NOD1_HUMAN - dbPTM
NOD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOD1_HUMAN
UniProt AC Q9Y239
Protein Name Nucleotide-binding oligomerization domain-containing protein 1
Gene Name NOD1
Organism Homo sapiens (Human).
Sequence Length 953
Subcellular Localization Cytoplasm. Cell membrane. Apical cell membrane. Basolateral cell membrane. Detected in the cytoplasm and at the cell membrane. Following bacterial infection, localizes to bacterial entry sites in the cell membrane. Recruited to the basolateral and ap
Protein Description Enhances caspase-9-mediated apoptosis. Induces NF-kappa-B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella effector proteins IpgB2 and OspB. Recruits NLRP10 to the cell membrane following bacterial infection..
Protein Sequence MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF
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
129PhosphorylationNTDPVSRYTQQLRHH
CCCHHHHHHHHHHHH
11.0329978859
130PhosphorylationTDPVSRYTQQLRHHL
CCHHHHHHHHHHHHC
14.5529978859
141PhosphorylationRHHLGRDSKFVLCYA
HHHCCCCCCEEEEEE
27.0029978859
217PhosphorylationMLLQRLQSLWATGRL
HHHHHHHHHHHHCCC
30.39-
249S-palmitoylationFKESDRLCLQDLLFK
CHHHHHHHHHHHHHH
3.1429575903
328UbiquitinationKLLKGASKLLTARTG
CHHHHHHHHHHHCCC
47.16-
334PhosphorylationSKLLTARTGIEVPRQ
HHHHHHCCCCCCCHH
39.79-
597PhosphorylationLFLCGLLSKAKQKLL
HHHHHHHHHHHHHHH
35.2924719451
627PhosphorylationLWAHLFSSLRGYLKS
HHHHHHHHHHHHHHC
18.1024719451
754UbiquitinationVLSEELTKYKIVTYL
ECCHHHHHCCEEEEE
58.11-
784UbiquitinationTKILDECKGLTHLKL
HHHHHHCCCCCEEEC
55.71-
797PhosphorylationKLGKNKITSEGGKYL
ECCCCEEECCCHHEE
23.4924719451
798PhosphorylationLGKNKITSEGGKYLA
CCCCEEECCCHHEEE
37.4024719451

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
-KUbiquitinationE3 ubiquitin ligaseRNF34Q969K3
PMID:25012219

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOD1_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 NOD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOD1_HUMANNOD1physical
10329646
CASP1_HUMANCASP1physical
10329646
CASP2_HUMANCASP2physical
10329646
CASP4_HUMANCASP4physical
10329646
CASP8_HUMANCASP8physical
10329646
CASP9_HUMANCASP9physical
10329646
RIPK2_HUMANRIPK2physical
10329646
CFLAR_HUMANCFLARphysical
10329646
HS90A_HUMANHSP90AA1physical
17435760
SGT1_HUMANSUGT1physical
17435760
CSN6_HUMANCOPS6physical
17337451
SGT1_HUMANSUGT1physical
17420470
HS90A_HUMANHSP90AA1physical
17420470
PSA7_HUMANPSMA7physical
23839082
SOX8_HUMANSOX8physical
21988832
RNF34_HUMANRNF34physical
25012219
A16L1_HUMANATG16L1physical
19898471
NOD2_HUMANNOD2physical
19898471
RIPK2_HUMANRIPK2physical
23300079
A16L1_HUMANATG16L1physical
23300079
UBC_HUMANUBCphysical
23300079
NOD1_HUMANNOD1physical
23300079

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOD1_HUMAN

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Related Literatures of Post-Translational Modification

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