CE290_HUMAN - dbPTM
CE290_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CE290_HUMAN
UniProt AC O15078
Protein Name Centrosomal protein of 290 kDa
Gene Name CEP290
Organism Homo sapiens (Human).
Sequence Length 2479
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Nucleus . Cell projection, cilium . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cyt
Protein Description Involved in early and late steps in cilia formation. Its association with CCP110 is required for inhibition of primary cilia formation by CCP110. [PubMed: 18694559 May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles (CCVs Required for the centrosomal recruitment of RAB8A and for the targeting of centriole satellite proteins to centrosomes such as of PCM1]
Protein Sequence MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSKDDEIIEYQQMLHNLREKLKNAQLDADKSNVMALQQGIQERDSQIKMLTEQVEQYTKEMEKNTCIIEDLKNELQRNKGASTLSQQTHMKIQSTLDILKEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVVEIKNCKNQIKIRDREIEILTKEINKLELKISDFLDENEALRERVGLEPKTMIDLTEFRNSKHLKQQQYRAENQILLKEIESLEEERLDLKKKIRQMAQERGKRSATSGLTTEDLNLTENISQGDRISERKLDLLSLKNMSEAQSKNEFLSRELIEKERDLERSRTVIAKFQNKLKELVEENKQLEEGMKEILQAIKEMQKDPDVKGGETSLIIPSLERLVNAIESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAINYSQQLAKANLKIDHLEKETSLLRQSEGSNVVFKGIDLPDGIAPSSASIINSQNEYLIHLLQELENKEKKLKNLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKETWKTESKTIKEEKRKLEDQVQQDAIKVKEYNNLLNALQMDSDEMKKILAENSRKITVLQVNEKSLIRQYTTLVELERQLRKENEKQKNELLSMEAEVCEKIGCLQRFKEMAIFKIAALQKVVDNSVSLSELELANKQYNELTAKYRDILQKDNMLVQRTSNLEHLECENISLKEQVESINKELEITKEKLHTIEQAWEQETKLGNESSMDKAKKSITNSDIVSISKKITMLEMKELNERQRAEHCQKMYEHLRTSLKQMEERNFELETKFAELTKINLDAQKVEQMLRDELADSVSKAVSDADRQRILELEKNEMELKVEVSKLREISDIARRQVEILNAQQQSRDKEVESLRMQLLDYQAQSDEKSLIAKLHQHNVSLQLSEATALGKLESITSKLQKMEAYNLRLEQKLDEKEQALYYARLEGRNRAKHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDTKGAQKVINWHMKIEELRLQELKLNRELVKDKEEIKYLNNIISEYERTISSLEEEIVQQNKFHEERQMAWDQREVDLERQLDIFDRQQNEILNAAQKFEEATGSIPDPSLPLPNQLEIALRKIKENIRIILETRATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLRLPATAEREKLIAELGRKEMEPKSHHTLKIAHQTIANMQARLNQKEEVLKKYQRLLEKAREEQREIVKKHEEDLHILHHRLELQADSSLNKFKQTAWDLMKQSPTPVPTNKHFIRLAEMEQTVAEQDDSLSSLLVKLKKVSQDLERQREITELKVKEFENIKLQLQENHEDEVKKVKAEVEDLKYLLDQSQKESQCLKSELQAQKEANSRAPTTTMRNLVERLKSQLALKEKQQKALSRALLELRAEMTAAAEERIISATSQKEAHLNVQQIVDRHTRELKTQVEDLNENLLKLKEALKTSKNRENSLTDNLNDLNNELQKKQKAYNKILREKEEIDQENDELKRQIKRLTSGLQGKPLTDNKQSLIEELQRKVKKLENQLEGKVEEVDLKPMKEKNAKEELIRWEEGKKWQAKIEGIRNKLKEKEGEVFTLTKQLNTLKDLFAKADKEKLTLQRKLKTTGMTVDQVLGIRALESEKELEELKKRNLDLENDILYMRAHQALPRDSVVEDLHLQNRYLQEKLHALEKQFSKDTYSKPSISGIESDDHCQREQELQKENLKLSSENIELKFQLEQANKDLPRLKNQVRDLKEMCEFLKKEKAEVQRKLGHVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGILTSEKMANIEQENEKLKAELEKLKAHLGHQLSMHYESKTKGTEKIIAENERLRKELKKETDAAEKLRIAKNNLEILNEKMTVQLEETGKRLQFAESRGPQLEGADSKSWKSIVVTRMYETKLKELETDIAKKNQSITDLKQLVKEATEREQKVNKYNEDLEQQIKILKHVPEGAETEQGLKRELQVLRLANHQLDKEKAELIHQIEANKDQSGAESTIPDADQLKEKIKDLETQLKMSDLEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKVKKLSEQLGVELTSPVAASEEFEDEEESPVNFPIY
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
31PhosphorylationLADNLLISLSKVEVN
HHHHHHHHHHHHCHH
26.9326074081
78 (in isoform 2)Ubiquitination-52.36-
93 (in isoform 2)Ubiquitination-56.4921890473
102 (in isoform 2)Ubiquitination-36.1321890473
105 (in isoform 2)Ubiquitination-21.8121890473
140AcetylationDMEKELEKEKKVNEQ
HHHHHHHHHHHHHHH
83.7418528975
185UbiquitinationQDIIDYQKQIDSQKE
HHHHHHHHHHHHHHH
42.88-
191UbiquitinationQKQIDSQKETLLSRR
HHHHHHHHHHHHHHC
57.53-
213PhosphorylationSQLSKKNYELIQYLD
HHHHHHHHHHHHHHH
22.46-
348PhosphorylationAQLDADKSNVMALQQ
CCCCCHHHHHHHHHH
34.8920860994
368PhosphorylationDSQIKMLTEQVEQYT
HHHHHHHHHHHHHHH
22.3729978859
374PhosphorylationLTEQVEQYTKEMEKN
HHHHHHHHHHHHHHC
13.2823663014
375PhosphorylationTEQVEQYTKEMEKNT
HHHHHHHHHHHHHCC
21.8823663014
382PhosphorylationTKEMEKNTCIIEDLK
HHHHHHCCCCHHHHH
19.02-
451PhosphorylationALKRLKDYESGVYGL
HHHHHCHHHCCCCCH
15.4821712546
456PhosphorylationKDYESGVYGLEDAVV
CHHHCCCCCHHHHEE
21.3721712546
484UbiquitinationREIEILTKEINKLEL
HHHHHHHHHHHHHHC
53.83-
512UbiquitinationERVGLEPKTMIDLTE
HHHCCCCCCCEEHHH
41.15-
527UbiquitinationFRNSKHLKQQQYRAE
HCCCHHHHHHHHHHH
45.86-
567PhosphorylationAQERGKRSATSGLTT
HHHHCCCCCCCCCCH
39.1121406692
569PhosphorylationERGKRSATSGLTTED
HHCCCCCCCCCCHHH
25.2720068231
570PhosphorylationRGKRSATSGLTTEDL
HCCCCCCCCCCHHHH
31.3621406692
573PhosphorylationRSATSGLTTEDLNLT
CCCCCCCCHHHHCCC
31.5021406692
574PhosphorylationSATSGLTTEDLNLTE
CCCCCCCHHHHCCCC
32.3221406692
580PhosphorylationTTEDLNLTENISQGD
CHHHHCCCCCCCCCC
26.3920068231
584PhosphorylationLNLTENISQGDRISE
HCCCCCCCCCCCCCH
39.4321406692
593UbiquitinationGDRISERKLDLLSLK
CCCCCHHHHHHHHHC
42.15-
598PhosphorylationERKLDLLSLKNMSEA
HHHHHHHHHCCCCHH
44.5924719451
600UbiquitinationKLDLLSLKNMSEAQS
HHHHHHHCCCCHHHH
47.42-
608UbiquitinationNMSEAQSKNEFLSRE
CCCHHHHHHHHHCHH
48.71-
672PhosphorylationPDVKGGETSLIIPSL
CCCCCCCCEEHHHCH
31.9127251275
673PhosphorylationDVKGGETSLIIPSLE
CCCCCCCEEHHHCHH
17.1727251275
688PhosphorylationRLVNAIESKNAEGIF
HHHHHHHCCCCCCCC
25.7024719451
724UbiquitinationQELRESRKEAINYSQ
HHHHHHHHHHHHHHH
61.86-
729PhosphorylationSRKEAINYSQQLAKA
HHHHHHHHHHHHHHC
11.1825003641
730PhosphorylationRKEAINYSQQLAKAN
HHHHHHHHHHHHHCC
13.6325003641
735UbiquitinationNYSQQLAKANLKIDH
HHHHHHHHCCCCCHH
46.5321890473
737 (in isoform 1)Ubiquitination-40.9521890473
745UbiquitinationLKIDHLEKETSLLRQ
CCCHHHHHHHHHHHH
73.06-
748PhosphorylationDHLEKETSLLRQSEG
HHHHHHHHHHHHCCC
26.8824719451
820PhosphorylationAVIRHQQSLLYKEYL
HHHHHHHHHHHHHHH
17.4829083192
823PhosphorylationRHQQSLLYKEYLSEK
HHHHHHHHHHHHCCC
13.6829083192
826PhosphorylationQSLLYKEYLSEKETW
HHHHHHHHHCCCCCH
16.0429083192
828PhosphorylationLLYKEYLSEKETWKT
HHHHHHHCCCCCHHC
45.8029083192
830UbiquitinationYKEYLSEKETWKTES
HHHHHCCCCCHHCCC
58.0021890473
832PhosphorylationEYLSEKETWKTESKT
HHHCCCCCHHCCCHH
43.24-
832 (in isoform 1)Ubiquitination-43.2421890473
846AcetylationTIKEEKRKLEDQVQQ
HHHHHHHHHHHHHHH
68.2618584311
859AcetylationQQDAIKVKEYNNLLN
HHHHHHHHHHHHHHH
49.8618584321
883PhosphorylationKKILAENSRKITVLQ
HHHHHHCCCCEEEEE
26.84-
895PhosphorylationVLQVNEKSLIRQYTT
EEEECHHHHHHHHHH
23.8919664995
902PhosphorylationSLIRQYTTLVELERQ
HHHHHHHHHHHHHHH
24.71-
951UbiquitinationFKIAALQKVVDNSVS
HHHHHHHHHHHCCCC
45.11-
1002PhosphorylationHLECENISLKEQVES
HHHEECCCHHHHHHH
44.9924719451
1017PhosphorylationINKELEITKEKLHTI
HHHHHHHHHHHHHHH
24.6324670416
1023PhosphorylationITKEKLHTIEQAWEQ
HHHHHHHHHHHHHHH
36.3229083192
1032PhosphorylationEQAWEQETKLGNESS
HHHHHHHHHCCCCCH
31.1225599653
1033UbiquitinationQAWEQETKLGNESSM
HHHHHHHHCCCCCHH
54.3621890473
1035 (in isoform 1)Ubiquitination-37.1021890473
1042UbiquitinationGNESSMDKAKKSITN
CCCCHHHHHHHHCCH
54.1621890473
1044UbiquitinationESSMDKAKKSITNSD
CCHHHHHHHHCCHHH
53.44-
1044 (in isoform 1)Ubiquitination-53.4421890473
1045UbiquitinationSSMDKAKKSITNSDI
CHHHHHHHHCCHHHH
52.5321890473
1046PhosphorylationSMDKAKKSITNSDIV
HHHHHHHHCCHHHHH
33.6628555341
1047 (in isoform 1)Ubiquitination-6.0821890473
1060PhosphorylationVSISKKITMLEMKEL
HHHHHHHHHHHHHHH
25.2820071362
1125PhosphorylationLRDELADSVSKAVSD
HHHHHHHHHHHHCCH
23.7628060719
1127PhosphorylationDELADSVSKAVSDAD
HHHHHHHHHHCCHHH
20.8928060719
1131PhosphorylationDSVSKAVSDADRQRI
HHHHHHCCHHHHHHH
31.7628060719
1159PhosphorylationVSKLREISDIARRQV
HHHHHHHHHHHHHHH
20.4321815630
1178UbiquitinationAQQQSRDKEVESLRM
HHHHHCHHHHHHHHH
63.65-
1209PhosphorylationKLHQHNVSLQLSEAT
HHHHCCCEEEEHHHH
18.7318187866
1251PhosphorylationEKEQALYYARLEGRN
HHHHHHHHHHHHCCH
6.0118083107
1287PhosphorylationLAQQEKFSKTMIQLQ
HHHHHHHHHHHHHHH
37.9827174698
1289PhosphorylationQQEKFSKTMIQLQND
HHHHHHHHHHHHHHH
20.5027174698
1336UbiquitinationEELISTLKDTKGAQK
HHHHHHHHCCCCHHH
64.54-
1360UbiquitinationELRLQELKLNRELVK
HHHHHHHCCCHHHHC
42.85-
1382 (in isoform 2)Ubiquitination-12.1521890473
1385PhosphorylationIISEYERTISSLEEE
HHHHHHHHHHHHHHH
17.1727050516
1517UbiquitinationPATAEREKLIAELGR
CCHHHHHHHHHHHCC
51.95-
1552UbiquitinationMQARLNQKEEVLKKY
HHHHHHHHHHHHHHH
55.56-
1594PhosphorylationRLELQADSSLNKFKQ
HHHHHCCCCHHHHHH
39.4820873877
1595PhosphorylationLELQADSSLNKFKQT
HHHHCCCCHHHHHHH
36.1920873877
1598UbiquitinationQADSSLNKFKQTAWD
HCCCCHHHHHHHHHH
60.27-
1600UbiquitinationDSSLNKFKQTAWDLM
CCCHHHHHHHHHHHH
48.63-
1608UbiquitinationQTAWDLMKQSPTPVP
HHHHHHHHCCCCCCC
55.72-
1610PhosphorylationAWDLMKQSPTPVPTN
HHHHHHCCCCCCCCC
25.8128985074
1618UbiquitinationPTPVPTNKHFIRLAE
CCCCCCCHHHHHHHH
42.23-
1636PhosphorylationTVAEQDDSLSSLLVK
HHHHCCCCHHHHHHH
38.1422210691
1638PhosphorylationAEQDDSLSSLLVKLK
HHCCCCHHHHHHHHH
23.9222210691
1639PhosphorylationEQDDSLSSLLVKLKK
HCCCCHHHHHHHHHH
30.8922210691
1658PhosphorylationLERQREITELKVKEF
HHHHHHHHHHHHHHH
30.4323403867
1684AcetylationEDEVKKVKAEVEDLK
HHHHHHHHHHHHHHH
47.947677519
1691AcetylationKAEVEDLKYLLDQSQ
HHHHHHHHHHHHHHH
46.297677529
1692PhosphorylationAEVEDLKYLLDQSQK
HHHHHHHHHHHHHHH
21.5728122231
1697PhosphorylationLKYLLDQSQKESQCL
HHHHHHHHHHHHHHH
42.7725599653
1731AcetylationRNLVERLKSQLALKE
HHHHHHHHHHHHHHH
42.2312655493
1737AcetylationLKSQLALKEKQQKAL
HHHHHHHHHHHHHHH
58.2012655503
1788UbiquitinationDRHTRELKTQVEDLN
HHHHHHHHHHHHHHH
31.96-
1814PhosphorylationTSKNRENSLTDNLND
HCCCHHHHHHHCHHH
28.0825072903
1816PhosphorylationKNRENSLTDNLNDLN
CCHHHHHHHCHHHHH
23.7425072903
1828AcetylationDLNNELQKKQKAYNK
HHHHHHHHHHHHHHH
70.5620167786
1833PhosphorylationLQKKQKAYNKILREK
HHHHHHHHHHHHHHH
24.8329457462
1840AcetylationYNKILREKEEIDQEN
HHHHHHHHHHHHHHC
54.9720167786
1864UbiquitinationLTSGLQGKPLTDNKQ
HHHCCCCCCCCCCHH
24.72-
1906UbiquitinationPMKEKNAKEELIRWE
HCCCCCHHHHHHHHH
62.20-
1916MethylationLIRWEEGKKWQAKIE
HHHHHHHHHHHHHHH
54.8623644510
1921MethylationEGKKWQAKIEGIRNK
HHHHHHHHHHHHHHH
26.6223644510
1959PhosphorylationKADKEKLTLQRKLKT
HHCHHHCHHHHHHHH
31.73-
1966PhosphorylationTLQRKLKTTGMTVDQ
HHHHHHHHCCCCHHH
38.73-
1982PhosphorylationLGIRALESEKELEEL
HHHHHHHCHHHHHHH
55.6126471730
2002PhosphorylationDLENDILYMRAHQAL
CCHHCHHHHHHHHCC
5.72-
2013PhosphorylationHQALPRDSVVEDLHL
HHCCCCCCHHHHHHH
29.3728348404
2034UbiquitinationEKLHALEKQFSKDTY
HHHHHHHHHHCCCCC
58.45-
2043UbiquitinationFSKDTYSKPSISGIE
HCCCCCCCCCCCCCC
32.16-
2045PhosphorylationKDTYSKPSISGIESD
CCCCCCCCCCCCCCC
32.8727251275
2069PhosphorylationQKENLKLSSENIELK
HHHHHCCCHHHHHHH
33.7420068231
2070PhosphorylationKENLKLSSENIELKF
HHHHCCCHHHHHHHH
45.1320068231
2126PhosphorylationGSGRSGKTIPELEKT
CCCCCCCCHHHHHHH
45.34-
2133PhosphorylationTIPELEKTIGLMKKV
CHHHHHHHHHHHHHH
15.7627155012
2155PhosphorylationNEQLKKASGILTSEK
HHHHHHHHCCCCHHH
34.9320860994
2172UbiquitinationNIEQENEKLKAELEK
CHHHHHHHHHHHHHH
67.86-
2189PhosphorylationAHLGHQLSMHYESKT
HHHHHHHHHHHHCCC
9.2827251275
2238PhosphorylationEILNEKMTVQLEETG
HHHCHHCEEEHHHHH
19.0327174698
2244PhosphorylationMTVQLEETGKRLQFA
CEEEHHHHHCCHHHH
38.3327174698
2284PhosphorylationTKLKELETDIAKKNQ
HHHHHHHHHHHHHCC
45.38-
2292PhosphorylationDIAKKNQSITDLKQL
HHHHHCCCHHHHHHH
36.5326471730
2294PhosphorylationAKKNQSITDLKQLVK
HHHCCCHHHHHHHHH
40.2926471730
2304PhosphorylationKQLVKEATEREQKVN
HHHHHHHHHHHHHHH
36.3516674116
2322UbiquitinationEDLEQQIKILKHVPE
HHHHHHHHHHHCCCC
37.3321890473
2324 (in isoform 1)Ubiquitination-2.3921890473
2338UbiquitinationAETEQGLKRELQVLR
CCCHHHHHHHHHHHH
51.13-
2369PhosphorylationIEANKDQSGAESTIP
HHHCCCCCCCCCCCC
50.5326471730
2373PhosphorylationKDQSGAESTIPDADQ
CCCCCCCCCCCCHHH
30.9729083192
2374PhosphorylationDQSGAESTIPDADQL
CCCCCCCCCCCHHHH
28.2128985074
2395PhosphorylationLETQLKMSDLEKQHL
HHHHHHHHHHHHHHH
37.1419413330
2437AcetylationNYKEEVKKNILLEEK
CCHHHHHHHHHHHHH
55.1620167786

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
-KUbiquitinationE3 ubiquitin ligaseMIB1Q86YT6
PMID:24121310

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CE290_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 CE290_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP97_HUMANCEP97physical
22441691
CEP76_HUMANCEP76physical
22441691
CP110_HUMANCCP110physical
22441691
ZN423_HUMANZNF423physical
22863007
CE170_HUMANCEP170physical
26638075
FR1OP_HUMANFGFR1OPphysical
26638075
OFD1_HUMANOFD1physical
26638075
CP131_HUMANCEP131physical
26638075
CC138_HUMANCCDC138physical
26638075
CP110_HUMANCCP110physical
26638075
CEP72_HUMANCEP72physical
26638075
CEP76_HUMANCEP76physical
26638075
CEP97_HUMANCEP97physical
26638075
FKBP4_HUMANFKBP4physical
26638075
HERC2_HUMANHERC2physical
26638075
IQCB1_HUMANIQCB1physical
26638075
CE162_HUMANCEP162physical
26638075
MED4_HUMANMED4physical
26638075
MIB1_HUMANMIB1physical
26638075
NEUL4_HUMANNEURL4physical
26638075
PTPRR_HUMANPTPRRphysical
26638075
PCNT_HUMANPCNTphysical
26638075
PIBF1_HUMANPIBF1physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
CCD77_HUMANCCDC77physical
26638075
KC1E_HUMANCSNK1Ephysical
26638075
ECH1_HUMANECH1physical
26638075
SREK1_HUMANSREK1physical
26638075
SPT5H_HUMANSUPT5Hphysical
26638075
LDHA_HUMANLDHAphysical
26638075
TADBP_HUMANTARDBPphysical
26638075
MARE1_HUMANMAPRE1physical
26638075
AKA12_HUMANAKAP12physical
26638075
NEP1_HUMANEMG1physical
26638075
KIF7_HUMANKIF7physical
26638075
PNMA2_HUMANPNMA2physical
26638075
SSBP_HUMANSSBP1physical
26638075
CAND1_HUMANCAND1physical
26638075
UBA1_HUMANUBA1physical
26638075
6PGD_HUMANPGDphysical
26638075
USO1_HUMANUSO1physical
26638075
SAHH_HUMANAHCYphysical
26638075
KAD2_HUMANAK2physical
26638075
AN32A_HUMANANP32Aphysical
26638075
ARPC3_HUMANARPC3physical
26638075
BAP31_HUMANBCAP31physical
26638075
CK049_HUMANC11orf49physical
26638075
CU002_HUMANC21orf2physical
26638075
CSPP1_HUMANCSPP1physical
26638075
NB5R3_HUMANCYB5R3physical
26638075
GYS1_HUMANGYS1physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HAUS8_HUMANHAUS8physical
26638075
ISOC1_HUMANISOC1physical
26638075
ERD22_HUMANKDELR2physical
26638075
LRC49_HUMANLRRC49physical
26638075
LUZP1_HUMANLUZP1physical
26638075
MIF_HUMANMIFphysical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
MTPN_HUMANMTPNphysical
26638075
NEK1_HUMANNEK1physical
26638075
PAWR_HUMANPAWRphysical
26638075
PCM1_HUMANPCM1physical
26638075
PLP2_HUMANPLP2physical
26638075
MPPB_HUMANPMPCBphysical
26638075
TEBP_HUMANPTGES3physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
TPGS1_HUMANTPGS1physical
26638075
WRP73_HUMANWRAP73physical
26638075
1433F_HUMANYWHAHphysical
26638075
CCD61_HUMANCCDC61physical
26638075
CE104_HUMANCEP104physical
26638075
CE350_HUMANCEP350physical
26638075
CHTOP_HUMANCHTOPphysical
26638075
DDX47_HUMANDDX47physical
26638075
FOPNL_HUMANFOPNLphysical
26638075
GPTC1_HUMANGPATCH1physical
26638075
HAUS1_HUMANHAUS1physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HMGN1_HUMANHMGN1physical
26638075
MOONR_HUMANKIAA0753physical
26638075
KIF14_HUMANKIF14physical
26638075
NEDD1_HUMANNEDD1physical
26638075
NDK7_HUMANNME7physical
26638075
TCHP_HUMANTCHPphysical
26638075
TBC31_HUMANTBC1D31physical
26638075
WDR83_HUMANWDR83physical
26638075

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610188Joubert syndrome 5 (JBTS5)
610189Senior-Loken syndrome 6 (SLSN6)
611755Leber congenital amaurosis 10 (LCA10)
611134Meckel syndrome 4 (MKS4)
0000269|PubMedNote=Antibodies against CEP290 are present in sera from patients with cutaneous T-cell lymphomas, but not in the healthy control population. {ECO
615991
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CE290_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2395, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1697, AND MASSSPECTROMETRY.

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