEEVFHRRQASLKKLAARQTRPVQPVAPRPEALAKSPCPSPGIRRGSENSSSEGGALRRGPYRRAKSEMSESRQGRGSAGEEEESLAILRRHVMSELLDTERAYVEELLCVLEGYAAEMDNPLMAHLLSTGLHNKKDVLFGNMEEIYHFHNRIFLRELENYTDCPELVGRCFLERMEDFQIYEKYCQNKPRSESLWRQCSDCPFFQECQRKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSRNCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKRGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMAAVGITENVKGDAKKFEIWYNAREEVYIVQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSQSLPLPAPTSTSPSRGNSRNIKKLEERKTDPLSLEGYVSSAPLTKPPEKGKGWSKTSHSLEAPEDDGGWSSAEEQINSSDAEEDGGLGPKKLVPGKYTVVADHEKGGPDALRVRSGDVVELVQEGDEGLWYVRDPTTGKEGWVPASSLSVRLGPSGSAQCLSSSGKAHVPRAHP
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
7 (in isoform 6)Phosphorylation-1.8529083192
7 (in isoform 9)Phosphorylation-1.8529083192
10 (in isoform 2)Phosphorylation-2.7626434776
13 (in isoform 2)Phosphorylation-35.7426434776
16 (in isoform 3)Phosphorylation-51.3821964256
17 (in isoform 2)Phosphorylation-28.2626434776
21 (in isoform 2)Phosphorylation-28.4126434776
24 (in isoform 3)Phosphorylation-37.45-
96PhosphorylationQDGSPVITFPDYPAF
CCCCCCEECCCCCCH		29.37-
114UbiquitinationPDKEFQNVMTYLTSI
CCHHHHHHHHHHHCC		1.7921890473
116PhosphorylationKEFQNVMTYLTSIPS
HHHHHHHHHHHCCCH		15.8824043423
117PhosphorylationEFQNVMTYLTSIPSL
HHHHHHHHHHCCCHH		7.0124043423
119PhosphorylationQNVMTYLTSIPSLQD
HHHHHHHHCCCHHHH		17.7524043423
120PhosphorylationNVMTYLTSIPSLQDA
HHHHHHHCCCHHHHC		29.8824043423
123PhosphorylationTYLTSIPSLQDAGIG
HHHHCCCHHHHCCCE		36.6724043423
123UbiquitinationTYLTSIPSLQDAGIG
HHHHCCCHHHHCCCE		36.6721890473
134UbiquitinationAGIGFILVIDRRRDK
CCCEEEEEEECCCCC		3.5121890473
141UbiquitinationVIDRRRDKWTSVKAS
EEECCCCCCHHHHHH		51.0322817900
150UbiquitinationTSVKASVLRIAASFP
HHHHHHHHHHHHCCC		2.8021890473
150 (in isoform 4)Ubiquitination-2.8021890473
152UbiquitinationVKASVLRIAASFPAN
HHHHHHHHHHCCCCC		3.0821890473
152 (in isoform 6)Ubiquitination-3.0821890473
156UbiquitinationVLRIAASFPANLQLV
HHHHHHCCCCCEEEE		5.9321890473
156 (in isoform 3)Ubiquitination-5.9321890473
158UbiquitinationRIAASFPANLQLVLV
HHHHCCCCCEEEEEE		27.6221890473
158 (in isoform 8)Ubiquitination-27.6221890473
161UbiquitinationASFPANLQLVLVLRP
HCCCCCEEEEEEECC		29.3622817900
177PhosphorylationGFFQRTLSDIAFKFN
CCHHHHHHHHHHHCC		26.76-
177UbiquitinationGFFQRTLSDIAFKFN
CCHHHHHHHHHHHCC		26.7622817900
179UbiquitinationFQRTLSDIAFKFNRD
HHHHHHHHHHHCCHH		4.3322817900
182UbiquitinationTLSDIAFKFNRDDFK
HHHHHHHHCCHHHHC		32.4821890473
182UbiquitinationTLSDIAFKFNRDDFK
HHHHHHHHCCHHHHC		32.4821890473
182UbiquitinationTLSDIAFKFNRDDFK
HHHHHHHHCCHHHHC		32.4821890473
182 (in isoform 1)Ubiquitination-32.4821890473
183UbiquitinationLSDIAFKFNRDDFKM
HHHHHHHCCHHHHCC		7.9722817900
185UbiquitinationDIAFKFNRDDFKMKV
HHHHHCCHHHHCCCC		48.2722817900
209UbiquitinationDLHGYIDKSQLTEDL
CCCCCCCHHHCCCCC		30.4621890473
209 (in isoform 2)Ubiquitination-30.4621890473
222PhosphorylationDLGGTLDYCHSRWLC
CCCCCHHHHHHHHHH		8.65-
232PhosphorylationSRWLCQRTAIESFAL
HHHHHHHHHHHHHHH		13.2022210691
236PhosphorylationCQRTAIESFALMVKQ
HHHHHHHHHHHHHHH		15.0922210691
236UbiquitinationCQRTAIESFALMVKQ
HHHHHHHHHHHHHHH		15.0922817900
250PhosphorylationQTAQMLQSFGTELAE
HHHHHHHHHCHHHHH		22.9822210691
266PhosphorylationELPNDVQSTSSVLCA
CCCCCCHHCCHHEEC		30.0626074081
267PhosphorylationLPNDVQSTSSVLCAH
CCCCCHHCCHHEECC		14.1326074081
268PhosphorylationPNDVQSTSSVLCAHT
CCCCHHCCHHEECCC		24.5626074081
269PhosphorylationNDVQSTSSVLCAHTE
CCCHHCCHHEECCCC		21.1426074081
275PhosphorylationSSVLCAHTEKKDKAK
CHHEECCCCCHHHHH		30.8626074081
364UbiquitinationEQGFREVKAILDAAS
HHHHHHHHHHHHHHH		25.59-
366PhosphorylationGFREVKAILDAASQK
HHHHHHHHHHHHHCH		2.72-
371PhosphorylationKAILDAASQKIATFT
HHHHHHHHCHHEEEC		33.45-
382PhosphorylationATFTDIGNSLAHVEH
EEECHHHHHHHHHHH		33.90-
396PhosphorylationHLLRDLASFEEKSGV
HHHHHHHHHHHHHCH		40.2524719451
412PhosphorylationVERARALSLDGEQLI
HHHHHHHCCCHHHHC		24.3520873877
424UbiquitinationQLIGNKHYAVDSIRP
HHCCCCCHHHHHHHH		15.2129967540
426UbiquitinationIGNKHYAVDSIRPKC
CCCCCHHHHHHHHHH		4.7129967540
430UbiquitinationHYAVDSIRPKCQELR
CHHHHHHHHHHHHHH		28.6929967540
455PhosphorylationARRRGLLSKSLELHR
HHHCCCHHHHHHHHH		25.8224719451
457PhosphorylationRRGLLSKSLELHRRL
HCCCHHHHHHHHHHH		24.57-
480PhosphorylationEGIYLLASQPVDKCQ
HCEEEEECCCCCHHC		34.68-
542PhosphorylationKVFQKQASMEEVFHR
HHHHHHHCHHHHHHH		25.0028348404
548PhosphorylationASMEEVFHRRQASLK
HCHHHHHHHHHHHHH		29.23-
552PhosphorylationEVFHRRQASLKKLAA
HHHHHHHHHHHHHHH		18.28-
559PhosphorylationASLKKLAARQTRPVQ
HHHHHHHHCCCCCCC		17.98-
562PhosphorylationKKLAARQTRPVQPVA
HHHHHCCCCCCCCCC		31.2423312004
578PhosphorylationRPEALAKSPCPSPGI
CHHHHHCCCCCCCCC		26.5720873877
579PhosphorylationPEALAKSPCPSPGIR
HHHHHCCCCCCCCCC		33.07-
582PhosphorylationLAKSPCPSPGIRRGS
HHCCCCCCCCCCCCC		42.3420873877
589PhosphorylationSPGIRRGSENSSSEG
CCCCCCCCCCCCCCC		31.6223663014
590PhosphorylationPGIRRGSENSSSEGG
CCCCCCCCCCCCCCC		65.05-
592PhosphorylationIRRGSENSSSEGGAL
CCCCCCCCCCCCCCC		31.0528857561
593PhosphorylationRRGSENSSSEGGALR
CCCCCCCCCCCCCCC		43.9524702127
594PhosphorylationRGSENSSSEGGALRR
CCCCCCCCCCCCCCC		39.8323312004
608AcetylationRGPYRRAKSEMSESR
CCCCHHHHHHHCCCC		45.177976037
609PhosphorylationGPYRRAKSEMSESRQ
CCCHHHHHHHCCCCC		37.2326437602
612PhosphorylationRRAKSEMSESRQGRG
HHHHHHHCCCCCCCC		28.5028102081
620PhosphorylationESRQGRGSAGEEEES
CCCCCCCCCCCHHHH		31.5730266825
627PhosphorylationSAGEEEESLAILRRH
CCCCHHHHHHHHHHH		26.7827732954
699UbiquitinationHNRIFLRELENYTDC
HHHHHHHHHCCCCCC		63.6829967540
701UbiquitinationRIFLRELENYTDCPE
HHHHHHHCCCCCCHH		43.3629967540
705UbiquitinationRELENYTDCPELVGR
HHHCCCCCCHHHHHH		35.3029967540
736PhosphorylationQNKPRSESLWRQCSD
CCCCCCHHHHHHHCC		34.1824719451
762PhosphorylationDHKLSLDSYLLKPVQ
CCCCCCCHHHHHHHH		23.9924719451
763PhosphorylationHKLSLDSYLLKPVQR
CCCCCCHHHHHHHHH		18.7324719451
784PhosphorylationLLKEMLKYSRNCEGA
HHHHHHHHCCCCCCC		14.65-
785PhosphorylationLKEMLKYSRNCEGAE
HHHHHHHCCCCCCCH		18.54-
835PhosphorylationGKLLMQGSFSVWTDH
HHHHHHCCCEEECCC		9.4722210691
840PhosphorylationQGSFSVWTDHKRGHT
HCCCEEECCCCCCCH		26.5222210691
893PhosphorylationPSYSYKQSLNMAAVG
CCCCHHHHHCCEEEC		19.98-
902PhosphorylationNMAAVGITENVKGDA
CCEEECCCCCCCCCH		18.64-
935PhosphorylationPTPEIKAAWVNEIRK
CCHHHHHHHHHHHHH		13.02-
942PhosphorylationAWVNEIRKVLTSQLQ
HHHHHHHHHHHHHHH		47.4632142685
943PhosphorylationWVNEIRKVLTSQLQA
HHHHHHHHHHHHHHH		5.1833259812
944PhosphorylationVNEIRKVLTSQLQAC
HHHHHHHHHHHHHHH		4.2332142685
945PhosphorylationNEIRKVLTSQLQACR
HHHHHHHHHHHHHHH		19.8832142685
947PhosphorylationIRKVLTSQLQACREA
HHHHHHHHHHHHHHH		32.1532142685
948PhosphorylationRKVLTSQLQACREAS
HHHHHHHHHHHHHHH		3.3232142685
949PhosphorylationKVLTSQLQACREASQ
HHHHHHHHHHHHHHH		30.6833259812
951PhosphorylationLTSQLQACREASQHR
HHHHHHHHHHHHHHH		2.3232142685
962PhosphorylationSQHRALEQSQSLPLP
HHHHHHHHHCCCCCC		47.85-
963PhosphorylationQHRALEQSQSLPLPA
HHHHHHHHCCCCCCC		16.6222496350
965PhosphorylationRALEQSQSLPLPAPT
HHHHHHCCCCCCCCC		36.8819276368
972PhosphorylationSLPLPAPTSTSPSRG
CCCCCCCCCCCCCCC		46.9030278072
973PhosphorylationLPLPAPTSTSPSRGN
CCCCCCCCCCCCCCC		26.3130278072
974PhosphorylationPLPAPTSTSPSRGNS
CCCCCCCCCCCCCCC		47.3230278072
975PhosphorylationLPAPTSTSPSRGNSR
CCCCCCCCCCCCCCC		22.2030278072
977PhosphorylationAPTSTSPSRGNSRNI
CCCCCCCCCCCCCCH		53.2230278072
981PhosphorylationTSPSRGNSRNIKKLE
CCCCCCCCCCHHHHH		29.5424117733
992PhosphorylationKKLEERKTDPLSLEG
HHHHHCCCCCCCCCE		49.4225002506
996PhosphorylationERKTDPLSLEGYVSS
HCCCCCCCCCEEECC		29.7525002506
1000PhosphorylationDPLSLEGYVSSAPLT
CCCCCCEEECCCCCC		6.4323312004
1002PhosphorylationLSLEGYVSSAPLTKP
CCCCEEECCCCCCCC		16.5825002506
1003PhosphorylationSLEGYVSSAPLTKPP
CCCEEECCCCCCCCC		24.7025002506
1007PhosphorylationYVSSAPLTKPPEKGK
EECCCCCCCCCCCCC		40.21-
1019PhosphorylationKGKGWSKTSHSLEAP
CCCCCCCCCCCCCCC		26.5925954137
1033PhosphorylationPEDDGGWSSAEEQIN
CCCCCCCCCHHHHHC		23.9725921289
1034PhosphorylationEDDGGWSSAEEQINS
CCCCCCCCHHHHHCC		32.9425921289
1041PhosphorylationSAEEQINSSDAEEDG
CHHHHHCCCCCCCCC		31.0925954137
1042PhosphorylationAEEQINSSDAEEDGG
HHHHHCCCCCCCCCC		36.0325954137
1086 (in isoform 10)Phosphorylation-62.6727251275
1088 (in isoform 10)Phosphorylation-22.6027251275
1088 (in isoform 9)Phosphorylation-22.6027251275
1090 (in isoform 9)Phosphorylation-68.0227251275
1093 (in isoform 10)Phosphorylation-10.6327251275
1094 (in isoform 10)Phosphorylation-7.2227251275
1095 (in isoform 10)Phosphorylation-3.6527251275
1095 (in isoform 9)Phosphorylation-3.6527251275
1096 (in isoform 9)Phosphorylation-28.6127251275
1097 (in isoform 10)Phosphorylation-34.5527251275
1097 (in isoform 9)Phosphorylation-34.5527251275
1098 (in isoform 10)Phosphorylation-22.6927251275
1099 (in isoform 9)Phosphorylation-53.0927251275
1100 (in isoform 9)Phosphorylation-52.2027251275
1101 (in isoform 10)Phosphorylation-28.6127251275
1103 (in isoform 9)Phosphorylation-60.6827251275
1112PhosphorylationWVPASSLSVRLGPSG
EEEHHHEEEEECCCC		13.7224719451
1118PhosphorylationLSVRLGPSGSAQCLS
EEEEECCCCCCHHHH		43.5123312004
1120PhosphorylationVRLGPSGSAQCLSSS
EEECCCCCCHHHHCC		21.3623312004
1125PhosphorylationSGSAQCLSSSGKAHV
CCCCHHHHCCCCCCC		30.0423312004
1126PhosphorylationGSAQCLSSSGKAHVP
CCCHHHHCCCCCCCC		30.1123312004
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 MCF2L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCF2L_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 MCF2L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAC1_HUMANRAC1physical
14701795
CDC42_HUMANCDC42physical
14701795
CDC42_HUMANCDC42physical
11889037
RHOA_HUMANRHOAphysical
12006984
GBB1_HUMANGNB1physical
10518015
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 MCF2L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, AND MASSSPECTROMETRY.

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