SHLB2_HUMAN - dbPTM
SHLB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHLB2_HUMAN
UniProt AC Q9NR46
Protein Name Endophilin-B2
Gene Name SH3GLB2
Organism Homo sapiens (Human).
Sequence Length 395
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MDFNMKKLASDAGIFFTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTEKILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMADAASELGPTTPYGKTLIKVAEAEKQLGAAERDFIHTASISFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLKKAKAAEAKATTVPDFQETRPRNYILSASASALWNDEVDKAEQELRVAQTEFDRQAEVTRLLLEGISSTHVNHLRCLHEFVKSQTTYYAQCYRHMLDLQKQLGRFPGTFVGTTEPASPPLSSTSPTTAAATMPVVPSVASLAPPGEASLCLEEVAPPASGTRKARVLYDYEAADSSELALLADELITVYSLPGMDPDWLIGERGNKKGKVPVTYLELLS
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-------MDFNMKKL
-------CCCCHHHH
13.8222814378
6Methylation--MDFNMKKLASDAG
--CCCCHHHHHHHHC
45.82-
7Methylation-MDFNMKKLASDAGI
-CCCCHHHHHHHHCC
38.22-
7Ubiquitination-MDFNMKKLASDAGI
-CCCCHHHHHHHHCC
38.22-
10PhosphorylationFNMKKLASDAGIFFT
CCHHHHHHHHCCEEH
38.1327499020
17PhosphorylationSDAGIFFTRAVQFTE
HHHCCEEHHHHHHCH
13.6323186163
26 (in isoform 2)Ubiquitination-48.8721890473
26UbiquitinationAVQFTEEKFGQAEKT
HHHHCHHHHCCCHHH
48.8721890473
32UbiquitinationEKFGQAEKTELDAHF
HHHCCCHHHHHHHHH
50.76-
48PhosphorylationNLLARADSTKNWTEK
HHHHHHHHCCCHHHH
40.0527461979
49PhosphorylationLLARADSTKNWTEKI
HHHHHHHCCCHHHHH
29.0127461979
50UbiquitinationLARADSTKNWTEKIL
HHHHHHCCCHHHHHH
55.21-
53PhosphorylationADSTKNWTEKILRQT
HHHCCCHHHHHHHHH
36.4727461979
55UbiquitinationSTKNWTEKILRQTEV
HCCCHHHHHHHHHHH
39.40-
77PhosphorylationARVEEFLYEKLDRKV
HHHHHHHHHHHCCCC
19.1521945579
77 (in isoform 2)Phosphorylation-19.1527642862
79UbiquitinationVEEFLYEKLDRKVPS
HHHHHHHHHCCCCCC
41.9721906983
79 (in isoform 1)Ubiquitination-41.9721890473
79 (in isoform 2)Ubiquitination-41.9721890473
97PhosphorylationNGELLAQYMADAASE
CHHHHHHHHHHHHHH
6.6729496907
108PhosphorylationAASELGPTTPYGKTL
HHHHHCCCCCCCHHH
38.31-
109PhosphorylationASELGPTTPYGKTLI
HHHHCCCCCCCHHHH
20.04-
111PhosphorylationELGPTTPYGKTLIKV
HHCCCCCCCHHHHHH
29.2129496907
117UbiquitinationPYGKTLIKVAEAEKQ
CCCHHHHHHHHHHHH
38.21-
123 (in isoform 1)Ubiquitination-58.8521890473
123 (in isoform 2)Ubiquitination-58.8521890473
123UbiquitinationIKVAEAEKQLGAAER
HHHHHHHHHHCCCCH
58.8521906983
137PhosphorylationRDFIHTASISFLTPL
HHHCHHHHHHHCHHC
21.6626270265
139PhosphorylationFIHTASISFLTPLRN
HCHHHHHHHCHHCHH
16.2326270265
142PhosphorylationTASISFLTPLRNFLE
HHHHHHCHHCHHHHC
20.4725159151
153 (in isoform 1)Ubiquitination-40.4921890473
153AcetylationNFLEGDWKTISKERR
HHHCCCHHHHHHHHH
40.4925953088
153 (in isoform 2)Ubiquitination-40.4921890473
153UbiquitinationNFLEGDWKTISKERR
HHHCCCHHHHHHHHH
40.4921906983
173UbiquitinationRLDLDACKARLKKAK
CCCHHHHHHHHHHHH
37.96-
178AcetylationACKARLKKAKAAEAK
HHHHHHHHHHHHHCC
60.767664671
180AcetylationKARLKKAKAAEAKAT
HHHHHHHHHHHCCCC
57.947664683
185AcetylationKAKAAEAKATTVPDF
HHHHHHCCCCCCCCH
37.467664695
185 (in isoform 1)Ubiquitination-37.4621890473
185UbiquitinationKAKAAEAKATTVPDF
HHHHHHCCCCCCCCH
37.4621906983
187PhosphorylationKAAEAKATTVPDFQE
HHHHCCCCCCCCHHH
27.8528348404
188PhosphorylationAAEAKATTVPDFQET
HHHCCCCCCCCHHHC
34.6026657352
195PhosphorylationTVPDFQETRPRNYIL
CCCCHHHCCCCCEEE
34.8821712546
198MethylationDFQETRPRNYILSAS
CHHHCCCCCEEEEEE
45.34-
203PhosphorylationRPRNYILSASASALW
CCCCEEEEEEHHHHC
15.6028464451
204 (in isoform 2)Phosphorylation-12.9827642862
205PhosphorylationRNYILSASASALWND
CCEEEEEEHHHHCCH
21.2725849741
207PhosphorylationYILSASASALWNDEV
EEEEEEHHHHCCHHH
22.7728464451
230MethylationVAQTEFDRQAEVTRL
HHHHHHHHHHHHHHH
42.82-
259PhosphorylationCLHEFVKSQTTYYAQ
HHHHHHHHCHHHHHH
27.70-
262PhosphorylationEFVKSQTTYYAQCYR
HHHHHCHHHHHHHHH
13.60-
263PhosphorylationFVKSQTTYYAQCYRH
HHHHCHHHHHHHHHH
10.53-
276UbiquitinationRHMLDLQKQLGRFPG
HHHHHHHHHHCCCCC
55.5821890473
276 (in isoform 1)Ubiquitination-55.5821890473
288PhosphorylationFPGTFVGTTEPASPP
CCCCEEECCCCCCCC
23.7628348404
289PhosphorylationPGTFVGTTEPASPPL
CCCEEECCCCCCCCC
33.7628348404
293PhosphorylationVGTTEPASPPLSSTS
EECCCCCCCCCCCCC
37.4526074081
297PhosphorylationEPASPPLSSTSPTTA
CCCCCCCCCCCCCCC
37.0326074081
298PhosphorylationPASPPLSSTSPTTAA
CCCCCCCCCCCCCCH
40.3626074081
299PhosphorylationASPPLSSTSPTTAAA
CCCCCCCCCCCCCHH
35.0426074081
300PhosphorylationSPPLSSTSPTTAAAT
CCCCCCCCCCCCHHC
23.3826074081
302PhosphorylationPLSSTSPTTAAATMP
CCCCCCCCCCHHCCC
28.9126074081
303PhosphorylationLSSTSPTTAAATMPV
CCCCCCCCCHHCCCC
20.0626074081
307PhosphorylationSPTTAAATMPVVPSV
CCCCCHHCCCCCCCH
19.7926074081
313PhosphorylationATMPVVPSVASLAPP
HCCCCCCCHHHCCCC
20.7826074081
316O-linked_GlycosylationPVVPSVASLAPPGEA
CCCCCHHHCCCCCCC
23.94OGP
316PhosphorylationPVVPSVASLAPPGEA
CCCCCHHHCCCCCCC
23.9426074081
363PhosphorylationLLADELITVYSLPGM
HHHHHEEEHHCCCCC
26.4730257219
365PhosphorylationADELITVYSLPGMDP
HHHEEEHHCCCCCCC
8.8830257219
366PhosphorylationDELITVYSLPGMDPD
HHEEEHHCCCCCCCC
24.6130257219
390PhosphorylationKGKVPVTYLELLS--
CCCCCCEEEHHCC--
9.8328102081
395PhosphorylationVTYLELLS-------
CEEEHHCC-------
51.2921712546

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 SHLB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHLB2_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 SHLB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD158_HUMANCCDC158physical
16189514
SH3K1_HUMANSH3KBP1physical
11894096
SHLB1_HUMANSH3GLB1physical
11161816
SHLB1_HUMANSH3GLB1physical
20562859
UBA5_HUMANUBA5physical
20562859
PGK1_HUMANPGK1physical
20562859
FKBP4_HUMANFKBP4physical
20562859
PA2G4_HUMANPA2G4physical
20562859
KDM1A_HUMANKDM1Aphysical
23455924
AASD1_HUMANAARSD1physical
22863883
LZTL1_HUMANLZTFL1physical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
TBCD_HUMANTBCDphysical
22863883
THG1_HUMANTHG1Lphysical
22863883
RHOA_HUMANRHOAphysical
16849557

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 SHLB2_HUMAN

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Related Literatures of Post-Translational Modification

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