CAB39_HUMAN - dbPTM
CAB39_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAB39_HUMAN
UniProt AC Q9Y376
Protein Name Calcium-binding protein 39
Gene Name CAB39
Organism Homo sapiens (Human).
Sequence Length 341
Subcellular Localization Cytoplasm .
Protein Description Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1..
Protein Sequence MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEKEPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYICTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQAKLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRPAQQEA
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
8PhosphorylationMPFPFGKSHKSPADI
CCCCCCCCCCCHHHH		36.2023312004
11PhosphorylationPFGKSHKSPADIVKN
CCCCCCCCHHHHHHH		21.6421815630
20UbiquitinationADIVKNLKESMAVLE
HHHHHHHHHHHHHHH		58.07-
28UbiquitinationESMAVLEKQDISDKK
HHHHHHHHCCCCHHH		49.46-
45UbiquitinationKATEEVSKNLVAMKE
HHHHHHHHHHHHHHH		60.5221890473
45UbiquitinationKATEEVSKNLVAMKE
HHHHHHHHHHHHHHH		60.5221890473
1962-HydroxyisobutyrylationKDLLTRHKLLSAEFL
HHHHHHHHHHCHHHH		48.08-
199PhosphorylationLTRHKLLSAEFLEQH
HHHHHHHCHHHHHHH		35.8720068231
207PhosphorylationAEFLEQHYDRFFSEY
HHHHHHHHHHHHHHH		14.4420068231
209MethylationFLEQHYDRFFSEYEK
HHHHHHHHHHHHHHH		27.61-
212PhosphorylationQHYDRFFSEYEKLLH
HHHHHHHHHHHHHHC		36.24-
220PhosphorylationEYEKLLHSENYVTKR
HHHHHHCCCCCCCHH		27.7528152594
223PhosphorylationKLLHSENYVTKRQSL
HHHCCCCCCCHHHHH		12.8728152594
225PhosphorylationLHSENYVTKRQSLKL
HCCCCCCCHHHHHHH		15.3428152594
226UbiquitinationHSENYVTKRQSLKLL
CCCCCCCHHHHHHHH		38.09-
2262-HydroxyisobutyrylationHSENYVTKRQSLKLL
CCCCCCCHHHHHHHH		38.09-
297AcetylationPILDILLKNQAKLIE
CHHHHHHHCHHHHHH		43.5019608861
297UbiquitinationPILDILLKNQAKLIE
CHHHHHHHCHHHHHH		43.5019608861
301AcetylationILLKNQAKLIEFLSK
HHHHCHHHHHHHHHH		39.9923749302
301UbiquitinationILLKNQAKLIEFLSK
HHHHCHHHHHHHHHH		39.9921890473
301UbiquitinationILLKNQAKLIEFLSK
HHHHCHHHHHHHHHH		39.9921890473
307PhosphorylationAKLIEFLSKFQNDRT
HHHHHHHHHHCCCCC		36.4221815630
308AcetylationKLIEFLSKFQNDRTE
HHHHHHHHHCCCCCC		53.7926051181
308UbiquitinationKLIEFLSKFQNDRTE
HHHHHHHHHCCCCCC		53.79-
313MethylationLSKFQNDRTEDEQFN
HHHHCCCCCCCCCCC		47.79-
325PhosphorylationQFNDEKTYLVKQIRD
CCCHHHHHHHHHHHH		22.14-
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 CAB39_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAB39_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 CAB39_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EBLN2_HUMANEBLN2physical
17353931
STRAA_HUMANSTRADAphysical
14730349
VP26B_HUMANVPS26Bphysical
22939629
AP2B1_HUMANAP2B1physical
26344197
FAHD1_HUMANFAHD1physical
26344197
SIN3A_HUMANSIN3Aphysical
26344197
TACO1_HUMANTACO1physical
26344197
UBE2N_HUMANUBE2Nphysical
26344197
UBL5_HUMANUBL5physical
26344197
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 CAB39_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-297, AND MASS SPECTROMETRY.

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