NLRP1_HUMAN - dbPTM
NLRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NLRP1_HUMAN
UniProt AC Q9C000
Protein Name NACHT, LRR and PYD domains-containing protein 1
Gene Name NLRP1
Organism Homo sapiens (Human).
Sequence Length 1473
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Inflammasome . Nucleus . Nucleocytoplasmic distribution in lymphoid organs (probably in T-cells) and in neurons. In epithelial cells, predominantly cytoplasmic.
Protein Description As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. [PubMed: 22665479]
Protein Sequence MAGGAWGRLACYLEFLKKEELKEFQLLLANKAHSRSSSGETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQEGAGHSPSFPYSPSEPHLGSPSQPTSTAVLMPWIHELPAGCTQGSERRVLRQLPDTSGRRWREISASLLYQALPSSPDHESPSQESPNAPTSTAVLGSWGSPPQPSLAPREQEAPGTQWPLDETSGIYYTEIREREREKSEKGRPPWAAVVGTPPQAHTSLQPHHHPWEPSVRESLCSTWPWKNEDFNQKFTQLLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFGPGLDTQEPRIVILQGAAGIGKSTLARQVKEAWGRGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAPIRQILSRPERLLFILDGVDEPGWVLQEPSSELCLHWSQPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFSESSRKEYFYRYFTDERQAIRAFRLVKSNKELWALCLVPWVSWLACTCLMQQMKRKEKLTLTSKTTTTLCLHYLAQALQAQPLGPQLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQEHPIPLSYSFIHLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKTLEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLSQGRNLMQWVPSLQLLLQPHSLESLHCLYETRNKTFLTQVMAHFEEMGMCVETDMELLVCTFCIKFSRHVKKLQLIEGRQHRSTWSPTMVVLFRWVPVTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQELRALEQEKPQLLIFSRRKPSVMTPTEGLDTGEMSNSTSSLKRQRLGSERAASHVAQANLKLLDVSKIFPIAEIAEESSPEVVPVELLCVPSPASQGDLHTKPLGTDDDFWGPTGPVATEVVDKEKNLYRVHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHSWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDTSLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKMIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSIRKAIDDLEMKFQFVRIHKPPPLTPLYMGCRYTVSGSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKDKKDETLVWEALVKPGDLMPATTLIPPARIAVPSPLDAPQLLHFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMELWEKGSKKGLLPLSS
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
41PhosphorylationSRSSSGETPAQPEKT
CCCCCCCCCCCCCCC
-
193PhosphorylationWGSPPQPSLAPREQE
CCCCCCCCCCCCCCC
24719451
291PhosphorylationLQRPHPRSQDPLVKR
HCCCCCCCCCCCCCC
24719451
297UbiquitinationRSQDPLVKRSWPDYV
CCCCCCCCCCCCCHH
-
297UbiquitinationRSQDPLVKRSWPDYV
CCCCCCCCCCCCCHH
-
340UbiquitinationQGAAGIGKSTLARQV
ECCCCCCHHHHHHHH
-
340UbiquitinationQGAAGIGKSTLARQV
ECCCCCCHHHHHHHH
-
823PhosphorylationSGNSLSHSAVKSLCK
CCCCCCHHHHHHHHH
-
826UbiquitinationSLSHSAVKSLCKTLR
CCCHHHHHHHHHHCC
29967540
855UbiquitinationGLTAEDCKDLAFGLR
CCCHHHHHHHHHHCC
-
855UbiquitinationGLTAEDCKDLAFGLR
CCCHHHHHHHHHHCC
-
990PhosphorylationIFSRRKPSVMTPTEG
EEECCCCCCCCCCCC
22210691
993PhosphorylationRRKPSVMTPTEGLDT
CCCCCCCCCCCCCCC
22210691
995PhosphorylationKPSVMTPTEGLDTGE
CCCCCCCCCCCCCCC
22210691
1000PhosphorylationTPTEGLDTGEMSNST
CCCCCCCCCCCCCCC
22210691
1004PhosphorylationGLDTGEMSNSTSSLK
CCCCCCCCCCCHHHH
22210691
1007PhosphorylationTGEMSNSTSSLKRQR
CCCCCCCCHHHHHHH
22210691
1008PhosphorylationGEMSNSTSSLKRQRL
CCCCCCCHHHHHHHH
22210691
1009PhosphorylationEMSNSTSSLKRQRLG
CCCCCCHHHHHHHHC
22210691
1297PhosphorylationYTVSGSGSGMLEILP
EEECCCCCCCEEECC
21888424
1428AcetylationTRPSQMRKLFSLSQS
CCHHHHHHHHHHCHH
12650559
1439AcetylationLSQSWDRKCKDGLYQ
HCHHHHHHCHHHHHH
12650569

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 NLRP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NLRP1_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 NLRP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CASP9_HUMANCASP9physical
11076957
CASP2_HUMANCASP2physical
11076957
CLH1_HUMANCLTCphysical
26344197
KC1E_HUMANCSNK1Ephysical
26344197
IF6_HUMANEIF6physical
26344197
SMC2_HUMANSMC2physical
26344197

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NLRP1_HUMAN

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Related Literatures of Post-Translational Modification

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