NELL1_HUMAN - dbPTM
NELL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NELL1_HUMAN
UniProt AC Q92832
Protein Name Protein kinase C-binding protein NELL1
Gene Name NELL1
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization Cytoplasm . Nucleus envelope . Secreted. Colocalizes with ATRAID on the nuclear envelope and the perinuclear region.
Protein Description Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization..
Protein Sequence MPMDLILVVWFCVCTARTVVGFGMDPDLQMDIVTELDLVNTTLGVAQVSGMHNASKAFLFQDIEREIHAAPHVSEKLIQLFRNKSEFTILATVQQKPSTSGVILSIRELEHSYFELESSGLRDEIRYHYIHNGKPRTEALPYRMADGQWHKVALSVSASHLLLHVDCNRIYERVIDPPDTNLPPGINLWLGQRNQKHGLFKGIIQDGKIIFMPNGYITQCPNLNHTCPTCSDFLSLVQGIMDLQELLAKMTAKLNYAETRLSQLENCHCEKTCQVSGLLYRDQDSWVDGDHCRNCTCKSGAVECRRMSCPPLNCSPDSLPVHIAGQCCKVCRPKCIYGGKVLAEGQRILTKSCRECRGGVLVKITEMCPPLNCSEKDHILPENQCCRVCRGHNFCAEGPKCGENSECKNWNTKATCECKSGYISVQGDSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCVPGYIRVDDFSCTEHDECGSGQHNCDENAICTNTVQGHSCTCKPGYVGNGTICRAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECSEGIIECHNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGLKHNGQVWTLKEDRCSVCSCKDGKIFCRRTACDCQNPSADLFCCPECDTRVTSQCLDQNGHKLYRSGDNWTHSCQQCRCLEGEVDCWPLTCPNLSCEYTAILEGECCPRCVSDPCLADNITYDIRKTCLDSYGVSRLSGSVWTMAGSPCTTCKCKNGRVCCSVDFECLQNN
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
40N-linked_GlycosylationVTELDLVNTTLGVAQ
EEHHHHHHCCCCHHC
34.34UniProtKB CARBOHYD
53N-linked_GlycosylationAQVSGMHNASKAFLF
HCCCCCCCCCEEHHH
36.70UniProtKB CARBOHYD
83N-linked_GlycosylationKLIQLFRNKSEFTIL
HHHHHHCCCCCEEEE
44.89UniProtKB CARBOHYD
105PhosphorylationSTSGVILSIRELEHS
CCCCEEEEEEEEECE
14.42-
224N-linked_GlycosylationITQCPNLNHTCPTCS
EEECCCCCCCCCCHH
34.75UniProtKB CARBOHYD
294N-linked_GlycosylationVDGDHCRNCTCKSGA
CCCCCCCCCCCCCCC
30.74UniProtKB CARBOHYD
340UbiquitinationPKCIYGGKVLAEGQR
CCCEECCEEEEECCE
29.70-
351UbiquitinationEGQRILTKSCRECRG
ECCEEECHHHHHCCC
44.08-
372N-linked_GlycosylationTEMCPPLNCSEKDHI
EECCCCCCCCCCCCC
32.80UniProtKB CARBOHYD
511N-linked_GlycosylationCKPGYVGNGTICRAF
ECCCCCCCCCEEHHH
34.10UniProtKB CARBOHYD
562N-linked_GlycosylationEGIIECHNHSRCVNL
CCHHEECCCCCCCCC
46.63UniProtKB CARBOHYD
609N-linked_GlycosylationLRTHTCWNDSACINL
ECCCCCCCCCCCEEE
35.19UniProtKB CARBOHYD
708N-linked_GlycosylationKLYRSGDNWTHSCQQ
EEEECCCCCCCCCCC
49.42UniProtKB CARBOHYD
732N-linked_GlycosylationCWPLTCPNLSCEYTA
EEEEECCCCCEEEEE
46.89UniProtKB CARBOHYD
758N-linked_GlycosylationSDPCLADNITYDIRK
CCCCCCCCCEEEHHH
23.93UniProtKB CARBOHYD

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 NELL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NELL1_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 NELL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MATN2_HUMANMATN2physical
28514442
PFKAP_HUMANPFKPphysical
28514442
FBX27_HUMANFBXO27physical
28514442
PXDN_HUMANPXDNphysical
28514442
ZN260_HUMANZNF260physical
28514442
TRM2_HUMANTRMT2Bphysical
28514442
EMIL2_HUMANEMILIN2physical
28514442
PRPK_HUMANTP53RKphysical
28514442
TIMP3_HUMANTIMP3physical
28514442
EGFL7_HUMANEGFL7physical
28514442
RPOM_HUMANPOLRMTphysical
28514442
TYW3_HUMANTYW3physical
28514442
LTBP4_HUMANLTBP4physical
28514442
CEP44_HUMANCEP44physical
28514442
FBLN1_HUMANFBLN1physical
28514442
LAMB2_HUMANLAMB2physical
28514442
OBSL1_HUMANOBSL1physical
28514442
CJ088_HUMANC10orf88physical
28514442
CHK1_HUMANCHEK1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NELL1_HUMAN

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Related Literatures of Post-Translational Modification

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