DDX1_HUMAN - dbPTM
DDX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX1_HUMAN
UniProt AC Q92499
Protein Name ATP-dependent RNA helicase DDX1
Gene Name DDX1
Organism Homo sapiens (Human).
Sequence Length 740
Subcellular Localization Nucleus. Cytoplasm. Cytoplasmic granule. Localized with MBNL1, TIAL1 and YBX1 in stress granules upon stress. Localized with CSTF2 in cleavage bodies. Forms large aggregates called DDX1 bodies. Relocalized into multiple foci (IR-induced foci or IRIF)
Protein Description Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation. [PubMed: 24870230; (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs.; (Microbial infection) Required for Coronavirus IBV replication.]
Protein Sequence MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
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
65PhosphorylationIPVIQIVYETLKDQQ
CCHHHHHHHHHHHHH		12.5827642862
75UbiquitinationLKDQQEGKKGKTTIK
HHHHHCCCCCCCEEE		58.56-
76UbiquitinationKDQQEGKKGKTTIKT
HHHHCCCCCCCEEEC		76.21-
80PhosphorylationEGKKGKTTIKTGASV
CCCCCCCEEECCHHH		24.7822817900
82AcetylationKKGKTTIKTGASVLN
CCCCCEEECCHHHHH		38.5225953088
82UbiquitinationKKGKTTIKTGASVLN
CCCCCEEECCHHHHH		38.52-
83PhosphorylationKGKTTIKTGASVLNK
CCCCEEECCHHHHHH		33.8428857561
86PhosphorylationTTIKTGASVLNKWQM
CEEECCHHHHHHCCC		28.6028857561
90UbiquitinationTGASVLNKWQMNPYD
CCHHHHHHCCCCCCC		34.3421890473
90UbiquitinationTGASVLNKWQMNPYD
CCHHHHHHCCCCCCC		34.3421890473
90AcetylationTGASVLNKWQMNPYD
CCHHHHHHCCCCCCC		34.3425953088
90UbiquitinationTGASVLNKWQMNPYD
CCHHHHHHCCCCCCC		34.3421890473
96PhosphorylationNKWQMNPYDRGSAFA
HHCCCCCCCCCCCEE		17.1725839225
98MethylationWQMNPYDRGSAFAIG
CCCCCCCCCCCEEEC		34.81-
106PhosphorylationGSAFAIGSDGLCCQS
CCCEEECCCCCCCCC		23.5328348404
113PhosphorylationSDGLCCQSREVKEWH
CCCCCCCCCCCHHHH		19.2528857561
117AcetylationCCQSREVKEWHGCRA
CCCCCCCHHHHCCCC		50.7823749302
117UbiquitinationCCQSREVKEWHGCRA
CCCCCCCHHHHCCCC		50.78-
132AcetylationTKGLMKGKHYYEVSC
CCCCCCCCCEEEEEE		23.9426051181
132UbiquitinationTKGLMKGKHYYEVSC
CCCCCCCCCEEEEEE		23.94-
134PhosphorylationGLMKGKHYYEVSCHD
CCCCCCCEEEEEECC		12.5728152594
135PhosphorylationLMKGKHYYEVSCHDQ
CCCCCCEEEEEECCC		15.0128152594
138PhosphorylationGKHYYEVSCHDQGLC
CCCEEEEEECCCCCE		8.1928152594
155PhosphorylationGWSTMQASLDLGTDK
CCEEEHEEEECCCCC		12.9127251275
170PhosphorylationFGFGFGGTGKKSHNK
CCCCCCCCCCCCCCC		46.3229396449
1722-HydroxyisobutyrylationFGFGGTGKKSHNKQF
CCCCCCCCCCCCCCC		51.44-
172AcetylationFGFGGTGKKSHNKQF
CCCCCCCCCCCCCCC		51.4425953088
172MalonylationFGFGGTGKKSHNKQF
CCCCCCCCCCCCCCC		51.4426320211
172UbiquitinationFGFGGTGKKSHNKQF
CCCCCCCCCCCCCCC		51.44-
177UbiquitinationTGKKSHNKQFDNYGE
CCCCCCCCCCCCCCC		47.09-
204UbiquitinationDIDKGHVKFSKNGKD
EECCCEEEECCCCEE		37.94-
206PhosphorylationDKGHVKFSKNGKDLG
CCCEEEECCCCEECE		21.3525599653
231GlutathionylationNQALFPACVLKNAEL
CCCCHHHHHCCCCEE		3.6122555962
234AcetylationLFPACVLKNAELKFN
CHHHHHCCCCEEEEC		33.4425953088
234MalonylationLFPACVLKNAELKFN
CHHHHHCCCCEEEEC		33.4426320211
234MethylationLFPACVLKNAELKFN
CHHHHHCCCCEEEEC		33.4423583077
234UbiquitinationLFPACVLKNAELKFN
CHHHHHCCCCEEEEC		33.44-
239AcetylationVLKNAELKFNFGEEE
HCCCCEEEECCCCCC		29.7519608861
239UbiquitinationVLKNAELKFNFGEEE
HCCCCEEEECCCCCC		29.7519608861
252AcetylationEEFKFPPKDGFVALS
CCCCCCCCCCEEEEE		71.3826051181
259PhosphorylationKDGFVALSKAPDGYI
CCCEEEEEECCCCEE		19.6221406692
260AcetylationDGFVALSKAPDGYIV
CCEEEEEECCCCEEE		65.8626051181
260UbiquitinationDGFVALSKAPDGYIV
CCEEEEEECCCCEEE		65.86-
265PhosphorylationLSKAPDGYIVKSQHS
EEECCCCEEEEECCC		15.2128152594
2682-HydroxyisobutyrylationAPDGYIVKSQHSGNA
CCCCEEEEECCCCCC		34.54-
268AcetylationAPDGYIVKSQHSGNA
CCCCEEEEECCCCCC		34.5419608861
268UbiquitinationAPDGYIVKSQHSGNA
CCCCEEEEECCCCCC		34.5419608861
280PhosphorylationGNAQVTQTKFLPNAP
CCCEEEEEEECCCCC		17.88-
281UbiquitinationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7821890473
281UbiquitinationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7821890473
281AcetylationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7819608861
281MalonylationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7826320211
281SumoylationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7828112733
281UbiquitinationNAQVTQTKFLPNAPK
CCEEEEEEECCCCCC		34.7821890473
288UbiquitinationKFLPNAPKALIVEPS
EECCCCCCEEEECCC		54.1121890473
288UbiquitinationKFLPNAPKALIVEPS
EECCCCCCEEEECCC		54.1121890473
288UbiquitinationKFLPNAPKALIVEPS
EECCCCCCEEEECCC		54.1121890473
307UbiquitinationEQTLNNIKQFKKYID
HHHHHHHHHHHHHCC		52.3721890473
307UbiquitinationEQTLNNIKQFKKYID
HHHHHHHHHHHHHCC		52.3721890473
307AcetylationEQTLNNIKQFKKYID
HHHHHHHHHHHHHCC		52.3725953088
307MalonylationEQTLNNIKQFKKYID
HHHHHHHHHHHHHCC		52.3726320211
307UbiquitinationEQTLNNIKQFKKYID
HHHHHHHHHHHHHCC		52.3721890473
311UbiquitinationNNIKQFKKYIDNPKL
HHHHHHHHHCCCHHH		49.04-
3172-HydroxyisobutyrylationKKYIDNPKLRELLII
HHHCCCHHHHHHEEE		67.44-
317AcetylationKKYIDNPKLRELLII
HHHCCCHHHHHHEEE		67.4423749302
317MalonylationKKYIDNPKLRELLII
HHHCCCHHHHHHEEE		67.4426320211
317UbiquitinationKKYIDNPKLRELLII
HHHCCCHHHHHHEEE		67.44-
358UbiquitinationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.0021890473
358UbiquitinationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.0021890473
3582-HydroxyisobutyrylationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.00-
358AcetylationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.0025953088
358MalonylationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.0026320211
358UbiquitinationDDLVSTGKLNLSQVR
HHHHHCCCCCHHHEE		34.0021890473
377PhosphorylationDEADGLLSQGYSDFI
ECCCCHHHCCHHHHH		26.97-
380PhosphorylationDGLLSQGYSDFINRM
CCHHHCCHHHHHHHH		9.46-
381PhosphorylationGLLSQGYSDFINRMH
CHHHCCHHHHHHHHH		32.63-
3992-HydroxyisobutyrylationPQVTSDGKRLQVIVC
CEECCCCCEEEEEEE		55.73-
399AcetylationPQVTSDGKRLQVIVC
CEECCCCCEEEEEEE		55.73156387
416AcetylationTLHSFDVKKLSEKIM
EECCCCHHHHHHHHH		50.2523749302
417AcetylationLHSFDVKKLSEKIMH
ECCCCHHHHHHHHHC		58.0326051181
4212-HydroxyisobutyrylationDVKKLSEKIMHFPTW
CHHHHHHHHHCCCCE		41.79-
432AcetylationFPTWVDLKGEDSVPD
CCCEECCCCCCCCCC		56.6525953088
432SumoylationFPTWVDLKGEDSVPD
CCCEECCCCCCCCCC		56.65-
432UbiquitinationFPTWVDLKGEDSVPD
CCCEECCCCCCCCCC		56.65-
436PhosphorylationVDLKGEDSVPDTVHH
ECCCCCCCCCCCCEE		31.1130266825
440PhosphorylationGEDSVPDTVHHVVVP
CCCCCCCCCEEEEEE		18.7030266825
4512-HydroxyisobutyrylationVVVPVNPKTDRLWER
EEEECCCCCHHHHHH		58.83-
451UbiquitinationVVVPVNPKTDRLWER
EEEECCCCCHHHHHH		58.83-
461MethylationRLWERLGKSHIRTDD
HHHHHHCCCCCCCCC		43.37-
461UbiquitinationRLWERLGKSHIRTDD
HHHHHHCCCCCCCCC		43.37-
472MalonylationRTDDVHAKDNTRPGA
CCCCCCCCCCCCCCC		36.3126320211
472UbiquitinationRTDDVHAKDNTRPGA
CCCCCCCCCCCCCCC		36.31-
475PhosphorylationDVHAKDNTRPGANSP
CCCCCCCCCCCCCCH		48.6622167270
481PhosphorylationNTRPGANSPEMWSEA
CCCCCCCCHHHHHHH		23.0022167270
486PhosphorylationANSPEMWSEAIKILK
CCCHHHHHHHHHHHC		18.8130266825
490UbiquitinationEMWSEAIKILKGEYA
HHHHHHHHHHCCHHH		49.38-
493UbiquitinationSEAIKILKGEYAVRA
HHHHHHHCCHHHHHH		53.84-
496PhosphorylationIKILKGEYAVRAIKE
HHHHCCHHHHHHHHH		21.0429496907
505AcetylationVRAIKEHKMDQAIIF
HHHHHHCCCCEEEEE		45.3125953088
505MalonylationVRAIKEHKMDQAIIF
HHHHHHCCCCEEEEE		45.3126320211
513GlutathionylationMDQAIIFCRTKIDCD
CCEEEEEECCEECCC		3.6822555962
516AcetylationAIIFCRTKIDCDNLE
EEEEECCEECCCCHH		19.7323749302
516MalonylationAIIFCRTKIDCDNLE
EEEEECCEECCCCHH		19.7326320211
516UbiquitinationAIIFCRTKIDCDNLE
EEEEECCEECCCCHH		19.73-
519GlutathionylationFCRTKIDCDNLEQYF
EECCEECCCCHHHHC		4.2122555962
535AcetylationQQGGGPDKKGHQFSC
HCCCCCCCCCCEEEE		64.8825953088
535UbiquitinationQQGGGPDKKGHQFSC
HCCCCCCCCCCEEEE		64.88-
536UbiquitinationQGGGPDKKGHQFSCV
CCCCCCCCCCEEEEE		69.84-
541PhosphorylationDKKGHQFSCVCLHGD
CCCCCEEEEEEECCC		10.0828857561
571GlutathionylationGDVRFLICTDVAARG
CCEEEEEEECHHHCC		2.6422555962
5962-HydroxyisobutyrylationNVTLPDEKQNYVHRI
EEECCHHHCCHHHHH		51.75-
596AcetylationNVTLPDEKQNYVHRI
EEECCHHHCCHHHHH		51.7523954790
596UbiquitinationNVTLPDEKQNYVHRI
EEECCHHHCCHHHHH		51.75-
599PhosphorylationLPDEKQNYVHRIGRV
CCHHHCCHHHHHCCC		8.6426657352
621PhosphorylationLAISLVATEKEKVWY
EEEEEEEECCHHHEE		39.86-
628PhosphorylationTEKEKVWYHVCSSRG
ECCHHHEEEECCCCC		6.3321082442
632PhosphorylationKVWYHVCSSRGKGCY
HHEEEECCCCCCCCC		23.2130108239
633PhosphorylationVWYHVCSSRGKGCYN
HEEEECCCCCCCCCC		39.6728450419
634MethylationWYHVCSSRGKGCYNT
EEEECCCCCCCCCCC		34.25-
639PhosphorylationSSRGKGCYNTRLKED
CCCCCCCCCCEECCC		28.3920068231
641PhosphorylationRGKGCYNTRLKEDGG
CCCCCCCCEECCCCC		15.7620068231
671PhosphorylationEHLNCTISQVEPDIK
HHHCCCHHHCCCCCC		15.26-
687UbiquitinationPVDEFDGKVTYGQKR
CHHHCCCEEEECCEE		32.99-
6932-HydroxyisobutyrylationGKVTYGQKRAAGGGS
CEEEECCEECCCCCC		39.37-
693AcetylationGKVTYGQKRAAGGGS
CEEEECCEECCCCCC		39.3725953088
693UbiquitinationGKVTYGQKRAAGGGS
CEEEECCEECCCCCC		39.37-
700PhosphorylationKRAAGGGSYKGHVDI
EECCCCCCCCCCCEE		27.2628857561
701PhosphorylationRAAGGGSYKGHVDIL
ECCCCCCCCCCCEEE		25.0228985074
702AcetylationAAGGGSYKGHVDILA
CCCCCCCCCCCEEEC		44.2125953088
702UbiquitinationAAGGGSYKGHVDILA
CCCCCCCCCCCEEEC		44.21-
724PhosphorylationALEKEAQTSFLHLGY
HHHHHHHHCHHHHCC		28.6126074081
725PhosphorylationLEKEAQTSFLHLGYL
HHHHHHHCHHHHCCC		17.4626074081
731PhosphorylationTSFLHLGYLPNQLFR
HCHHHHCCCHHHHHC		25.9125884760
739PhosphorylationLPNQLFRTF------
CHHHHHCCC------		26.7726074081
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
377SPhosphorylationKinaseATMQ13315
PSP
671SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX1_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 DDX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSTF2_HUMANCSTF2physical
11598190
HNRPK_HUMANHNRNPKphysical
12183465
ATM_HUMANATMphysical
18710941
MRE11_HUMANMRE11Aphysical
18710941
RAD50_HUMANRAD50physical
18710941
NBN_HUMANNBNphysical
18710941
A4_HUMANAPPphysical
21832049
HNRPM_HUMANHNRNPMphysical
22939629
PP1A_HUMANPPP1CAphysical
22939629
EF1A1_HUMANEEF1A1physical
22939629
ROA1_HUMANHNRNPA1physical
22939629
FA98B_HUMANFAM98Bphysical
22939629
RN168_HUMANRNF168physical
22939629
RANB9_HUMANRANBP9physical
22939629
GEMI5_HUMANGEMIN5physical
22939629
STRN_HUMANSTRNphysical
22939629
TMED9_HUMANTMED9physical
22939629
HMCN1_HUMANHMCN1physical
22939629
PLOD3_HUMANPLOD3physical
22939629
SCRB2_HUMANSCARB2physical
22939629
XPO1_HUMANXPO1physical
22939629
FGOP2_HUMANFGFR1OP2physical
22939629
S30BP_HUMANSAP30BPphysical
22939629
IF2A_HUMANEIF2S1physical
22939629
MCCA_HUMANMCCC1physical
22939629
RFA2_HUMANRPA2physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
P5CS_HUMANALDH18A1physical
22939629
TPR_HUMANTPRphysical
22939629
VASP_HUMANVASPphysical
22939629
HEXI1_HUMANHEXIM1physical
22939629
KATL2_HUMANKATNAL2physical
22939629
STRP1_HUMANSTRIP1physical
22939629
POP1_HUMANPOP1physical
22939629
HYAS1_HUMANHAS1physical
22939629
HNRPD_HUMANHNRNPDphysical
22939629
PLOD1_HUMANPLOD1physical
22939629
LS14A_HUMANLSM14Aphysical
22939629
RBM4_HUMANRBM4physical
22939629
RC3H1_HUMANRC3H1physical
22939629
RHOA_HUMANRHOAphysical
22939629
NU133_HUMANNUP133physical
22939629
NDK7_HUMANNME7physical
21988832
ABCF1_HUMANABCF1physical
22863883
CN166_HUMANC14orf166physical
22863883
RTCB_HUMANRTCBphysical
22863883
NELFB_HUMANNELFBphysical
22863883
YBOX3_HUMANYBX3physical
22863883
EIF3K_HUMANEIF3Kphysical
22863883
ROA2_HUMANHNRNPA2B1physical
22863883
HNRPM_HUMANHNRNPMphysical
22863883
HNRPU_HUMANHNRNPUphysical
22863883
IF2B3_HUMANIGF2BP3physical
22863883
ILF2_HUMANILF2physical
22863883
K1C18_HUMANKRT18physical
22863883
MRE11_HUMANMRE11Aphysical
22863883
NMT1_HUMANNMT1physical
22863883
PDCD6_HUMANPDCD6physical
22863883
RPAC1_HUMANPOLR1Cphysical
22863883
SYQ_HUMANQARSphysical
22863883
RFC2_HUMANRFC2physical
22863883
RFC4_HUMANRFC4physical
22863883
RL26L_HUMANRPL26L1physical
22863883
RL27_HUMANRPL27physical
22863883
YBOX1_HUMANYBX1physical
22863883
CN166_HUMANC14orf166physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
4EBP1_HUMANEIF4EBP1physical
26344197
FA98A_HUMANFAM98Aphysical
26344197
FA98B_HUMANFAM98Bphysical
26344197
PICAL_HUMANPICALMphysical
26344197
RAVR1_HUMANRAVER1physical
26344197
RTCB_HUMANRTCBphysical
26344197
THUM1_HUMANTHUMPD1physical
26344197
FCL_HUMANTSTA3physical
26344197
HDAC1_HUMANHDAC1physical
27173435
XYLT2_HUMANXYLT2physical
27173435
RTCB_HUMANRTCBphysical
27173435
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 DDX1_HUMAN

loading...

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-239; LYS-268 AND LYS-281,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-80 AND THR-83, 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-628, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory