B2L13_HUMAN - dbPTM
B2L13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID B2L13_HUMAN
UniProt AC Q9BXK5
Protein Name Bcl-2-like protein 13
Gene Name BCL2L13
Organism Homo sapiens (Human).
Sequence Length 485
Subcellular Localization Isoform 2: Mitochondrion membrane
Single-pass membrane protein . Nucleus .
Isoform 1: Nucleus .
Protein Description May promote the activation of caspase-3 and apoptosis..
Protein Sequence MASSSTVPLGFHYETKYVVLSYLGLLSQEKLQEQHLSSPQGVQLDIASQSLDQEILLKVKTEIEEELKSLDKEISEAFTSTGFDRHTSPVFSPANPESSMEDCLAHLGEKVSQELKEPLHKALQMLLSQPVTYQAFRECTLETTVHASGWNKILVPLVLLRQMLLELTRRGQEPLSALLQFGVTYLEDYSAEYIIQQGGWGTVFSLESEEEEYPGITAEDSNDIYILPSDNSGQVSPPESPTVTTSWQSESLPVSLSASQSWHTESLPVSLGPESWQQIAMDPEEVKSLDSNGAGEKSENNSSNSDIVHVEKEEVPEGMEEAAVASVVLPARELQEALPEAPAPLLPHITATSLLGTREPDTEVITVEKSSPATSLFVELDEEEVKAATTEPTEVEEVVPALEPTETLLSEKEINAREESLVEELSPASEKKPVPPSEGKSRLSPAGEMKPMPLSEGKSILLFGGAAAVAILAVAIGVALALRKK
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
3Phosphorylation-----MASSSTVPLG
-----CCCCCCCCCC		24.4322115753
4Phosphorylation----MASSSTVPLGF
----CCCCCCCCCCC		22.0822115753
5Phosphorylation---MASSSTVPLGFH
---CCCCCCCCCCCC		30.8122115753
6Phosphorylation--MASSSTVPLGFHY
--CCCCCCCCCCCCC		28.2622115753
37PhosphorylationKLQEQHLSSPQGVQL
HHHHHHCCCCCCCEE		37.5430278072
38PhosphorylationLQEQHLSSPQGVQLD
HHHHHCCCCCCCEEE		27.8330278072
48PhosphorylationGVQLDIASQSLDQEI
CCEEEHHCCCCCHHH		22.1928450419
50PhosphorylationQLDIASQSLDQEILL
EEEHHCCCCCHHHHH		31.2727251275
60UbiquitinationQEILLKVKTEIEEEL
HHHHHHHHHHHHHHH		38.56-
61PhosphorylationEILLKVKTEIEEELK
HHHHHHHHHHHHHHH		45.2225278378
68UbiquitinationTEIEEELKSLDKEIS
HHHHHHHHHHCHHHH		52.86-
69PhosphorylationEIEEELKSLDKEISE
HHHHHHHHHCHHHHH		55.1925278378
72UbiquitinationEELKSLDKEISEAFT
HHHHHHCHHHHHHHH		63.34-
92PhosphorylationRHTSPVFSPANPESS
CCCCCCCCCCCCCCC		24.2827050516
110UbiquitinationCLAHLGEKVSQELKE
HHHHHHHHHHHHHHH		45.44-
116UbiquitinationEKVSQELKEPLHKAL
HHHHHHHHHHHHHHH		57.44-
132PhosphorylationMLLSQPVTYQAFREC
HHHCCCCHHHHHHHC		19.3224260401
133PhosphorylationLLSQPVTYQAFRECT
HHCCCCHHHHHHHCC		9.7024260401
168PhosphorylationRQMLLELTRRGQEPL
HHHHHHHHHCCCCCH		14.6727542207
232PhosphorylationYILPSDNSGQVSPPE
EEECCCCCCCCCCCC		35.2826074081
236PhosphorylationSDNSGQVSPPESPTV
CCCCCCCCCCCCCCE		27.1826074081
240PhosphorylationGQVSPPESPTVTTSW
CCCCCCCCCCEEECE		31.4826074081
242PhosphorylationVSPPESPTVTTSWQS
CCCCCCCCEEECEEC		39.5026074081
255PhosphorylationQSESLPVSLSASQSW
ECCCCCCEEEECCCE		18.0524275569
257PhosphorylationESLPVSLSASQSWHT
CCCCCEEEECCCEEC		20.5424275569
259PhosphorylationLPVSLSASQSWHTES
CCCEEEECCCEECCC		22.7526074081
261PhosphorylationVSLSASQSWHTESLP
CEEEECCCEECCCCC		20.5226074081
264PhosphorylationSASQSWHTESLPVSL
EECCCEECCCCCCCC		22.4726074081
266PhosphorylationSQSWHTESLPVSLGP
CCCEECCCCCCCCCH		38.8424275569
270PhosphorylationHTESLPVSLGPESWQ
ECCCCCCCCCHHHHH		26.1824275569
275PhosphorylationPVSLGPESWQQIAMD
CCCCCHHHHHHHCCC		33.0624275569
288PhosphorylationMDPEEVKSLDSNGAG
CCHHHHHCCCCCCCC		42.4529255136
288UbiquitinationMDPEEVKSLDSNGAG
CCHHHHHCCCCCCCC		42.4521890473
291PhosphorylationEEVKSLDSNGAGEKS
HHHHCCCCCCCCCCC		42.3229255136
298PhosphorylationSNGAGEKSENNSSNS
CCCCCCCCCCCCCCC		41.0529255136
302PhosphorylationGEKSENNSSNSDIVH
CCCCCCCCCCCCCEE		42.3429255136
303PhosphorylationEKSENNSSNSDIVHV
CCCCCCCCCCCCEEE		42.3429255136
305PhosphorylationSENNSSNSDIVHVEK
CCCCCCCCCCEEEEH		30.5729255136
326PhosphorylationMEEAAVASVVLPARE
HHHHHHHEEEEEHHH		13.2224275569
350PhosphorylationAPLLPHITATSLLGT
CCCCCCEEHHHCCCC		22.3528348404
352PhosphorylationLLPHITATSLLGTRE
CCCCEEHHHCCCCCC		15.9721712546
353PhosphorylationLPHITATSLLGTREP
CCCEEHHHCCCCCCC		21.0928348404
357PhosphorylationTATSLLGTREPDTEV
EHHHCCCCCCCCCEE		31.6528348404
362PhosphorylationLGTREPDTEVITVEK
CCCCCCCCEEEEEEC		42.7530108239
366PhosphorylationEPDTEVITVEKSSPA
CCCCEEEEEECCCCC		27.9930108239
370PhosphorylationEVITVEKSSPATSLF
EEEEEECCCCCEEEE		28.2230266825
371PhosphorylationVITVEKSSPATSLFV
EEEEECCCCCEEEEE		29.6225159151
374PhosphorylationVEKSSPATSLFVELD
EECCCCCEEEEEECC		29.3730278072
375PhosphorylationEKSSPATSLFVELDE
ECCCCCEEEEEECCH		23.1630278072
405PhosphorylationVVPALEPTETLLSEK
HHHCCCCHHHHCCHH		32.0229514088
407PhosphorylationPALEPTETLLSEKEI
HCCCCHHHHCCHHHH		35.1629514088
410PhosphorylationEPTETLLSEKEINAR
CCHHHHCCHHHHHHH		50.1329514088
412UbiquitinationTETLLSEKEINAREE
HHHHCCHHHHHHHHH		61.5921906983
412 (in isoform 1)Ubiquitination-61.5921890473
420PhosphorylationEINAREESLVEELSP
HHHHHHHHHHHHHCC		32.7219664994
426PhosphorylationESLVEELSPASEKKP
HHHHHHHCCCCCCCC		23.0029255136
429PhosphorylationVEELSPASEKKPVPP
HHHHCCCCCCCCCCC		54.0230266825
437PhosphorylationEKKPVPPSEGKSRLS
CCCCCCCCCCCCCCC		53.5725159151
440UbiquitinationPVPPSEGKSRLSPAG
CCCCCCCCCCCCCCC		28.49-
441PhosphorylationVPPSEGKSRLSPAGE
CCCCCCCCCCCCCCC		49.6823401153
444PhosphorylationSEGKSRLSPAGEMKP
CCCCCCCCCCCCCCC		16.1728355574
450 (in isoform 1)Ubiquitination-33.5821890473
450UbiquitinationLSPAGEMKPMPLSEG
CCCCCCCCCCCCCCC		33.582189047
455PhosphorylationEMKPMPLSEGKSILL
CCCCCCCCCCCEEEE		38.1323403867
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 B2L13_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of B2L13_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 B2L13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PLLP_HUMANPLLPphysical
25416956
TMUB2_HUMANTMUB2physical
25416956
TM128_HUMANTMEM128physical
25416956
TM86B_HUMANTMEM86Bphysical
25416956
SODC_HUMANSOD1physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of B2L13_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-426, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-426, ANDMASS SPECTROMETRY.

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