ABLM1_HUMAN - dbPTM
ABLM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABLM1_HUMAN
UniProt AC O14639
Protein Name Actin-binding LIM protein 1
Gene Name ABLIM1
Organism Homo sapiens (Human).
Sequence Length 778
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Associated with the cytoskeleton..
Protein Description May act as scaffold protein (By similarity). May play a role in the development of the retina. Has been suggested to play a role in axon guidance..
Protein Sequence MPAFLGLKCLGKLCSSEKSKVTSSERTSARGSNRKRLIVEDRRVSGTSFTAHRRATITHLLYLCPKDYCPRGRVCNSVDPFVAHPQDPHHPSEKPVIHCHKCGEPCKGEVLRVQTKHFHIKCFTCKVCGCDLAQGGFFIKNGEYLCTLDYQRMYGTRCHGCGEFVEGEVVTALGKTYHPNCFACTICKRPFPPGDRVTFNGRDCLCQLCAQPMSSSPKETTFSSNCAGCGRDIKNGQALLALDKQWHLGCFKCKSCGKVLTGEYISKDGAPYCEKDYQGLFGVKCEACHQFITGKVLEAGDKHYHPSCARCSRCNQMFTEGEEMYLQGSTVWHPDCKQSTKTEEKLRPTRTSSESIYSRPGSSIPGSPGHTIYAKVDNEILDYKDLAAIPKVKAIYDIERPDLITYEPFYTSGYDDKQERQSLGESPRTLSPTPSAEGYQDVRDRMIHRSTSQGSINSPVYSRHSYTPTTSRSPQHFHRPGNEPSSGRNSPLPYRPDSRPLTPTYAQAPKHFHVPDQGINIYRKPPIYKQHAALAAQSKSSEDIIKFSKFPAAQAPDPSETPKIETDHWPGPPSFAVVGPDMKRRSSGREEDDEELLRRRQLQEEQLMKLNSGLGQLILKEEMEKESRERSSLLASRYDSPINSASHIPSSKTASLPGYGRNGLHRPVSTDFAQYNSYGDVSGGVRDYQTLPDGHMPAMRMDRGVSMPNMLEPKIFPYEMLMVTNRGRNKILREVDRTRLERHLAPEVFREIFGMSIQEFDRLPLWRRNDMKKKAKLF
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
22PhosphorylationSSEKSKVTSSERTSA
CCCCCCCCCCHHHCC		30.2120806909
28PhosphorylationVTSSERTSARGSNRK
CCCCHHHCCCCCCCC		23.3820806915
38 (in isoform 5)Phosphorylation-3.5622673903
39 (in isoform 5)Phosphorylation-8.0825884760
40 (in isoform 5)Phosphorylation-38.5126657352
41 (in isoform 4)Phosphorylation-32.5627642862
44 (in isoform 5)Phosphorylation-6.88-
45 (in isoform 5)Phosphorylation-34.24-
52 (in isoform 5)Phosphorylation-19.3926437602
55 (in isoform 5)Phosphorylation-11.8726437602
57 (in isoform 5)Phosphorylation-1.9226437602
63 (in isoform 5)Phosphorylation-3.9823663014
64 (in isoform 5)Phosphorylation-2.1923663014
65 (in isoform 5)Phosphorylation-29.9218669648
69 (in isoform 5)Phosphorylation-2.3819901323
74 (in isoform 5)Phosphorylation-3.9525159151
121UbiquitinationQTKHFHIKCFTCKVC
EECCEEEEEEECCCC		18.09-
123 (in isoform 4)Phosphorylation-8.3621406692
124 (in isoform 4)Phosphorylation-22.3821406692
125 (in isoform 4)Phosphorylation-1.2328152594
127 (in isoform 4)Phosphorylation-3.5428152594
128 (in isoform 4)Phosphorylation-2.4728152594
129 (in isoform 4)Phosphorylation-15.8028152594
131 (in isoform 4)Phosphorylation-30.2630266825
145 (in isoform 4)Phosphorylation-1.2428796482
149 (in isoform 3)Phosphorylation-21.2621406692
150 (in isoform 3)Phosphorylation-10.9221406692
151 (in isoform 3)Phosphorylation-24.2728152594
153 (in isoform 3)Phosphorylation-1.8228152594
154 (in isoform 3)Phosphorylation-19.9628152594
155 (in isoform 3)Phosphorylation-9.4228152594
157 (in isoform 3)Phosphorylation-13.1830266825
171 (in isoform 3)Phosphorylation-22.7228796482
177 (in isoform 5)Phosphorylation-20.8321406692
178 (in isoform 5)Phosphorylation-16.6021406692
179 (in isoform 5)Phosphorylation-28.9528152594
181 (in isoform 5)Phosphorylation-2.4228152594
182 (in isoform 5)Phosphorylation-8.7628152594
183 (in isoform 5)Phosphorylation-7.5528152594
185PhosphorylationHPNCFACTICKRPFP
CCCCEEEEEECCCCC		26.4428857561
185 (in isoform 5)Phosphorylation-26.4430266825
199 (in isoform 5)Phosphorylation-9.2628796482
214PhosphorylationQLCAQPMSSSPKETT
HHHCCCCCCCCCCCC		34.0523401153
215PhosphorylationLCAQPMSSSPKETTF
HHCCCCCCCCCCCCC		44.3925159151
216PhosphorylationCAQPMSSSPKETTFS
HCCCCCCCCCCCCCC		32.4625159151
220PhosphorylationMSSSPKETTFSSNCA
CCCCCCCCCCCCCCC		38.9928857561
221PhosphorylationSSSPKETTFSSNCAG
CCCCCCCCCCCCCCC		23.7028857561
223PhosphorylationSPKETTFSSNCAGCG
CCCCCCCCCCCCCCC		20.6728857561
234UbiquitinationAGCGRDIKNGQALLA
CCCCCCCCCCCEEEE		60.35-
272PhosphorylationISKDGAPYCEKDYQG
ECCCCCCCCCCCCCC		16.8330278072
275UbiquitinationDGAPYCEKDYQGLFG
CCCCCCCCCCCCCCC		59.17-
277PhosphorylationAPYCEKDYQGLFGVK
CCCCCCCCCCCCCCC		18.6230278072
293PhosphorylationEACHQFITGKVLEAG
HHCCHHHHCCEEECC		32.0430278072
294 (in isoform 6)Phosphorylation-17.1722673903
295 (in isoform 6)Phosphorylation-34.6925884760
296PhosphorylationHQFITGKVLEAGDKH
CHHHHCCEEECCCCC		6.5527251275
296 (in isoform 6)Phosphorylation-6.5526657352
300 (in isoform 6)Phosphorylation-34.81-
301 (in isoform 6)Phosphorylation-41.42-
307PhosphorylationGDKHYHPSCARCSRC
CCCCCCCCHHCCCHH		13.7020068231
308 (in isoform 6)Phosphorylation-3.0526437602
311 (in isoform 6)Phosphorylation-1.2826437602
313PhosphorylationPSCARCSRCNQMFTE
CCHHCCCHHHCCCCC		27.3427251275
313 (in isoform 6)Phosphorylation-27.3426437602
319 (in isoform 6)Phosphorylation-37.4223663014
320 (in isoform 6)Phosphorylation-54.0323663014
321 (in isoform 6)Phosphorylation-32.8618669648
325PhosphorylationFTEGEEMYLQGSTVW
CCCCCCEEECCCEEE		10.1115144186
325 (in isoform 6)Phosphorylation-10.1119901323
330 (in isoform 6)Phosphorylation-34.1425159151
345UbiquitinationQSTKTEEKLRPTRTS
CCCCCHHHHCCCCCC		43.49-
349PhosphorylationTEEKLRPTRTSSESI
CHHHHCCCCCCCCCH		39.9030576142
351PhosphorylationEKLRPTRTSSESIYS
HHHCCCCCCCCCHHC		38.8023401153
352O-linked_GlycosylationKLRPTRTSSESIYSR
HHCCCCCCCCCHHCC		28.9020068230
352PhosphorylationKLRPTRTSSESIYSR
HHCCCCCCCCCHHCC		28.9023927012
353PhosphorylationLRPTRTSSESIYSRP
HCCCCCCCCCHHCCC		34.4521945579
355PhosphorylationPTRTSSESIYSRPGS
CCCCCCCCHHCCCCC		28.8621945579
357PhosphorylationRTSSESIYSRPGSSI
CCCCCCHHCCCCCCC		14.1221945579
358O-linked_GlycosylationTSSESIYSRPGSSIP
CCCCCHHCCCCCCCC		30.2620068230
358PhosphorylationTSSESIYSRPGSSIP
CCCCCHHCCCCCCCC		30.2621945579
362O-linked_GlycosylationSIYSRPGSSIPGSPG
CHHCCCCCCCCCCCC		27.9820068230
362PhosphorylationSIYSRPGSSIPGSPG
CHHCCCCCCCCCCCC		27.9821945579
363O-linked_GlycosylationIYSRPGSSIPGSPGH
HHCCCCCCCCCCCCC		38.4220068230
363PhosphorylationIYSRPGSSIPGSPGH
HHCCCCCCCCCCCCC		38.4221945579
367PhosphorylationPGSSIPGSPGHTIYA
CCCCCCCCCCCEEEE		23.5022167270
371O-linked_GlycosylationIPGSPGHTIYAKVDN
CCCCCCCEEEEEECC		22.9220068230
371PhosphorylationIPGSPGHTIYAKVDN
CCCCCCCEEEEEECC		22.9221945579
373PhosphorylationGSPGHTIYAKVDNEI
CCCCCEEEEEECCCC		11.0921945579
383PhosphorylationVDNEILDYKDLAAIP
ECCCCCCHHHHHCCC		11.7128796482
384UbiquitinationDNEILDYKDLAAIPK
CCCCCCHHHHHCCCC		46.03-
393UbiquitinationLAAIPKVKAIYDIER
HHCCCCCEEEEECCC		34.88-
396PhosphorylationIPKVKAIYDIERPDL
CCCCEEEEECCCCCC		18.7428796482
405PhosphorylationIERPDLITYEPFYTS
CCCCCCEEECCCCCC		29.1825884760
406PhosphorylationERPDLITYEPFYTSG
CCCCCEEECCCCCCC		18.0125884760
410PhosphorylationLITYEPFYTSGYDDK
CEEECCCCCCCCCCH		15.6525106551
411PhosphorylationITYEPFYTSGYDDKQ
EEECCCCCCCCCCHH		18.9628796482
412PhosphorylationTYEPFYTSGYDDKQE
EECCCCCCCCCCHHH		24.7928796482
414PhosphorylationEPFYTSGYDDKQERQ
CCCCCCCCCCHHHHH		22.2726552605
417UbiquitinationYTSGYDDKQERQSLG
CCCCCCCHHHHHHCC		51.68-
422PhosphorylationDDKQERQSLGESPRT
CCHHHHHHCCCCCCC		44.5628355574
426PhosphorylationERQSLGESPRTLSPT
HHHHCCCCCCCCCCC		20.2023401153
429O-linked_GlycosylationSLGESPRTLSPTPSA
HCCCCCCCCCCCCCC		34.6620068230
429PhosphorylationSLGESPRTLSPTPSA
HCCCCCCCCCCCCCC		34.6622167270
431PhosphorylationGESPRTLSPTPSAEG
CCCCCCCCCCCCCCC		26.5619664994
433PhosphorylationSPRTLSPTPSAEGYQ
CCCCCCCCCCCCCCH		26.8822167270
435PhosphorylationRTLSPTPSAEGYQDV
CCCCCCCCCCCCHHH		41.2422167270
439PhosphorylationPTPSAEGYQDVRDRM
CCCCCCCCHHHHHHC		7.9530266825
450O-linked_GlycosylationRDRMIHRSTSQGSIN
HHHCCCCCCCCCCCC		20.4620068230
450PhosphorylationRDRMIHRSTSQGSIN
HHHCCCCCCCCCCCC		20.4622167270
451PhosphorylationDRMIHRSTSQGSINS
HHCCCCCCCCCCCCC		25.6522167270
452O-linked_GlycosylationRMIHRSTSQGSINSP
HCCCCCCCCCCCCCC		33.5217525332
452O-linked_GlycosylationRMIHRSTSQGSINSP
HCCCCCCCCCCCCCC		33.5219664995
452PhosphorylationRMIHRSTSQGSINSP
HCCCCCCCCCCCCCC		33.5222167270
455O-linked_GlycosylationHRSTSQGSINSPVYS
CCCCCCCCCCCCCCC		15.8020068230
455PhosphorylationHRSTSQGSINSPVYS
CCCCCCCCCCCCCCC		15.8022167270
458PhosphorylationTSQGSINSPVYSRHS
CCCCCCCCCCCCCCC		17.6725159151
461PhosphorylationGSINSPVYSRHSYTP
CCCCCCCCCCCCCCC		11.9021945579
462O-linked_GlycosylationSINSPVYSRHSYTPT
CCCCCCCCCCCCCCC		24.6120068230
462PhosphorylationSINSPVYSRHSYTPT
CCCCCCCCCCCCCCC		24.6121945579
462 (in isoform 2)Phosphorylation-24.6127642862
465O-linked_GlycosylationSPVYSRHSYTPTTSR
CCCCCCCCCCCCCCC		29.5920068230
465PhosphorylationSPVYSRHSYTPTTSR
CCCCCCCCCCCCCCC		29.5929396449
466PhosphorylationPVYSRHSYTPTTSRS
CCCCCCCCCCCCCCC		15.6028796482
467PhosphorylationVYSRHSYTPTTSRSP
CCCCCCCCCCCCCCC		19.7125159151
469PhosphorylationSRHSYTPTTSRSPQH
CCCCCCCCCCCCCCC		29.6029396449
470PhosphorylationRHSYTPTTSRSPQHF
CCCCCCCCCCCCCCC		24.2827251275
471O-linked_GlycosylationHSYTPTTSRSPQHFH
CCCCCCCCCCCCCCC		32.9920068230
471PhosphorylationHSYTPTTSRSPQHFH
CCCCCCCCCCCCCCC		32.9927251275
473PhosphorylationYTPTTSRSPQHFHRP
CCCCCCCCCCCCCCC		28.7820068231
490PhosphorylationEPSSGRNSPLPYRPD
CCCCCCCCCCCCCCC		26.8426657352
494PhosphorylationGRNSPLPYRPDSRPL
CCCCCCCCCCCCCCC		42.3218083107
498PhosphorylationPLPYRPDSRPLTPTY
CCCCCCCCCCCCCCC		38.1824719451
502PhosphorylationRPDSRPLTPTYAQAP
CCCCCCCCCCCCCCC		19.109787149
505PhosphorylationSRPLTPTYAQAPKHF
CCCCCCCCCCCCCCC		9.6430803885
522PhosphorylationPDQGINIYRKPPIYK
CCCCCCEECCCCCHH		14.22105675
528PhosphorylationIYRKPPIYKQHAALA
EECCCCCHHHHHHHH		15.467125165
529MethylationYRKPPIYKQHAALAA
ECCCCCHHHHHHHHH		36.01-
529UbiquitinationYRKPPIYKQHAALAA
ECCCCCHHHHHHHHH		36.01-
538PhosphorylationHAALAAQSKSSEDII
HHHHHHHCCCHHHHH		29.7623403867
540PhosphorylationALAAQSKSSEDIIKF
HHHHHCCCHHHHHHH		44.1823927012
541PhosphorylationLAAQSKSSEDIIKFS
HHHHCCCHHHHHHHH		42.9223927012
546UbiquitinationKSSEDIIKFSKFPAA
CCHHHHHHHHCCCHH		43.87-
548PhosphorylationSEDIIKFSKFPAAQA
HHHHHHHHCCCHHHC		28.5223532336
549UbiquitinationEDIIKFSKFPAAQAP
HHHHHHHCCCHHHCC		59.50-
559PhosphorylationAAQAPDPSETPKIET
HHHCCCCCCCCCCCC		62.5728857561
561PhosphorylationQAPDPSETPKIETDH
HCCCCCCCCCCCCCC		33.9323532336
566PhosphorylationSETPKIETDHWPGPP
CCCCCCCCCCCCCCC		36.3227251275
586PhosphorylationGPDMKRRSSGREEDD
CCCCCCCCCCCCCCH		40.9722167270
587PhosphorylationPDMKRRSSGREEDDE
CCCCCCCCCCCCCHH		39.8125159151
612PhosphorylationEQLMKLNSGLGQLIL
HHHHHHHHHHHHHHH		45.9228674151
620SumoylationGLGQLILKEEMEKES
HHHHHHHHHHHHHHH		44.6328112733
631PhosphorylationEKESRERSSLLASRY
HHHHHHHHHHHHHHC		22.1524732914
632PhosphorylationKESRERSSLLASRYD
HHHHHHHHHHHHHCC		33.3524732914
636PhosphorylationERSSLLASRYDSPIN
HHHHHHHHHCCCCCC		31.2024732914
638PhosphorylationSSLLASRYDSPINSA
HHHHHHHCCCCCCCC		20.4823927012
640PhosphorylationLLASRYDSPINSASH
HHHHHCCCCCCCCCC		20.8130266825
644PhosphorylationRYDSPINSASHIPSS
HCCCCCCCCCCCCCC		31.6930266825
646PhosphorylationDSPINSASHIPSSKT
CCCCCCCCCCCCCCC		23.0523927012
650PhosphorylationNSASHIPSSKTASLP
CCCCCCCCCCCCCCC		43.8124732914
651O-linked_GlycosylationSASHIPSSKTASLPG
CCCCCCCCCCCCCCC		28.7720068230
651PhosphorylationSASHIPSSKTASLPG
CCCCCCCCCCCCCCC		28.7724732914
652UbiquitinationASHIPSSKTASLPGY
CCCCCCCCCCCCCCC		53.07-
653PhosphorylationSHIPSSKTASLPGYG
CCCCCCCCCCCCCCC		24.3530266825
655PhosphorylationIPSSKTASLPGYGRN
CCCCCCCCCCCCCCC		40.0919664994
659PhosphorylationKTASLPGYGRNGLHR
CCCCCCCCCCCCCCC		15.8023927012
669PhosphorylationNGLHRPVSTDFAQYN
CCCCCCCCCCHHHCC		25.5823401153
670PhosphorylationGLHRPVSTDFAQYNS
CCCCCCCCCHHHCCC		35.0623401153
675PhosphorylationVSTDFAQYNSYGDVS
CCCCHHHCCCCCCCC		11.5728796482
677O-linked_GlycosylationTDFAQYNSYGDVSGG
CCHHHCCCCCCCCCC		26.0920068230
677PhosphorylationTDFAQYNSYGDVSGG
CCHHHCCCCCCCCCC		26.0923401153
678PhosphorylationDFAQYNSYGDVSGGV
CHHHCCCCCCCCCCC		17.4421082442
682O-linked_GlycosylationYNSYGDVSGGVRDYQ
CCCCCCCCCCCCCCC		34.2720068230
682PhosphorylationYNSYGDVSGGVRDYQ
CCCCCCCCCCCCCCC		34.2723403867
688PhosphorylationVSGGVRDYQTLPDGH
CCCCCCCCCCCCCCC		7.8828796482
690PhosphorylationGGVRDYQTLPDGHMP
CCCCCCCCCCCCCCC		33.7530814553
706PhosphorylationMRMDRGVSMPNMLEP
CCCCCCCCCCCCCCC		31.2025159151
718PhosphorylationLEPKIFPYEMLMVTN
CCCCCCCHHHEEEEE		11.8346157241
724PhosphorylationPYEMLMVTNRGRNKI
CHHHEEEEECCHHHH		12.7746157235
726MethylationEMLMVTNRGRNKILR
HHEEEEECCHHHHHH		35.76-
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 ABLM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABLM1_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 ABLM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VIME_HUMANVIMphysical
16189514
BEGIN_HUMANBEGAINphysical
16189514
TRAF2_HUMANTRAF2physical
16189514
LDOC1_HUMANLDOC1physical
16189514
T22D4_HUMANTSC22D4physical
16189514
USBP1_HUMANUSHBP1physical
16189514
CACO2_HUMANCALCOCO2physical
16189514
HOOK2_HUMANHOOK2physical
16189514
ACTB_HUMANACTBphysical
9245787
A4_HUMANAPPphysical
21832049
ABRA_HUMANABRAphysical
17194709
CARD9_HUMANCARD9physical
25416956
NMT1_HUMANNMT1physical
26186194
SPCS_HUMANSEPSECSphysical
26186194
SPCS_HUMANSEPSECSphysical
28514442
NMT1_HUMANNMT1physical
28514442
1433Z_HUMANYWHAZphysical
28514442
CBY1_HUMANCBY1physical
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 ABLM1_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-367; TYR-373; SER-426;SER-431; THR-433 AND SER-435, 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 THR-429; SER-431; SER-435;TYR-439; SER-450; THR-451; SER-458 AND SER-655, 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-431; SER-435; SER-455;SER-458; SER-587; SER-640; SER-655 AND SER-706, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-458, 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 SER-473, AND MASSSPECTROMETRY.
"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-431; SER-452; SER-655AND SER-706, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-357; TYR-373; SER-435;TYR-439 AND TYR-461, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-461, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396; TYR-406 ANDTYR-410, AND MASS SPECTROMETRY.

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