ZNF24_HUMAN - dbPTM
ZNF24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF24_HUMAN
UniProt AC P17028
Protein Name Zinc finger protein 24
Gene Name ZNF24
Organism Homo sapiens (Human).
Sequence Length 368
Subcellular Localization Nucleus .
Protein Description Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence (By similarity). Has transcription repressor activity in vitro..
Protein Sequence MSAQSVEEDSILIIPTPDEEEKILRVKLEEDPDGEEGSSIPWNHLPDPEIFRQRFRQFGYQDSPGPREAVSQLRELCRLWLRPETHTKEQILELVVLEQFVAILPKELQTWVRDHHPENGEEAVTVLEDLESELDDPGQPVSLRRRKREVLVEDMVSQEEAQGLPSSELDAVENQLKWASWELHSLRHCDDDGRTENGALAPKQELPSALESHEVPGTLNMGVPQIFKYGETCFPKGRFERKRNPSRKKQHICDECGKHFSQGSALILHQRIHSGEKPYGCVECGKAFSRSSILVQHQRVHTGEKPYKCLECGKAFSQNSGLINHQRIHTGEKPYECVQCGKSYSQSSNLFRHQRRHNAEKLLNVVKV
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
2Phosphorylation------MSAQSVEED
------CCCCCCCCC		34.7129514088
5Phosphorylation---MSAQSVEEDSIL
---CCCCCCCCCCEE		31.0829514088
10PhosphorylationAQSVEEDSILIIPTP
CCCCCCCCEEEECCC		23.6725849741
16PhosphorylationDSILIIPTPDEEEKI
CCEEEECCCCHHHHE		32.7229514088
22UbiquitinationPTPDEEEKILRVKLE
CCCCHHHHEEEEEEE		50.7722817900
22SumoylationPTPDEEEKILRVKLE
CCCCHHHHEEEEEEE		50.7728112733
27SumoylationEEKILRVKLEEDPDG
HHHEEEEEEEECCCC		43.69-
27SumoylationEEKILRVKLEEDPDG
HHHEEEEEEEECCCC		43.6925114211
27UbiquitinationEEKILRVKLEEDPDG
HHHEEEEEEEECCCC		43.6922817900
38PhosphorylationDPDGEEGSSIPWNHL
CCCCCCCCCCCHHHC		28.5120068231
39PhosphorylationPDGEEGSSIPWNHLP
CCCCCCCCCCHHHCC		43.4525849741
56MethylationEIFRQRFRQFGYQDS
HHHHHHHHHHCCCCC		32.86115920413
63PhosphorylationRQFGYQDSPGPREAV
HHHCCCCCCCHHHHH		19.0721815630
125PhosphorylationENGEEAVTVLEDLES
CCCHHCCHHHHHHHH		26.8230624053
132PhosphorylationTVLEDLESELDDPGQ
HHHHHHHHHCCCCCC		51.2418669648
142PhosphorylationDDPGQPVSLRRRKRE
CCCCCCCCHHHHCHH		23.8820068231
147SumoylationPVSLRRRKREVLVED
CCCHHHHCHHHHHHH		51.6128112733
157PhosphorylationVLVEDMVSQEEAQGL
HHHHHHCCHHHHCCC		25.8227690223
166PhosphorylationEEAQGLPSSELDAVE
HHHCCCCHHHHHHHH		41.3027732954
167PhosphorylationEAQGLPSSELDAVEN
HHCCCCHHHHHHHHH		39.9927732954
177SumoylationDAVENQLKWASWELH
HHHHHHHHHHHHHHH		30.8328112733
180PhosphorylationENQLKWASWELHSLR
HHHHHHHHHHHHHCC		21.7028450419
185PhosphorylationWASWELHSLRHCDDD
HHHHHHHHCCCCCCC		39.4623186163
195PhosphorylationHCDDDGRTENGALAP
CCCCCCCCCCCCCCC		39.05-
203SumoylationENGALAPKQELPSAL
CCCCCCCCCCCCHHH		51.28-
236SumoylationYGETCFPKGRFERKR
CCCCCCCCCCCCCCC		42.3328112733
236UbiquitinationYGETCFPKGRFERKR
CCCCCCCCCCCCCCC		42.3329967540
236SumoylationYGETCFPKGRFERKR
CCCCCCCCCCCCCCC		42.33-
261PhosphorylationDECGKHFSQGSALIL
HHHHHCCCCCCCEEE		33.0917525332
264PhosphorylationGKHFSQGSALILHQR
HHCCCCCCCEEEEEC		16.5628555341
271MethylationSALILHQRIHSGEKP
CCEEEEECCCCCCCC		20.17115920409
274PhosphorylationILHQRIHSGEKPYGC
EEEECCCCCCCCCCE		46.4025159151
277SumoylationQRIHSGEKPYGCVEC
ECCCCCCCCCCEEEC		47.2528112733
277SumoylationQRIHSGEKPYGCVEC
ECCCCCCCCCCEEEC		47.25-
277AcetylationQRIHSGEKPYGCVEC
ECCCCCCCCCCEEEC		47.2525953088
279PhosphorylationIHSGEKPYGCVECGK
CCCCCCCCCEEECCC		33.9428152594
286SumoylationYGCVECGKAFSRSSI
CCEEECCCCCCCCEE		58.90-
286UbiquitinationYGCVECGKAFSRSSI
CCEEECCCCCCCCEE		58.90-
286SumoylationYGCVECGKAFSRSSI
CCEEECCCCCCCCEE		58.9028112733
289PhosphorylationVECGKAFSRSSILVQ
EECCCCCCCCEEEEE		35.7923186163
291PhosphorylationCGKAFSRSSILVQHQ
CCCCCCCCEEEEEEC		22.1123401153
292PhosphorylationGKAFSRSSILVQHQR
CCCCCCCEEEEEECE		20.8730266825
302PhosphorylationVQHQRVHTGEKPYKC
EEECEECCCCCCEEE		44.1529496963
305SumoylationQRVHTGEKPYKCLEC
CEECCCCCCEEEECC		55.80-
305UbiquitinationQRVHTGEKPYKCLEC
CEECCCCCCEEEECC		55.80-
305SumoylationQRVHTGEKPYKCLEC
CEECCCCCCEEEECC		55.80-
308SumoylationHTGEKPYKCLECGKA
CCCCCCEEEECCCCC		40.65-
308SumoylationHTGEKPYKCLECGKA
CCCCCCEEEECCCCC		40.65-
308UbiquitinationHTGEKPYKCLECGKA
CCCCCCEEEECCCCC		40.65-
314SumoylationYKCLECGKAFSQNSG
EEEECCCCCHHCCCC		58.90-
314SumoylationYKCLECGKAFSQNSG
EEEECCCCCHHCCCC		58.90-
317PhosphorylationLECGKAFSQNSGLIN
ECCCCCHHCCCCCCC		33.0625159151
320PhosphorylationGKAFSQNSGLINHQR
CCCHHCCCCCCCCCE		27.6027174698
330PhosphorylationINHQRIHTGEKPYEC
CCCCEEECCCCCEEE		44.6727273156
333UbiquitinationQRIHTGEKPYECVQC
CEEECCCCCEEEEEC		55.0029967540
333SumoylationQRIHTGEKPYECVQC
CEEECCCCCEEEEEC		55.00-
333AcetylationQRIHTGEKPYECVQC
CEEECCCCCEEEEEC		55.0026051181
333SumoylationQRIHTGEKPYECVQC
CEEECCCCCEEEEEC		55.00-
335PhosphorylationIHTGEKPYECVQCGK
EECCCCCEEEEECCC		32.7825218447
342SumoylationYECVQCGKSYSQSSN
EEEEECCCCCCCCCC		54.57-
342SumoylationYECVQCGKSYSQSSN
EEEEECCCCCCCCCC		54.57-
343PhosphorylationECVQCGKSYSQSSNL
EEEECCCCCCCCCCH		18.4627080861
344PhosphorylationCVQCGKSYSQSSNLF
EEECCCCCCCCCCHH		17.7627080861
345PhosphorylationVQCGKSYSQSSNLFR
EECCCCCCCCCCHHH		30.5827080861
347PhosphorylationCGKSYSQSSNLFRHQ
CCCCCCCCCCHHHHH		18.4327080861
348PhosphorylationGKSYSQSSNLFRHQR
CCCCCCCCCHHHHHH		29.8927080861
361AcetylationQRRHNAEKLLNVVKV
HHHHCHHHHHHCCCC		56.7325953088
361MethylationQRRHNAEKLLNVVKV
HHHHCHHHHHHCCCC		56.7323644510
361SumoylationQRRHNAEKLLNVVKV
HHHHCHHHHHHCCCC		56.73-
361SumoylationQRRHNAEKLLNVVKV
HHHHCHHHHHHCCCC		56.7328112733
367SumoylationEKLLNVVKV------
HHHHHCCCC------		37.63-
367UbiquitinationEKLLNVVKV------
HHHHHCCCC------		37.63-
367SumoylationEKLLNVVKV------
HHHHHCCCC------		37.6328112733
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 ZNF24_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF24_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 ZNF24_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN174_HUMANZNF174physical
10567577
CC130_HUMANCCDC130physical
16189514
ZN446_HUMANZNF446physical
16189514
ZSC32_HUMANZSCAN32physical
16189514
SCND1_HUMANSCAND1physical
16189514
APLP1_HUMANAPLP1physical
16169070
ERG28_HUMANC14orf1physical
16169070
CSN6_HUMANCOPS6physical
16169070
HAP1_HUMANHAP1physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
SETB1_HUMANSETDB1physical
16169070
RBM48_HUMANRBM48physical
16169070
KAT5_HUMANKAT5physical
16169070
CE126_HUMANKIAA1377physical
16169070
LRIF1_HUMANLRIF1physical
16169070
U119A_HUMANUNC119physical
16169070
ZBT16_HUMANZBTB16physical
16169070
DPYL1_HUMANCRMP1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
P53_HUMANTP53physical
16169070
TRI25_HUMANTRIM25physical
20211142
ZNHI3_HUMANZNHIT3physical
20211142
HMGB1_HUMANHMGB1physical
20195357
SEC62_HUMANSEC62physical
20195357
ZSC21_HUMANZSCAN21physical
25416956
DZIP3_HUMANDZIP3physical
25416956
TCAF1_HUMANFAM115Aphysical
25416956
TRIM1_HUMANMID2physical
25416956
ZSC32_HUMANZSCAN32physical
25416956
ZN446_HUMANZNF446physical
25416956
PGBD1_HUMANPGBD1physical
25416956
ZN483_HUMANZNF483physical
25416956
ZN396_HUMANZNF396physical
25416956
ZN446_HUMANZNF446physical
26186194
SCND1_HUMANSCAND1physical
26186194
ZN444_HUMANZNF444physical
26186194
PSMD1_HUMANPSMD1physical
26344197
TRI41_HUMANTRIM41physical
21516116
ZN446_HUMANZNF446physical
28514442
SCND1_HUMANSCAND1physical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
KCRM_HUMANCKMphysical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
ZN174_HUMANZNF174physical
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 ZNF24_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-132, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279 AND TYR-335, ANDMASS SPECTROMETRY.

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