CTR9_HUMAN - dbPTM
CTR9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTR9_HUMAN
UniProt AC Q6PD62
Protein Name RNA polymerase-associated protein CTR9 homolog
Gene Name CTR9
Organism Homo sapiens (Human).
Sequence Length 1173
Subcellular Localization Nucleus speckle. Found in speckles..
Protein Description Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity)..
Protein Sequence MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPSTQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAATEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPISKKKKRRKGSGSEQEGEDEEGGERKKKKRRRHPKGEEGSDDDETENGPKPKKRRPPKAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSNSDSDEDEQRKKCASSESDSDENQNKSGSEAGSPRRPRRQRSDQDSDSDQPSRKRRPSGSEQSDNESVQSGRSHSGVSENDSRPASPSAESDHESERGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD
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
5Phosphorylation---MSRGSIEIPLRD
---CCCCCEEEECCC
18.8823312004
32PhosphorylationPEGDEVISILKQEHT
CCCCCHHHHHCHHHH
27.3524719451
39PhosphorylationSILKQEHTQLHIWIA
HHHCHHHHHHHHHHH
31.8824043423
51PhosphorylationWIALALEYYKQGKTE
HHHHHHHHHHCCCHH
19.4724043423
52PhosphorylationIALALEYYKQGKTEE
HHHHHHHHHCCCHHH
6.3524043423
622-HydroxyisobutyrylationGKTEEFVKLLEAARI
CCHHHHHHHHHHHCC
53.31-
62UbiquitinationGKTEEFVKLLEAARI
CCHHHHHHHHHHHCC
53.3121906983
80UbiquitinationLDYRDHEKDQMTCLD
CCCCCCHHHHHHHHH
50.2529967540
92PhosphorylationCLDTLAAYYVQQARK
HHHHHHHHHHHHHHH
9.88-
93PhosphorylationLDTLAAYYVQQARKE
HHHHHHHHHHHHHHH
6.25-
111PhosphorylationDNKKDLITQATLLYT
CCHHHHHHHHHHHHH
21.3220068231
114PhosphorylationKDLITQATLLYTMAD
HHHHHHHHHHHHHHH
13.8920068231
117PhosphorylationITQATLLYTMADKII
HHHHHHHHHHHHHHH
9.5120068231
118PhosphorylationTQATLLYTMADKIIM
HHHHHHHHHHHHHHH
13.0720068231
159PhosphorylationFHFVLNQSPNNIPAL
EEEHHCCCCCCHHHH
28.6425159151
176AcetylationKACISFNKKDYRGAL
HHHHHCCCCCHHHHH
45.0426051181
177UbiquitinationACISFNKKDYRGALA
HHHHCCCCCHHHHHH
62.18-
187AcetylationRGALAYYKKALRTNP
HHHHHHHHHHHHHCC
20.9226051181
188UbiquitinationGALAYYKKALRTNPG
HHHHHHHHHHHHCCC
36.21-
210AcetylationGMGHCFVKLNKLEKA
CCCCCEEEHHHHHHH
26.5325953088
210UbiquitinationGMGHCFVKLNKLEKA
CCCCCEEEHHHHHHH
26.5329967540
252AcetylationNKEADSIKNGVQLLS
CCHHHHHHHHHHHHH
52.1526051181
252UbiquitinationNKEADSIKNGVQLLS
CCHHHHHHHHHHHHH
52.1521906983
263PhosphorylationQLLSRAYTIDPSNPM
HHHHHCEECCCCCHH
20.23-
282AcetylationLANHFFFKKDYSKVQ
HHHHHCCCCCHHHHH
39.3125953088
357AcetylationMYIYRGDKENASQCF
EEEEECCHHHHHHHH
56.5426051181
357UbiquitinationMYIYRGDKENASQCF
EEEEECCHHHHHHHH
56.54-
361PhosphorylationRGDKENASQCFEKVL
ECCHHHHHHHHHHHH
38.78-
366AcetylationNASQCFEKVLKAYPN
HHHHHHHHHHHHCCC
32.3926051181
366UbiquitinationNASQCFEKVLKAYPN
HHHHHHHHHHHHCCC
32.3922817900
369UbiquitinationQCFEKVLKAYPNNYE
HHHHHHHHHCCCCHH
49.1921906983
379UbiquitinationPNNYETMKILGSLYA
CCCHHHHHHHHHHHH
42.0521906983
3932-HydroxyisobutyrylationAASEDQEKRDIAKGH
HCCCCHHHHHHHHHH
50.14-
393AcetylationAASEDQEKRDIAKGH
HCCCCHHHHHHHHHH
50.1426051181
393UbiquitinationAASEDQEKRDIAKGH
HCCCCHHHHHHHHHH
50.1421906983
398UbiquitinationQEKRDIAKGHLKKVT
HHHHHHHHHHHHHHH
47.3922817900
444UbiquitinationATRILQEKVQADVPP
HHHHHHHHHHCCCCH
27.04-
471AcetylationLGNLGEAKKYFLASL
CCCHHHHHHHHHHHH
43.6425953088
471UbiquitinationLGNLGEAKKYFLASL
CCCHHHHHHHHHHHH
43.6422817900
4722-HydroxyisobutyrylationGNLGEAKKYFLASLD
CCHHHHHHHHHHHHH
48.56-
472UbiquitinationGNLGEAKKYFLASLD
CCHHHHHHHHHHHHH
48.5621890473
518AcetylationCEFHEAEKLYKNILR
HHHHHHHHHHHHHHH
65.2526822725
521UbiquitinationHEAEKLYKNILREHP
HHHHHHHHHHHHHCC
48.20-
544UbiquitinationLGAMARDKGNFYEAS
HHCHHHCCCCCCCCC
50.6421906983
548PhosphorylationARDKGNFYEASDWFK
HHCCCCCCCCCHHHH
18.0028152594
551PhosphorylationKGNFYEASDWFKEAL
CCCCCCCCHHHHHHH
24.3528152594
578UbiquitinationIGNLHLAKQEWGPGQ
HHHHHHHHCCCCCCH
55.9329967540
637AcetylationDRALAIYKQVLRNDA
HHHHHHHHHHHHHHH
28.0225953088
637MalonylationDRALAIYKQVLRNDA
HHHHHHHHHHHHHHH
28.0232601280
637UbiquitinationDRALAIYKQVLRNDA
HHHHHHHHHHHHHHH
28.0233845483
645UbiquitinationQVLRNDAKNLYAANG
HHHHHHHHHHHHHCC
50.8022817900
660UbiquitinationIGAVLAHKGYFREAR
HHHHHHCCCHHHHHH
50.1023000965
737UbiquitinationCGKLQECKQTLLKAR
CCCHHHHHHHHHHHC
45.6329967540
749PhosphorylationKARHVAPSDTVLMFN
HHCCCCCCCCHHHHH
35.8524719451
766PhosphorylationLVLQRLATSVLKDEK
HHHHHHHHHHHCCCC
24.7824719451
767PhosphorylationVLQRLATSVLKDEKS
HHHHHHHHHHCCCCC
21.6124719451
770AcetylationRLATSVLKDEKSNLK
HHHHHHHCCCCCCHH
62.7825953088
770UbiquitinationRLATSVLKDEKSNLK
HHHHHHHCCCCCCHH
62.7821906983
773UbiquitinationTSVLKDEKSNLKEVL
HHHHCCCCCCHHHHH
55.5722817900
777UbiquitinationKDEKSNLKEVLNAVK
CCCCCCHHHHHHHHH
50.4529967540
784UbiquitinationKEVLNAVKELELAHR
HHHHHHHHHHHHHHH
54.9222817900
7982-HydroxyisobutyrylationRYFSYLSKVGDKMRF
HHHHHHHHHCHHHHH
47.87-
798UbiquitinationRYFSYLSKVGDKMRF
HHHHHHHHHCHHHHH
47.8722817900
802UbiquitinationYLSKVGDKMRFDLAL
HHHHHCHHHHHHHHH
26.5022817900
812PhosphorylationFDLALAATEARQCSD
HHHHHHHHHHHHHHH
25.2721406692
820UbiquitinationEARQCSDLLSQAQYH
HHHHHHHHHHHHHHH
2.5922817900
825UbiquitinationSDLLSQAQYHVARAR
HHHHHHHHHHHHHHH
22.6422817900
831UbiquitinationAQYHVARARKQDEEE
HHHHHHHHHHCCHHH
17.1829967540
839UbiquitinationRKQDEEERELRAKQE
HHCCHHHHHHHHHHH
52.0824816145
844"N6,N6-dimethyllysine"EERELRAKQEQEKEL
HHHHHHHHHHHHHHH
48.19-
844MethylationEERELRAKQEQEKEL
HHHHHHHHHHHHHHH
48.19-
844UbiquitinationEERELRAKQEQEKEL
HHHHHHHHHHHHHHH
48.1921906983
849UbiquitinationRAKQEQEKELLRQKL
HHHHHHHHHHHHHHH
54.0521906983
855UbiquitinationEKELLRQKLLKEQEE
HHHHHHHHHHHHHHH
49.7229967540
863UbiquitinationLLKEQEEKRLREKEE
HHHHHHHHHHHHHHH
56.8524816145
873UbiquitinationREKEEQKKLLEQRAQ
HHHHHHHHHHHHHHH
58.9824816145
884AcetylationQRAQYVEKTKNILMF
HHHHHHHHHHCEEEE
55.5523749302
885PhosphorylationRAQYVEKTKNILMFT
HHHHHHHHHCEEEEC
18.8023532336
890SulfoxidationEKTKNILMFTGETEA
HHHHCEEEECCCCHH
2.2121406390
892PhosphorylationTKNILMFTGETEATK
HHCEEEECCCCHHCC
21.8320068231
895PhosphorylationILMFTGETEATKEKK
EEEECCCCHHCCCCC
32.0623532336
898PhosphorylationFTGETEATKEKKRGG
ECCCCHHCCCCCCCC
33.2420068231
899AcetylationTGETEATKEKKRGGG
CCCCHHCCCCCCCCC
74.6726051181
901PhosphorylationETEATKEKKRGGGGG
CCHHCCCCCCCCCCC
49.6932645325
911PhosphorylationGGGGGRRSKKGGEFD
CCCCCCCCCCCCCCC
37.0421712546
925PhosphorylationDEFVNDDTDDDLPIS
CHHCCCCCCCCCCCC
44.1619664994
932PhosphorylationTDDDLPISKKKKRRK
CCCCCCCCCCCCCCC
36.1622167270
941PhosphorylationKKKRRKGSGSEQEGE
CCCCCCCCCCCCCCC
42.0329255136
943PhosphorylationKRRKGSGSEQEGEDE
CCCCCCCCCCCCCCC
37.4929255136
967UbiquitinationRRRHPKGEEGSDDDE
CCCCCCCCCCCCCCC
66.3724816145
970PhosphorylationHPKGEEGSDDDETEN
CCCCCCCCCCCCCCC
40.9429255136
975PhosphorylationEGSDDDETENGPKPK
CCCCCCCCCCCCCCC
41.5722167270
991UbiquitinationRRPPKAEKKKAPKPE
CCCCHHHHCCCCCHH
65.5224816145
1003UbiquitinationKPERLPPSMKGKIKS
CHHHCCHHHCCCCCE
31.0533845483
1005AcetylationERLPPSMKGKIKSKA
HHCCHHHCCCCCEEE
62.4825953088
1015PhosphorylationIKSKAIISSSDDSSD
CCEEEEECCCCCCCC
20.0625159151
1016PhosphorylationKSKAIISSSDDSSDE
CEEEEECCCCCCCCH
27.6425159151
1017PhosphorylationSKAIISSSDDSSDED
EEEEECCCCCCCCHH
38.3525159151
1020PhosphorylationIISSSDDSSDEDKLK
EECCCCCCCCHHHHH
44.6825159151
1021PhosphorylationISSSDDSSDEDKLKI
ECCCCCCCCHHHHHH
52.6028355574
1027UbiquitinationSSDEDKLKIADEGHP
CCCHHHHHHCCCCCC
41.4033845483
1037PhosphorylationDEGHPRNSNSNSDSD
CCCCCCCCCCCCCCC
42.8029255136
1039PhosphorylationGHPRNSNSNSDSDED
CCCCCCCCCCCCCHH
37.2229255136
1041PhosphorylationPRNSNSNSDSDEDEQ
CCCCCCCCCCCHHHH
38.0129255136
1043PhosphorylationNSNSNSDSDEDEQRK
CCCCCCCCCHHHHHH
42.6021955146
1044PhosphorylationSNSNSDSDEDEQRKK
CCCCCCCCHHHHHHH
72.8133259812
1054PhosphorylationEQRKKCASSESDSDE
HHHHHHHHCCCCCCC
44.0729083192
1055PhosphorylationQRKKCASSESDSDEN
HHHHHHHCCCCCCCC
23.6925072903
1057PhosphorylationKKCASSESDSDENQN
HHHHHCCCCCCCCCC
44.3425072903
1059PhosphorylationCASSESDSDENQNKS
HHHCCCCCCCCCCCC
56.9828985074
1066PhosphorylationSDENQNKSGSEAGSP
CCCCCCCCCCCCCCC
55.9225159151
1068PhosphorylationENQNKSGSEAGSPRR
CCCCCCCCCCCCCCC
31.2220363803
1072PhosphorylationKSGSEAGSPRRPRRQ
CCCCCCCCCCCCCCC
23.4525159151
1081PhosphorylationRRPRRQRSDQDSDSD
CCCCCCCCCCCCCCC
31.1427273156
1085PhosphorylationRQRSDQDSDSDQPSR
CCCCCCCCCCCCCCC
33.1227273156
1087PhosphorylationRSDQDSDSDQPSRKR
CCCCCCCCCCCCCCC
41.9427273156
1091PhosphorylationDSDSDQPSRKRRPSG
CCCCCCCCCCCCCCC
44.8125884760
1097PhosphorylationPSRKRRPSGSEQSDN
CCCCCCCCCCCCCCC
53.8123401153
1099PhosphorylationRKRRPSGSEQSDNES
CCCCCCCCCCCCCCC
36.4829255136
1102PhosphorylationRPSGSEQSDNESVQS
CCCCCCCCCCCCCCC
38.0529255136
1106PhosphorylationSEQSDNESVQSGRSH
CCCCCCCCCCCCCCC
31.5423663014
1109PhosphorylationSDNESVQSGRSHSGV
CCCCCCCCCCCCCCC
33.7423663014
1112PhosphorylationESVQSGRSHSGVSEN
CCCCCCCCCCCCCCC
26.0620363803
1114PhosphorylationVQSGRSHSGVSENDS
CCCCCCCCCCCCCCC
41.9823312004
1117PhosphorylationGRSHSGVSENDSRPA
CCCCCCCCCCCCCCC
33.9220363803
1121PhosphorylationSGVSENDSRPASPSA
CCCCCCCCCCCCCCC
52.3120363803
1125PhosphorylationENDSRPASPSAESDH
CCCCCCCCCCCCCCC
23.2823312004
1127PhosphorylationDSRPASPSAESDHES
CCCCCCCCCCCCCCC
42.0220363803
1130PhosphorylationPASPSAESDHESERG
CCCCCCCCCCCCCCC
43.9425849741
1138PhosphorylationDHESERGSDNEGSGQ
CCCCCCCCCCCCCCC
43.4120873877
1143PhosphorylationRGSDNEGSGQGSGNE
CCCCCCCCCCCCCCC
23.0520873877
1147PhosphorylationNEGSGQGSGNESEPE
CCCCCCCCCCCCCCC
30.4721815630
1151PhosphorylationGQGSGNESEPEGSNN
CCCCCCCCCCCCCCC
63.5520873877
1156PhosphorylationNESEPEGSNNEASDR
CCCCCCCCCCCCCCC
34.5220873877
1172PhosphorylationSEHGSDDSD------
CCCCCCCCC------
50.6530242111

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
1081SPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTR9_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 CTR9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT3_HUMANSTAT3physical
17911113
CDC73_HUMANCDC73physical
18469135
RTF1_HUMANRTF1physical
18469135
PAF1_HUMANPAF1physical
18469135
LEO1_HUMANLEO1physical
18469135
LEO1_HUMANLEO1physical
20178742
CDC73_HUMANCDC73physical
20178742
RTF1_HUMANRTF1physical
20178742
WDR61_HUMANWDR61physical
20178742
PAF1_HUMANPAF1physical
20178742
CDC73_HUMANCDC73physical
20305087
LEO1_HUMANLEO1physical
20305087
PAF1_HUMANPAF1physical
20305087
WDR61_HUMANWDR61physical
20305087
LEO1_HUMANLEO1physical
22532828
CDC73_HUMANCDC73physical
22532828
LEO1_HUMANLEO1physical
22939629
PAF1_HUMANPAF1physical
22939629
RTF1_HUMANRTF1physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
SSRP1_HUMANSSRP1physical
22939629
RL12_HUMANRPL12physical
22939629
CDC73_HUMANCDC73physical
22863883
COG3_HUMANCOG3physical
22863883
RABL6_HUMANRABL6physical
22863883
CDC73_HUMANCDC73physical
26344197
CHD1_HUMANCHD1physical
26344197
CHD2_HUMANCHD2physical
26344197
ARBK1_HUMANADRBK1physical
26496610
AL3B1_HUMANALDH3B1physical
26496610
CCNT1_HUMANCCNT1physical
26496610
CDK9_HUMANCDK9physical
26496610
CETN2_HUMANCETN2physical
26496610
FINC_HUMANFN1physical
26496610
G6PD_HUMANG6PDphysical
26496610
FOXK2_HUMANFOXK2physical
26496610
NFIC_HUMANNFICphysical
26496610
PMS2_HUMANPMS2physical
26496610
RPB1_HUMANPOLR2Aphysical
26496610
RPB2_HUMANPOLR2Bphysical
26496610
RPB3_HUMANPOLR2Cphysical
26496610
RPB4_HUMANPOLR2Dphysical
26496610
RPB7_HUMANPOLR2Gphysical
26496610
PP1RA_HUMANPPP1R10physical
26496610
2A5D_HUMANPPP2R5Dphysical
26496610
GLYM_HUMANSHMT2physical
26496610
SPT5H_HUMANSUPT5Hphysical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
ELOC_HUMANTCEB1physical
26496610
ELOB_HUMANTCEB2physical
26496610
ELOA1_HUMANTCEB3physical
26496610
VEZF1_HUMANVEZF1physical
26496610
ELL_HUMANELLphysical
26496610
ARK72_HUMANAKR7A2physical
26496610
IF4G3_HUMANEIF4G3physical
26496610
NFS1_HUMANNFS1physical
26496610
TOX4_HUMANTOX4physical
26496610
ATP9A_HUMANATP9Aphysical
26496610
RPP38_HUMANRPP38physical
26496610
TACC2_HUMANTACC2physical
26496610
PRS23_HUMANPRSS23physical
26496610
ELL2_HUMANELL2physical
26496610
RPRD2_HUMANRPRD2physical
26496610
FKB15_HUMANFKBP15physical
26496610
TM131_HUMANTMEM131physical
26496610
PRP31_HUMANPRPF31physical
26496610
AFF4_HUMANAFF4physical
26496610
TAOK3_HUMANTAOK3physical
26496610
DGCR8_HUMANDGCR8physical
26496610
PAF1_HUMANPAF1physical
26496610
IWS1_HUMANIWS1physical
26496610
FGD6_HUMANFGD6physical
26496610
ACSA_HUMANACSS2physical
26496610
ERGI1_HUMANERGIC1physical
26496610
ANO3_HUMANANO3physical
26496610
SIN1_HUMANMAPKAP1physical
26496610
CDC73_HUMANCDC73physical
26496610
WDR61_HUMANWDR61physical
26496610
ZFP91_HUMANZFP91physical
26496610
NDEL1_HUMANNDEL1physical
26496610
KLF16_HUMANKLF16physical
26496610
F161A_HUMANFAM161Aphysical
26496610
ING5_HUMANING5physical
26496610
TJAP1_HUMANTJAP1physical
26496610
LEO1_HUMANLEO1physical
26496610
ACTBL_HUMANACTBL2physical
26496610
MYC_HUMANMYCphysical
26687678

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 CTR9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-970; SER-1015;SER-1016; SER-1017; SER-1020; SER-1021; SER-1037; SER-1039; SER-1041AND SER-1043, AND MASS SPECTROMETRY.
"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-1020 AND SER-1021, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941 AND SER-943, 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-925; SER-941; SER-943;SER-970; SER-1015; SER-1016; SER-1017; SER-1020 AND SER-1021, AND MASSSPECTROMETRY.
"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 THR-925, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND MASSSPECTROMETRY.

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