CXXC1_HUMAN - dbPTM
CXXC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CXXC1_HUMAN
UniProt AC Q9P0U4
Protein Name CXXC-type zinc finger protein 1
Gene Name CXXC1
Organism Homo sapiens (Human).
Sequence Length 656
Subcellular Localization Nucleus speckle . Associated with euchromatin. During mitosis, excluded from condensed chromosomes.
Protein Description Transcriptional activator that exhibits a unique DNA binding specificity for CpG unmethylated motifs with a preference for CpGG..
Protein Sequence MEGDGSDPEPPDAGEDSKSENGENAPIYCICRKPDINCFMIGCDNCNEWFHGDCIRITEKMAKAIREWYCRECREKDPKLEIRYRHKKSRERDGNERDSSEPRDEGGGRKRPVPDPDLQRRAGSGTGVGAMLARGSASPHKSSPQPLVATPSQHHQQQQQQIKRSARMCGECEACRRTEDCGHCDFCRDMKKFGGPNKIRQKCRLRQCQLRARESYKYFPSSLSPVTPSESLPRPRRPLPTQQQPQPSQKLGRIREDEGAVASSTVKEPPEATATPEPLSDEDLPLDPDLYQDFCAGAFDDHGLPWMSDTEESPFLDPALRKRAVKVKHVKRREKKSEKKKEERYKRHRQKQKHKDKWKHPERADAKDPASLPQCLGPGCVRPAQPSSKYCSDDCGMKLAANRIYEILPQRIQQWQQSPCIAEEHGKKLLERIRREQQSARTRLQEMERRFHELEAIILRAKQQAVREDEESNEGDSDDTDLQIFCVSCGHPINPRVALRHMERCYAKYESQTSFGSMYPTRIEGATRLFCDVYNPQSKTYCKRLQVLCPEHSRDPKVPADEVCGCPLVRDVFELTGDFCRLPKRQCNRHYCWEKLRRAEVDLERVRVWYKLDELFEQERNVRTAMTNRAGLLALMLHQTIQHDPLTTDLRSSADR
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
1Acetylation-------MEGDGSDP
-------CCCCCCCC		13.5021406692
6Phosphorylation--MEGDGSDPEPPDA
--CCCCCCCCCCCCC		55.5228355574
17PhosphorylationPPDAGEDSKSENGEN
CCCCCCCCCCCCCCC		33.5026074081
19PhosphorylationDAGEDSKSENGENAP
CCCCCCCCCCCCCCC		40.0020164059
28PhosphorylationNGENAPIYCICRKPD
CCCCCCEEEEECCCC		3.7626074081
63AcetylationRITEKMAKAIREWYC
HHHHHHHHHHHHHHH		40.6319608861
110UbiquitinationRDEGGGRKRPVPDPD
CCCCCCCCCCCCCHH		65.4129967540
124PhosphorylationDLQRRAGSGTGVGAM
HHHHHCCCCCCHHHH		32.0021815630
125UbiquitinationLQRRAGSGTGVGAML
HHHHCCCCCCHHHHH		26.1024816145
126PhosphorylationQRRAGSGTGVGAMLA
HHHCCCCCCHHHHHH		30.3221406692
131SulfoxidationSGTGVGAMLARGSAS
CCCCHHHHHHCCCCC		2.1821406390
136PhosphorylationGAMLARGSASPHKSS
HHHHHCCCCCCCCCC		21.7428152594
138PhosphorylationMLARGSASPHKSSPQ
HHHCCCCCCCCCCCC		29.2723927012
142PhosphorylationGSASPHKSSPQPLVA
CCCCCCCCCCCCCCC		44.1923927012
143PhosphorylationSASPHKSSPQPLVAT
CCCCCCCCCCCCCCC		32.1523927012
150PhosphorylationSPQPLVATPSQHHQQ
CCCCCCCCCCHHHHH		18.9223927012
152PhosphorylationQPLVATPSQHHQQQQ
CCCCCCCCHHHHHHH		37.4823401153
163MethylationQQQQQQIKRSARMCG
HHHHHHHHHHHHHHH		35.64-
163UbiquitinationQQQQQQIKRSARMCG
HHHHHHHHHHHHHHH		35.6429967540
198AcetylationKKFGGPNKIRQKCRL
HHHCCCHHHHHHHHH		42.2625953088
215PhosphorylationCQLRARESYKYFPSS
HHHHHHHHHHCCCCC		22.7523312004
216PhosphorylationQLRARESYKYFPSSL
HHHHHHHHHCCCCCC		12.6423312004
218PhosphorylationRARESYKYFPSSLSP
HHHHHHHCCCCCCCC		16.7021712546
221PhosphorylationESYKYFPSSLSPVTP
HHHHCCCCCCCCCCC		33.7323401153
222PhosphorylationSYKYFPSSLSPVTPS
HHHCCCCCCCCCCCC		32.8630266825
224PhosphorylationKYFPSSLSPVTPSES
HCCCCCCCCCCCCCC		21.1930266825
227PhosphorylationPSSLSPVTPSESLPR
CCCCCCCCCCCCCCC		25.2025159151
229PhosphorylationSLSPVTPSESLPRPR
CCCCCCCCCCCCCCC		30.3721712546
231PhosphorylationSPVTPSESLPRPRRP
CCCCCCCCCCCCCCC		48.2721712546
248PhosphorylationTQQQPQPSQKLGRIR
CCCCCCCCHHHCCCC		34.4028555341
250SumoylationQQPQPSQKLGRIRED
CCCCCCHHHCCCCCC		58.19-
250SumoylationQQPQPSQKLGRIRED
CCCCCCHHHCCCCCC		58.1928112733
250UbiquitinationQQPQPSQKLGRIRED
CCCCCCHHHCCCCCC		58.1924816145
250AcetylationQQPQPSQKLGRIRED
CCCCCCHHHCCCCCC		58.1923954790
263PhosphorylationEDEGAVASSTVKEPP
CCCCCCCCCCCCCCC		21.6829514088
264PhosphorylationDEGAVASSTVKEPPE
CCCCCCCCCCCCCCC		27.7330108239
265PhosphorylationEGAVASSTVKEPPEA
CCCCCCCCCCCCCCC		32.8530108239
308PhosphorylationDHGLPWMSDTEESPF
CCCCCCCCCCCCCCC		37.2026074081
310PhosphorylationGLPWMSDTEESPFLD
CCCCCCCCCCCCCCC		34.0526074081
328MethylationRKRAVKVKHVKRREK
HHHHHHHHHHHHHHH		36.64-
359UbiquitinationQKHKDKWKHPERADA
HHHHHHCCCHHHCCC		55.8329967540
363UbiquitinationDKWKHPERADAKDPA
HHCCCHHHCCCCCCC		42.0729967540
367AcetylationHPERADAKDPASLPQ
CHHHCCCCCCCCCCC		65.8726051181
367UbiquitinationHPERADAKDPASLPQ
CHHHCCCCCCCCCCC		65.8729967540
371 (in isoform 2)Ubiquitination-46.07-
371UbiquitinationADAKDPASLPQCLGP
CCCCCCCCCCCHHCC		46.0729967540
398UbiquitinationCSDDCGMKLAANRIY
CCCCCCCHHHHHHHH		21.9129967540
402 (in isoform 2)Ubiquitination-25.85-
402UbiquitinationCGMKLAANRIYEILP
CCCHHHHHHHHHHHH		25.8529967540
403MethylationGMKLAANRIYEILPQ
CCHHHHHHHHHHHHH		28.30-
405PhosphorylationKLAANRIYEILPQRI
HHHHHHHHHHHHHHH		8.1528796482
409PhosphorylationNRIYEILPQRIQQWQ
HHHHHHHHHHHHHHH		27.3727642862
418PhosphorylationRIQQWQQSPCIAEEH
HHHHHHHCCCHHHHH		13.4628555341
427UbiquitinationCIAEEHGKKLLERIR
CHHHHHHHHHHHHHH		42.0029967540
427AcetylationCIAEEHGKKLLERIR
CHHHHHHHHHHHHHH		42.0026051181
431UbiquitinationEHGKKLLERIRREQQ
HHHHHHHHHHHHHHH		57.4029967540
431 (in isoform 2)Ubiquitination-57.40-
432 (in isoform 2)Ubiquitination-27.90-
462UbiquitinationEAIILRAKQQAVRED
HHHHHHHHHHHHHCC		36.19-
466 (in isoform 2)Ubiquitination-6.31-
508UbiquitinationHMERCYAKYESQTSF
HHHHHHHHHCCCCCC		24.07-
509PhosphorylationMERCYAKYESQTSFG
HHHHHHHHCCCCCCC		16.79-
511PhosphorylationRCYAKYESQTSFGSM
HHHHHHCCCCCCCCC		35.35-
512 (in isoform 2)Ubiquitination-29.26-
513PhosphorylationYAKYESQTSFGSMYP
HHHHCCCCCCCCCCC		34.9927080861
514PhosphorylationAKYESQTSFGSMYPT
HHHCCCCCCCCCCCC		21.7027080861
521PhosphorylationSFGSMYPTRIEGATR
CCCCCCCCCCCCCCE		27.13-
539UbiquitinationDVYNPQSKTYCKRLQ
CCCCCCCHHHHHHHH		37.9629967540
543 (in isoform 2)Ubiquitination-45.81-
543UbiquitinationPQSKTYCKRLQVLCP
CCCHHHHHHHHHHCC		45.8129967540
557UbiquitinationPEHSRDPKVPADEVC
CCCCCCCCCCHHHCC		66.2029967540
561 (in isoform 2)Ubiquitination-42.67-
561UbiquitinationRDPKVPADEVCGCPL
CCCCCCHHHCCCCCC		42.6729967540
595UbiquitinationNRHYCWEKLRRAEVD
CCHHHHHHHHHCCCC		23.85-
599 (in isoform 2)Ubiquitination-18.09-
611UbiquitinationERVRVWYKLDELFEQ
HHHHHHHHHHHHHHH		33.48-
615 (in isoform 2)Ubiquitination-5.97-
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 CXXC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CXXC1_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 CXXC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SET1A_HUMANSETD1Aphysical
18082152
KMT2A_HUMANKMT2Aphysical
18082152
KMT2D_HUMANKMT2Dphysical
18082152
SET1A_HUMANSETD1Aphysical
19433449
SET1B_HUMANSETD1Bphysical
19433449
RBBP5_HUMANRBBP5physical
19433449
WDR5_HUMANWDR5physical
19433449
ASH2L_HUMANASH2Lphysical
19433449
WDR82_HUMANWDR82physical
19433449
SET1A_HUMANSETD1Aphysical
16253997
RBBP5_HUMANRBBP5physical
16253997
MEP50_HUMANWDR77physical
16253997
ASH2L_HUMANASH2Lphysical
16253997
WDR5_HUMANWDR5physical
16253997
H32_HUMANHIST2H3Cphysical
18082152
KIFC1_HUMANKIFC1physical
18082152
MEN1_HUMANMEN1physical
18082152
ASH2L_HUMANASH2Lphysical
18082152
WDR5_HUMANWDR5physical
18082152
RBBP5_HUMANRBBP5physical
18082152
DNMT1_HUMANDNMT1physical
18680430
SET1A_HUMANSETD1Aphysical
18680430
SET1B_HUMANSETD1Bphysical
18680430
ASH2L_HUMANASH2Lphysical
18680430
RBBP5_HUMANRBBP5physical
18680430
WDR5_HUMANWDR5physical
18680430
WDR82_HUMANWDR82physical
18680430
SET1A_HUMANSETD1Aphysical
17355966
SET1B_HUMANSETD1Bphysical
17355966
SET1B_HUMANSETD1Bphysical
22939629
SET1A_HUMANSETD1Aphysical
19410543
ASH2L_HUMANASH2Lphysical
19410543
RBBP5_HUMANRBBP5physical
19410543
WDR5_HUMANWDR5physical
19410543
WDR82_HUMANWDR82physical
19410543
ASH2L_HUMANASH2Lphysical
23870121
RBBP5_HUMANRBBP5physical
23870121
WDR5_HUMANWDR5physical
23870121
SET1A_HUMANSETD1Aphysical
23870121
SET1B_HUMANSETD1Bphysical
23870121
DPY30_HUMANDPY30physical
23870121
WDR82_HUMANWDR82physical
23870121
HCFC1_HUMANHCFC1physical
23870121
EP300_HUMANEP300physical
23870121
P53_HUMANTP53physical
23870121
HCFC1_HUMANHCFC1physical
26496610
RBBP5_HUMANRBBP5physical
26496610
RING2_HUMANRNF2physical
26496610
ASH2L_HUMANASH2Lphysical
26496610
K2C75_HUMANKRT75physical
26496610
SET1A_HUMANSETD1Aphysical
26496610
WDR5_HUMANWDR5physical
26496610
SET1B_HUMANSETD1Bphysical
26496610
DPY30_HUMANDPY30physical
26496610
BOD1_HUMANBOD1physical
26496610
BD1L1_HUMANBOD1L1physical
26496610
SET1B_HUMANSETD1Bphysical
28514442
SET1A_HUMANSETD1Aphysical
28514442
BOD1_HUMANBOD1physical
28514442
BD1L1_HUMANBOD1L1physical
28514442
ASH2L_HUMANASH2Lphysical
28514442
RBBP5_HUMANRBBP5physical
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 CXXC1_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-63, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND THR-227, ANDMASS SPECTROMETRY.

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