ZN521_HUMAN - dbPTM
ZN521_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN521_HUMAN
UniProt AC Q96K83
Protein Name Zinc finger protein 521
Gene Name ZNF521
Organism Homo sapiens (Human).
Sequence Length 1311
Subcellular Localization Nucleus.
Protein Description Transcription factor that can both act as an activator or a repressor depending on the context. Involved in BMP signaling and in the regulation of the immature compartment of the hematopoietic system. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved specification of B-cell lineage; this interaction preventing EBF1 to bind DNA and activate target genes..
Protein Sequence MSRRKQAKPRSLKDPNCKLEDKTEDGEALDCKKRPEDGEELEDEAVHSCDSCLQVFESLSDITEHKINQCQLTDGVDVEDDPTCSWPASSPSSKDQTSPSHGEGCDFGEEEGGPGLPYPCQFCDKSFSRLSYLKHHEQSHSDKLPFKCTYCSRLFKHKRSRDRHIKLHTGDKKYHCSECDAAFSRSDHLKIHLKTHTSNKPYKCAICRRGFLSSSSLHGHMQVHERNKDGSQSGSRMEDWKMKDTQKCSQCEEGFDFPEDLQKHIAECHPECSPNEDRAALQCVYCHELFVEETSLMNHMEQVHSGEKKNSCSICSESFHTVEELYSHMDSHQQPESCNHSNSPSLVTVGYTSVSSTTPDSNLSVDSSTMVEAAPPIPKSRGRKRAAQQTPDMTGPSSKQAKVTYSCIYCNKQLFSSLAVLQIHLKTMHLDKPEQAHICQYCLEVLPSLYNLNEHLKQVHEAQDPGLIVSAMPAIVYQCNFCSEVVNDLNTLQEHIRCSHGFANPAAKDSNAFFCPHCYMGFLTDSSLEEHIRQVHCDLSGSRFGSPVLGTPKEPVVEVYSCSYCTNSPIFNSVLKLNKHIKENHKNIPLALNYIHNGKKSRALSPLSPVAIEQTSLKMMQAVGGAPARPTGEYICNQCGAKYTSLDSFQTHLKTHLDTVLPKLTCPQCNKEFPNQESLLKHVTIHFMITSTYYICESCDKQFTSVDDLQKHLLDMHTFVFFRCTLCQEVFDSKVSIQLHLAVKHSNEKKVYRCTSCNWDFRNETDLQLHVKHNHLENQGKVHKCIFCGESFGTEVELQCHITTHSKKYNCKFCSKAFHAIILLEKHLREKHCVFETKTPNCGTNGASEQVQKEEVELQTLLTNSQESHNSHDGSEEDVDTSEPMYGCDICGAAYTMETLLQNHQLRDHNIRPGESAIVKKKAELIKGNYKCNVCSRTFFSENGLREHMQTHLGPVKHYMCPICGERFPSLLTLTEHKVTHSKSLDTGNCRICKMPLQSEEEFLEHCQMHPDLRNSLTGFRCVVCMQTVTSTLELKIHGTFHMQKTGNGSAVQTTGRGQHVQKLYKCASCLKEFRSKQDLVKLDINGLPYGLCAGCVNLSKSASPGINVPPGTNRPGLGQNENLSAIEGKGKVGGLKTRCSSCNVKFESESELQNHIQTIHRELVPDSNSTQLKTPQVSPMPRISPSQSDEKKTYQCIKCQMVFYNEWDIQVHVANHMIDEGLNHECKLCSQTFDSPAKLQCHLIEHSFEGMGGTFKCPVCFTVFVQANKLQQHIFSAHGQEDKIYDCTQCPQKFFFQTELQNHTMTQHSS
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
89PhosphorylationPTCSWPASSPSSKDQ
CCCCCCCCCCCCCCC		38.4127251275
90PhosphorylationTCSWPASSPSSKDQT
CCCCCCCCCCCCCCC		30.7927251275
97PhosphorylationSPSSKDQTSPSHGEG
CCCCCCCCCCCCCCC		53.3828348404
98PhosphorylationPSSKDQTSPSHGEGC
CCCCCCCCCCCCCCC		20.8326657352
100PhosphorylationSKDQTSPSHGEGCDF
CCCCCCCCCCCCCCC		43.8424961811
128PhosphorylationQFCDKSFSRLSYLKH
CCCCCCCHHHHHHHH		39.1317081983
149PhosphorylationDKLPFKCTYCSRLFK
CCCCCCCHHHHHHHH		28.3125690035
150PhosphorylationKLPFKCTYCSRLFKH
CCCCCCHHHHHHHHC		9.6324719451
273PhosphorylationAECHPECSPNEDRAA
HHHCCCCCCCCCHHH		29.1523401153
390PhosphorylationRKRAAQQTPDMTGPS
CHHHHHCCCCCCCCC		14.8024173317
398PhosphorylationPDMTGPSSKQAKVTY
CCCCCCCCHHCEEEE		31.7422210691
540PhosphorylationRQVHCDLSGSRFGSP
HHHHHCCCCCCCCCC		22.8227251275
542PhosphorylationVHCDLSGSRFGSPVL
HHHCCCCCCCCCCCC		22.5127251275
546PhosphorylationLSGSRFGSPVLGTPK
CCCCCCCCCCCCCCC		14.7730266825
551PhosphorylationFGSPVLGTPKEPVVE
CCCCCCCCCCCCEEE		27.3330266825
560PhosphorylationKEPVVEVYSCSYCTN
CCCEEEEEECCCCCC		7.1728450419
561PhosphorylationEPVVEVYSCSYCTNS
CCEEEEEECCCCCCC		11.1928450419
563PhosphorylationVVEVYSCSYCTNSPI
EEEEEECCCCCCCHH		19.8028450419
564PhosphorylationVEVYSCSYCTNSPIF
EEEEECCCCCCCHHH		13.9728450419
601PhosphorylationYIHNGKKSRALSPLS
HHHCCCCCCCCCCCC		26.6928450419
605PhosphorylationGKKSRALSPLSPVAI
CCCCCCCCCCCCCCC		23.8623401153
608PhosphorylationSRALSPLSPVAIEQT
CCCCCCCCCCCCHHH		22.2530266825
615PhosphorylationSPVAIEQTSLKMMQA
CCCCCHHHCHHHHHH		24.2023403867
616PhosphorylationPVAIEQTSLKMMQAV
CCCCHHHCHHHHHHH		26.2023403867
678PhosphorylationKEFPNQESLLKHVTI
CCCCCHHHHHHHHHH		29.2724719451
970PhosphorylationICGERFPSLLTLTEH
CCCCCCCCCEEEEEC		33.04-
1018PhosphorylationPDLRNSLTGFRCVVC
HHHHHHCCCCEEEEE		33.8124719451
1046PhosphorylationGTFHMQKTGNGSAVQ
EEEEEEECCCCCEEE		20.98-
1054PhosphorylationGNGSAVQTTGRGQHV
CCCCEEEECCCCHHH		25.31-
10662-HydroxyisobutyrylationQHVQKLYKCASCLKE
HHHHHHHHHHHHHHH		33.49-
1102PhosphorylationGCVNLSKSASPGINV
HHCCCCCCCCCCCCC		30.5127251275
1104PhosphorylationVNLSKSASPGINVPP
CCCCCCCCCCCCCCC		30.6524173317
1113PhosphorylationGINVPPGTNRPGLGQ
CCCCCCCCCCCCCCC		33.5527251275
1146SumoylationRCSSCNVKFESESEL
CCCCCCCCCCCHHHH		29.4428112733
1168PhosphorylationHRELVPDSNSTQLKT
HHHHCCCCCCCCCCC		26.9828450419
1170PhosphorylationELVPDSNSTQLKTPQ
HHCCCCCCCCCCCCC		22.8328450419
1171PhosphorylationLVPDSNSTQLKTPQV
HCCCCCCCCCCCCCC		42.0228450419
1175PhosphorylationSNSTQLKTPQVSPMP
CCCCCCCCCCCCCCC		27.7827732954
1179PhosphorylationQLKTPQVSPMPRISP
CCCCCCCCCCCCCCC		15.3828450419
1185O-linked_GlycosylationVSPMPRISPSQSDEK
CCCCCCCCCCCCCCH		21.5630379171
1185PhosphorylationVSPMPRISPSQSDEK
CCCCCCCCCCCCCCH		21.5623401153
1263PhosphorylationFKCPVCFTVFVQANK
CCCCEEEEEEEECCH		14.12-
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 ZN521_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN521_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 ZN521_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD1_HUMANSMAD1physical
14630787
SMAD4_HUMANSMAD4physical
14630787
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 ZN521_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-608, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory