BAIP2_HUMAN - dbPTM
BAIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAIP2_HUMAN
UniProt AC Q9UQB8
Protein Name Brain-specific angiogenesis inhibitor 1-associated protein 2
Gene Name BAIAP2
Organism Homo sapiens (Human).
Sequence Length 552
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Detected throughout the cytoplasm in the absence of specific binding partners. Detected in filopodia and close to membran
Protein Description Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection. Participates in actin bundling when associated with EPS8, promoting filopodial protrusions..
Protein Sequence MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSRNPFAHVQLKPTVTNDRCDLSAQGPEGREHGDGSARTLAGR
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
2Phosphorylation------MSLSRSEEM
------CCCCHHHHH		34.7422617229
2 (in isoform 5)Phosphorylation-34.7424719451
4Phosphorylation----MSLSRSEEMHR
----CCCCHHHHHHH		26.8423090842
6Phosphorylation--MSLSRSEEMHRLT
--CCCCHHHHHHHHH		34.2423090842
17PhosphorylationHRLTENVYKTIMEQF
HHHHHHHHHHHHHHH		17.6225106551
38PhosphorylationFIAMGKNYEKALAGV
HHHCCCCHHHHHHHH		23.4629496907
40UbiquitinationAMGKNYEKALAGVTY
HCCCCHHHHHHHHHH		38.04-
52PhosphorylationVTYAAKGYFDALVKM
HHHHHHHHHHHHHHH		9.51-
58UbiquitinationGYFDALVKMGELASE
HHHHHHHHHHHHHHC		41.88-
70UbiquitinationASESQGSKELGDVLF
HHCCCCCHHHHHHHH		64.8821906983
70 (in isoform 1)Ubiquitination-64.8821906983
70 (in isoform 2)Ubiquitination-64.8821906983
70 (in isoform 3)Ubiquitination-64.8821906983
70 (in isoform 4)Ubiquitination-64.8821906983
70 (in isoform 5)Ubiquitination-64.8821906983
70 (in isoform 6)Ubiquitination-64.8821906983
96PhosphorylationQLEEMLKSFHNELLT
HHHHHHHHHHHHHHH		27.9820068231
108UbiquitinationLLTQLEQKVELDSRY
HHHHHHHHHHHCHHH		28.44-
115PhosphorylationKVELDSRYLSAALKK
HHHHCHHHHHHHHHH		14.6828152594
121UbiquitinationRYLSAALKKYQTEQR
HHHHHHHHHHHHHHH		44.71-
1222-HydroxyisobutyrylationYLSAALKKYQTEQRS
HHHHHHHHHHHHHHC		43.36-
125PhosphorylationAALKKYQTEQRSKGD
HHHHHHHHHHHCCCH		30.88-
157PhosphorylationGSKNPQKYSDKELQY
CCCCCCCCCHHHHHH		19.4928152594
157 (in isoform 4)Phosphorylation-19.49-
157 (in isoform 5)Phosphorylation-19.49-
158PhosphorylationSKNPQKYSDKELQYI
CCCCCCCCHHHHHHH		49.6028152594
160AcetylationNPQKYSDKELQYIDA
CCCCCCHHHHHHHHH		55.1523236377
160UbiquitinationNPQKYSDKELQYIDA
CCCCCCHHHHHHHHH		55.1521906983
160 (in isoform 1)Ubiquitination-55.1521906983
160 (in isoform 2)Ubiquitination-55.1521906983
160 (in isoform 3)Ubiquitination-55.1521906983
160 (in isoform 4)Ubiquitination-55.1521906983
160 (in isoform 5)Ubiquitination-55.1521906983
160 (in isoform 6)Ubiquitination-55.1521906983
164PhosphorylationYSDKELQYIDAISNK
CCHHHHHHHHHHHCC		17.2521945579
171AcetylationYIDAISNKQGELENY
HHHHHHCCCCHHHHH		53.5426051181
171UbiquitinationYIDAISNKQGELENY
HHHHHHCCCCHHHHH		53.5421906983
171 (in isoform 1)Ubiquitination-53.5421906983
171 (in isoform 2)Ubiquitination-53.5421906983
171 (in isoform 3)Ubiquitination-53.5421906983
171 (in isoform 4)Ubiquitination-53.5421906983
171 (in isoform 5)Ubiquitination-53.5421906983
171 (in isoform 6)Ubiquitination-53.5421906983
178PhosphorylationKQGELENYVSDGYKT
CCCHHHHHHCCCHHH		7.6125394399
180PhosphorylationGELENYVSDGYKTAL
CHHHHHHCCCHHHHC		18.2429978859
184UbiquitinationNYVSDGYKTALTEER
HHHCCCHHHHCHHHH		32.6221906983
184 (in isoform 1)Ubiquitination-32.6221906983
184 (in isoform 2)Ubiquitination-32.6221906983
184 (in isoform 3)Ubiquitination-32.6221906983
184 (in isoform 4)Ubiquitination-32.6221906983
184 (in isoform 5)Ubiquitination-32.6221906983
184 (in isoform 6)Ubiquitination-32.6221906983
188PhosphorylationDGYKTALTEERRRFC
CCHHHHCHHHHHHHH		33.0827251275
206UbiquitinationEKQCAVAKNSAAYHS
HHHHHHHCCCHHHHH		44.85-
216UbiquitinationAAYHSKGKELLAQKL
HHHHHHCHHHHHHHC		49.26-
235UbiquitinationQACADPSKIPERAVQ
HHHCCHHHCHHHHHH		68.61-
249PhosphorylationQLMQQVASNGATLPS
HHHHHHHHCCCCCCH		36.6223403867
253PhosphorylationQVASNGATLPSALSA
HHHHCCCCCCHHHHH		40.3728102081
253 (in isoform 5)Phosphorylation-40.3724719451
256PhosphorylationSNGATLPSALSASKS
HCCCCCCHHHHHCCC		44.9829255136
256 (in isoform 5)Phosphorylation-44.9824719451
259PhosphorylationATLPSALSASKSNLV
CCCCHHHHHCCCCEE		30.1630266825
261PhosphorylationLPSALSASKSNLVIS
CCHHHHHCCCCEEEC		32.9930266825
261 (in isoform 4)Phosphorylation-32.99-
261 (in isoform 5)Phosphorylation-32.9924719451
263PhosphorylationSALSASKSNLVISDP
HHHHHCCCCEEECCC		32.6626657352
275UbiquitinationSDPIPGAKPLPVPPE
CCCCCCCCCCCCCHH		53.6621906983
275 (in isoform 1)Ubiquitination-53.6621906983
275 (in isoform 2)Ubiquitination-53.6621906983
275 (in isoform 3)Ubiquitination-53.6621906983
275 (in isoform 4)Ubiquitination-53.6621906983
275 (in isoform 5)Ubiquitination-53.6621906983
275 (in isoform 6)Ubiquitination-53.6621906983
291PhosphorylationAPFVGRMSAQESTPI
HHHCCCCCCCCCCCC		25.9921945579
291 (in isoform 5)Phosphorylation-25.9924719451
295PhosphorylationGRMSAQESTPIMNGV
CCCCCCCCCCCCCCC		27.6621945579
295 (in isoform 5)Phosphorylation-27.6624719451
296PhosphorylationRMSAQESTPIMNGVT
CCCCCCCCCCCCCCC		18.9721945579
296 (in isoform 4)Phosphorylation-18.97-
296 (in isoform 5)Phosphorylation-18.97-
303PhosphorylationTPIMNGVTGPDGEDY
CCCCCCCCCCCCCCC		44.3821945579
310PhosphorylationTGPDGEDYSPWADRK
CCCCCCCCCHHHCCC		16.6021945579
310 (in isoform 4)Phosphorylation-16.60-
310 (in isoform 5)Phosphorylation-16.60-
311PhosphorylationGPDGEDYSPWADRKA
CCCCCCCCHHHCCCC		26.7021945579
311 (in isoform 4)Phosphorylation-26.70-
311 (in isoform 5)Phosphorylation-26.70-
322UbiquitinationDRKAAQPKSLSPPQS
CCCCCCCCCCCCCCH		52.53-
323PhosphorylationRKAAQPKSLSPPQSQ
CCCCCCCCCCCCCHH		40.5430266825
323 (in isoform 4)Phosphorylation-40.54-
323 (in isoform 5)Phosphorylation-40.5424719451
325PhosphorylationAAQPKSLSPPQSQSK
CCCCCCCCCCCHHHH		41.4425159151
325 (in isoform 4)Phosphorylation-41.44-
325 (in isoform 5)Phosphorylation-41.4424719451
329PhosphorylationKSLSPPQSQSKLSDS
CCCCCCCHHHHCCCC		42.0430266825
331PhosphorylationLSPPQSQSKLSDSYS
CCCCCHHHHCCCCCC		40.5923403867
332UbiquitinationSPPQSQSKLSDSYSN
CCCCHHHHCCCCCCC		44.3621906983
332 (in isoform 1)Ubiquitination-44.3621906983
332 (in isoform 2)Ubiquitination-44.3621906983
332 (in isoform 3)Ubiquitination-44.3621906983
332 (in isoform 4)Ubiquitination-44.3621906983
332 (in isoform 5)Ubiquitination-44.3621906983
332 (in isoform 6)Ubiquitination-44.3621906983
334PhosphorylationPQSQSKLSDSYSNTL
CCHHHHCCCCCCCCC		28.3921945579
336PhosphorylationSQSKLSDSYSNTLPV
HHHHCCCCCCCCCCC		27.3821945579
336 (in isoform 5)Phosphorylation-27.3824719451
337PhosphorylationQSKLSDSYSNTLPVR
HHHCCCCCCCCCCCC		15.7821945579
338PhosphorylationSKLSDSYSNTLPVRK
HHCCCCCCCCCCCCC		27.5621945579
338 (in isoform 4)Phosphorylation-27.56-
338 (in isoform 5)Phosphorylation-27.5624719451
340PhosphorylationLSDSYSNTLPVRKSV
CCCCCCCCCCCCCCC		26.8819664994
340 (in isoform 4)Phosphorylation-26.88-
340 (in isoform 5)Phosphorylation-26.8824719451
346PhosphorylationNTLPVRKSVTPKNSY
CCCCCCCCCCCCCCC		22.2118669648
346 (in isoform 4)Phosphorylation-22.21-
346 (in isoform 5)Phosphorylation-22.2124719451
348PhosphorylationLPVRKSVTPKNSYAT
CCCCCCCCCCCCCCC		35.3221712546
348 (in isoform 4)Phosphorylation-35.32-
348 (in isoform 5)Phosphorylation-35.3224719451
350UbiquitinationVRKSVTPKNSYATTE
CCCCCCCCCCCCCCC		49.51-
352PhosphorylationKSVTPKNSYATTENK
CCCCCCCCCCCCCCC		23.4425849741
352 (in isoform 5)Phosphorylation-23.4424719451
353PhosphorylationSVTPKNSYATTENKT
CCCCCCCCCCCCCCC		19.8423927012
355PhosphorylationTPKNSYATTENKTLP
CCCCCCCCCCCCCCC		26.8123927012
356PhosphorylationPKNSYATTENKTLPR
CCCCCCCCCCCCCCC		29.4123927012
359UbiquitinationSYATTENKTLPRSSS
CCCCCCCCCCCCCHH		45.252190698
359 (in isoform 1)Ubiquitination-45.2521906983
359 (in isoform 2)Ubiquitination-45.2521906983
359 (in isoform 3)Ubiquitination-45.2521906983
359 (in isoform 4)Ubiquitination-45.2521906983
359 (in isoform 5)Ubiquitination-45.2521906983
360PhosphorylationYATTENKTLPRSSSM
CCCCCCCCCCCCHHH		54.2823401153
360 (in isoform 5)Phosphorylation-54.2824719451
364PhosphorylationENKTLPRSSSMAAGL
CCCCCCCCHHHHHHC		25.4830266825
365PhosphorylationNKTLPRSSSMAAGLE
CCCCCCCHHHHHHCH		25.9730266825
366PhosphorylationKTLPRSSSMAAGLER
CCCCCCHHHHHHCHH		17.4319664994
366 (in isoform 4)Phosphorylation-17.43-
366 (in isoform 5)Phosphorylation-17.4324719451
384PhosphorylationMRVKAIFSHAAGDNS
HHEEEEEECCCCCCC		13.2030266825
391PhosphorylationSHAAGDNSTLLSFKE
ECCCCCCCEEEEECC		25.7730266825
392PhosphorylationHAAGDNSTLLSFKEG
CCCCCCCEEEEECCC		37.6630266825
392 (in isoform 5)Phosphorylation-37.6624719451
395PhosphorylationGDNSTLLSFKEGDLI
CCCCEEEEECCCCEE		37.0725849741
395 (in isoform 5)Phosphorylation-37.0724719451
403PhosphorylationFKEGDLITLLVPEAR
ECCCCEEEEEEECCC		22.7224732914
432PhosphorylationGWFPFSYTRVLDSDG
CEECCEEEEEECCCC		17.07-
437PhosphorylationSYTRVLDSDGSDRLH
EEEEEECCCCCCCCE		39.4428857561
440PhosphorylationRVLDSDGSDRLHMSL
EEECCCCCCCCEEEE		25.2528985074
440 (in isoform 5)Phosphorylation-25.2524719451
446PhosphorylationGSDRLHMSLQQGKSS
CCCCCEEEECCCCCC		16.5728857561
446 (in isoform 5)Phosphorylation-16.5724719451
452PhosphorylationMSLQQGKSSSTGNLL
EEECCCCCCCCCCCC		36.0230266825
452 (in isoform 4)Phosphorylation-36.02-
452 (in isoform 5)Phosphorylation-36.0224719451
453PhosphorylationSLQQGKSSSTGNLLD
EECCCCCCCCCCCCC		35.0930266825
453 (in isoform 4)Phosphorylation-35.09-
453 (in isoform 5)Phosphorylation-35.09-
454PhosphorylationLQQGKSSSTGNLLDK
ECCCCCCCCCCCCCH		47.6425159151
454 (in isoform 4)Phosphorylation-47.64-
454 (in isoform 5)Phosphorylation-47.64-
455PhosphorylationQQGKSSSTGNLLDKD
CCCCCCCCCCCCCHH		31.8530266825
455 (in isoform 4)Phosphorylation-31.85-
455 (in isoform 5)Phosphorylation-31.85-
471PhosphorylationLAIPPPDYGAASRAF
CCCCCCCCCHHHCCC		17.9028152594
471 (in isoform 4)Phosphorylation-17.90-
471 (in isoform 5)Phosphorylation-17.90-
475PhosphorylationPPDYGAASRAFPAQT
CCCCCHHHCCCCCCC		24.4928152594
482PhosphorylationSRAFPAQTASGFKQR
HCCCCCCCCCCCCCC		25.5429396449
484PhosphorylationAFPAQTASGFKQRPY
CCCCCCCCCCCCCCC		48.4225159151
484 (in isoform 5)Phosphorylation-48.4224719451
491PhosphorylationSGFKQRPYSVAVPAF
CCCCCCCCEEECCCC		20.2621945579
492PhosphorylationGFKQRPYSVAVPAFS
CCCCCCCEEECCCCC		13.2921945579
492 (in isoform 5)Phosphorylation-13.2924719451
499PhosphorylationSVAVPAFSQGLDDYG
EEECCCCCCCCCCCC		25.9921945579
499 (in isoform 4)Phosphorylation-25.99-
499 (in isoform 5)Phosphorylation-25.9924719451
505PhosphorylationFSQGLDDYGARSMSR
CCCCCCCCCCCCCCC		16.6121945579
509PhosphorylationLDDYGARSMSRNPFA
CCCCCCCCCCCCCCC		22.1528555341
509 (in isoform 4)Phosphorylation-22.1527251275
509 (in isoform 5)Phosphorylation-22.1525849741
510 (in isoform 6)Phosphorylation-3.4827251275
511 (in isoform 4)Phosphorylation-30.1030266825
511 (in isoform 5)Phosphorylation-30.1025849741
512 (in isoform 4)Phosphorylation-46.3130266825
512 (in isoform 5)Phosphorylation-46.3122617229
512 (in isoform 6)Phosphorylation-46.3130266825
513 (in isoform 6)Phosphorylation-28.8330266825
514 (in isoform 4)Phosphorylation-27.0530266825
515 (in isoform 6)Phosphorylation-9.3130266825
516 (in isoform 4)Phosphorylation-11.8230266825
517 (in isoform 6)Phosphorylation-14.2930266825
519 (in isoform 4)Phosphorylation-33.6223090842
520 (in isoform 4)Phosphorylation-7.5428355574
520 (in isoform 6)Phosphorylation-7.5423090842
521 (in isoform 6)Phosphorylation-22.8828355574
523PhosphorylationAHVQLKPTVTNDRCD
CEEEECCCCCCCCCC		38.0726437602
523 (in isoform 2)Phosphorylation-38.0727251275
525 (in isoform 2)Phosphorylation-33.6027251275
529 (in isoform 2)Phosphorylation-7.4227251275
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
366SPhosphorylationKinasePRKAA2P54646
GPS
366SPhosphorylationKinaseMARK2Q7KZI7
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAIP2_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 BAIP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPN90_HUMANNCKIPSDphysical
16189514
EPS8_HUMANEPS8physical
15289329
LIN7B_RATLin7bphysical
14596909
ERG28_HUMANC14orf1physical
16169070
SHAN1_HUMANSHANK1physical
12504591
CDC42_HUMANCDC42physical
12504591
CDC42_HUMANCDC42physical
11696321
ENAH_HUMANENAHphysical
11696321
ATN1_HUMANATN1physical
10332026
WASF2_HUMANWASF2physical
11130076
RAC1_HUMANRAC1physical
11130076
CDC42_HUMANCDC42physical
11130076
PAK1_HUMANPAK1physical
11130076
A4_HUMANAPPphysical
21832049
CDC42_HUMANCDC42physical
11157984
RAC1_HUMANRAC1physical
11157984
RHOA_HUMANRHOAphysical
11157984
RTN4_HUMANRTN4physical
21988832
WASL_HUMANWASLphysical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
BAIP2_HUMANBAIAP2physical
25416956
PRR13_HUMANPRR13physical
25416956
CS025_HUMANC19orf25physical
25416956
NCKP1_HUMANNCKAP1physical
26186194
CYFP2_HUMANCYFIP2physical
26186194
CYFP1_HUMANCYFIP1physical
26186194
EPS8_HUMANEPS8physical
26186194
BI2L1_HUMANBAIAP2L1physical
26186194
GDS1_HUMANRAP1GDS1physical
26186194
K1522_HUMANKIAA1522physical
26186194
ABI1_HUMANABI1physical
26186194
WASF2_HUMANWASF2physical
26186194
CS025_HUMANC19orf25physical
21516116
CRY1_HUMANCRY1physical
26496610
KC1E_HUMANCSNK1Ephysical
26496610
DECR_HUMANDECR1physical
26496610
WASL_HUMANWASLphysical
26496610
MPZL1_HUMANMPZL1physical
26496610
ABI1_HUMANABI1physical
26496610
WASF2_HUMANWASF2physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
CYFP1_HUMANCYFIP1physical
26496610
PPIL2_HUMANPPIL2physical
26496610
TFB1M_HUMANTFB1Mphysical
26496610
BI2L1_HUMANBAIAP2L1physical
26496610
K1522_HUMANKIAA1522physical
26496610
RBM26_HUMANRBM26physical
26496610
CHMP6_HUMANCHMP6physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
BI2L1_HUMANBAIAP2L1physical
28514442
K1522_HUMANKIAA1522physical
28514442
ABI1_HUMANABI1physical
28514442
WASF2_HUMANWASF2physical
28514442
GDS1_HUMANRAP1GDS1physical
28514442
NCKP1_HUMANNCKAP1physical
28514442
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
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 BAIP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-325 AND SER-454, 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-296; TYR-310; SER-323;SER-325; SER-346; THR-348 AND SER-366, AND MASS SPECTROMETRY.
"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-325, AND MASSSPECTROMETRY.
"Dentatorubral-pallidoluysian atrophy protein interacts through aproline-rich region near polyglutamine with the SH3 domain of aninsulin receptor tyrosine kinase substrate.";
Okamura-Oho Y., Miyashita T., Ohmi K., Yamada M.;
Hum. Mol. Genet. 8:947-957(1999).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), PHOSPHORYLATION ATTYROSINE RESIDUES, SUBCELLULAR LOCATION, INTERACTION WITH ATN1, ANDTISSUE SPECIFICITY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-337, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-157, 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-337; TYR-491 ANDTYR-505, AND MASS SPECTROMETRY.

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