CNTRL_HUMAN - dbPTM
CNTRL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNTRL_HUMAN
UniProt AC Q7Z7A1
Protein Name Centriolin
Gene Name CNTRL
Organism Homo sapiens (Human).
Sequence Length 2325
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody, Midbody ring .
Protein Description Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission..
Protein Sequence MKKGSQQKIFSKAKIPSSSHSPIPSSMSNMRSRSLSPLIGSETLPFHSGGQWCEQVEIADENNMLLDYQDHKGADSHAGVRYITEALIKKLTKQDNLALIKSLNLSLSKDGGKKFKYIENLEKCVKLEVLNLSYNLIGKIEKLDKLLKLRELNLSYNKISKIEGIENMCNLQKLNLAGNEIEHIPVWLGKKLKSLRVLNLKGNKISSLQDISKLKPLQDLISLILVENPVVTLPHYLQFTIFHLRSLESLEGQPVTTQDRQEAFERFSLEEVERLERDLEKKMIETEELKSKQTRFLEEIKNQDKLNKSLKEEAMLQKQSCEELKSDLNTKNELLKQKTIELTRACQKQYELEQELAFYKIDAKFEPLNYYPSEYAEIDKAPDESPYIGKSRYKRNMFATESYIIDSAQAVQIKKMEPDEQLRNDHMNLRGHTPLDTQLEDKEKKISAAQTRLSELHDEIEKAEQQILRATEEFKQLEEAIQLKKISEAGKDLLYKQLSGRLQLVNKLRQEALDLELQMEKQKQEIAGKQKEIKDLQIAIDSLDSKDPKHSHMKAQKSGKEQQLDIMNKQYQQLESRLDEILSRIAKETEEIKDLEEQLTEGQIAANEALKKDLEGVISGLQEYLGTIKGQATQAQNECRKLRDEKETLLQRLTEVEQERDQLEIVAMDAENMRKELAELESALQEQHEVNASLQQTQGDLSAYEAELEARLNLRDAEANQLKEELEKVTRLTQLEQSALQAELEKERQALKNALGKAQFSEEKEQENSELHAKLKHLQDDNNLLKQQLKDFQNHLNHVVDGLVRPEEVAARVDELRRKLKLGTGEMNIHSPSDVLGKSLADLQKQFSEILARSKWERDEAQVRERKLQEEMALQQEKLATGQEEFRQACERALEARMNFDKRQHEARIQQMENEIHYLQENLKSMEEIQGLTDLQLQEADEEKERILAQLRELEKKKKLEDAKSQEQVFGLDKELKKLKKAVATSDKLATAELTIAKDQLKSLHGTVMKINQERAEELQEAERFSRKAAQAARDLTRAEAEIELLQNLLRQKGEQFRLEMEKTGVGTGANSQVLEIEKLNETMERQRTEIARLQNVLDLTGSDNKGGFENVLEEIAELRREVSYQNDYISSMADPFKRRGYWYFMPPPPSSKVSSHSSQATKDSGVGLKYSASTPVRKPRPGQQDGKEGSQPPPASGYWVYSPIRSGLHKLFPSRDADSGGDSQEESELDDQEEPPFVPPPGYMMYTVLPDGSPVPQGMALYAPPPPLPNNSRPLTPGTVVYGPPPAGAPMVYGPPPPNFSIPFIPMGVLHCNVPEHHNLENEVSRLEDIMQHLKSKKREERWMRASKRQSEKEMEELHHNIDDLLQEKKSLECEVEELHRTVQKRQQQKDFIDGNVESLMTELEIEKSLKHHEDIVDEIECIEKTLLKRRSELREADRLLAEAESELSCTKEKTKNAVEKFTDAKRSLLQTESDAEELERRAQETAVNLVKADQQLRSLQADAKDLEQHKIKQEEILKEINKIVAAKDSDFQCLSKKKEKLTEELQKLQKDIEMAERNEDHHLQVLKESEVLLQAKRAELEKLKSQVTSQQQEMAVLDRQLGHKKEELHLLQGSMVQAKADLQEALRLGETEVTEKCNHIREVKSLLEELSFQKGELNVQISERKTQLTLIKQEIEKEEENLQVVLRQMSKHKTELKNILDMLQLENHELQGLKLQHDQRVSELEKTQVAVLEEKLELENLQQISQQQKGEIEWQKQLLERDKREIERMTAESRALQSCVECLSKEKEDLQEKCDIWEKKLAQTKRVLAAAEENSKMEQSNLEKLELNVRKLQQELDQLNRDKLSLHNDISAMQQQLQEKREAVNSLQEELANVQDHLNLAKQDLLHTTKHQDVLLSEQTRLQKDISEWANRFEDCQKEEETKQQQLQVLQNEIEENKLKLVQQEMMFQRLQKERESEESKLETSKVTLKEQQHQLEKELTDQKSKLDQVLSKVLAAEERVRTLQEEERWCESLEKTLSQTKRQLSEREQQLVEKSGELLALQKEADSMRADFSLLRNQFLTERKKAEKQVASLKEALKIQRSQLEKNLLEQKQENSCIQKEMATIELVAQDNHERARRLMKELNQMQYEYTELKKQMANQKDLERRQMEISDAMRTLKSEVKDEIRTSLKNLNQFLPELPADLEAILERNENLEGELESLKENLPFTMNEGPFEEKLNFSQVHIMDEHWRGEALREKLRHREDRLKAQLRHCMSKQAEVLIKGKRQTEGTLHSLRRQVDALGELVTSTSADSASSPSLSQLESSLTEDSQLGQNQEKNASAR
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
11PhosphorylationGSQQKIFSKAKIPSS
CCCHHHHCCCCCCCC
34.8724719451
17PhosphorylationFSKAKIPSSSHSPIP
HCCCCCCCCCCCCCC
48.2028857561
18PhosphorylationSKAKIPSSSHSPIPS
CCCCCCCCCCCCCCH
27.0728857561
19PhosphorylationKAKIPSSSHSPIPSS
CCCCCCCCCCCCCHH
32.1128857561
21PhosphorylationKIPSSSHSPIPSSMS
CCCCCCCCCCCHHHC
26.8628857561
25PhosphorylationSSHSPIPSSMSNMRS
CCCCCCCHHHCCCCC
39.1229978859
26PhosphorylationSHSPIPSSMSNMRSR
CCCCCCHHHCCCCCC
22.3729978859
28PhosphorylationSPIPSSMSNMRSRSL
CCCCHHHCCCCCCCC
29.4429978859
101UbiquitinationQDNLALIKSLNLSLS
CCCHHHHHHCCCEEC
50.1421890473
101 (in isoform 1)Ubiquitination-50.1421890473
101 (in isoform 5)Ubiquitination-50.1421890473
102PhosphorylationDNLALIKSLNLSLSK
CCHHHHHHCCCEECC
18.5923909892
106PhosphorylationLIKSLNLSLSKDGGK
HHHHCCCEECCCCCC
29.5324719451
108PhosphorylationKSLNLSLSKDGGKKF
HHCCCEECCCCCCCC
25.8928450419
116UbiquitinationKDGGKKFKYIENLEK
CCCCCCCHHHCCHHH
54.95-
117PhosphorylationDGGKKFKYIENLEKC
CCCCCCHHHCCHHHH
19.3219664994
194PhosphorylationWLGKKLKSLRVLNLK
HHCHHCCCCEEEECC
31.6628258704
206PhosphorylationNLKGNKISSLQDISK
ECCCCCCCCHHHHHC
26.9728258704
212PhosphorylationISSLQDISKLKPLQD
CCCHHHHHCCCCHHH
39.9828258704
286PhosphorylationLEKKMIETEELKSKQ
HHHHHHCHHHHHHHH
24.6817924679
301UbiquitinationTRFLEEIKNQDKLNK
HHHHHHHHCHHHHCH
52.41-
338AcetylationKNELLKQKTIELTRA
HHHHHHHHHHHHHHH
50.2930587605
360UbiquitinationEQELAFYKIDAKFEP
HHHHHHHCCCCCCCC
27.88-
364UbiquitinationAFYKIDAKFEPLNYY
HHHCCCCCCCCCCCC
46.65-
370PhosphorylationAKFEPLNYYPSEYAE
CCCCCCCCCHHHHCC
25.16-
375PhosphorylationLNYYPSEYAEIDKAP
CCCCHHHHCCCCCCC
17.5527642862
380UbiquitinationSEYAEIDKAPDESPY
HHHCCCCCCCCCCCC
68.43-
387PhosphorylationKAPDESPYIGKSRYK
CCCCCCCCCCCHHCC
31.4227642862
390UbiquitinationDESPYIGKSRYKRNM
CCCCCCCCHHCCCCC
23.38-
433PhosphorylationHMNLRGHTPLDTQLE
CCCCCCCCCCCCCCC
28.5030108239
437PhosphorylationRGHTPLDTQLEDKEK
CCCCCCCCCCCHHHH
42.6130108239
485AcetylationEEAIQLKKISEAGKD
HHHHHHHHHHHHCHH
61.127667019
487PhosphorylationAIQLKKISEAGKDLL
HHHHHHHHHHCHHHH
30.2117137347
491AcetylationKKISEAGKDLLYKQL
HHHHHHCHHHHHHHH
52.857667027
496AcetylationAGKDLLYKQLSGRLQ
HCHHHHHHHHHHHHH
44.747667035
542PhosphorylationDLQIAIDSLDSKDPK
HHHHHHHHCCCCCCC
28.1525332170
545PhosphorylationIAIDSLDSKDPKHSH
HHHHHCCCCCCCCCC
44.2325332170
583PhosphorylationSRLDEILSRIAKETE
HHHHHHHHHHHHHHH
27.5724719451
618 (in isoform 2)Ubiquitination-3.8821890473
619PhosphorylationKDLEGVISGLQEYLG
HHHHHHHHHHHHHHH
30.9220068231
624PhosphorylationVISGLQEYLGTIKGQ
HHHHHHHHHHHHHHH
9.4720068231
627PhosphorylationGLQEYLGTIKGQATQ
HHHHHHHHHHHHHHH
19.5420068231
693PhosphorylationEQHEVNASLQQTQGD
HHHHHHHHHHHHHCC
22.85-
738PhosphorylationRLTQLEQSALQAELE
HHHHHHHHHHHHHHH
22.9025627689
746UbiquitinationALQAELEKERQALKN
HHHHHHHHHHHHHHH
71.47-
752UbiquitinationEKERQALKNALGKAQ
HHHHHHHHHHHHHHH
43.09-
761PhosphorylationALGKAQFSEEKEQEN
HHHHHHCCHHHHHHH
32.5328731282
786UbiquitinationQDDNNLLKQQLKDFQ
HCCCCHHHHHHHHHH
38.88-
821UbiquitinationDELRRKLKLGTGEMN
HHHHHHHCCCCCCCC
48.16-
824PhosphorylationRRKLKLGTGEMNIHS
HHHHCCCCCCCCCCC
40.17-
831PhosphorylationTGEMNIHSPSDVLGK
CCCCCCCCHHHHHCH
23.4630266825
833PhosphorylationEMNIHSPSDVLGKSL
CCCCCCHHHHHCHHH
43.2830266825
848PhosphorylationADLQKQFSEILARSK
HHHHHHHHHHHHHCC
22.64-
854PhosphorylationFSEILARSKWERDEA
HHHHHHHCCHHHHHH
36.1920068231
867UbiquitinationEAQVRERKLQEEMAL
HHHHHHHHHHHHHHH
50.17-
964UbiquitinationKKKLEDAKSQEQVFG
HHCHHHHHHHHHHHC
66.06-
974UbiquitinationEQVFGLDKELKKLKK
HHHHCCHHHHHHHHH
70.73-
988UbiquitinationKAVATSDKLATAELT
HHHHCCCHHHHHHHH
39.53-
991PhosphorylationATSDKLATAELTIAK
HCCCHHHHHHHHHCH
30.9729396449
995PhosphorylationKLATAELTIAKDQLK
HHHHHHHHHCHHHHH
15.4724114839
998UbiquitinationTAELTIAKDQLKSLH
HHHHHHCHHHHHHHH
52.24-
1002UbiquitinationTIAKDQLKSLHGTVM
HHCHHHHHHHHHHHE
45.39-
1010UbiquitinationSLHGTVMKINQERAE
HHHHHHEHHCHHHHH
33.88-
1026PhosphorylationLQEAERFSRKAAQAA
HHHHHHHHHHHHHHH
38.8123403867
1053UbiquitinationLQNLLRQKGEQFRLE
HHHHHHHCCHHHHHE
58.96-
1072PhosphorylationGVGTGANSQVLEIEK
CCCCCCCHHEEEHHH
22.5730108239
1101PhosphorylationLQNVLDLTGSDNKGG
HHHHHHHCCCCCCCC
34.0228348404
1103PhosphorylationNVLDLTGSDNKGGFE
HHHHHCCCCCCCCHH
32.5427067055
1106UbiquitinationDLTGSDNKGGFENVL
HHCCCCCCCCHHHHH
66.46-
1124PhosphorylationAELRREVSYQNDYIS
HHHHHHHHCCCCHHH
19.0927251275
1139MethylationSMADPFKRRGYWYFM
HCCCCCCCCCCEEEC
37.32-
1162PhosphorylationSSHSSQATKDSGVGL
CCCCCCCCCCCCCCC
27.96-
1165PhosphorylationSSQATKDSGVGLKYS
CCCCCCCCCCCCEEC
36.6124247654
1170MethylationKDSGVGLKYSASTPV
CCCCCCCEECCCCCC
31.09-
1170UbiquitinationKDSGVGLKYSASTPV
CCCCCCCEECCCCCC
31.0921890473
1170 (in isoform 1)Ubiquitination-31.0921890473
1170 (in isoform 5)Ubiquitination-31.0921890473
1175PhosphorylationGLKYSASTPVRKPRP
CCEECCCCCCCCCCC
26.0628555341
1197PhosphorylationGSQPPPASGYWVYSP
CCCCCCCCCCEEEEC
37.8826471730
1199PhosphorylationQPPPASGYWVYSPIR
CCCCCCCCEEEECCC
6.8226471730
1202PhosphorylationPASGYWVYSPIRSGL
CCCCCEEEECCCCCH
8.4526471730
1203PhosphorylationASGYWVYSPIRSGLH
CCCCEEEECCCCCHH
12.3028985074
1211UbiquitinationPIRSGLHKLFPSRDA
CCCCCHHHHCCCCCC
57.79-
1348PhosphorylationEERWMRASKRQSEKE
HHHHHHHHHHHCHHH
20.2924719451
1371UbiquitinationDDLLQEKKSLECEVE
HHHHHHHHHHHHHHH
60.57-
1372PhosphorylationDLLQEKKSLECEVEE
HHHHHHHHHHHHHHH
40.2330266825
1453UbiquitinationESELSCTKEKTKNAV
HHHHHCCHHHHHHHH
62.63-
1469PhosphorylationKFTDAKRSLLQTESD
HHHHHHHHHHCCCCC
32.5030108239
1473PhosphorylationAKRSLLQTESDAEEL
HHHHHHCCCCCHHHH
37.1128450419
1475PhosphorylationRSLLQTESDAEELER
HHHHCCCCCHHHHHH
45.5728450419
1493UbiquitinationETAVNLVKADQQLRS
HHHHHHHHHHHHHHH
49.78-
1542UbiquitinationCLSKKKEKLTEELQK
HHHHHHHHHHHHHHH
70.37-
1544PhosphorylationSKKKEKLTEELQKLQ
HHHHHHHHHHHHHHH
38.18-
1569UbiquitinationDHHLQVLKESEVLLQ
CHHHHHHHHHHHHHH
61.41-
1578UbiquitinationSEVLLQAKRAELEKL
HHHHHHHHHHHHHHH
38.90-
1621UbiquitinationQGSMVQAKADLQEAL
CCCHHHHHHHHHHHH
25.91-
1638UbiquitinationGETEVTEKCNHIREV
CCHHHHHHCCHHHHH
30.85-
1646UbiquitinationCNHIREVKSLLEELS
CCHHHHHHHHHHHHC
30.54-
1653PhosphorylationKSLLEELSFQKGELN
HHHHHHHCCCCCCEE
28.9827067055
1668PhosphorylationVQISERKTQLTLIKQ
EEECCHHHHHHHHHH
34.7222817900
1671PhosphorylationSERKTQLTLIKQEIE
CCHHHHHHHHHHHHH
19.3322817900
1716UbiquitinationNHELQGLKLQHDQRV
CHHCCCCCCCCCHHH
53.58-
1724PhosphorylationLQHDQRVSELEKTQV
CCCCHHHHHHHHHHH
38.3628188228
1728UbiquitinationQRVSELEKTQVAVLE
HHHHHHHHHHHHHHH
57.81-
1751UbiquitinationQQISQQQKGEIEWQK
HHHHHHHCCHHHHHH
54.92-
1758UbiquitinationKGEIEWQKQLLERDK
CCHHHHHHHHHHHHH
43.94-
1772PhosphorylationKREIERMTAESRALQ
HHHHHHHHHHHHHHH
33.23-
1775PhosphorylationIERMTAESRALQSCV
HHHHHHHHHHHHHHH
22.01-
1795UbiquitinationEKEDLQEKCDIWEKK
CHHHHHHHHCHHHHH
25.01-
1847PhosphorylationQLNRDKLSLHNDISA
HHHHHHHHHHHHHHH
33.0727732954
1884UbiquitinationQDHLNLAKQDLLHTT
HHHHHHHHHHHHHHH
47.73-
1890PhosphorylationAKQDLLHTTKHQDVL
HHHHHHHHHHHHHHH
37.1925072903
1891PhosphorylationKQDLLHTTKHQDVLL
HHHHHHHHHHHHHHH
18.7825072903
1906UbiquitinationSEQTRLQKDISEWAN
CCHHHHHHHHHHHHH
62.72-
1925UbiquitinationCQKEEETKQQQLQVL
HHHHHHHHHHHHHHH
49.76-
1940UbiquitinationQNEIEENKLKLVQQE
HHHHHHHHHHHHHHH
50.72-
1959PhosphorylationRLQKERESEESKLET
HHHHHHHCHHHHHHH
53.5423403867
1962PhosphorylationKERESEESKLETSKV
HHHHCHHHHHHHHCC
38.1923403867
1966PhosphorylationSEESKLETSKVTLKE
CHHHHHHHHCCCHHH
44.2623403867
1967PhosphorylationEESKLETSKVTLKEQ
HHHHHHHHCCCHHHH
18.76-
1968UbiquitinationESKLETSKVTLKEQQ
HHHHHHHCCCHHHHH
46.81-
1972UbiquitinationETSKVTLKEQQHQLE
HHHCCCHHHHHHHHH
44.08-
1995UbiquitinationKLDQVLSKVLAAEER
HHHHHHHHHHHHHHH
36.79-
2037UbiquitinationREQQLVEKSGELLAL
HHHHHHHHHHHHHHH
57.17-
2046UbiquitinationGELLALQKEADSMRA
HHHHHHHHHHHHHHH
56.57-
2056PhosphorylationDSMRADFSLLRNQFL
HHHHHHHHHHHHHHH
27.35-
2064PhosphorylationLLRNQFLTERKKAEK
HHHHHHHHHHHHHHH
34.7224719451
2075PhosphorylationKAEKQVASLKEALKI
HHHHHHHHHHHHHHH
40.9123917254
2089AcetylationIQRSQLEKNLLEQKQ
HHHHHHHHHHHHHHH
62.5824471179
2089UbiquitinationIQRSQLEKNLLEQKQ
HHHHHHHHHHHHHHH
62.58-
2095UbiquitinationEKNLLEQKQENSCIQ
HHHHHHHHHHCHHHH
50.64-
2137UbiquitinationQYEYTELKKQMANQK
HHHHHHHHHHHCCHH
34.43-
2161UbiquitinationSDAMRTLKSEVKDEI
HHHHHHHHHHHHHHH
43.91-
2171PhosphorylationVKDEIRTSLKNLNQF
HHHHHHHHHHHHHHH
27.7424247654
2173UbiquitinationDEIRTSLKNLNQFLP
HHHHHHHHHHHHHHC
60.19-
2202PhosphorylationNLEGELESLKENLPF
CCHHHHHHHHHHCCC
58.3229970186
2223PhosphorylationFEEKLNFSQVHIMDE
HHHCCCCCCEEECCH
30.1628122231
2258UbiquitinationQLRHCMSKQAEVLIK
HHHHHHHHHCEEECC
27.01-
2270PhosphorylationLIKGKRQTEGTLHSL
ECCCCCCCHHHHHHH
40.1824043423
2273PhosphorylationGKRQTEGTLHSLRRQ
CCCCCHHHHHHHHHH
18.3124043423
2276PhosphorylationQTEGTLHSLRRQVDA
CCHHHHHHHHHHHHH
27.0424043423
2290PhosphorylationALGELVTSTSADSAS
HHHHHHHCCCCCCCC
16.94-
2291PhosphorylationLGELVTSTSADSASS
HHHHHHCCCCCCCCC
20.68-
2292PhosphorylationGELVTSTSADSASSP
HHHHHCCCCCCCCCC
29.82-

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 CNTRL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNTRL_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 CNTRL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABRAL_HUMANABRACLphysical
26638075
ANR26_HUMANANKRD26physical
26638075
ANR28_HUMANANKRD28physical
26638075
RHG21_HUMANARHGAP21physical
26638075
CP131_HUMANCEP131physical
26638075
TM256_HUMANTMEM256physical
26638075
CALR_HUMANCALRphysical
26638075
CAMP3_HUMANCAMSAP3physical
26638075
C2D1A_HUMANCC2D1Aphysical
26638075
CC138_HUMANCCDC138physical
26638075
CCD14_HUMANCCDC14physical
26638075
CCNB1_HUMANCCNB1physical
26638075
CE128_HUMANCEP128physical
26638075
CE152_HUMANCEP152physical
26638075
CE162_HUMANCEP162physical
26638075
CE170_HUMANCEP170physical
26638075
CE350_HUMANCEP350physical
26638075
CEP89_HUMANCEP89physical
26638075
CKAP2_HUMANCKAP2physical
26638075
CKAP5_HUMANCKAP5physical
26638075
KCRB_HUMANCKBphysical
26638075
CLAP1_HUMANCLASP1physical
26638075
CLH1_HUMANCLTCphysical
26638075
COPB2_HUMANCOPB2physical
26638075
CSPP1_HUMANCSPP1physical
26638075
CSRP1_HUMANCSRP1physical
26638075
NB5R3_HUMANCYB5R3physical
26638075
DAPK3_HUMANDAPK3physical
26638075
ODB2_HUMANDBTphysical
26638075
DLG5_HUMANDLG5physical
26638075
DYN2_HUMANDNM2physical
26638075
DESP_HUMANDSPphysical
26638075
DYHC1_HUMANDYNC1H1physical
26638075
RB6I2_HUMANERC1physical
26638075
ERLN2_HUMANERLIN2physical
26638075
EXOC4_HUMANEXOC4physical
26638075
GANAB_HUMANGANABphysical
26638075
GPTC1_HUMANGPATCH1physical
26638075
GTSE1_HUMANGTSE1physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HAUS8_HUMANHAUS8physical
26638075
HXK1_HUMANHK1physical
26638075
HYOU1_HUMANHYOU1physical
26638075
IDH3B_HUMANIDH3Bphysical
26638075
IF2B2_HUMANIGF2BP2physical
26638075
ERD22_HUMANKDELR2physical
26638075
MOONR_HUMANKIAA0753physical
26638075
K1671_HUMANKIAA1671physical
26638075
KIF14_HUMANKIF14physical
26638075
KIF7_HUMANKIF7physical
26638075
LMO7_HUMANLMO7physical
26638075
LONM_HUMANLONP1physical
26638075
LUZP1_HUMANLUZP1physical
26638075
M4K4_HUMANMAP4K4physical
26638075
MED4_HUMANMED4physical
26638075
MIB1_HUMANMIB1physical
26638075
NAA15_HUMANNAA15physical
26638075
NCK5L_HUMANNCKAP5Lphysical
26638075
NEDD1_HUMANNEDD1physical
26638075
NDK7_HUMANNME7physical
26638075
NNTM_HUMANNNTphysical
26638075
NU205_HUMANNUP205physical
26638075
ODFP2_HUMANODF2physical
26638075
OFD1_HUMANOFD1physical
26638075
PCM1_HUMANPCM1physical
26638075
ODPA_HUMANPDHA1physical
26638075
PDIA3_HUMANPDIA3physical
26638075
PDIA4_HUMANPDIA4physical
26638075
PIBF1_HUMANPIBF1physical
26638075
PLK1_HUMANPLK1physical
26638075
RPB3_HUMANPOLR2Cphysical
26638075
KAPCA_HUMANPRKACAphysical
26638075
PWP2_HUMANPWP2physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB35_HUMANRAB35physical
26638075
RAB5B_HUMANRAB5Bphysical
26638075
RAB7A_HUMANRAB7Aphysical
26638075
RAB8A_HUMANRAB8Aphysical
26638075
RAB9A_HUMANRAB9Aphysical
26638075
RPAP2_HUMANRPAP2physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
SC24C_HUMANSEC24Cphysical
26638075
SGPL1_HUMANSGPL1physical
26638075
SHKB1_HUMANSHKBP1physical
26638075
SLAI2_HUMANSLAIN2physical
26638075
S39A7_HUMANSLC39A7physical
26638075
SOAT1_HUMANSOAT1physical
26638075
SRBS1_HUMANSORBS1physical
26638075
SRSF2_HUMANSRSF2physical
26638075
SSRG_HUMANSSR3physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
TANC1_HUMANTANC1physical
26638075
ZO1_HUMANTJP1physical
26638075
ZO2_HUMANTJP2physical
26638075
TNR6A_HUMANTNRC6Aphysical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
ASPP2_HUMANTP53BP2physical
26638075
TRA2A_HUMANTRA2Aphysical
26638075
TRI26_HUMANTRIM26physical
26638075
TTF2_HUMANTTF2physical
26638075
TTK_HUMANTTKphysical
26638075
TTL12_HUMANTTLL12physical
26638075
GCP2_HUMANTUBGCP2physical
26638075
GCP3_HUMANTUBGCP3physical
26638075
TXLNA_HUMANTXLNAphysical
26638075
TXLNG_HUMANTXLNGphysical
26638075
RENT1_HUMANUPF1physical
26638075
VIME_HUMANVIMphysical
26638075
WDR83_HUMANWDR83physical
26638075
WRP73_HUMANWRAP73physical
26638075
SYYM_HUMANYARS2physical
26638075
1433F_HUMANYWHAHphysical
26638075
ZN326_HUMANZNF326physical
26638075
ZN622_HUMANZNF622physical
26638075
ARHGI_HUMANARHGEF18physical
26638075
ARHG2_HUMANARHGEF2physical
26638075
AURKB_HUMANAURKBphysical
26638075
C2CD3_HUMANC2CD3physical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
CE85L_HUMANCEP85Lphysical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
HAUS2_HUMANHAUS2physical
26638075
HAUS5_HUMANHAUS5physical
26638075
HSDL2_HUMANHSDL2physical
26638075
IFT81_HUMANIFT81physical
26638075
C170B_HUMANCEP170Bphysical
26638075
LC7L2_HUMANLUC7L2physical
26638075
MA7D3_HUMANMAP7D3physical
26638075
MGST3_HUMANMGST3physical
26638075
MPP9_HUMANMPHOSPH9physical
26638075
MTPN_HUMANMTPNphysical
26638075
NIN_HUMANNINphysical
26638075
PCNT_HUMANPCNTphysical
26638075
PR38B_HUMANPRPF38Bphysical
26638075
PSDE_HUMANPSMD14physical
26638075
PSMD7_HUMANPSMD7physical
26638075
RB11B_HUMANRAB11Bphysical
26638075
FTM_HUMANRPGRIP1Lphysical
26638075
SPAT2_HUMANSPATA2physical
26638075
SQSTM_HUMANSQSTM1physical
26638075
SRP09_HUMANSRP9physical
26638075
TCHP_HUMANTCHPphysical
26638075
VP33A_HUMANVPS33Aphysical
26638075
TBC31_HUMANTBC1D31physical
26638075
COX3_HUMANCOX3physical
26638075

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 CNTRL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117 AND THR-286, ANDMASS SPECTROMETRY.
"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 THR-1668 AND THR-1671, ANDMASS SPECTROMETRY.

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