ZPR1_HUMAN - dbPTM
ZPR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZPR1_HUMAN
UniProt AC O75312
Protein Name Zinc finger protein ZPR1
Gene Name ZPR1
Organism Homo sapiens (Human).
Sequence Length 459
Subcellular Localization Nucleus. Nucleus, nucleolus. Nucleus, gem. Nucleus, Cajal body. Cytoplasm, perinuclear region. Cytoplasm. Cell projection, axon. Cell projection, growth cone. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cone
Protein Description Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death..
Protein Sequence MAASGAVEPGPPGAAVAPSPAPAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDALVITHYNRTRQQEEMLGLQEEAPAEKPEEEDLRNEVLQFSTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLAPQR
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
4Phosphorylation----MAASGAVEPGP
----CCCCCCCCCCC		20.1126074081
19PhosphorylationPGAAVAPSPAPAPPP
CCCCCCCCCCCCCCC		24.7729255136
49PhosphorylationQQPTEIESLCMNCYC
CCCCCHHHHHHHHHC		32.31-
65PhosphorylationGMTRLLLTKIPFFRE
HHHHHHHHCCHHHHH		27.22-
66AcetylationMTRLLLTKIPFFREI
HHHHHHHCCHHHHHH		48.6425953088
66UbiquitinationMTRLLLTKIPFFREI
HHHHHHHCCHHHHHH		48.64-
86UbiquitinationSCEHCGWNNTEIQSA
CCCCCCCCCCEEEEC		30.7229967540
119UbiquitinationDMNREVVKTDSAATR
HHCCCEEECCCHHHC		52.3633845483
127UbiquitinationTDSAATRIPELDFEI
CCCHHHCCCCCCCCC		2.4333845483
140UbiquitinationEIPAFSQKGALTTVE
CCCCCCCCCCCHHHH		44.9829967540
181UbiquitinationRIDEFIVKLKELKQV
HHHHHHHHHHHHHCC		49.3733845483
190PhosphorylationKELKQVASPFTLIID
HHHHCCCCCEEEEEE		22.9927050516
193PhosphorylationKQVASPFTLIIDDPS
HCCCCCEEEEEECCC		22.0425159151
200PhosphorylationTLIIDDPSGNSFVEN
EEEEECCCCCCCCCC		58.5624043423
203PhosphorylationIDDPSGNSFVENPHA
EECCCCCCCCCCCCC		33.9124043423
220PhosphorylationKDDALVITHYNRTRQ
CCCEEEEECCCHHHH		15.7224043423
222PhosphorylationDALVITHYNRTRQQE
CEEEEECCCHHHHHH		9.5524043423
225PhosphorylationVITHYNRTRQQEEML
EEECCCHHHHHHHHH		29.2324043423
245UbiquitinationAPAEKPEEEDLRNEV
CCCCCCCHHHHHHHH		66.4032142685
245NeddylationAPAEKPEEEDLRNEV
CCCCCCCHHHHHHHH		66.4032015554
284SulfoxidationHFKEVIIMATNCENC
CCCEEEEEEECCCCC		2.3030846556
299UbiquitinationGHRTNEVKSGGAVEP
CCCCCCCCCCCCCCC		36.8932142685
299NeddylationGHRTNEVKSGGAVEP
CCCCCCCCCCCCCCC		36.8932015554
312PhosphorylationEPLGTRITLHITDAS
CCCCCEEEEEECCHH		14.7021406692
313UbiquitinationPLGTRITLHITDASD
CCCCEEEEEECCHHH		2.2729967540
316PhosphorylationTRITLHITDASDMTR
CEEEEEECCHHHHHH		18.1121406692
319PhosphorylationTLHITDASDMTRDLL
EEEECCHHHHHHHHH		30.6321406692
322PhosphorylationITDASDMTRDLLKSE
ECCHHHHHHHHHHCC		26.4821406692
367UbiquitinationDIRELVTKNPFTLGD
HHHHHHHCCCCCCCC		55.9629967540
371PhosphorylationLVTKNPFTLGDSSNP
HHHCCCCCCCCCCCC		30.9628555341
375PhosphorylationNPFTLGDSSNPGQTE
CCCCCCCCCCCCHHH		30.1622199227
376PhosphorylationPFTLGDSSNPGQTER
CCCCCCCCCCCHHHH		52.3521815630
381PhosphorylationDSSNPGQTERLQEFS
CCCCCCHHHHHHHHH		29.0523186163
434PhosphorylationKVERYKRTFDQNEEL
HHHHHHHHCCCCCCC		27.6722468782
446SulfoxidationEELGLNDMKTEGYEA
CCCCCCCCCCCCCCC		5.8721406390
448PhosphorylationLGLNDMKTEGYEAGL
CCCCCCCCCCCCCCC		28.1822468782
451PhosphorylationNDMKTEGYEAGLAPQ
CCCCCCCCCCCCCCC		9.0728796482
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 ZPR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZPR1_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 ZPR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZYX_HUMANZYXphysical
22939629
ARI1_HUMANARIH1physical
22863883
HSF1_HUMANHSF1physical
22863883
OGT1_HUMANOGTphysical
22863883
RPR1B_HUMANRPRD1Bphysical
22863883
TM1L1_HUMANTOM1L1physical
22863883
SAE2_HUMANUBA2physical
22863883
EF1A1_HUMANEEF1A1physical
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 ZPR1_HUMAN

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Related Literatures of Post-Translational Modification

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