ZN622_HUMAN - dbPTM
ZN622_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN622_HUMAN
UniProt AC Q969S3
Protein Name Zinc finger protein 622
Gene Name ZNF622
Organism Homo sapiens (Human).
Sequence Length 477
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May behave as an activator of the bound transcription factor, MYBL2, and be involved in embryonic development..
Protein Sequence MATYTCITCRVAFRDADMQRAHYKTDWHRYNLRRKVASMAPVTAEGFQERVRAQRAVAEEESKGSATYCTVCSKKFASFNAYENHLKSRRHVELEKKAVQAVNRKVEMMNEKNLEKGLGVDSVDKDAMNAAIQQAIKAQPSMSPKKAPPAPAKEARNVVAVGTGGRGTHDRDPSEKPPRLQWFEQQAKKLAKQQEEDSEEEEEDLDGDDWEDIDSDEELECEDTEAMDDVVEQDAEEEEAEEGPPLGAIPITDCLFCSHHSSSLMKNVAHMTKDHSFFIPDIEYLSDIKGLIKYLGEKVGVGKICLWCNEKGKSFYSTEAVQAHMNDKSHCKLFTDGDAALEFADFYDFRSSYPDHKEGEDPNKAEELPSEKNLEYDDETMELILPSGARVGHRSLMRYYKQRFGLSRAVAVAKNRKAVGRVLQQYRALGWTGSTGAALMRERDMQYVQRMKSKWMLKTGMKNNATKQMHFRVQVRF
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
2Acetylation------MATYTCITC
------CCCEEEEEE		14.8722223895
24UbiquitinationDMQRAHYKTDWHRYN
HHHHHHHCCCHHHHH		30.0929967540
35UbiquitinationHRYNLRRKVASMAPV
HHHHHHHHHHHCCCC		35.4024816145
39SulfoxidationLRRKVASMAPVTAEG
HHHHHHHCCCCCHHH		3.3521406390
52MethylationEGFQERVRAQRAVAE
HHHHHHHHHHHHHHH		31.09115920537
63UbiquitinationAVAEEESKGSATYCT
HHHHHHHCCCCEEEE		61.2333845483
68PhosphorylationESKGSATYCTVCSKK
HHCCCCEEEEECCHH		5.95-
74UbiquitinationTYCTVCSKKFASFNA
EEEEECCHHCCCCCH		46.9422817900
74AcetylationTYCTVCSKKFASFNA
EEEEECCHHCCCCCH		46.9426051181
75UbiquitinationYCTVCSKKFASFNAY
EEEECCHHCCCCCHH		29.8422817900
78PhosphorylationVCSKKFASFNAYENH
ECCHHCCCCCHHHHH		23.3625159151
87UbiquitinationNAYENHLKSRRHVEL
CHHHHHHHHHHCHHH		34.0729967540
962-HydroxyisobutyrylationRRHVELEKKAVQAVN
HHCHHHHHHHHHHHH		59.67-
97UbiquitinationRHVELEKKAVQAVNR
HCHHHHHHHHHHHHH		44.4027667366
105SumoylationAVQAVNRKVEMMNEK
HHHHHHHHHHHHHHH		37.03-
105SumoylationAVQAVNRKVEMMNEK
HHHHHHHHHHHHHHH		37.03-
105UbiquitinationAVQAVNRKVEMMNEK
HHHHHHHHHHHHHHH		37.0329967540
112AcetylationKVEMMNEKNLEKGLG
HHHHHHHHHHHCCCC		62.9226051181
112UbiquitinationKVEMMNEKNLEKGLG
HHHHHHHHHHHCCCC		62.9222817900
116UbiquitinationMNEKNLEKGLGVDSV
HHHHHHHCCCCCCCC		63.7022817900
122PhosphorylationEKGLGVDSVDKDAMN
HCCCCCCCCCHHHHH		29.7921815630
125AcetylationLGVDSVDKDAMNAAI
CCCCCCCHHHHHHHH		45.2726051181
125UbiquitinationLGVDSVDKDAMNAAI
CCCCCCCHHHHHHHH		45.2721906983
128SulfoxidationDSVDKDAMNAAIQQA
CCCCHHHHHHHHHHH		5.1321406390
137UbiquitinationAAIQQAIKAQPSMSP
HHHHHHHHCCCCCCC		43.9429967540
141PhosphorylationQAIKAQPSMSPKKAP
HHHHCCCCCCCCCCC		21.5830266825
143PhosphorylationIKAQPSMSPKKAPPA
HHCCCCCCCCCCCCC		37.5923401153
153UbiquitinationKAPPAPAKEARNVVA
CCCCCCHHHHCCEEE		51.3429967540
163PhosphorylationRNVVAVGTGGRGTHD
CCEEEECCCCCCCCC		29.8425159151
166MethylationVAVGTGGRGTHDRDP
EEECCCCCCCCCCCC		48.45115368507
168PhosphorylationVGTGGRGTHDRDPSE
ECCCCCCCCCCCCCC		21.1723312004
174PhosphorylationGTHDRDPSEKPPRLQ
CCCCCCCCCCCCCHH		63.6430576142
176UbiquitinationHDRDPSEKPPRLQWF
CCCCCCCCCCCHHHH		65.7424816145
188AcetylationQWFEQQAKKLAKQQE
HHHHHHHHHHHHHHH		43.9425953088
273UbiquitinationKNVAHMTKDHSFFIP
HHHHHHHCCCCCCCC		45.9629967540
276PhosphorylationAHMTKDHSFFIPDIE
HHHHCCCCCCCCCHH		31.8025159151
284PhosphorylationFFIPDIEYLSDIKGL
CCCCCHHHHHCHHHH		16.3117360941
286PhosphorylationIPDIEYLSDIKGLIK
CCCHHHHHCHHHHHH		36.0724719451
289UbiquitinationIEYLSDIKGLIKYLG
HHHHHCHHHHHHHHH		53.2929967540
298UbiquitinationLIKYLGEKVGVGKIC
HHHHHHHHCCCCEEE		42.3529967540
311UbiquitinationICLWCNEKGKSFYST
EEEEECCCCCCEECH		58.61-
313UbiquitinationLWCNEKGKSFYSTEA
EEECCCCCCEECHHH		48.7529967540
314PhosphorylationWCNEKGKSFYSTEAV
EECCCCCCEECHHHH		37.7821771788
318PhosphorylationKGKSFYSTEAVQAHM
CCCCEECHHHHHHHC		19.3121771788
328UbiquitinationVQAHMNDKSHCKLFT
HHHHCCCCCCCEEEC		36.7829967540
347PhosphorylationALEFADFYDFRSSYP
HHHHHHHHCHHHHCC		18.08-
351PhosphorylationADFYDFRSSYPDHKE
HHHHCHHHHCCCCCC		33.93-
352PhosphorylationDFYDFRSSYPDHKEG
HHHCHHHHCCCCCCC		36.11-
353PhosphorylationFYDFRSSYPDHKEGE
HHCHHHHCCCCCCCC		17.58-
357UbiquitinationRSSYPDHKEGEDPNK
HHHCCCCCCCCCCCC		74.8529967540
364UbiquitinationKEGEDPNKAEELPSE
CCCCCCCCHHCCCCC		63.6633845483
370PhosphorylationNKAEELPSEKNLEYD
CCHHCCCCCCCCCCC		74.0528985074
372UbiquitinationAEELPSEKNLEYDDE
HHCCCCCCCCCCCHH		71.7829967540
407PhosphorylationYKQRFGLSRAVAVAK
HHHHHCCHHHHHHHH		20.69-
414UbiquitinationSRAVAVAKNRKAVGR
HHHHHHHHCHHHHHH		51.1629967540
426PhosphorylationVGRVLQQYRALGWTG
HHHHHHHHHHHCCCC		5.72-
432PhosphorylationQYRALGWTGSTGAAL
HHHHHCCCCCHHHHH		21.32-
434PhosphorylationRALGWTGSTGAALMR
HHHCCCCCHHHHHHH		19.12-
435PhosphorylationALGWTGSTGAALMRE
HHCCCCCHHHHHHHH		31.98-
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
314SPhosphorylationKinaseMAP3K5Q99683
GPS
318TPhosphorylationKinaseMAP3K5Q99683
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN622_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 ZN622_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYBB_HUMANMYBL2physical
12645566
MELK_HUMANMELKphysical
11802789
ZN622_HUMANZNF622physical
11802789
A4_HUMANAPPphysical
21832049
AGAL_HUMANGLAphysical
22863883
UBFD1_HUMANUBFD1physical
22863883
DJC21_HUMANDNAJC21physical
24778252
IF6_HUMANEIF6physical
24778252
UFL1_HUMANUFL1physical
24778252
LSG1_HUMANLSG1physical
24778252
MMTA2_HUMANC1orf35physical
24778252
NMD3_HUMANNMD3physical
24778252
NOC3L_HUMANNOC3Lphysical
24778252
POP1_HUMANPOP1physical
24778252
STAU1_HUMANSTAU1physical
24778252
HECD1_HUMANHECTD1physical
24778252
SPB1_HUMANFTSJ3physical
24778252
BRX1_HUMANBRIX1physical
24778252
KRR1_HUMANKRR1physical
24778252
MRT4_HUMANMRTO4physical
26344197
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 ZN622_HUMAN

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Related Literatures of Post-Translational Modification
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-276, AND MASSSPECTROMETRY.

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