UACA_MOUSE - dbPTM
UACA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UACA_MOUSE
UniProt AC Q8CGB3
Protein Name Uveal autoantigen with coiled-coil domains and ankyrin repeats
Gene Name Uaca
Organism Mus musculus (Mouse).
Sequence Length 1411
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Expressed diffusely in cytoplasm.
Protein Description Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1.; Modulates isoactin dynamics to regulate the morphological alterations required for cell growth and motility. Interaction with ARF6 may modulate cell shape and motility after injury (By similarity). May be involved in multiple neurite formation. [PubMed: 23624502]
Protein Sequence MKSLKSRLWKQDAPGPTSPSSPTAVASTQSAEWNKYDDRLMKAAERGDVEKVSSILAKKGVHPGKLDVEGRSAFHVVASKGNLECLNAILTHGIDVATRDSAGRNALHLAAKYGHALCLQKLLQYNCPTEHVDLQGRTALHDAVMADCPSSIQLLCDHGASVNAKDIDGRTPLVLATQMCRPTICQLLIDRGADVNSRDKQNRTALMLGCEYGCRDAVEVLVKNGADLTLLDALGHDSSYYARIGDNLDILNLLKTASENTNKGRELWRKGPPLQQRNLSHTQDEGSVKSTQREQREPHSFQDLEIENEDLREKLRKIQQEQRILLDKVNGLQLQLNEEVMVADDLESEREKPKSLLAAKEKQHEESLRTIEALKNRFKYFESDHPGPGSYPSNRKEDMLHKQGQMYTTEPQCASPGIPPHMHSRSMLRPLELSLPSQTSYSENEILKKELETLRTYYDSAKQDRLKFQNELAHKVAECKALALECERVKEDSDEQIKQLEDALKDVQKRMYESEGKVKQMQTHFLALKEHLTNEAATGSHRIIEELREQLKDLKGKYEGASAEVGKLRSQIKQSEMLVGEFKRDEGRLVEENKRLQKECGTCEVELERRGRRVVELEGQLKELGAKLALSVPTEKFESMKSSLSNDINEKVKRLAEVGRDYESAQGEIRQLKRDLESVRAQHIRPEEHEQLRSRLEQKSGELGKKVSELTLKNQTLQKDVEKLHADNKLLNQQVHSLTVEMKTRYVPLRVSEEMKRSHDVNVEDLNKKLSEATQRYAEKKQEAERLLAENDKLTKNVSRLEAVFVAPEKHEKELMGLKSNIAELKKQLSELNKKCGEGQEKIRALMSENSSLKKTLSSQYVPAKTHEEVKASLNSTVEKTNRALLEAKKRFDDTSQEVSKLRDENEVLRRNLENVQNQMKADYVSLEEHSRRMSTVSQSLKEAQEANAAILADHRQGQEEIVSLHAEIKAQKKELDTIQECIKLKYAPLARLEECERKFKATEKGLKEQLSEQTHKCRQRDEEVKKGKQENERLRADLAALQKELQDRNALAEEAREAERALSGKADELSKQLKDLSQKYSDVKSEREKLVEEKAKQASEILAAQNLLQKQPVPLEQVEALKKSLNGTIEQLKEELRSKQRCLEREQQTVSQLQQLLENQKNSSVTLAEHLKLKEALEKEVGIMKASLREKEEESQKKTKEVSKLQTEVQTTKQALKNLETREVVDMSKYKATKNDLETQISNLNDKLASLNRKYDQACEEKVSAKDEKELLHLSIEQEIRDQKERCDKSLTTIMELQQRIQESAKQIEAKDNKITELLNDVERLKQALNGLSQLTYSSGSPTKRQSQLVDTLQQRVRDLQQQLADADRQHQEVIAIYRTHLLSAAQGHMDEDVQAALLQIIQMRQGLVC
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-------MKSLKSRL
-------CCCHHHHH		31.47-
17PhosphorylationKQDAPGPTSPSSPTA
CCCCCCCCCCCCCCC		60.2223375375
18PhosphorylationQDAPGPTSPSSPTAV
CCCCCCCCCCCCCCC		26.3923375375
20PhosphorylationAPGPTSPSSPTAVAS
CCCCCCCCCCCCCCC		49.0323375375
21PhosphorylationPGPTSPSSPTAVAST
CCCCCCCCCCCCCCC		29.6523384938
54PhosphorylationGDVEKVSSILAKKGV
CCHHHHHHHHHHCCC		25.3025338131
85GlutathionylationASKGNLECLNAILTH
ECCCCHHHHHHHHHC		3.9124333276
101PhosphorylationIDVATRDSAGRNALH
CCEECCCCCHHHHHH		29.3625159016
280PhosphorylationPLQQRNLSHTQDEGS
CCHHCCCCCCCCCCC		28.2126824392
282PhosphorylationQQRNLSHTQDEGSVK
HHCCCCCCCCCCCCC		34.0526643407
287PhosphorylationSHTQDEGSVKSTQRE
CCCCCCCCCCCCHHH		25.0726643407
290PhosphorylationQDEGSVKSTQREQRE
CCCCCCCCCHHHHCC		27.8428973931
300PhosphorylationREQREPHSFQDLEIE
HHHCCCCCCCCHHCC		35.0126824392
380PhosphorylationALKNRFKYFESDHPG
HHHHHHHHCCCCCCC		15.1829514104
453PhosphorylationILKKELETLRTYYDS
HHHHHHHHHHHHHHH		33.8817203969
705AcetylationQKSGELGKKVSELTL
HHHHHHHHHHHHHHH		63.732383563
716PhosphorylationELTLKNQTLQKDVEK
HHHHHCHHHHHHHHH		40.3230387612
768AcetylationVNVEDLNKKLSEATQ
CCHHHHHHHHHHHHH		63.4919857397
851PhosphorylationRALMSENSSLKKTLS
HHHHCCCCHHHHHHH		32.7525338131
852PhosphorylationALMSENSSLKKTLSS
HHHCCCCHHHHHHHC		56.6529514104
858PhosphorylationSSLKKTLSSQYVPAK
CHHHHHHHCCCCCCC		22.1929514104
861PhosphorylationKKTLSSQYVPAKTHE
HHHHHCCCCCCCCHH		15.4529514104
873PhosphorylationTHEEVKASLNSTVEK
CHHHHHHHHHHHHHH		23.5121454597
876PhosphorylationEVKASLNSTVEKTNR
HHHHHHHHHHHHHHH		38.8421454597
935PhosphorylationEEHSRRMSTVSQSLK
HHHHHHHHHHHHHHH		24.6822817900
936PhosphorylationEHSRRMSTVSQSLKE
HHHHHHHHHHHHHHH		18.1629472430
938PhosphorylationSRRMSTVSQSLKEAQ
HHHHHHHHHHHHHHH		17.7229472430
940PhosphorylationRMSTVSQSLKEAQEA
HHHHHHHHHHHHHHH		33.6229472430
1134AcetylationNGTIEQLKEELRSKQ
CCHHHHHHHHHHHHH		49.1622902405
1200PhosphorylationEEESQKKTKEVSKLQ
HHHHHHHHHHHHHHH		39.2027742792
1229PhosphorylationTREVVDMSKYKATKN
CHHHCCHHHHHCCCH		28.5028285833
1251PhosphorylationNLNDKLASLNRKYDQ
HHHHHHHHHHHHHHH		36.2929514104
1334PhosphorylationKQALNGLSQLTYSSG
HHHHHHHHHCCCCCC		25.2525168779
1337PhosphorylationLNGLSQLTYSSGSPT
HHHHHHCCCCCCCCC		17.4525168779
1339PhosphorylationGLSQLTYSSGSPTKR
HHHHCCCCCCCCCHH		24.0026643407
1340PhosphorylationLSQLTYSSGSPTKRQ
HHHCCCCCCCCCHHH		32.6426643407
1342PhosphorylationQLTYSSGSPTKRQSQ
HCCCCCCCCCHHHHH		31.2026643407
1344PhosphorylationTYSSGSPTKRQSQLV
CCCCCCCCHHHHHHH		40.3226643407
1348PhosphorylationGSPTKRQSQLVDTLQ
CCCCHHHHHHHHHHH		29.5225338131
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 UACA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UACA_MOUSE !!
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 UACA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEG4_MOUSELgals4physical
14961764
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UACA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453, AND MASSSPECTROMETRY.

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