BIRC1_HUMAN - dbPTM
BIRC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BIRC1_HUMAN
UniProt AC Q13075
Protein Name Baculoviral IAP repeat-containing protein 1
Gene Name NAIP
Organism Homo sapiens (Human).
Sequence Length 1403
Subcellular Localization
Protein Description Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.; Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila..
Protein Sequence MATQQKASDERISQFDHNLLPELSALLGLDAVQLAKELEEEEQKERAKMQKGYNSQMRSEAKRLKTFVTYEPYSSWIPQEMAAAGFYFTGVKSGIQCFCCSLILFGAGLTRLPIEDHKRFHPDCGFLLNKDVGNIAKYDIRVKNLKSRLRGGKMRYQEEEARLASFRNWPFYVQGISPCVLSEAGFVFTGKQDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLRSKKSSEEITQYIQSYKGFVDITGEHFVNSWVQRELPMASAYCNDSIFAYEELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQNMKSSAEVTPDLQSRGELCELLETTSESNLEDSIAVGPIVPEMAQGEAQWFQEAKNLNEQLRAAYTSASFRHMSLLDISSDLATDHLLGCDLSIASKHISKPVQEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQLKNQVLFLLDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPFYNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSFDDVAVFKSYMERLSLRNKATAEILKATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDEDLTMCLMSKFTAQRLRPFYRFLSPAFQEFLAGMRLIELLDSDRQEHQDLGLYHLKQINSPMMTVSAYNNFLNYVSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLRGLWQICPQAYFSMVSEHLLVLALKTAYQSNTVAACSPFVLQFLQGRTLTLGALNLQYFFDHPESLSLLRSIHFPIRGNKTSPRAHFSVLETCFDKSQVPTIDQDYASAFEPMNEWERNLAEKEDNVKSYMDMQRRASPDLSTGYWKLSPKQYKIPCLEVDVNDIDVVGQDMLEILMTVFSASQRIELHLNHSRGFIESIRPALELSKASVTKCSISKLELSAAEQELLLTLPSLESLEVSGTIQSQDQIFPNLDKFLCLKELSVDLEGNINVFSVIPEEFPNFHHMEKLLIQISAEYDPSKLVKLIQNSPNLHVFHLKCNFFSDFGSLMTMLVSCKKLTEIKFSDSFFQAVPFVASLPNFISLKILNLEGQQFPDEETSEKFAYILGSLSNLEELILPTGDGIYRVAKLIIQQCQQLHCLRVLSFFKTLNDDSVVEIAKVAISGGFQKLENLKLSINHKITEEGYRNFFQALDNMPNLQELDISRHFTECIKAQATTVKSLSQCVLRLPRLIRLNMLSWLLDADDIALLNVMKERHPQSKYLTILQKWILPFSPIIQK
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
137UbiquitinationKDVGNIAKYDIRVKN
CCCCCHHHHHHHHHC
39.3921890473
165PhosphorylationEEEARLASFRNWPFY
HHHHHHHHHCCCCCH
29.3624719451
420PhosphorylationSASFRHMSLLDISSD
HHHHHHHHHHCCCCC
21.47-
531PhosphorylationLEKEGSVTEMCVRNI
HHCCCCHHHHHHHHH
21.5022468782
628PhosphorylationRLRKFMVYFGKNQSL
HHHHHHHHHCCCCHH
8.53-
675PhosphorylationKSYMERLSLRNKATA
HHHHHHHHCCCHHHH
31.3523532336
780PhosphorylationYHLKQINSPMMTVSA
CCHHHCCCCCEEHHH
18.7930576142
800PhosphorylationNYVSSLPSTKAGPKI
HHHHCCCCCCCCHHH
48.0830576142
932PhosphorylationTSPRAHFSVLETCFD
CCCCCCCHHHHHHCC
18.8728857561
982PhosphorylationMDMQRRASPDLSTGY
HHHHHHCCCCCCCCC
19.6928450419
987PhosphorylationRASPDLSTGYWKLSP
HCCCCCCCCCCCCCH
41.40-
989PhosphorylationSPDLSTGYWKLSPKQ
CCCCCCCCCCCCHHH
10.23-
1043PhosphorylationHSRGFIESIRPALEL
CCCCHHHHHHHHHHH
21.05-
1051PhosphorylationIRPALELSKASVTKC
HHHHHHHHHCCCCEE
19.46-
1056PhosphorylationELSKASVTKCSISKL
HHHHCCCCEECCHHH
24.6829666759
1066PhosphorylationSISKLELSAAEQELL
CCHHHCCCHHHHHHH
18.9624043423
1075PhosphorylationAEQELLLTLPSLESL
HHHHHHHHCCCCCCC
36.2724043423
1078PhosphorylationELLLTLPSLESLEVS
HHHHHCCCCCCCEEC
48.1324043423
1081PhosphorylationLTLPSLESLEVSGTI
HHCCCCCCCEECCCC
34.8124043423
1085PhosphorylationSLESLEVSGTIQSQD
CCCCCEECCCCCCHH
22.3524043423
1087PhosphorylationESLEVSGTIQSQDQI
CCCEECCCCCCHHHC
14.3424043423
1090PhosphorylationEVSGTIQSQDQIFPN
EECCCCCCHHHCCCC
31.6924043423
1168PhosphorylationHLKCNFFSDFGSLMT
EEECCCHHCHHHHHH
28.0828509920
1172PhosphorylationNFFSDFGSLMTMLVS
CCHHCHHHHHHHHHH
18.2428509920
1175PhosphorylationSDFGSLMTMLVSCKK
HCHHHHHHHHHHCCC
16.7928634298
1179PhosphorylationSLMTMLVSCKKLTEI
HHHHHHHHCCCCCCC
19.0928509920
1273PhosphorylationRVLSFFKTLNDDSVV
HHHHHHHCCCCCCHH
26.1529083192
1278PhosphorylationFKTLNDDSVVEIAKV
HHCCCCCCHHHHEEE
30.8129083192
1398PhosphorylationQKWILPFSPIIQK--
HHHHCCCCCCCCC--
17.1628450419

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 BIRC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BIRC1_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 BIRC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DBLOH_HUMANDIABLOphysical
15280366
XAF1_HUMANXAF1physical
17613533
M3K7_HUMANMAP3K7physical
11865055

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BIRC1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP