TB22B_HUMAN - dbPTM
TB22B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TB22B_HUMAN
UniProt AC Q9NU19
Protein Name TBC1 domain family member 22B
Gene Name TBC1D22B
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MAAENSKQFWKRSAKLPGSIQPVYGAQHPPLDPRLTKNFIKERSKVNTVPLKNKKASSFHEFARNTSDAWDIGDDEEEDFSSPSFQTLNSKVALATAAQVLENHSKLRVKPERSQSTTSDVPANYKVIKSSSDAQLSRNSSDTCLRNPLHKQQSLPLRPIIPLVARISDQNASGAPPMTVREKTRLEKFRQLLSSQNTDLDELRKCSWPGVPREVRPITWRLLSGYLPANTERRKLTLQRKREEYFGFIEQYYDSRNEEHHQDTYRQIHIDIPRTNPLIPLFQQPLVQEIFERILFIWAIRHPASGYVQGINDLVTPFFVVFLSEYVEEDVENFDVTNLSQDMLRSIEADSFWCMSKLLDGIQDNYTFAQPGIQKKVKALEELVSRIDEQVHNHFRRYEVEYLQFAFRWMNNLLMRELPLRCTIRLWDTYQSEPEGFSHFHLYVCAAFLIKWRKEILDEEDFQGLLMLLQNLPTIHWGNEEIGLLLAEAYRLKYMFADAPNHYRR
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
2Acetylation------MAAENSKQF
------CCCHHHHHH
24.3923572552
13PhosphorylationSKQFWKRSAKLPGSI
HHHHHHHHCCCCCCC
26.48-
24PhosphorylationPGSIQPVYGAQHPPL
CCCCCCCCCCCCCCC
17.2727642862
57PhosphorylationPLKNKKASSFHEFAR
CCCCCCCHHHHHHHH
42.2826657352
58PhosphorylationLKNKKASSFHEFARN
CCCCCCHHHHHHHHC
35.1725159151
66PhosphorylationFHEFARNTSDAWDIG
HHHHHHCCCCCCCCC
23.5628348404
67PhosphorylationHEFARNTSDAWDIGD
HHHHHCCCCCCCCCC
28.9628348404
114PhosphorylationLRVKPERSQSTTSDV
CCCCCCCCCCCCCCC
27.1621955146
116PhosphorylationVKPERSQSTTSDVPA
CCCCCCCCCCCCCCC
34.5923401153
117PhosphorylationKPERSQSTTSDVPAN
CCCCCCCCCCCCCCC
23.7621955146
118PhosphorylationPERSQSTTSDVPANY
CCCCCCCCCCCCCCE
28.3322115753
119PhosphorylationERSQSTTSDVPANYK
CCCCCCCCCCCCCEE
36.3822115753
125PhosphorylationTSDVPANYKVIKSSS
CCCCCCCEEEEECCC
14.5623403867
129UbiquitinationPANYKVIKSSSDAQL
CCCEEEEECCCCHHH
47.4729967540
130PhosphorylationANYKVIKSSSDAQLS
CCEEEEECCCCHHHH
24.7730242111
131PhosphorylationNYKVIKSSSDAQLSR
CEEEEECCCCHHHHC
27.5130242111
132PhosphorylationYKVIKSSSDAQLSRN
EEEEECCCCHHHHCC
44.0228102081
137PhosphorylationSSSDAQLSRNSSDTC
CCCCHHHHCCCCCCH
19.8228555341
140PhosphorylationDAQLSRNSSDTCLRN
CHHHHCCCCCCHHCC
28.6023403867
141PhosphorylationAQLSRNSSDTCLRNP
HHHHCCCCCCHHCCH
40.2523401153
143PhosphorylationLSRNSSDTCLRNPLH
HHCCCCCCHHCCHHH
18.5223403867
154PhosphorylationNPLHKQQSLPLRPII
CHHHCCCCCCCCCCH
29.4730266825
168PhosphorylationIPLVARISDQNASGA
HHHHHCCCCCCCCCC
27.8225002506
178SulfoxidationNASGAPPMTVREKTR
CCCCCCCCCHHHHHH
5.4221406390
219PhosphorylationPREVRPITWRLLSGY
CCCCCCCCHHHHCCC
13.7627251275
224PhosphorylationPITWRLLSGYLPANT
CCCHHHHCCCCCCCH
29.9528857561
226PhosphorylationTWRLLSGYLPANTER
CHHHHCCCCCCCHHH
13.2127251275
231PhosphorylationSGYLPANTERRKLTL
CCCCCCCHHHHHHHH
32.7327251275
264PhosphorylationNEEHHQDTYRQIHID
CHHHHHHHCCEEEEE
17.6528787133
375UbiquitinationFAQPGIQKKVKALEE
CCCCCHHHHHHHHHH
58.5829967540
503PhosphorylationFADAPNHYRR-----
HCCCCCCCCC-----
18.0927642862

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 TB22B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TB22B_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 TB22B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEX11_HUMANTEX11physical
25416956
TRI54_HUMANTRIM54physical
25416956
PNMA5_HUMANPNMA5physical
25416956
K1C40_HUMANKRT40physical
25416956
DEUP1_HUMANCCDC67physical
25416956
CCD57_HUMANCCDC57physical
25416956
TB22A_HUMANTBC1D22Aphysical
28514442
CLC4K_HUMANCD207physical
28514442
S1A7A_HUMANS100A7Aphysical
28514442
NGAL_HUMANLCN2physical
28514442
RDHE2_HUMANSDR16C5physical
28514442
ST2B1_HUMANSULT2B1physical
28514442
KLK7_HUMANKLK7physical
28514442
KLK10_HUMANKLK10physical
28514442
PEPL_HUMANPPLphysical
28514442
PA24E_HUMANPLA2G4Ephysical
28514442
INVO_HUMANIVLphysical
28514442
SPB8_HUMANSERPINB8physical
28514442
POF1B_HUMANPOF1Bphysical
28514442
PLBL1_HUMANPLBD1physical
28514442
SPB4_HUMANSERPINB4physical
28514442
I36RA_HUMANIL36RNphysical
28514442
DR9C7_HUMANSDR9C7physical
28514442
TYPH_HUMANTYMPphysical
28514442
EPIPL_HUMANEPPK1physical
28514442
SPB5_HUMANSERPINB5physical
28514442
PPAP_HUMANACPPphysical
28514442
EVPL_HUMANEVPLphysical
28514442
SPB7_HUMANSERPINB7physical
28514442
AACT_HUMANSERPINA3physical
28514442
CH3L2_HUMANCHI3L2physical
28514442
ARSF_HUMANARSFphysical
28514442
ILEU_HUMANSERPINB1physical
28514442
IL1RA_HUMANIL1RNphysical
28514442
AK1BA_HUMANAKR1B10physical
28514442
5NT3A_HUMANNT5C3Aphysical
28514442
STS_HUMANSTSphysical
28514442
CATL2_HUMANCTSVphysical
28514442
S10A7_HUMANS100A7physical
28514442
HUTH_HUMANHALphysical
28514442
TGM1_HUMANTGM1physical
28514442
NEUR2_HUMANNEU2physical
28514442
S100P_HUMANS100Pphysical
28514442
CRBG1_HUMANAIM1physical
28514442
CATH_HUMANCTSHphysical
28514442
ES8L1_HUMANEPS8L1physical
28514442
SAP3_HUMANGM2Aphysical
28514442
CAPG_HUMANCAPGphysical
28514442
STAT3_HUMANSTAT3physical
28514442
SPB3_HUMANSERPINB3physical
28514442
CALL5_HUMANCALML5physical
28514442
RNAS7_HUMANRNASE7physical
28514442
ECM1_HUMANECM1physical
28514442
LX12B_HUMANALOX12Bphysical
28514442
SBSN_HUMANSBSNphysical
28514442
CBPA4_HUMANCPA4physical
28514442
S10A8_HUMANS100A8physical
28514442
ANXA8_HUMANANXA8physical
28514442
TRI29_HUMANTRIM29physical
28514442
S10A9_HUMANS100A9physical
28514442
GSDMA_HUMANGSDMAphysical
28514442
NAL10_HUMANNLRP10physical
28514442
TGM3_HUMANTGM3physical
28514442
HMOX1_HUMANHMOX1physical
28514442
SPB13_HUMANSERPINB13physical
28514442
ARL8B_HUMANARL8Bphysical
28514442
CPNS2_HUMANCAPNS2physical
28514442
CAN1_HUMANCAPN1physical
28514442
ARF6_HUMANARF6physical
28514442
CASPE_HUMANCASP14physical
28514442
ASAH1_HUMANASAH1physical
28514442
S10AG_HUMANS100A16physical
28514442
DSG1_HUMANDSG1physical
28514442
FBX50_HUMANNCCRP1physical
28514442
CYTM_HUMANCST6physical
28514442
CBPM_HUMANCPMphysical
28514442
GCP60_HUMANACBD3physical
28514442
GLNA_HUMANGLULphysical
28514442
ZA2G_HUMANAZGP1physical
28514442

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 TB22B_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-168, AND MASSSPECTROMETRY.

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