IWS1_HUMAN - dbPTM
IWS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IWS1_HUMAN
UniProt AC Q96ST2
Protein Name Protein IWS1 homolog
Gene Name IWS1
Organism Homo sapiens (Human).
Sequence Length 819
Subcellular Localization Nucleus .
Protein Description Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription..
Protein Sequence MDSEYYSGDQSDDGGATPVQDERDSGSDGEDDVNEQHSGSDTGSVERHSENETSDREDGLPKGHHVTDSENDEPLNLNASDSESEELHRQKDSDSESEERAEPPASDSENEDVNQHGSDSESEETRKLPGSDSENEELLNGHASDSENEDVGKHPASDSEIEELQKSPASDSETEDALKPQISDSESEEPPRHQASDSENEEPPKPRMSDSESEELPKPQVSDSESEEPPRHQASDSENEELPKPRISDSESEDPPRHQASDSENEELPKPRISDSESEDPPRNQASDSENEELPKPRVSDSESEGPQKGPASDSETEDASRHKQKPESDDDSDRENKGEDTEMQNDSFHSDSHMDRKKFHSSDSEEEEHKKQKMDSDEDEKEGEEEKVAKRKAAVLSDSEDEEKASAKKSRVVSDADDSDSDAVSDKSGKREKTIASDSEEEAGKELSDKKNEEKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKGETQVKEAEDSDSDDNIKRGKHMDFLSDFEMMLQRKKSMSGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPAVVMHLKKQDLKETFIDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPSVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSRPIFGLTSNYKGMTREEREQRDLEQMPQRRRMNSTGGQTPRRDLEKVLTGEEKALRPGDPGFCARARVPMPSNKDYVVRPKWNVEMESSRFQATSKKGISRLDKQMRKFTDIRKKSRSAHAVKISIEGNKMPL
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-------MDSEYYSG
-------CCCCCCCC		13.2822814378
3Phosphorylation-----MDSEYYSGDQ
-----CCCCCCCCCC		26.6327732954
3 (in isoform 2)Phosphorylation-26.6324043423
5Phosphorylation---MDSEYYSGDQSD
---CCCCCCCCCCCC		13.5923663014
5 (in isoform 2)Phosphorylation-13.5924043423
6Phosphorylation--MDSEYYSGDQSDD
--CCCCCCCCCCCCC		11.3523663014
6 (in isoform 2)Phosphorylation-11.3524043423
7Phosphorylation-MDSEYYSGDQSDDG
-CCCCCCCCCCCCCC		34.6823663014
7 (in isoform 2)Phosphorylation-34.6824043423
11PhosphorylationEYYSGDQSDDGGATP
CCCCCCCCCCCCCCC		42.2723663014
11 (in isoform 2)Phosphorylation-42.2724043423
17PhosphorylationQSDDGGATPVQDERD
CCCCCCCCCCCCCCC		27.5420363803
17 (in isoform 2)Phosphorylation-27.5424043423
23 (in isoform 2)Phosphorylation-52.2424043423
25PhosphorylationPVQDERDSGSDGEDD
CCCCCCCCCCCCCCC		46.5522167270
25 (in isoform 3)Phosphorylation-46.5522210691
26 (in isoform 2)Phosphorylation-33.7624043423
27PhosphorylationQDERDSGSDGEDDVN
CCCCCCCCCCCCCCC		46.5223401153
27 (in isoform 3)Phosphorylation-46.5222210691
28 (in isoform 2)Phosphorylation-68.9424043423
38PhosphorylationDDVNEQHSGSDTGSV
CCCCCCCCCCCCCCC		39.4223663014
40PhosphorylationVNEQHSGSDTGSVER
CCCCCCCCCCCCCCC		34.7125849741
42PhosphorylationEQHSGSDTGSVERHS
CCCCCCCCCCCCCCC		32.8123663014
44PhosphorylationHSGSDTGSVERHSEN
CCCCCCCCCCCCCCC		23.9325849741
49PhosphorylationTGSVERHSENETSDR
CCCCCCCCCCCCCCC		48.6229255136
49 (in isoform 3)Phosphorylation-48.6222210691
53PhosphorylationERHSENETSDREDGL
CCCCCCCCCCCCCCC		47.7323401153
53 (in isoform 3)Phosphorylation-47.7326657352
54PhosphorylationRHSENETSDREDGLP
CCCCCCCCCCCCCCC		28.6129255136
54 (in isoform 3)Phosphorylation-28.6126657352
56 (in isoform 3)Phosphorylation-43.6122210691
67PhosphorylationLPKGHHVTDSENDEP
CCCCCCCCCCCCCCC		29.4730266825
67 (in isoform 3)Phosphorylation-29.4729743597
69PhosphorylationKGHHVTDSENDEPLN
CCCCCCCCCCCCCCC		29.0024300666
80PhosphorylationEPLNLNASDSESEEL
CCCCCCCCCHHHHHH		40.3624300666
82PhosphorylationLNLNASDSESEELHR
CCCCCCCHHHHHHHH		40.2924300666
84PhosphorylationLNASDSESEELHRQK
CCCCCHHHHHHHHHC		40.0830266825
93PhosphorylationELHRQKDSDSESEER
HHHHHCCCCCCCHHH		50.5028985074
95PhosphorylationHRQKDSDSESEERAE
HHHCCCCCCCHHHCC		47.1528176443
97PhosphorylationQKDSDSESEERAEPP
HCCCCCCCHHHCCCC		49.0228176443
106PhosphorylationERAEPPASDSENEDV
HHCCCCCCCCCCCCH		47.6617081983
108PhosphorylationAEPPASDSENEDVNQ
CCCCCCCCCCCCHHH		39.5616565220
118PhosphorylationEDVNQHGSDSESEET
CCHHHCCCCCCCHHH		35.5228985074
120PhosphorylationVNQHGSDSESEETRK
HHHCCCCCCCHHHCC		44.7324461736
122PhosphorylationQHGSDSESEETRKLP
HCCCCCCCHHHCCCC		44.6917081983
131PhosphorylationETRKLPGSDSENEEL
HHCCCCCCCHHCHHH		35.7022115753
133PhosphorylationRKLPGSDSENEELLN
CCCCCCCHHCHHHHC		43.9816565220
144PhosphorylationELLNGHASDSENEDV
HHHCCCCCCCCCCCC		35.6722115753
146PhosphorylationLNGHASDSENEDVGK
HCCCCCCCCCCCCCC		39.5626055452
157PhosphorylationDVGKHPASDSEIEEL
CCCCCCCCHHHHHHH		46.2329255136
159PhosphorylationGKHPASDSEIEELQK
CCCCCCHHHHHHHHH		37.6726503892
167PhosphorylationEIEELQKSPASDSET
HHHHHHHCCCCCCCC		16.8520873877
170PhosphorylationELQKSPASDSETEDA
HHHHCCCCCCCCHHH		45.0825159151
172PhosphorylationQKSPASDSETEDALK
HHCCCCCCCCHHHHC		43.8725159151
174PhosphorylationSPASDSETEDALKPQ
CCCCCCCCHHHHCCC		43.0220873877
183PhosphorylationDALKPQISDSESEEP
HHHCCCCCCCCCCCC		29.8121082442
185PhosphorylationLKPQISDSESEEPPR
HCCCCCCCCCCCCCC		35.9128985074
187PhosphorylationPQISDSESEEPPRHQ
CCCCCCCCCCCCCCC		51.7320873877
196PhosphorylationEPPRHQASDSENEEP
CCCCCCCCCCCCCCC		34.7929255136
198PhosphorylationPRHQASDSENEEPPK
CCCCCCCCCCCCCCC		39.5629255136
198UbiquitinationPRHQASDSENEEPPK
CCCCCCCCCCCCCCC		39.5624816145
209PhosphorylationEPPKPRMSDSESEEL
CCCCCCCCCCCCCCC		38.9825159151
211PhosphorylationPKPRMSDSESEELPK
CCCCCCCCCCCCCCC		35.4025159151
213PhosphorylationPRMSDSESEELPKPQ
CCCCCCCCCCCCCCC		40.0825022875
222PhosphorylationELPKPQVSDSESEEP
CCCCCCCCCCCCCCC		30.1221082442
224PhosphorylationPKPQVSDSESEEPPR
CCCCCCCCCCCCCCC		35.2021082442
226PhosphorylationPQVSDSESEEPPRHQ
CCCCCCCCCCCCCCC		51.7325022875
235PhosphorylationEPPRHQASDSENEEL
CCCCCCCCCCCCCCC		34.7929255136
237PhosphorylationPRHQASDSENEELPK
CCCCCCCCCCCCCCC		39.5629255136
248PhosphorylationELPKPRISDSESEDP
CCCCCCCCCCCCCCC		36.0429255136
250PhosphorylationPKPRISDSESEDPPR
CCCCCCCCCCCCCCC		35.9129255136
252PhosphorylationPRISDSESEDPPRHQ
CCCCCCCCCCCCCCC		51.7829255136
261PhosphorylationDPPRHQASDSENEEL
CCCCCCCCCCCCCCC		34.7929255136
263PhosphorylationPRHQASDSENEELPK
CCCCCCCCCCCCCCC		39.5629255136
274PhosphorylationELPKPRISDSESEDP
CCCCCCCCCCCCCCC		36.0429255136
276PhosphorylationPKPRISDSESEDPPR
CCCCCCCCCCCCCCC		35.9129255136
278PhosphorylationPRISDSESEDPPRNQ
CCCCCCCCCCCCCCC		51.7829255136
287PhosphorylationDPPRNQASDSENEEL
CCCCCCCCCCCCCCC		31.7229255136
289PhosphorylationPRNQASDSENEELPK
CCCCCCCCCCCCCCC		39.5629255136
300PhosphorylationELPKPRVSDSESEGP
CCCCCCCCCCCCCCC		36.3829255136
302PhosphorylationPKPRVSDSESEGPQK
CCCCCCCCCCCCCCC		35.2023401153
304PhosphorylationPRVSDSESEGPQKGP
CCCCCCCCCCCCCCC		52.3729255136
313PhosphorylationGPQKGPASDSETEDA
CCCCCCCCCCCCHHH		44.8129255136
315PhosphorylationQKGPASDSETEDASR
CCCCCCCCCCHHHHH		43.8729255136
317PhosphorylationGPASDSETEDASRHK
CCCCCCCCHHHHHHC		43.0229255136
321PhosphorylationDSETEDASRHKQKPE
CCCCHHHHHHCCCCC		47.4423927012
329PhosphorylationRHKQKPESDDDSDRE
HHCCCCCCCCCCCCC		55.6720164059
333O-linked_GlycosylationKPESDDDSDRENKGE
CCCCCCCCCCCCCCC		45.6330379171
333PhosphorylationKPESDDDSDRENKGE
CCCCCCCCCCCCCCC		45.6320164059
342PhosphorylationRENKGEDTEMQNDSF
CCCCCCCCCCCCCCC		29.1128102081
348PhosphorylationDTEMQNDSFHSDSHM
CCCCCCCCCCCCCHH		32.2027362937
351PhosphorylationMQNDSFHSDSHMDRK
CCCCCCCCCCHHCHH		38.5127362937
353PhosphorylationNDSFHSDSHMDRKKF
CCCCCCCCHHCHHHH		24.5928102081
362PhosphorylationMDRKKFHSSDSEEEE
HCHHHHCCCCCHHHH		38.6929255136
363PhosphorylationDRKKFHSSDSEEEEH
CHHHHCCCCCHHHHH		36.2629255136
365PhosphorylationKKFHSSDSEEEEHKK
HHHCCCCCHHHHHHH		49.1829255136
377PhosphorylationHKKQKMDSDEDEKEG
HHHHHCCCHHHHHHC		39.1329255136
398PhosphorylationKRKAAVLSDSEDEEK
HHHHHHHCCCCHHHH		32.2729255136
400PhosphorylationKAAVLSDSEDEEKAS
HHHHHCCCCHHHHHH		43.5029255136
405UbiquitinationSDSEDEEKASAKKSR
CCCCHHHHHHHHHCC		45.6624816145
407PhosphorylationSEDEEKASAKKSRVV
CCHHHHHHHHHCCCC		52.2523927012
409AcetylationDEEKASAKKSRVVSD
HHHHHHHHHCCCCCC		49.1119829111
410UbiquitinationEEKASAKKSRVVSDA
HHHHHHHHCCCCCCC		43.1224816145
411PhosphorylationEKASAKKSRVVSDAD
HHHHHHHCCCCCCCC		29.6030576142
415PhosphorylationAKKSRVVSDADDSDS
HHHCCCCCCCCCCCC		24.9929255136
420PhosphorylationVVSDADDSDSDAVSD
CCCCCCCCCCCCCCC		39.2929255136
422PhosphorylationSDADDSDSDAVSDKS
CCCCCCCCCCCCCCC		31.2729255136
426PhosphorylationDSDSDAVSDKSGKRE
CCCCCCCCCCCCCCC		40.8329255136
429PhosphorylationSDAVSDKSGKREKTI
CCCCCCCCCCCCCCC		55.3126055452
434AcetylationDKSGKREKTIASDSE
CCCCCCCCCCCCCCH		49.636508079
435PhosphorylationKSGKREKTIASDSEE
CCCCCCCCCCCCCHH		19.6122167270
438PhosphorylationKREKTIASDSEEEAG
CCCCCCCCCCHHHHH		37.5129255136
440PhosphorylationEKTIASDSEEEAGKE
CCCCCCCCHHHHHHH		44.4029255136
449PhosphorylationEEAGKELSDKKNEEK
HHHHHHHHHHHHHHH		48.7723927012
461PhosphorylationEEKDLFGSDSESGNE
HHHCCCCCCCCCCCH		30.5429997176
463PhosphorylationKDLFGSDSESGNEEE
HCCCCCCCCCCCHHH		35.0529997176
465PhosphorylationLFGSDSESGNEEENL
CCCCCCCCCCHHHCH		51.3629997176
480PhosphorylationIADIFGESGDEEEEE
HHHHHCCCCCHHHHH		52.5026074081
489PhosphorylationDEEEEEFTGFNQEDL
CHHHHHHCCCCHHHH		44.1129997176
503PhosphorylationLEEEKGETQVKEAED
HHHHHCCCCCCCCCC		47.5328634120
511PhosphorylationQVKEAEDSDSDDNIK
CCCCCCCCCCCCCCH		30.4429255136
513PhosphorylationKEAEDSDSDDNIKRG
CCCCCCCCCCCCHHH		51.3029255136
518UbiquitinationSDSDDNIKRGKHMDF
CCCCCCCHHHHHHHH		62.44-
521UbiquitinationDDNIKRGKHMDFLSD
CCCCHHHHHHHHHHH		39.53-
527PhosphorylationGKHMDFLSDFEMMLQ
HHHHHHHHHHHHHHH		40.0027422710
532UbiquitinationFLSDFEMMLQRKKSM
HHHHHHHHHHHHHHH		1.9624816145
551PhosphorylationRRNRDGGTFISDADD
CCCCCCCCCCCCHHH		24.2729116813
554PhosphorylationRDGGTFISDADDVVS
CCCCCCCCCHHHHHH		23.6629116813
560UbiquitinationISDADDVVSAMIVKM
CCCHHHHHHHHHHHH		3.7721890473
560 (in isoform 2)Ubiquitination-3.7721890473
560 (in isoform 3)Ubiquitination-3.7721890473
576UbiquitinationEAAEEDRQLNNQKKP
HHHHHHHHHHHCCCH		61.9524816145
589PhosphorylationKPALKKLTLLPAVVM
CHHHHHHCHHHHHHH		34.8220068231
600AcetylationAVVMHLKKQDLKETF
HHHHHHHHHHHHHHH		56.2420167786
604AcetylationHLKKQDLKETFIDSG
HHHHHHHHHHHHHHH		64.1020167786
606PhosphorylationKKQDLKETFIDSGVM
HHHHHHHHHHHHHHH		25.0528387310
610PhosphorylationLKETFIDSGVMSAIK
HHHHHHHHHHHHHHH		28.5928387310
614PhosphorylationFIDSGVMSAIKEWLS
HHHHHHHHHHHHHHC		25.1628387310
621PhosphorylationSAIKEWLSPLPDRSL
HHHHHHHCCCCCCCC		26.0121815630
626MethylationWLSPLPDRSLPALKI
HHCCCCCCCCCHHHH		37.85115480703
6322-HydroxyisobutyrylationDRSLPALKIREELLK
CCCCCHHHHHHHHHH		41.65-
653AcetylationSVSQETLKHSGIGRA
CCCHHHHHHCCCCHH		43.0525953088
712SulfoxidationEQRDLEQMPQRRRMN
HHHHHHHCHHHHHHH		1.9221406390
720PhosphorylationPQRRRMNSTGGQTPR
HHHHHHHCCCCCCCH		21.0629255136
721PhosphorylationQRRRMNSTGGQTPRR
HHHHHHCCCCCCCHH		40.0827273156
725PhosphorylationMNSTGGQTPRRDLEK
HHCCCCCCCHHHHHH		23.2623401153
739AcetylationKVLTGEEKALRPGDP
HHHCCCHHHCCCCCC		48.7125953088
739UbiquitinationKVLTGEEKALRPGDP
HHHCCCHHHCCCCCC		48.7124816145
744UbiquitinationEEKALRPGDPGFCAR
CHHHCCCCCCCCCCE		47.5124816145
762PhosphorylationPMPSNKDYVVRPKWN
CCCCCCCCEECCCCC		11.49-
767AcetylationKDYVVRPKWNVEMES
CCCEECCCCCEEECC		40.6125953088
767UbiquitinationKDYVVRPKWNVEMES
CCCEECCCCCEEECC		40.6122817900
767 (in isoform 1)Ubiquitination-40.6121890473
772UbiquitinationRPKWNVEMESSRFQA
CCCCCEEECCCHHHC		5.4321890473
7822-HydroxyisobutyrylationSRFQATSKKGISRLD
CHHHCCCHHHHHHHH		51.14-
782AcetylationSRFQATSKKGISRLD
CHHHCCCHHHHHHHH		51.1425953088
783MethylationRFQATSKKGISRLDK
HHHCCCHHHHHHHHH		62.33116253573
783UbiquitinationRFQATSKKGISRLDK
HHHCCCHHHHHHHHH		62.3324816145
788UbiquitinationSKKGISRLDKQMRKF
CHHHHHHHHHHHHHH		8.4524816145
794MethylationRLDKQMRKFTDIRKK
HHHHHHHHHHHHHHH		47.47115971569
796PhosphorylationDKQMRKFTDIRKKSR
HHHHHHHHHHHHHHC		33.2924719451
811PhosphorylationSAHAVKISIEGNKMP
CCCEEEEEEECCCCC		14.6328555341
816UbiquitinationKISIEGNKMPL----
EEEEECCCCCC----		53.39-
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
720SPhosphorylationKinaseAKT1P31749
PSP
720SPhosphorylationKinaseAKT3Q9Y243
PSP
721TPhosphorylationKinaseAKT1P31749
PSP
721TPhosphorylationKinaseAKT3Q9Y243
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IWS1_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 IWS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPT6H_HUMANSUPT6Hphysical
19141475
SETD2_HUMANSETD2physical
19141475
RPB1_HUMANPOLR2Aphysical
19141475
STAT2_HUMANSTAT2physical
21988832
ERIC2_HUMANERICH2physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
CTR9_HUMANCTR9physical
26344197
PRCC_HUMANPRCCphysical
26496610
SPT5H_HUMANSUPT5Hphysical
26496610
CTDP1_HUMANCTDP1physical
26496610
BRE1B_HUMANRNF40physical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
SF3B5_HUMANSF3B5physical
26496610
DAB2P_HUMANDAB2IPphysical
26496610
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 IWS1_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 SER-287; SER-289; SER-315;SER-398; SER-400; THR-435; SER-438 AND SER-440, AND MASS SPECTROMETRY.
"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-157; SER-159; SER-170;SER-172; SER-300; SER-302; SER-304; SER-313; SER-315; SER-398;SER-400; THR-435; SER-438 AND SER-440, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398; SER-400; SER-438AND SER-440, AND MASS 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 SER-69; SER-80; SER-82;SER-276; SER-278; SER-287; SER-289; SER-313; SER-315; SER-377;SER-398; SER-400; SER-407; SER-415; SER-420; SER-422; SER-426;SER-429; SER-438; SER-440; SER-511 AND SER-513, AND MASS SPECTROMETRY.
"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 SER-377, 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-400, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASSSPECTROMETRY.
"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 SER-398; SER-400; SER-438AND SER-440, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"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-274; SER-276; SER-313;SER-315; SER-398; SER-400; SER-407; SER-438 AND SER-440, 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-131; SER-133; SER-144;SER-146; SER-157; SER-159; SER-248; SER-250; SER-261; SER-263;SER-274; SER-276; SER-287; SER-289; SER-313; SER-315; SER-329;SER-333; SER-362; SER-363; SER-365; SER-377; SER-398; SER-400;SER-415; SER-420; SER-422; SER-426; SER-438; SER-440; SER-461;SER-463; SER-465; SER-480; SER-511 AND SER-513, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-400, ANDMASS SPECTROMETRY.
"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 SER-95; SER-170; SER-183;SER-185; SER-222; SER-224; SER-287; SER-289; SER-315; SER-398;SER-400; SER-422; SER-426; SER-438 AND SER-440, AND MASS SPECTROMETRY.

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