TB22A_HUMAN - dbPTM
TB22A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TB22A_HUMAN
UniProt AC Q8WUA7
Protein Name TBC1 domain family member 22A
Gene Name TBC1D22A
Organism Homo sapiens (Human).
Sequence Length 517
Subcellular Localization
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MASDGARKQFWKRSNSKLPGSIQHVYGAQHPPFDPLLHGTLLRSTAKMPTTPVKAKRVSTFQEFESNTSDAWDAGEDDDELLAMAAESLNSEVVMETANRVLRNHSQRQGRPTLQEGPGLQQKPRPEAEPPSPPSGDLRLVKSVSESHTSCPAESASDAAPLQRSQSLPHSATVTLGGTSDPSTLSSSALSEREASRLDKFKQLLAGPNTDLEELRRLSWSGIPKPVRPMTWKLLSGYLPANVDRRPATLQRKQKEYFAFIEHYYDSRNDEVHQDTYRQIHIDIPRMSPEALILQPKVTEIFERILFIWAIRHPASGYVQGINDLVTPFFVVFICEYIEAEEVDTVDVSGVPAEVLCNIEADTYWCMSKLLDGIQDNYTFAQPGIQMKVKMLEELVSRIDEQVHRHLDQHEVRYLQFAFRWMNNLLMREVPLRCTIRLWDTYQSEPDGFSHFHLYVCAAFLVRWRKEILEEKDFQELLLFLQNLPTAHWDDEDISLLLAEAYRLKFAFADAPNHYKK
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------MASDGARKQ
------CCCHHHHHH		19.1423572552
12UbiquitinationGARKQFWKRSNSKLP
HHHHHHHHHCCCCCC		47.43-
14PhosphorylationRKQFWKRSNSKLPGS
HHHHHHHCCCCCCCC		41.5524719451
16PhosphorylationQFWKRSNSKLPGSIQ
HHHHHCCCCCCCCCE		36.4928857561
21PhosphorylationSNSKLPGSIQHVYGA
CCCCCCCCCEEECCC		19.6928796482
26PhosphorylationPGSIQHVYGAQHPPF
CCCCEEECCCCCCCC		12.4828796482
44O-linked_GlycosylationLHGTLLRSTAKMPTT
HCHHHHHHCCCCCCC		32.4630379171
50PhosphorylationRSTAKMPTTPVKAKR
HHCCCCCCCCCCCCE		39.9920068231
51PhosphorylationSTAKMPTTPVKAKRV
HCCCCCCCCCCCCEE		21.8820068231
106PhosphorylationNRVLRNHSQRQGRPT
HHHHHHCHHHCCCCC		30.5224247654
113PhosphorylationSQRQGRPTLQEGPGL
HHHCCCCCCCCCCCC		39.4523927012
118 (in isoform 3)Phosphorylation-39.3021406692
128 (in isoform 2)Phosphorylation-36.9622210691
130 (in isoform 2)Phosphorylation-41.5422210691
131 (in isoform 2)Phosphorylation-51.4722210691
132PhosphorylationRPEAEPPSPPSGDLR
CCCCCCCCCCCCCCE		61.2229255136
135PhosphorylationAEPPSPPSGDLRLVK
CCCCCCCCCCCEEEE		48.6122167270
136 (in isoform 3)Phosphorylation-43.6921406692
143PhosphorylationGDLRLVKSVSESHTS
CCCEEEEECCCCCCC		24.3223927012
145PhosphorylationLRLVKSVSESHTSCP
CEEEEECCCCCCCCC		40.2423401153
147PhosphorylationLVKSVSESHTSCPAE
EEEECCCCCCCCCCC		25.2623927012
149PhosphorylationKSVSESHTSCPAESA
EECCCCCCCCCCCCH		41.1023927012
150PhosphorylationSVSESHTSCPAESAS
ECCCCCCCCCCCCHH		16.8123927012
155UbiquitinationHTSCPAESASDAAPL
CCCCCCCCHHCCCCC		34.87-
155PhosphorylationHTSCPAESASDAAPL
CCCCCCCCHHCCCCC		34.8723663014
157PhosphorylationSCPAESASDAAPLQR
CCCCCCHHCCCCCCC		36.7428450419
165PhosphorylationDAAPLQRSQSLPHSA
CCCCCCCCCCCCCCE		15.9125159151
167PhosphorylationAPLQRSQSLPHSATV
CCCCCCCCCCCCEEE		45.1523927012
171PhosphorylationRSQSLPHSATVTLGG
CCCCCCCCEEEEECC		24.5630278072
173PhosphorylationQSLPHSATVTLGGTS
CCCCCCEEEEECCCC		19.6230278072
175PhosphorylationLPHSATVTLGGTSDP
CCCCEEEEECCCCCH		18.4830278072
179PhosphorylationATVTLGGTSDPSTLS
EEEEECCCCCHHHCC		28.3223927012
180PhosphorylationTVTLGGTSDPSTLSS
EEEECCCCCHHHCCH		51.2923927012
183PhosphorylationLGGTSDPSTLSSSAL
ECCCCCHHHCCHHHC		47.1523927012
184PhosphorylationGGTSDPSTLSSSALS
CCCCCHHHCCHHHCC		35.7323927012
186PhosphorylationTSDPSTLSSSALSER
CCCHHHCCHHHCCHH		23.4920068231
187PhosphorylationSDPSTLSSSALSERE
CCHHHCCHHHCCHHH		23.8123927012
188PhosphorylationDPSTLSSSALSEREA
CHHHCCHHHCCHHHH		29.8323927012
191PhosphorylationTLSSSALSEREASRL
HCCHHHCCHHHHHHH		34.0323927012
196PhosphorylationALSEREASRLDKFKQ
HCCHHHHHHHHHHHH		28.7321406692
202UbiquitinationASRLDKFKQLLAGPN
HHHHHHHHHHHCCCC		45.86-
219PhosphorylationLEELRRLSWSGIPKP
HHHHHHHHCCCCCCC		19.8620068231
221PhosphorylationELRRLSWSGIPKPVR
HHHHHHCCCCCCCCC		24.3820068231
236PhosphorylationPMTWKLLSGYLPANV
CCCHHHHHCCCCCCC		35.5128857561
288PhosphorylationHIDIPRMSPEALILQ
EEECCCCCHHHEECC		22.37-
515PhosphorylationFADAPNHYKK-----
HCCCCCCCCC-----		27.4127642862
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 TB22A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TB22A_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 TB22A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS71L_HUMANHSPA1Lphysical
26186194
GCP60_HUMANACBD3physical
26186194
ADRO_HUMANFDXRphysical
26186194
ACSL4_HUMANACSL4physical
26186194
FWCH2_HUMANFLYWCH2physical
26186194
BIRC6_HUMANBIRC6physical
26186194
BIG1_HUMANARFGEF1physical
26186194
QSOX2_HUMANQSOX2physical
26186194
MICU1_HUMANMICU1physical
26186194
KIRR1_HUMANKIRRELphysical
26186194
MICU2_HUMANMICU2physical
26186194
DNJB4_HUMANDNAJB4physical
26186194
SPT6H_HUMANSUPT6Hphysical
26186194
EFNB3_HUMANEFNB3physical
26186194
EPHA4_HUMANEPHA4physical
26186194
EXOG_HUMANEXOGphysical
26186194
MET13_HUMANMETTL13physical
26186194
NECT2_HUMANPVRL2physical
26186194
DNJB5_HUMANDNAJB5physical
26186194
AMRA1_HUMANAMBRA1physical
26186194
SPT6H_HUMANSUPT6Hphysical
28514442
EFNB3_HUMANEFNB3physical
28514442
MICU2_HUMANMICU2physical
28514442
EPHA4_HUMANEPHA4physical
28514442
DNJB5_HUMANDNAJB5physical
28514442
EXOG_HUMANEXOGphysical
28514442
KIRR1_HUMANKIRRELphysical
28514442
MICU1_HUMANMICU1physical
28514442
GCP60_HUMANACBD3physical
28514442
ACSL4_HUMANACSL4physical
28514442
NECT2_HUMANPVRL2physical
28514442
FWCH2_HUMANFLYWCH2physical
28514442
ADRO_HUMANFDXRphysical
28514442
DNJB4_HUMANDNAJB4physical
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 TB22A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.

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