UACA_HUMAN - dbPTM
UACA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UACA_HUMAN
UniProt AC Q9BZF9
Protein Name Uveal autoantigen with coiled-coil domains and ankyrin repeats
Gene Name UACA
Organism Homo sapiens (Human).
Sequence Length 1416
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 (By similarity).; 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. May be involved in multiple neurite formation (By similarity)..
Protein Sequence MKSLKSRLRRQDVPGPASSGAAAASAHAADWNKYDDRLMKAAERGDVEKVTSILAKKGVNPGKLDVEGRSVFHVVTSKGNLECLNAILIHGVDITTSDTAGRNALHLAAKYGHALCLQKLLQYNCPTEHADLQGRTALHDAAMADCPSSIQLLCDHGASVNAKDVDGRTPLVLATQMSRPTICQLLIDRGADVNSRDKQNRTALMLGCEYGCRDAVEVLIKNGADISLLDALGHDSSYYARIGDNLDILTLLKTASENTNKGRELWKKGPSLQQRNLTHMQDEVNVKSHQREHQNIQDLEIENEDLKERLRKIQQEQRILLDKVNGLQLQLNEEVMVADDLESEREKLKSLLAAKEKQHEESLRTIEALKNRFKYFESDHLGSGSHFSNRKEDMLLKQGQMYMADSQCTSPGIPAHMQSRSMLRPLELSLPSQTSYSENEILKKELEAMRTFCESAKQDRLKLQNELAHKVAECKALALECERVKEDSDEQIKQLEDALKDVQKRMYESEGKVKQMQTHFLALKEHLTSEAASGNHRLTEELKDQLKDLKVKYEGASAEVGKLRNQIKQNEMIVEEFKRDEGKLIEENKRLQKELSMCEMEREKKGRKVTEMEGQAKELSAKLALSIPAEKFENMKSSLSNEVNEKAKKLVEMEREHEKSLSEIRQLKRELENVKAKLAQHVKPEEHEQVKSRLEQKSGELGKKITELTLKNQTLQKEIEKVYLDNKLLKEQAHNLTIEMKNHYVPLKVSEDMKKSHDAIIDDLNRKLLDVTQKYTEKKLEMEKLLLENDSLSKDVSRLETVFVPPEKHEKEIIALKSNIVELKKQLSELKKKCGEDQEKIHALTSENTNLKKMMSNQYVPVKTHEEVKMTLNDTLAKTNRELLDVKKKFEDINQEFVKIKDKNEILKRNLENTQNQIKAEYISLAEHEAKMSSLSQSMRKVQDSNAEILANYRKGQEEIVTLHAEIKAQKKELDTIQECIKVKYAPIVSFEECERKFKATEKELKDQLSEQTQKYSVSEEEVKKNKQENDKLKKEIFTLQKDLRDKTVLIEKSHEMERALSRKTDELNKQLKDLSQKYTEVKNVKEKLVEENAKQTSEILAVQNLLQKQHVPLEQVEALKKSLNGTIENLKEELKSMQRCYEKEQQTVTKLHQLLENQKNSSVPLAEHLQIKEAFEKEVGIIKASLREKEEESQNKMEEVSKLQSEVQNTKQALKKLETREVVDLSKYKATKSDLETQISSLNEKLANLNRKYEEVCEEVLHAKKKEISAKDEKELLHFSIEQEIKDQKERCDKSLTTITELQRRIQESAKQIEAKDNKITELLNDVERLKQALNGLSQLTYTSGNPTKRQSQLIDTLQHQVKSLEQQLADADRQHQEVIAIYRTHLLSAAQGHMDEDVQEALLQIIQMRQGLVC
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
31.4722814378
34PhosphorylationHAADWNKYDDRLMKA
HHHCHHHHHHHHHHH
21.6227642862
36UbiquitinationADWNKYDDRLMKAAE
HCHHHHHHHHHHHHH
42.3929967540
43UbiquitinationDRLMKAAERGDVEKV
HHHHHHHHCCCHHHH
63.1529967540
49UbiquitinationAERGDVEKVTSILAK
HHCCCHHHHHHHHHH
51.1429967540
51PhosphorylationRGDVEKVTSILAKKG
CCCHHHHHHHHHHCC
22.55-
52PhosphorylationGDVEKVTSILAKKGV
CCHHHHHHHHHHCCC
20.70-
56MalonylationKVTSILAKKGVNPGK
HHHHHHHHCCCCCCC
46.7626320211
56UbiquitinationKVTSILAKKGVNPGK
HHHHHHHHCCCCCCC
46.7629967540
57AcetylationVTSILAKKGVNPGKL
HHHHHHHCCCCCCCC
63.5812432665
57UbiquitinationVTSILAKKGVNPGKL
HHHHHHHCCCCCCCC
63.58-
76PhosphorylationRSVFHVVTSKGNLEC
CEEEEEEECCCCHHH
24.5127251275
77PhosphorylationSVFHVVTSKGNLECL
EEEEEEECCCCHHHH
27.2726471730
111PhosphorylationALHLAAKYGHALCLQ
HHHHHHHHHHHHHHH
14.9328102081
119AcetylationGHALCLQKLLQYNCP
HHHHHHHHHHHCCCC
37.9126051181
169PhosphorylationAKDVDGRTPLVLATQ
CCCCCCCCCCEEEEC
26.8920860994
175PhosphorylationRTPLVLATQMSRPTI
CCCCEEEECCCCHHH
22.2020860994
210PhosphorylationALMLGCEYGCRDAVE
HHHHCCCCCCHHHHH
26.1227642862
236PhosphorylationLDALGHDSSYYARIG
HHHCCCCCCHHCCCC
17.9927642862
236UbiquitinationLDALGHDSSYYARIG
HHHCCCCCCHHCCCC
17.9921963094
237PhosphorylationDALGHDSSYYARIGD
HHCCCCCCHHCCCCC
28.3727642862
239PhosphorylationLGHDSSYYARIGDNL
CCCCCCHHCCCCCCC
7.4327642862
240UbiquitinationGHDSSYYARIGDNLD
CCCCCHHCCCCCCCH
6.5921963094
250PhosphorylationGDNLDILTLLKTASE
CCCCHHHHHHHHHHC
30.3129255136
253UbiquitinationLDILTLLKTASENTN
CHHHHHHHHHHCCCH
45.2021963094
268AcetylationKGRELWKKGPSLQQR
HHHHHHHCCCCHHHH
65.5530593181
271PhosphorylationELWKKGPSLQQRNLT
HHHHCCCCHHHHCCC
47.6926437602
273UbiquitinationWKKGPSLQQRNLTHM
HHCCCCHHHHCCCCC
44.5221963094
274UbiquitinationKKGPSLQQRNLTHMQ
HCCCCHHHHCCCCCC
41.3329967540
287UbiquitinationMQDEVNVKSHQREHQ
CCHHHHHHHHHHHHC
36.7029967540
294UbiquitinationKSHQREHQNIQDLEI
HHHHHHHCCCHHHHH
43.9229967540
307UbiquitinationEIENEDLKERLRKIQ
HHCCHHHHHHHHHHH
53.7829967540
336UbiquitinationLQLNEEVMVADDLES
ECCCCCEECCCCCHH
2.0229967540
349UbiquitinationESEREKLKSLLAAKE
HHHHHHHHHHHHHHH
50.5629967540
357UbiquitinationSLLAAKEKQHEESLR
HHHHHHHHHHHHHHH
57.1429967540
370UbiquitinationLRTIEALKNRFKYFE
HHHHHHHHHHHHHHC
53.8029967540
375PhosphorylationALKNRFKYFESDHLG
HHHHHHHHHCCCCCC
15.1823401153
378PhosphorylationNRFKYFESDHLGSGS
HHHHHHCCCCCCCCC
22.0423401153
383PhosphorylationFESDHLGSGSHFSNR
HCCCCCCCCCCCCCC
43.4123401153
385PhosphorylationSDHLGSGSHFSNRKE
CCCCCCCCCCCCCHH
24.0523401153
388PhosphorylationLGSGSHFSNRKEDML
CCCCCCCCCCHHHHH
30.2423401153
402PhosphorylationLLKQGQMYMADSQCT
HHHCCCEEECCCCCC
4.9321945579
406PhosphorylationGQMYMADSQCTSPGI
CCEEECCCCCCCCCC
20.0221945579
409PhosphorylationYMADSQCTSPGIPAH
EECCCCCCCCCCCHH
30.2521945579
410PhosphorylationMADSQCTSPGIPAHM
ECCCCCCCCCCCHHH
28.8421945579
419PhosphorylationGIPAHMQSRSMLRPL
CCCHHHHCCCCCCCE
20.8121945579
421PhosphorylationPAHMQSRSMLRPLEL
CHHHHCCCCCCCEEE
27.6728857561
429PhosphorylationMLRPLELSLPSQTSY
CCCCEEECCCCCCCC
28.9420068231
432PhosphorylationPLELSLPSQTSYSEN
CEEECCCCCCCCCHH
51.9220068231
434PhosphorylationELSLPSQTSYSENEI
EECCCCCCCCCHHHH
33.6920068231
435PhosphorylationLSLPSQTSYSENEIL
ECCCCCCCCCHHHHH
21.0120068231
436PhosphorylationSLPSQTSYSENEILK
CCCCCCCCCHHHHHH
24.3220068231
437PhosphorylationLPSQTSYSENEILKK
CCCCCCCCHHHHHHH
33.4420068231
462UbiquitinationSAKQDRLKLQNELAH
HHHHHHHHHHHHHHH
49.2532015554
475MalonylationAHKVAECKALALECE
HHHHHHHHHHHHHCH
37.6326320211
475UbiquitinationAHKVAECKALALECE
HHHHHHHHHHHHHCH
37.6332015554
478UbiquitinationVAECKALALECERVK
HHHHHHHHHHCHHHC
13.2321890473
493MethylationEDSDEQIKQLEDALK
CCCHHHHHHHHHHHH
48.83-
504"N6,N6-dimethyllysine"DALKDVQKRMYESEG
HHHHHHHHHHHHCCC
38.69-
504MethylationDALKDVQKRMYESEG
HHHHHHHHHHHHCCC
38.69-
518PhosphorylationGKVKQMQTHFLALKE
CHHHHHHHHHHHHHH
14.84-
549AcetylationLKDQLKDLKVKYEGA
HHHHHHHCCCCCCCC
7.0319608861
5522-HydroxyisobutyrylationQLKDLKVKYEGASAE
HHHHCCCCCCCCHHH
35.68-
553PhosphorylationLKDLKVKYEGASAEV
HHHCCCCCCCCHHHH
23.6820068231
562AcetylationGASAEVGKLRNQIKQ
CCHHHHHHHHHHHHH
49.8319608861
596PhosphorylationKRLQKELSMCEMERE
HHHHHHHHHHHHHHH
23.6028509920
626PhosphorylationLSAKLALSIPAEKFE
HHHHHHHHCCHHHHH
22.40-
6312-HydroxyisobutyrylationALSIPAEKFENMKSS
HHHCCHHHHHHHHHH
61.15-
6462-HydroxyisobutyrylationLSNEVNEKAKKLVEM
HHHHHHHHHHHHHHH
61.37-
662PhosphorylationREHEKSLSEIRQLKR
HHHHHHHHHHHHHHH
37.7624719451
703UbiquitinationQKSGELGKKITELTL
HHHCHHHHHHHHHHH
54.3422817900
704MalonylationKSGELGKKITELTLK
HHCHHHHHHHHHHHC
53.7326320211
706O-linked_GlycosylationGELGKKITELTLKNQ
CHHHHHHHHHHHCCH
33.5530379171
706UbiquitinationGELGKKITELTLKNQ
CHHHHHHHHHHHCCH
33.5521890473
710UbiquitinationKKITELTLKNQTLQK
HHHHHHHHCCHHHHH
8.4022817900
713UbiquitinationTELTLKNQTLQKEIE
HHHHHCCHHHHHHHH
41.8421890473
714UbiquitinationELTLKNQTLQKEIEK
HHHHCCHHHHHHHHH
40.3222817900
716UbiquitinationTLKNQTLQKEIEKVY
HHCCHHHHHHHHHHH
44.7322817900
717UbiquitinationLKNQTLQKEIEKVYL
HCCHHHHHHHHHHHH
64.8721890473
717MalonylationLKNQTLQKEIEKVYL
HCCHHHHHHHHHHHH
64.8726320211
717UbiquitinationLKNQTLQKEIEKVYL
HCCHHHHHHHHHHHH
64.8721890473
719UbiquitinationNQTLQKEIEKVYLDN
CHHHHHHHHHHHHCC
8.8221890473
723PhosphorylationQKEIEKVYLDNKLLK
HHHHHHHHHCCHHHH
21.2928152594
727UbiquitinationEKVYLDNKLLKEQAH
HHHHHCCHHHHHHHH
55.6622817900
730UbiquitinationYLDNKLLKEQAHNLT
HHCCHHHHHHHHCCC
59.2122817900
736UbiquitinationLKEQAHNLTIEMKNH
HHHHHHCCCEEEECC
3.5122817900
737PhosphorylationKEQAHNLTIEMKNHY
HHHHHCCCEEEECCE
21.8727251275
739UbiquitinationQAHNLTIEMKNHYVP
HHHCCCEEEECCEEC
38.5821890473
744PhosphorylationTIEMKNHYVPLKVSE
CEEEECCEECEECCH
17.1028674419
747UbiquitinationMKNHYVPLKVSEDMK
EECCEECEECCHHHH
6.4522817900
750UbiquitinationHYVPLKVSEDMKKSH
CEECEECCHHHHHHC
26.7121890473
774MalonylationKLLDVTQKYTEKKLE
HHHHHHHHHHHHHHH
44.7826320211
775PhosphorylationLLDVTQKYTEKKLEM
HHHHHHHHHHHHHHH
15.4323403867
776PhosphorylationLDVTQKYTEKKLEME
HHHHHHHHHHHHHHH
48.6523403867
791PhosphorylationKLLLENDSLSKDVSR
HHHHCCCCCCCCHHH
46.2320068231
793PhosphorylationLLENDSLSKDVSRLE
HHCCCCCCCCHHHHE
30.6620068231
801PhosphorylationKDVSRLETVFVPPEK
CCHHHHEEEECCCHH
24.6828674151
8112-HydroxyisobutyrylationVPPEKHEKEIIALKS
CCCHHCHHHHHHHHH
54.66-
817MalonylationEKEIIALKSNIVELK
HHHHHHHHHCHHHHH
32.2232601280
8242-HydroxyisobutyrylationKSNIVELKKQLSELK
HHCHHHHHHHHHHHH
25.60-
824MalonylationKSNIVELKKQLSELK
HHCHHHHHHHHHHHH
25.6026320211
845PhosphorylationQEKIHALTSENTNLK
HHHHHHHHCCCCCHH
34.4823403867
846PhosphorylationEKIHALTSENTNLKK
HHHHHHHCCCCCHHH
29.6923403867
849PhosphorylationHALTSENTNLKKMMS
HHHHCCCCCHHHHHC
37.5723403867
8522-HydroxyisobutyrylationTSENTNLKKMMSNQY
HCCCCCHHHHHCCCC
40.47-
875PhosphorylationVKMTLNDTLAKTNRE
HHHHHHHHHHHHHHH
27.7822210691
879PhosphorylationLNDTLAKTNRELLDV
HHHHHHHHHHHHHHH
33.6222210691
8872-HydroxyisobutyrylationNRELLDVKKKFEDIN
HHHHHHHHHHHHHHC
50.33-
922PhosphorylationQNQIKAEYISLAEHE
HHHHHHHHHHHHHHH
10.7327642862
953PhosphorylationNAEILANYRKGQEEI
CHHHHHHHHCCCHHE
14.22-
9722-HydroxyisobutyrylationAEIKAQKKELDTIQE
HHHHHHHHHHHHHHH
51.97-
972MalonylationAEIKAQKKELDTIQE
HHHHHHHHHHHHHHH
51.9732601280
984AcetylationIQECIKVKYAPIVSF
HHHHHHCCCCCCCCH
30.6025953088
984MalonylationIQECIKVKYAPIVSF
HHHHHHCCCCCCCCH
30.6026320211
985PhosphorylationQECIKVKYAPIVSFE
HHHHHCCCCCCCCHH
22.1627642862
1013PhosphorylationKDQLSEQTQKYSVSE
HHHHHHHHHHCCCCH
23.9925690035
1016PhosphorylationLSEQTQKYSVSEEEV
HHHHHHHCCCCHHHH
12.4223403867
1017PhosphorylationSEQTQKYSVSEEEVK
HHHHHHCCCCHHHHH
26.6323403867
1019PhosphorylationQTQKYSVSEEEVKKN
HHHHCCCCHHHHHHC
33.09-
1035SumoylationQENDKLKKEIFTLQK
HHHHHHHHHHHHHHH
67.49-
1035MalonylationQENDKLKKEIFTLQK
HHHHHHHHHHHHHHH
67.4926320211
1035SumoylationQENDKLKKEIFTLQK
HHHHHHHHHHHHHHH
67.4925218447
10472-HydroxyisobutyrylationLQKDLRDKTVLIEKS
HHHHHCCCEEEEECC
33.81-
1048PhosphorylationQKDLRDKTVLIEKSH
HHHHCCCEEEEECCH
25.49-
10532-HydroxyisobutyrylationDKTVLIEKSHEMERA
CCEEEEECCHHHHHH
50.55-
1062PhosphorylationHEMERALSRKTDELN
HHHHHHHHHHHHHHH
30.65-
1065PhosphorylationERALSRKTDELNKQL
HHHHHHHHHHHHHHH
33.3322817900
1079PhosphorylationLKDLSQKYTEVKNVK
HHHHHHHHHHHHCHH
10.6522817900
1123PhosphorylationQVEALKKSLNGTIEN
HHHHHHHHHCCHHHH
26.02-
1144AcetylationSMQRCYEKEQQTVTK
HHHHHHHHHHHHHHH
34.0626051181
1151MalonylationKEQQTVTKLHQLLEN
HHHHHHHHHHHHHHH
39.3726320211
1202PhosphorylationQNKMEEVSKLQSEVQ
HHHHHHHHHHHHHHH
30.8122210691
1206PhosphorylationEEVSKLQSEVQNTKQ
HHHHHHHHHHHHHHH
50.6125159151
1211PhosphorylationLQSEVQNTKQALKKL
HHHHHHHHHHHHHHH
13.8722210691
1212AcetylationQSEVQNTKQALKKLE
HHHHHHHHHHHHHHC
40.9219829971
1216AcetylationQNTKQALKKLETREV
HHHHHHHHHHCHHHH
59.3319829979
12282-HydroxyisobutyrylationREVVDLSKYKATKSD
HHHCCHHHHCCCHHH
59.05-
1228AcetylationREVVDLSKYKATKSD
HHHCCHHHHCCCHHH
59.0519829987
1232PhosphorylationDLSKYKATKSDLETQ
CHHHHCCCHHHHHHH
27.2523312004
1234PhosphorylationSKYKATKSDLETQIS
HHHCCCHHHHHHHHH
42.9723312004
12652-HydroxyisobutyrylationCEEVLHAKKKEISAK
HHHHHHHHHHCCCCC
54.34-
1281PhosphorylationEKELLHFSIEQEIKD
HHHHHHHHHHHHHHH
17.9227251275
1298PhosphorylationERCDKSLTTITELQR
HHHCHHHHHHHHHHH
24.2020860994
1339PhosphorylationKQALNGLSQLTYTSG
HHHHHHHHHCCCCCC
25.25-
1342PhosphorylationLNGLSQLTYTSGNPT
HHHHHHCCCCCCCCC
19.6721945579
1343PhosphorylationNGLSQLTYTSGNPTK
HHHHHCCCCCCCCCH
13.9024719451
1344PhosphorylationGLSQLTYTSGNPTKR
HHHHCCCCCCCCCHH
25.5621945579
1345PhosphorylationLSQLTYTSGNPTKRQ
HHHCCCCCCCCCHHH
26.5921945579
1349PhosphorylationTYTSGNPTKRQSQLI
CCCCCCCCHHHHHHH
42.7424719451
1353PhosphorylationGNPTKRQSQLIDTLQ
CCCCHHHHHHHHHHH
30.8730266825
1358PhosphorylationRQSQLIDTLQHQVKS
HHHHHHHHHHHHHHH
22.7130266825

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UACA_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 UACA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP48_HUMANUSP48physical
22939629
K1C40_HUMANKRT40physical
25416956

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 UACA_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-562, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1065, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND MASSSPECTROMETRY.

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