ZIC1_HUMAN - dbPTM
ZIC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZIC1_HUMAN
UniProt AC Q15915
Protein Name Zinc finger protein ZIC 1
Gene Name ZIC1
Organism Homo sapiens (Human).
Sequence Length 447
Subcellular Localization Nucleus. Cytoplasm. Localizes in the cytoplasm in presence of MDFIC overexpression..
Protein Description Acts as a transcriptional activator. Involved in neurogenesis. Plays important roles in the early stage of organogenesis of the CNS, as well as during dorsal spinal cord development and maturation of the cerebellum. Involved in the spatial distribution of mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a role in the regulation of MF axon pathway choice. Promotes MF migration towards ipsilaterally-located cerebellar territories. May have a role in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1 and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3' (By similarity)..
Protein Sequence MLLDAGPQYPAIGVTTFGASRHHSAGDVAERDVGLGINPFADGMGAFKLNPSSHELASAGQTAFTSQAPGYAAAAALGHHHHPGHVGSYSSAAFNSTRDFLFRNRGFGDAAAAASAQHSLFAASAGGFGGPHGHTDAAGHLLFPGLHEQAAGHASPNVVNGQMRLGFSGDMYPRPEQYGQVTSPRSEHYAAPQLHGYGPMNVNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSSQGSQPSPAASSGYESSTPPTIVSPSTDNPTTSSLSPSSSAVHHTAGHSALSSNFNEWYV
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
9PhosphorylationLLDAGPQYPAIGVTT
CCCCCCCCCCEEEEE
9.58-
15PhosphorylationQYPAIGVTTFGASRH
CCCCEEEEEECCCCC
15.9317081983
16PhosphorylationYPAIGVTTFGASRHH
CCCEEEEEECCCCCC
20.0517081983
20PhosphorylationGVTTFGASRHHSAGD
EEEEECCCCCCCCCC
32.3117081983
172PhosphorylationLGFSGDMYPRPEQYG
CCCCCCCCCCHHHCC
10.7927732954
178PhosphorylationMYPRPEQYGQVTSPR
CCCCHHHCCCCCCCC
14.0927732954
182PhosphorylationPEQYGQVTSPRSEHY
HHHCCCCCCCCCCCC
25.7327732954
183PhosphorylationEQYGQVTSPRSEHYA
HHCCCCCCCCCCCCC
21.3227732954
245PhosphorylationPKKSCNKTFSTMHEL
CCHHCCCCHHHHHHH
14.61-
247PhosphorylationKSCNKTFSTMHELVT
HHCCCCHHHHHHHHH
30.01-
297PhosphorylationVNHIRVHTGEKPFPC
EEEEEEECCCCCCCC
44.15-
311AcetylationCPFPGCGKVFARSEN
CCCCCCCCEEEECCC
37.95-
325PhosphorylationNLKIHKRTHTGEKPF
CEEEECCCCCCCCCE
28.7023312004
327PhosphorylationKIHKRTHTGEKPFKC
EEECCCCCCCCCEEC
46.5629496963
375PhosphorylationDKSYTHPSSLRKHMK
CCCCCCHHHHHHHEE
34.1127732954
376PhosphorylationKSYTHPSSLRKHMKV
CCCCCHHHHHHHEEC
36.3227732954

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 ZIC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZIC1_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 ZIC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLI1_HUMANGLI1physical
11238441
GLI2_HUMANGLI2physical
11238441
GLI3_HUMANGLI3physical
11238441
DR9C7_HUMANSDR9C7physical
28514442
PLBL1_HUMANPLBD1physical
28514442
GDPD3_HUMANGDPD3physical
28514442
CATH_HUMANCTSHphysical
28514442
S10A7_HUMANS100A7physical
28514442
SPB4_HUMANSERPINB4physical
28514442
CPNS2_HUMANCAPNS2physical
28514442
CBPA4_HUMANCPA4physical
28514442
PA24E_HUMANPLA2G4Ephysical
28514442
RNAS7_HUMANRNASE7physical
28514442
AACT_HUMANSERPINA3physical
28514442
SPB3_HUMANSERPINB3physical
28514442
CATL2_HUMANCTSVphysical
28514442
ILEU_HUMANSERPINB1physical
28514442
CASPE_HUMANCASP14physical
28514442
LX12B_HUMANALOX12Bphysical
28514442
TGM1_HUMANTGM1physical
28514442
S100P_HUMANS100Pphysical
28514442
KLK7_HUMANKLK7physical
28514442
SAP3_HUMANGM2Aphysical
28514442
ZA2G_HUMANAZGP1physical
28514442
NGAL_HUMANLCN2physical
28514442
PPAP_HUMANACPPphysical
28514442
ECM1_HUMANECM1physical
28514442
HUTH_HUMANHALphysical
28514442
INVO_HUMANIVLphysical
28514442
GSDMA_HUMANGSDMAphysical
28514442
ARGI1_HUMANARG1physical
28514442
FBX50_HUMANNCCRP1physical
28514442
ASAH1_HUMANASAH1physical
28514442
IMPA2_HUMANIMPA2physical
28514442
S10AG_HUMANS100A16physical
28514442
APOD_HUMANAPODphysical
28514442
KPRP_HUMANKPRPphysical
28514442
SPB13_HUMANSERPINB13physical
28514442
S10AE_HUMANS100A14physical
28514442
S10A9_HUMANS100A9physical
28514442
CYTA_HUMANCSTAphysical
28514442
CAN1_HUMANCAPN1physical
28514442
LOXE3_HUMANALOXE3physical
28514442
G3P_HUMANGAPDHphysical
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 ZIC1_HUMAN

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Related Literatures of Post-Translational Modification

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