SPB9_HUMAN - dbPTM
SPB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPB9_HUMAN
UniProt AC P50453
Protein Name Serpin B9
Gene Name SERPINB9
Organism Homo sapiens (Human).
Sequence Length 376
Subcellular Localization Cytoplasm.
Protein Description Granzyme B inhibitor..
Protein Sequence METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP
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
1Acetylation-------METLSNAS
-------CCCCCCCC		8.8422223895
3Phosphorylation-----METLSNASGT
-----CCCCCCCCHH		33.90-
10PhosphorylationTLSNASGTFAIRLLK
CCCCCCHHHHHHHHH		13.8529083192
50PhosphorylationLLGAKGNTATQMAQA
HHCCCCCHHHHHHHH		39.4929449344
52PhosphorylationGAKGNTATQMAQALS
CCCCCHHHHHHHHHC		19.4829449344
59PhosphorylationTQMAQALSLNTEEDI
HHHHHHHCCCCHHHH		23.6929449344
62PhosphorylationAQALSLNTEEDIHRA
HHHHCCCCHHHHHHH		46.1529449344
72PhosphorylationDIHRAFQSLLTEVNK
HHHHHHHHHHHHHHH		20.9221712546
96AcetylationANRLFGEKTCQFLST
HHHHHCHHHHHHHHH		55.7930585503
96UbiquitinationANRLFGEKTCQFLST
HHHHHCHHHHHHHHH		55.79-
102PhosphorylationEKTCQFLSTFKESCL
HHHHHHHHHHHHHHH		32.8423312004
103PhosphorylationKTCQFLSTFKESCLQ
HHHHHHHHHHHHHHH		40.6523312004
117AcetylationQFYHAELKELSFIRA
HHHHHHHHHHHHHHH		48.387406513
138UbiquitinationHINTWVSKKTEGKIE
HHHHHHHHCCCCCHH		54.84-
138AcetylationHINTWVSKKTEGKIE
HHHHHHHHCCCCCHH		54.8430585509
151PhosphorylationIEELLPGSSIDAETR
HHHHCCCCCCCHHHH		23.3722817900
152PhosphorylationEELLPGSSIDAETRL
HHHCCCCCCCHHHHH		30.3322817900
166PhosphorylationLVLVNAIYFKGKWNE
HHEEEEEEECCCCCC		9.2327259358
170UbiquitinationNAIYFKGKWNEPFDE
EEEEECCCCCCCCCC		47.65-
199PhosphorylationQRPVQMMYQEATFKL
CCCCHHHHHHHHHHH		9.6228450419
203PhosphorylationQMMYQEATFKLAHVG
HHHHHHHHHHHHHHH		22.1328450419
252PhosphorylationSLTFEKLTAWTKPDC
CCCHHHCCCCCCCCC		31.0821406692
255PhosphorylationFEKLTAWTKPDCMKS
HHHCCCCCCCCCCCC		30.1821406692
297UbiquitinationVDAFQQGKADLSAMS
HHHHHHCCCCHHHHH		34.1021906983
310S-nitrosylationMSAERDLCLSKFVHK
HHHHHHHHHHHHHHH		4.7724105792
313UbiquitinationERDLCLSKFVHKSFV
HHHHHHHHHHHHHHE		38.16-
350S-nitrosylationMESGPRFCADHPFLF
HHHCCCCCCCCCEEE		4.6124105792
366PhosphorylationIRHNRANSILFCGRF
EECCCCCEEEEEECC		21.4919664994
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 SPB9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPB9_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 SPB9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ECH1_HUMANECH1physical
16169070
GBP2_HUMANGBP2physical
16169070
GDF9_HUMANGDF9physical
16169070
PKHM1_HUMANPLEKHM1physical
16169070
ERG28_HUMANC14orf1physical
16169070
CSN6_HUMANCOPS6physical
16169070
PR40A_HUMANPRPF40Aphysical
16169070
XRCC6_HUMANXRCC6physical
16169070
CC90B_HUMANCCDC90Bphysical
16169070
IGS21_HUMANIGSF21physical
16169070
SETB1_HUMANSETDB1physical
16169070
ZHX1_HUMANZHX1physical
16169070
MED31_HUMANMED31physical
16169070
RBM48_HUMANRBM48physical
16169070
G3P_HUMANGAPDHphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
TLE1_HUMANTLE1physical
16169070
P53_HUMANTP53physical
16169070
TBB2A_HUMANTUBB2Aphysical
16169070
UBR1_HUMANUBR1physical
16169070
U119A_HUMANUNC119physical
16169070
BRD7_HUMANBRD7physical
16169070
DPYL1_HUMANCRMP1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
TRAF5_HUMANTRAF5physical
25416956
CASP1_HUMANCASP1physical
10477277
CASP4_HUMANCASP4physical
10477277
CASP8_HUMANCASP8physical
17479112
CASPA_HUMANCASP10physical
17479112
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 SPB9_HUMAN

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Related Literatures of Post-Translational Modification

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