TBC24_HUMAN - dbPTM
TBC24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC24_HUMAN
UniProt AC Q9ULP9
Protein Name TBC1 domain family member 24
Gene Name TBC1D24
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Cytoplasm . Partially expressed at the plasma membrane.
Protein Description May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function..
Protein Sequence MDSPGYNCFVDKDKMDAAIQDLGPKELSCTELQELKQLARQGYWAQSHALRGKVYQRLIRDIPCRTVTPDASVYSDIVGKIVGKHSSSCLPLPEFVDNTQVPSYCLNARGEGAVRKILLCLANQFPDISFCPALPAVVALLLHYSIDEAECFEKACRILACNDPGRRLIDQSFLAFESSCMTFGDLVNKYCQAAHKLMVAVSEDVLQVYADWQRWLFGELPLCYFARVFDVFLVEGYKVLYRVALAILKFFHKVRAGQPLESDSVKQDIRTFVRDIAKTVSPEKLLEKAFAIRLFSRKEIQLLQMANEKALKQKGITVKQKSVSLSKRQFVHLAVHAENFRSEIVSVREMRDIWSWVPERFALCQPLLLFSSLQHGYSLARFYFQCEGHEPTLLLIKTTQKEVCGAYLSTDWSERNKFGGKLGFFGTGECFVFRLQPEVQRYEWVVIKHPELTKPPPLMAAEPTAPLSHSASSDPADRLSPFLAARHFNLPSKTESMFMAGGSDCLIVGGGGGQALYIDGDLNRGRTSHCDTFNNQPLCSENFLIAAVEAWGFQDPDTQ
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-----MDSPGYNCFV
-----CCCCCCCCEE		20.9425159151
12AcetylationGYNCFVDKDKMDAAI
CCCCEECHHHHHHHH		54.6827452117
28PhosphorylationDLGPKELSCTELQEL
HHCCCCCCCHHHHHH		21.7826657352
30PhosphorylationGPKELSCTELQELKQ
CCCCCCCHHHHHHHH		36.0327251275
36UbiquitinationCTELQELKQLARQGY
CHHHHHHHHHHHCCH		42.3829967540
80 (in isoform 2)Ubiquitination-24.2721890473
80 (in isoform 1)Ubiquitination-24.2721890473
80UbiquitinationVYSDIVGKIVGKHSS
HHHHHHHHHHCCCCC		24.2721890473
80UbiquitinationVYSDIVGKIVGKHSS
HHHHHHHHHHCCCCC		24.2721906983
84UbiquitinationIVGKIVGKHSSSCLP
HHHHHHCCCCCCCCC		29.4423503661
253UbiquitinationAILKFFHKVRAGQPL
HHHHHHHHHHCCCCC		28.4132142685
266 (in isoform 1)Ubiquitination-46.3221890473
266 (in isoform 2)Ubiquitination-46.3221890473
266UbiquitinationPLESDSVKQDIRTFV
CCCCCCHHHHHHHHH		46.3229967540
278UbiquitinationTFVRDIAKTVSPEKL
HHHHHHHHHCCHHHH		50.2027667366
284AcetylationAKTVSPEKLLEKAFA
HHHCCHHHHHHHHHH		62.8523236377
284MalonylationAKTVSPEKLLEKAFA
HHHCCHHHHHHHHHH		62.8526320211
284UbiquitinationAKTVSPEKLLEKAFA
HHHCCHHHHHHHHHH		62.8529967540
288UbiquitinationSPEKLLEKAFAIRLF
CHHHHHHHHHHHHHH		49.0919608861
288AcetylationSPEKLLEKAFAIRLF
CHHHHHHHHHHHHHH		49.0919608861
288MalonylationSPEKLLEKAFAIRLF
CHHHHHHHHHHHHHH		49.0926320211
298UbiquitinationAIRLFSRKEIQLLQM
HHHHHCHHHHHHHHH		58.95-
305SulfoxidationKEIQLLQMANEKALK
HHHHHHHHHCHHHHH		4.3321406390
312AcetylationMANEKALKQKGITVK
HHCHHHHHHCCCCEE		55.6219608861
314AcetylationNEKALKQKGITVKQK
CHHHHHHCCCCEEEE		51.1719608861
319AcetylationKQKGITVKQKSVSLS
HHCCCCEEEEEECCC		43.2725953088
319UbiquitinationKQKGITVKQKSVSLS
HHCCCCEEEEEECCC		43.2727667366
322PhosphorylationGITVKQKSVSLSKRQ
CCCEEEEEECCCHHH		17.9123532336
324PhosphorylationTVKQKSVSLSKRQFV
CEEEEEECCCHHHHH		33.7326437602
346PhosphorylationNFRSEIVSVREMRDI
HHHHHCEEHHHHHHH		22.5524719451
421AcetylationERNKFGGKLGFFGTG
HHCCCCCCCEEECCC		45.9025953088
442PhosphorylationLQPEVQRYEWVVIKH
ECHHHEEEEEEEEEC		9.3227642862
453PhosphorylationVIKHPELTKPPPLMA
EEECHHHCCCCCCEE		39.5828857561
454UbiquitinationIKHPELTKPPPLMAA
EECHHHCCCCCCEEC		69.06-
464PhosphorylationPLMAAEPTAPLSHSA
CCEECCCCCCCCCCC		32.2030108239
468PhosphorylationAEPTAPLSHSASSDP
CCCCCCCCCCCCCCH		17.8427794612
470PhosphorylationPTAPLSHSASSDPAD
CCCCCCCCCCCCHHH		26.8627794612
472PhosphorylationAPLSHSASSDPADRL
CCCCCCCCCCHHHHH		37.9829255136
473PhosphorylationPLSHSASSDPADRLS
CCCCCCCCCHHHHHH		47.5329255136
474PhosphorylationLSHSASSDPADRLSP
CCCCCCCCHHHHHHH		39.6532142685
480PhosphorylationSDPADRLSPFLAARH
CCHHHHHHHHHHHHH		17.9429255136
492PhosphorylationARHFNLPSKTESMFM
HHHCCCCCCCHHHEE		56.2124719451
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 TBC24_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC24_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 TBC24_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TBC24_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605021Familial infantile myoclonic epilepsy (FIME)
615338Epileptic encephalopathy, early infantile, 16 (EIEE16)
616044Deafness, autosomal dominant, 65 (DFNA65)
220500Deafness, onychodystrophy, osteodystrophy, mental retardation, and seizures syndrome (DOORS)
614617Deafness, autosomal recessive, 86 (DFNB86)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TBC24_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-312; LYS-314 ANDLYS-319, AND MASS SPECTROMETRY.

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