ZBT44_HUMAN - dbPTM
ZBT44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT44_HUMAN
UniProt AC Q8NCP5
Protein Name Zinc finger and BTB domain-containing protein 44
Gene Name ZBTB44
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Nucleus.
Protein Description May be involved in transcriptional regulation..
Protein Sequence MGVKTFTHSSSSHSQEMLGKLNMLRNDGHFCDITIRVQDKIFRAHKVVLAACSDFFRTKLVGQAEDENKNVLDLHHVTVTGFIPLLEYAYTATLSINTENIIDVLAAASYMQMFSVASTCSEFMKSSILWNTPNSQPEKGLDAGQENNSNCNFTSRDGSISPVSSECSVVERTIPVCRESRRKRKSYIVMSPESPVKCGTQTSSPQVLNSSASYSENRNQPVDSSLAFPWTFPFGIDRRIQPEKVKQAENTRTLELPGPSETGRRMADYVTCESTKTTLPLGTEEDVRVKVERLSDEEVHEEVSQPVSASQSSLSDQQTVPGSEQVQEDLLISPQSSSIGSVDEGVSEGLPTLQSTSSTNAPPDDDDRLENVQYPYQLYIAPSTSSTERPSPNGPDRPFQCPTCGVRFTRIQNLKQHMLIHSGIKPFQCDRCGKKFTRAYSLKMHRLKHEGKRCFRCQICSATFTSFGEYKHHMRVSRHIIRKPRIYECKTCGAMLTNSGNLIVHLRSLNHEASELANYFQSSDFLVPDYLNQEQEETLVQYDLGEHGFESNSSVQMPVISQYHSKGKEP
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
4Sumoylation----MGVKTFTHSSS
----CCCCCCCCCCC		31.9928112733
5Phosphorylation---MGVKTFTHSSSS
---CCCCCCCCCCCC		31.2124719451
12PhosphorylationTFTHSSSSHSQEMLG
CCCCCCCCHHHHHHH		29.1624719451
132PhosphorylationKSSILWNTPNSQPEK
HHHHCCCCCCCCCCC		16.5626074081
135PhosphorylationILWNTPNSQPEKGLD
HCCCCCCCCCCCCCC		48.6017525332
135 (in isoform 3)Phosphorylation-48.60-
149PhosphorylationDAGQENNSNCNFTSR
CCCCCCCCCCCEECC		55.1030576142
159PhosphorylationNFTSRDGSISPVSSE
CEECCCCCCCCCCCC		24.9630266825
161PhosphorylationTSRDGSISPVSSECS
ECCCCCCCCCCCCCE		22.4319664994
161 (in isoform 3)Phosphorylation-22.4324719451
164PhosphorylationDGSISPVSSECSVVE
CCCCCCCCCCCEEEE		24.6530266825
164 (in isoform 3)Phosphorylation-24.6527251275
165PhosphorylationGSISPVSSECSVVER
CCCCCCCCCCEEEEE		42.7425159151
168PhosphorylationSPVSSECSVVERTIP
CCCCCCCEEEEEECH		25.7523927012
180PhosphorylationTIPVCRESRRKRKSY
ECHHHHHHHCCCCEE		20.31-
186 (in isoform 3)Phosphorylation-24.9127251275
186PhosphorylationESRRKRKSYIVMSPE
HHHCCCCEEEEECCC		24.9129255136
187PhosphorylationSRRKRKSYIVMSPES
HHCCCCEEEEECCCC		10.6929255136
191PhosphorylationRKSYIVMSPESPVKC
CCEEEEECCCCCCCC		18.0225159151
191 (in isoform 3)Phosphorylation-18.0227251275
194PhosphorylationYIVMSPESPVKCGTQ
EEEECCCCCCCCCCC		38.0823401153
194 (in isoform 3)Phosphorylation-38.0824719451
200PhosphorylationESPVKCGTQTSSPQV
CCCCCCCCCCCCCCH		37.8428464451
202PhosphorylationPVKCGTQTSSPQVLN
CCCCCCCCCCCCHHC		30.8928450419
203PhosphorylationVKCGTQTSSPQVLNS
CCCCCCCCCCCHHCC		30.1528464451
204PhosphorylationKCGTQTSSPQVLNSS
CCCCCCCCCCHHCCC		23.8028464451
204 (in isoform 3)Phosphorylation-23.8027251275
231PhosphorylationSSLAFPWTFPFGIDR
CHHCCCCCCCCCCCC		22.97-
269PhosphorylationTGRRMADYVTCESTK
HCCCCCCEEEECCCC		6.52-
290SumoylationTEEDVRVKVERLSDE
CHHHHEEEEEECCHH		28.0225772364
290SumoylationTEEDVRVKVERLSDE
CHHHHEEEEEECCHH		28.02-
391PhosphorylationTSSTERPSPNGPDRP
CCCCCCCCCCCCCCC		36.9027794612
440 (in isoform 3)Phosphorylation-15.9624719451
440PhosphorylationGKKFTRAYSLKMHRL
CCCHHHHHHHHHHHC		15.9624719451
441 (in isoform 3)Phosphorylation-22.1124719451
441PhosphorylationKKFTRAYSLKMHRLK
CCHHHHHHHHHHHCC		22.1124719451
453MethylationRLKHEGKRCFRCQIC
HCCCCCCEEEECEEC		35.35115387721
463 (in isoform 2)Phosphorylation-15.9125690035
465PhosphorylationQICSATFTSFGEYKH
EECCEEEECCCCCHH		20.8430631047
470 (in isoform 2)Phosphorylation-18.9225690035
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 ZBT44_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBT44_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 ZBT44_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT44_HUMANZBTB44physical
25416956
SMYD1_HUMANSMYD1physical
25416956
F124A_HUMANFAM124Aphysical
25416956
UBA3_HUMANUBA3physical
26186194
MYH14_HUMANMYH14physical
26186194
UBP7_HUMANUSP7physical
26186194
SCRIB_HUMANSCRIBphysical
26186194
ULA1_HUMANNAE1physical
26186194
KLH21_HUMANKLHL21physical
26186194
KLH20_HUMANKLHL20physical
26186194
DCA16_HUMANDCAF16physical
26186194
SAHH3_HUMANAHCYL2physical
26186194
TRI11_HUMANTRIM11physical
26186194
KLH21_HUMANKLHL21physical
28514442
SCRIB_HUMANSCRIBphysical
28514442
ULA1_HUMANNAE1physical
28514442
UBP7_HUMANUSP7physical
28514442
DCA16_HUMANDCAF16physical
28514442
UBA3_HUMANUBA3physical
28514442
TRI11_HUMANTRIM11physical
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 ZBT44_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-194, ANDMASS SPECTROMETRY.
"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-161, 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-135, AND MASSSPECTROMETRY.

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