3BP5_HUMAN - dbPTM
3BP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 3BP5_HUMAN
UniProt AC O60239
Protein Name SH3 domain-binding protein 5
Gene Name SH3BP5
Organism Homo sapiens (Human).
Sequence Length 455
Subcellular Localization Mitochondrion .
Protein Description Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death..
Protein Sequence MDAALKRSRSEEPAEILPPARDEEEEEEEGMEQGLEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPRGCGVGAEGSSTSVEDLPGSKPEPDAISVASEAFEDDSCSNFVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVVRPGSLDLPSPVSLSEFGMMFPVLGPRSECSGASSPECEVERGDRAEGAENKTSDKANNNRGLSSSSGSGGSSKSQSSTSPEGQALENRMKQLSLQCSKGRDGIIADIKMVQIG
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
6Ubiquitination--MDAALKRSRSEEP
--CCHHHHCCCCCCC		43.53-
8PhosphorylationMDAALKRSRSEEPAE
CCHHHHCCCCCCCHH		38.2729978859
10PhosphorylationAALKRSRSEEPAEIL
HHHHCCCCCCCHHCC		47.7829978859
51UbiquitinationRIQGELEKLNQSTDD
HHHHHHHHHHCCHHH		66.42-
55PhosphorylationELEKLNQSTDDINRR
HHHHHHCCHHHHHHH		32.5025159151
56PhosphorylationLEKLNQSTDDINRRE
HHHHHCCHHHHHHHH		28.1124719451
91UbiquitinationLDELVKKIGKAVEDS
HHHHHHHHHHHHHCC		5.9221890473
93UbiquitinationELVKKIGKAVEDSKP
HHHHHHHHHHHCCCC		53.37-
99UbiquitinationGKAVEDSKPYWEARR
HHHHHCCCCHHHHHH		55.22-
101PhosphorylationAVEDSKPYWEARRVA
HHHCCCCHHHHHHHH		21.44-
117UbiquitinationQAQLEAQKATQDFQR
HHHHHHHHHHHHHHH		61.52-
133UbiquitinationTEVLRAAKETISLAE
HHHHHHHHHHHHHHH		55.17-
135PhosphorylationVLRAAKETISLAEQR
HHHHHHHHHHHHHHH		18.37-
137PhosphorylationRAAKETISLAEQRLL
HHHHHHHHHHHHHHH		29.0120068231
173UbiquitinationVMEAEQTKTRSELVH
HHHHHHHCCHHHHHH		41.45-
181UbiquitinationTRSELVHKETAARYN
CHHHHHHHHHHHHHH		49.64-
208PhosphorylationLKRAINKSKPYFELK
HHHHHHCCCCCHHHH		34.0822817900
209UbiquitinationKRAINKSKPYFELKA
HHHHHCCCCCHHHHH		45.40-
215UbiquitinationSKPYFELKAKYYVQL
CCCCHHHHHHEEEEH		35.3221890473
217UbiquitinationPYFELKAKYYVQLEQ
CCHHHHHHEEEEHHH		35.21-
226UbiquitinationYVQLEQLKKTVDDLQ
EEEHHHHHHHHHHHH		46.20-
227UbiquitinationVQLEQLKKTVDDLQA
EEHHHHHHHHHHHHH		63.47-
235UbiquitinationTVDDLQAKLTLAKGE
HHHHHHHHHHHHHHH		29.10-
235MethylationTVDDLQAKLTLAKGE
HHHHHHHHHHHHHHH		29.10-
235AcetylationTVDDLQAKLTLAKGE
HHHHHHHHHHHHHHH		29.107851103
235TrimethylationTVDDLQAKLTLAKGE
HHHHHHHHHHHHHHH		29.10-
240UbiquitinationQAKLTLAKGEYKMAL
HHHHHHHHHHHHHHH		56.22-
240MethylationQAKLTLAKGEYKMAL
HHHHHHHHHHHHHHH		56.2223644510
240"N6,N6-dimethyllysine"QAKLTLAKGEYKMAL
HHHHHHHHHHHHHHH		56.22-
244UbiquitinationTLAKGEYKMALKNLE
HHHHHHHHHHHHHHH		17.25-
248UbiquitinationGEYKMALKNLEMISD
HHHHHHHHHHHHCHH		50.3721890473
263PhosphorylationEIHERRRSSAMGPRG
HHHHHHHHHHCCCCC		22.1928102081
264PhosphorylationIHERRRSSAMGPRGC
HHHHHHHHHCCCCCC		22.0624260401
346PhosphorylationPAVVRPGSLDLPSPV
CCCCCCCCCCCCCCC		22.7627732954
351PhosphorylationPGSLDLPSPVSLSEF
CCCCCCCCCCCHHHH		45.2727732954
354PhosphorylationLDLPSPVSLSEFGMM
CCCCCCCCHHHHCCC		29.5727732954
356PhosphorylationLPSPVSLSEFGMMFP
CCCCCCHHHHCCCEE		24.3127732954
369PhosphorylationFPVLGPRSECSGASS
EEECCCCHHCCCCCC		46.1928270605
372PhosphorylationLGPRSECSGASSPEC
CCCCHHCCCCCCCCC		33.0823663014
375PhosphorylationRSECSGASSPECEVE
CHHCCCCCCCCCEEC		50.3721712546
376PhosphorylationSECSGASSPECEVER
HHCCCCCCCCCEECC		24.9621712546
393UbiquitinationRAEGAENKTSDKANN
CCCCCCCCCCCCCCC		40.69-
405PhosphorylationANNNRGLSSSSGSGG
CCCCCCCCCCCCCCC		30.8829978859
406PhosphorylationNNNRGLSSSSGSGGS
CCCCCCCCCCCCCCC		33.3029978859
407PhosphorylationNNRGLSSSSGSGGSS
CCCCCCCCCCCCCCC		35.0329978859
408PhosphorylationNRGLSSSSGSGGSSK
CCCCCCCCCCCCCCC		38.6429978859
410PhosphorylationGLSSSSGSGGSSKSQ
CCCCCCCCCCCCCCC		41.7630576142
413PhosphorylationSSSGSGGSSKSQSST
CCCCCCCCCCCCCCC		37.8130576142
414PhosphorylationSSGSGGSSKSQSSTS
CCCCCCCCCCCCCCC		39.3329978859
415UbiquitinationSGSGGSSKSQSSTSP
CCCCCCCCCCCCCCH		54.9621890473
416PhosphorylationGSGGSSKSQSSTSPE
CCCCCCCCCCCCCHH		36.9223663014
418PhosphorylationGGSSKSQSSTSPEGQ
CCCCCCCCCCCHHHH		42.5525262027
419PhosphorylationGSSKSQSSTSPEGQA
CCCCCCCCCCHHHHH		25.8525262027
420PhosphorylationSSKSQSSTSPEGQAL
CCCCCCCCCHHHHHH		54.2525159151
421PhosphorylationSKSQSSTSPEGQALE
CCCCCCCCHHHHHHH		23.9325159151
432UbiquitinationQALENRMKQLSLQCS
HHHHHHHHHHHHHCC		44.87-
439PhosphorylationKQLSLQCSKGRDGII
HHHHHHCCCCCCCEE		25.7825159151
440UbiquitinationQLSLQCSKGRDGIIA
HHHHHCCCCCCCEEE		66.64-
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
351SPhosphorylationKinaseMAPK9P45984
Uniprot
351SPhosphorylationKinaseMAPK12P53778
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 3BP5_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 3BP5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK08_HUMANMAPK8physical
12167088
MK09_HUMANMAPK9physical
12167088
MK10_HUMANMAPK10physical
12167088
BTK_HUMANBTKphysical
9571151
BTK_HUMANBTKphysical
10339589
DYST_HUMANDSTphysical
17043677
SYNE1_HUMANSYNE1physical
17043677
TNKS1_HUMANTNKSphysical
17043677
SOS1_HUMANSOS1physical
17043677
SPTB2_HUMANSPTBN1physical
17043677
A4_HUMANAPPphysical
21832049
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 3BP5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.

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