ZCRB1_HUMAN - dbPTM
ZCRB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZCRB1_HUMAN
UniProt AC Q8TBF4
Protein Name Zinc finger CCHC-type and RNA-binding motif-containing protein 1
Gene Name ZCRB1
Organism Homo sapiens (Human).
Sequence Length 217
Subcellular Localization Nucleus, nucleoplasm .
Protein Description
Protein Sequence MSGGLAPSKSTVYVSNLPFSLTNNDLYRIFSKYGKVVKVTIMKDKDTRKSKGVAFILFLDKDSAQNCTRAINNKQLFGRVIKASIAIDNGRAAEFIRRRNYFDKSKCYECGESGHLSYACPKNMLGEREPPKKKEKKKKKKAPEPEEEIEEVEESEDEGEDPALDSLSQAIAFQQAKIEEEQKKWKPSSGVPSTSDDSRRPRIKKSTYFSDEEELSD
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
8PhosphorylationMSGGLAPSKSTVYVS
CCCCCCCCCCEEEEE		33.36-
13PhosphorylationAPSKSTVYVSNLPFS
CCCCCEEEEECCCEE		9.76-
27PhosphorylationSLTNNDLYRIFSKYG
ECCCCHHHHHHHHCC		12.43-
31PhosphorylationNDLYRIFSKYGKVVK
CHHHHHHHHCCCEEE		23.6924719451
40PhosphorylationYGKVVKVTIMKDKDT
CCCEEEEEEECCCCC		15.05-
74UbiquitinationCTRAINNKQLFGRVI
HHHHHHCHHHHHHHH		43.84-
104UbiquitinationRRRNYFDKSKCYECG
HHCCCCCHHHCCCCC		41.75-
155PhosphorylationEIEEVEESEDEGEDP
HHHHHHHCCCCCCCH		36.5225159151
166PhosphorylationGEDPALDSLSQAIAF
CCCHHHHHHHHHHHH		30.6728176443
168PhosphorylationDPALDSLSQAIAFQQ
CHHHHHHHHHHHHHH		22.8628176443
184UbiquitinationKIEEEQKKWKPSSGV
HHHHHHHHCCCCCCC		61.21-
186AcetylationEEEQKKWKPSSGVPS
HHHHHHCCCCCCCCC		43.8526051181
186UbiquitinationEEEQKKWKPSSGVPS
HHHHHHCCCCCCCCC		43.85-
188PhosphorylationEQKKWKPSSGVPSTS
HHHHCCCCCCCCCCC		35.6821406692
189PhosphorylationQKKWKPSSGVPSTSD
HHHCCCCCCCCCCCC		52.9521406692
193PhosphorylationKPSSGVPSTSDDSRR
CCCCCCCCCCCCCCC		37.8321406692
194PhosphorylationPSSGVPSTSDDSRRP
CCCCCCCCCCCCCCC		30.0621406692
195PhosphorylationSSGVPSTSDDSRRPR
CCCCCCCCCCCCCCC		43.7021406692
198PhosphorylationVPSTSDDSRRPRIKK
CCCCCCCCCCCCCCC		34.8721406692
206PhosphorylationRRPRIKKSTYFSDEE
CCCCCCCCCCCCCHH		24.2828152594
207PhosphorylationRPRIKKSTYFSDEEE
CCCCCCCCCCCCHHH		37.1523403867
208PhosphorylationPRIKKSTYFSDEEEL
CCCCCCCCCCCHHHH		14.2623927012
210PhosphorylationIKKSTYFSDEEELSD
CCCCCCCCCHHHHCC		33.4325159151
216PhosphorylationFSDEEELSD------
CCCHHHHCC------		44.5523927012
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 ZCRB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZCRB1_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 ZCRB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U2AFM_HUMANZRSR2physical
28514442
H11_HUMANHIST1H1Aphysical
28514442
PDCD7_HUMANPDCD7physical
28514442
U1SBP_HUMANSNRNP35physical
28514442
RBM40_HUMANRNPC3physical
28514442
SNR48_HUMANSNRNP48physical
28514442
YBOX2_HUMANYBX2physical
28514442
RL26L_HUMANRPL26L1physical
28514442
RS27A_HUMANRPS27Aphysical
28514442
ZC3H8_HUMANZC3H8physical
28514442
DKC1_HUMANDKC1physical
28514442
ZBT11_HUMANZBTB11physical
28514442
CTCF_HUMANCTCFphysical
28514442
RBM19_HUMANRBM19physical
28514442
RS2_HUMANRPS2physical
28514442
SF3B2_HUMANSF3B2physical
28514442
SF3B1_HUMANSF3B1physical
28514442
LARP1_HUMANLARP1physical
28514442
GAR1_HUMANGAR1physical
28514442
NOP53_HUMANGLTSCR2physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
H14_HUMANHIST1H1Ephysical
28514442
RENT1_HUMANUPF1physical
28514442
H2AY_HUMANH2AFYphysical
28514442
STAU2_HUMANSTAU2physical
28514442
GLYR1_HUMANGLYR1physical
28514442
YBOX1_HUMANYBX1physical
28514442
NOL12_HUMANNOL12physical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
RS3A_HUMANRPS3Aphysical
28514442
MK67I_HUMANNIFKphysical
28514442
RS3_HUMANRPS3physical
28514442
RSSA_HUMANRPSAphysical
28514442
SYFM_HUMANFARS2physical
28514442
RL19_HUMANRPL19physical
28514442
PURA_HUMANPURAphysical
28514442
KRR1_HUMANKRR1physical
28514442
RPF1_HUMANRPF1physical
28514442
UTP23_HUMANUTP23physical
28514442
RS5_HUMANRPS5physical
28514442
NSA2_HUMANNSA2physical
28514442
LARP7_HUMANLARP7physical
28514442
RU17_HUMANSNRNP70physical
28514442
CCD86_HUMANCCDC86physical
28514442
DDX21_HUMANDDX21physical
28514442
KRI1_HUMANKRI1physical
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 ZCRB1_HUMAN

loading...

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-155; SER-210 ANDSER-216, AND MASS SPECTROMETRY.
"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-210 AND SER-216, 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-155; SER-210 ANDSER-216, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-210 ANDSER-216, AND MASS SPECTROMETRY.

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