HTSF1_HUMAN - dbPTM
HTSF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HTSF1_HUMAN
UniProt AC O43719
Protein Name HIV Tat-specific factor 1
Gene Name HTATSF1
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization Nucleus .
Protein Description Functions as a general transcription factor playing a role in the process of transcriptional elongation. May mediate the reciprocal stimulatory effect of splicing on transcriptional elongation. In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus..
Protein Sequence MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFRDPEEADYCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEANRGLRRSDSVSASERAGPSRARHFSEHPSTSKMNAQETATGMAFEEPIDEKKFEKTEDGGEFEEGASENNAKESSPEKEAEEGCPEKESEEGCPKRGFEGSCSQKESEEGNPVRGSEEDSPKKESKKKTLKNDCEENGLAKESEDDLNKESEEEVGPTKESEEDDSEKESDEDCSEKQSEDGSEREFEENGLEKDLDEEGSEKELHENVLDKELEENDSENSEFEDDGSEKVLDEEGSEREFDEDSDEKEEEEDTYEKVFDDESDEKEDEEYADEKGLEAADKKAEEGDADEKLFEESDDKEDEDADGKEVEDADEKLFEDDDSNEKLFDEEEDSSEKLFDDSDERGTLGGFGSVEEGPLSTGSSFILSSDDDDDDI
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
2Acetylation------MSGTNLDGN
------CCCCCCCCC		55.0919664995
2Phosphorylation------MSGTNLDGN
------CCCCCCCCC		55.0925159151
4Phosphorylation----MSGTNLDGNDE
----CCCCCCCCCHH		25.8719664995
17MethylationDEFDEQLRMQELYGD
HHHHHHHHHHHHHCC		25.16115918237
22PhosphorylationQLRMQELYGDGKDGD
HHHHHHHHCCCCCCC		16.6528796482
30PhosphorylationGDGKDGDTQTDAGGE
CCCCCCCCCCCCCCC		38.6128796482
32PhosphorylationGKDGDTQTDAGGEPD
CCCCCCCCCCCCCCC		29.8828796482
40PhosphorylationDAGGEPDSLGQQPTD
CCCCCCCCCCCCCCC		45.1528796482
46PhosphorylationDSLGQQPTDTPYEWD
CCCCCCCCCCCCCCC		48.4428796482
48PhosphorylationLGQQPTDTPYEWDLD
CCCCCCCCCCCCCCC		30.1928796482
50PhosphorylationQQPTDTPYEWDLDKK
CCCCCCCCCCCCCCC		31.5728796482
56UbiquitinationPYEWDLDKKAWFPKI
CCCCCCCCCCCCCCC		52.2529967540
57UbiquitinationYEWDLDKKAWFPKIT
CCCCCCCCCCCCCCC		50.98-
64PhosphorylationKAWFPKITEDFIATY
CCCCCCCCHHHHHHH		35.3130175587
71PhosphorylationTEDFIATYQANYGFS
CHHHHHHHHHHCCCC		9.15-
75PhosphorylationIATYQANYGFSNDGA
HHHHHHHCCCCCCCC		23.67-
78PhosphorylationYQANYGFSNDGASSS
HHHHCCCCCCCCCCC		29.6430175587
86PhosphorylationNDGASSSTANVEDVH
CCCCCCCCCCHHHHH		24.9730576142
104AcetylationAEEPPQEKAPEPTDA
CCCCCCCCCCCCCCH		65.0826051181
104UbiquitinationAEEPPQEKAPEPTDA
CCCCCCCCCCCCCCH		65.0821906983
119UbiquitinationRKKGEKRKAESGWFH
HHHCCCCCCCCCCEE		68.5229967540
122PhosphorylationGEKRKAESGWFHVEE
CCCCCCCCCCEEEEE		46.3025159151
154PhosphorylationDEFIQLMSKFGIIMR
HHHHHHHHHHCCEEC		33.16-
160SulfoxidationMSKFGIIMRDPQTEE
HHHHCCEECCCCCCE		3.6221406390
169AcetylationDPQTEEFKVKLYKDN
CCCCCEEEEEEEECC		41.5623749302
169UbiquitinationDPQTEEFKVKLYKDN
CCCCCEEEEEEEECC		41.5633845483
1742-HydroxyisobutyrylationEFKVKLYKDNQGNLK
EEEEEEEECCCCCCC		61.72-
174AcetylationEFKVKLYKDNQGNLK
EEEEEEEECCCCCCC		61.7223749302
174UbiquitinationEFKVKLYKDNQGNLK
EEEEEEEECCCCCCC		61.7229967540
181UbiquitinationKDNQGNLKGDGLCCY
ECCCCCCCCCCEEEE		59.9829967540
1902-HydroxyisobutyrylationDGLCCYLKRESVELA
CCEEEEEHHHHHHHH		27.87-
190AcetylationDGLCCYLKRESVELA
CCEEEEEHHHHHHHH		27.8725953088
190UbiquitinationDGLCCYLKRESVELA
CCEEEEEHHHHHHHH		27.8733845483
193PhosphorylationCCYLKRESVELALKL
EEEEHHHHHHHHHHH		25.5627067055
199UbiquitinationESVELALKLLDEDEI
HHHHHHHHHCCHHHC		41.2021963094
207MethylationLLDEDEIRGYKLHVE
HCCHHHCCCEEEEEE		40.10115918241
210AcetylationEDEIRGYKLHVEVAK
HHHCCCEEEEEEEEE		34.6325953088
210UbiquitinationEDEIRGYKLHVEVAK
HHHCCCEEEEEEEEE		34.6329967540
217AcetylationKLHVEVAKFQLKGEY
EEEEEEEEHHHCCCC		38.5325953088
217UbiquitinationKLHVEVAKFQLKGEY
EEEEEEEEHHHCCCC		38.5321890473
221SumoylationEVAKFQLKGEYDASK
EEEEHHHCCCCCCCH		38.62-
221SumoylationEVAKFQLKGEYDASK
EEEEHHHCCCCCCCH		38.62-
221UbiquitinationEVAKFQLKGEYDASK
EEEEHHHCCCCCCCH		38.6223000965
224PhosphorylationKFQLKGEYDASKKKK
EHHHCCCCCCCHHHH		26.02-
239UbiquitinationKCKDYKKKLSMQQKQ
HHHHHHHHHHHHHHH		41.4623000965
241PhosphorylationKDYKKKLSMQQKQLD
HHHHHHHHHHHHHHC		24.3526074081
245AcetylationKKLSMQQKQLDWRPE
HHHHHHHHHHCCCHH		35.6225953088
245UbiquitinationKKLSMQQKQLDWRPE
HHHHHHHHHHCCCHH		35.6223000965
297AcetylationDLRVECSKFGQIRKL
HHHHHHHHHCCCHHH		66.2325953088
297UbiquitinationDLRVECSKFGQIRKL
HHHHHHHHHCCCHHH		66.2324816145
303UbiquitinationSKFGQIRKLLLFDRH
HHHCCCHHHEEECCC		45.1522817900
309MethylationRKLLLFDRHPDGVAS
HHHEEECCCCCCEEE		35.58115918245
316PhosphorylationRHPDGVASVSFRDPE
CCCCCEEEEEECCHH		18.8522210691
318PhosphorylationPDGVASVSFRDPEEA
CCCEEEEEECCHHHC		16.4522210691
327NitrationRDPEEADYCIQTLDG
CCHHHCCEEEEECCC		9.86-
327PhosphorylationRDPEEADYCIQTLDG
CCHHHCCEEEEECCC		9.8622210691
331PhosphorylationEADYCIQTLDGRWFG
HCCEEEEECCCCEEC		13.6022210691
350PhosphorylationTAQAWDGTTDYQVEE
EEEEECCCCCCEEEC		17.6428348404
351PhosphorylationAQAWDGTTDYQVEET
EEEECCCCCCEEECH		37.9328348404
353PhosphorylationAWDGTTDYQVEETSR
EECCCCCCEEECHHH		16.62-
358PhosphorylationTDYQVEETSREREER
CCCEEECHHHHHHHH		21.4123898821
359PhosphorylationDYQVEETSREREERL
CCEEECHHHHHHHHH		35.1128348404
367MethylationREREERLRGWEAFLN
HHHHHHHHHHHHHHC		55.17115918249
380MethylationLNAPEANRGLRRSDS
HCCHHHHHCCCCCCC		53.2080702789
385PhosphorylationANRGLRRSDSVSASE
HHHCCCCCCCCCHHH		28.0130266825
387PhosphorylationRGLRRSDSVSASERA
HCCCCCCCCCHHHHC		21.1525159151
389PhosphorylationLRRSDSVSASERAGP
CCCCCCCCHHHHCCC		29.9930266825
391PhosphorylationRSDSVSASERAGPSR
CCCCCCHHHHCCCHH		21.8028176443
393MethylationDSVSASERAGPSRAR
CCCCHHHHCCCHHHH		42.20115918253
397PhosphorylationASERAGPSRARHFSE
HHHHCCCHHHHHCCC		37.3423090842
400MethylationRAGPSRARHFSEHPS
HCCCHHHHHCCCCCC		30.21115918257
403PhosphorylationPSRARHFSEHPSTSK
CHHHHHCCCCCCCCC		28.9523401153
407PhosphorylationRHFSEHPSTSKMNAQ
HHCCCCCCCCCCCHH		47.4225159151
408PhosphorylationHFSEHPSTSKMNAQE
HCCCCCCCCCCCHHH		36.5021712546
409PhosphorylationFSEHPSTSKMNAQET
CCCCCCCCCCCHHHH		33.9621712546
410AcetylationSEHPSTSKMNAQETA
CCCCCCCCCCHHHHH		35.9425953088
411SulfoxidationEHPSTSKMNAQETAT
CCCCCCCCCHHHHHH		5.1421406390
416PhosphorylationSKMNAQETATGMAFE
CCCCHHHHHHCCCCC		19.8929978859
418PhosphorylationMNAQETATGMAFEEP
CCHHHHHHCCCCCCC		34.6028464451
429SumoylationFEEPIDEKKFEKTED
CCCCCCHHHEEECCC		60.04-
429AcetylationFEEPIDEKKFEKTED
CCCCCCHHHEEECCC		60.0425953088
429SumoylationFEEPIDEKKFEKTED
CCCCCCHHHEEECCC		60.0428112733
429UbiquitinationFEEPIDEKKFEKTED
CCCCCCHHHEEECCC		60.0432015554
430SumoylationEEPIDEKKFEKTEDG
CCCCCHHHEEECCCC		57.6228112733
434PhosphorylationDEKKFEKTEDGGEFE
CHHHEEECCCCCCCC		31.9225159151
445PhosphorylationGEFEEGASENNAKES
CCCCCCCCCCCCCCC		52.2825159151
452PhosphorylationSENNAKESSPEKEAE
CCCCCCCCCHHHHHH		50.9529255136
453PhosphorylationENNAKESSPEKEAEE
CCCCCCCCHHHHHHC		37.8629255136
456AcetylationAKESSPEKEAEEGCP
CCCCCHHHHHHCCCC		66.6626051181
465AcetylationAEEGCPEKESEEGCP
HHCCCCCCCCCCCCC		52.2426051181
467PhosphorylationEGCPEKESEEGCPKR
CCCCCCCCCCCCCCC		52.6023927012
473AcetylationESEEGCPKRGFEGSC
CCCCCCCCCCCCCCC		70.0526051181
473UbiquitinationESEEGCPKRGFEGSC
CCCCCCCCCCCCCCC		70.0529967540
479PhosphorylationPKRGFEGSCSQKESE
CCCCCCCCCCCCCCC		11.9123401153
481PhosphorylationRGFEGSCSQKESEEG
CCCCCCCCCCCCCCC		46.0829255136
483AcetylationFEGSCSQKESEEGNP
CCCCCCCCCCCCCCC		47.0826051181
483UbiquitinationFEGSCSQKESEEGNP
CCCCCCCCCCCCCCC		47.0833845483
485PhosphorylationGSCSQKESEEGNPVR
CCCCCCCCCCCCCCC		48.2430266825
494PhosphorylationEGNPVRGSEEDSPKK
CCCCCCCCCCCCCCH		27.5229255136
498PhosphorylationVRGSEEDSPKKESKK
CCCCCCCCCCHHHHH		41.7329255136
503PhosphorylationEDSPKKESKKKTLKN
CCCCCHHHHHHHHHH		59.6724732914
504AcetylationDSPKKESKKKTLKND
CCCCHHHHHHHHHHH		60.4220167786
505AcetylationSPKKESKKKTLKNDC
CCCHHHHHHHHHHHH		61.3420167786
506AcetylationPKKESKKKTLKNDCE
CCHHHHHHHHHHHHH		63.9320167786
507PhosphorylationKKESKKKTLKNDCEE
CHHHHHHHHHHHHHH		52.4226074081
509AcetylationESKKKTLKNDCEENG
HHHHHHHHHHHHHCC		56.8425953088
509UbiquitinationESKKKTLKNDCEENG
HHHHHHHHHHHHHCC		56.8432015554
521PhosphorylationENGLAKESEDDLNKE
HCCCCCCCHHHCCHH		45.6923927012
529PhosphorylationEDDLNKESEEEVGPT
HHHCCHHCHHHHCCC		52.5029255136
536PhosphorylationSEEEVGPTKESEEDD
CHHHHCCCCCCCCCC		41.3323403867
539PhosphorylationEVGPTKESEEDDSEK
HHCCCCCCCCCCCCC		48.0930576142
544PhosphorylationKESEEDDSEKESDED
CCCCCCCCCCCCCCC		63.9925849741
548PhosphorylationEDDSEKESDEDCSEK
CCCCCCCCCCCHHHH		58.3230576142
553PhosphorylationKESDEDCSEKQSEDG
CCCCCCHHHHHCCCC		61.2120873877
557PhosphorylationEDCSEKQSEDGSERE
CCHHHHHCCCCCHHH		49.0425159151
561PhosphorylationEKQSEDGSEREFEEN
HHHCCCCCHHHHHHC		45.8928355574
579PhosphorylationKDLDEEGSEKELHEN
CCCCCCCCHHHHHHH		49.1029255136
597PhosphorylationKELEENDSENSEFED
HHHHHCCCCCCCCCC		50.7023927012
600PhosphorylationEENDSENSEFEDDGS
HHCCCCCCCCCCCCC		39.3425159151
607PhosphorylationSEFEDDGSEKVLDEE
CCCCCCCCCEEECCC		41.0423927012
616PhosphorylationKVLDEEGSEREFDED
EEECCCCCCCCCCCC		36.4429255136
624PhosphorylationEREFDEDSDEKEEEE
CCCCCCCCCCHHHHH		45.6922167270
633PhosphorylationEKEEEEDTYEKVFDD
CHHHHHHHHHHHCCC		36.5420201521
634PhosphorylationKEEEEDTYEKVFDDE
HHHHHHHHHHHCCCC		26.5223927012
642PhosphorylationEKVFDDESDEKEDEE
HHHCCCCCCHHHHHH		59.0529255136
650PhosphorylationDEKEDEEYADEKGLE
CHHHHHHHHHHHHHH		19.8030278072
661AcetylationKGLEAADKKAEEGDA
HHHHHHHHHHHCCCC		49.5123749302
676PhosphorylationDEKLFEESDDKEDED
CHHHHHCCCCCCCCC		43.8629255136
702PhosphorylationKLFEDDDSNEKLFDE
HHCCCCCCCCCCCCC		54.6119664994
705UbiquitinationEDDDSNEKLFDEEED
CCCCCCCCCCCCCCC		59.7229967540
713PhosphorylationLFDEEEDSSEKLFDD
CCCCCCCCCCCCCCC		43.6129255136
714PhosphorylationFDEEEDSSEKLFDDS
CCCCCCCCCCCCCCC		51.5819664994
716UbiquitinationEEEDSSEKLFDDSDE
CCCCCCCCCCCCCCC		57.3029967540
721PhosphorylationSEKLFDDSDERGTLG
CCCCCCCCCCCCCCC		43.1219664994
726PhosphorylationDDSDERGTLGGFGSV
CCCCCCCCCCCCCCC		28.5725137130
732PhosphorylationGTLGGFGSVEEGPLS
CCCCCCCCCCCCCCC		24.8820873877
739PhosphorylationSVEEGPLSTGSSFIL
CCCCCCCCCCCCEEE		33.5820873877
740PhosphorylationVEEGPLSTGSSFILS
CCCCCCCCCCCEEEC		49.0920873877
742PhosphorylationEGPLSTGSSFILSSD
CCCCCCCCCEEECCC		23.3620068231
743PhosphorylationGPLSTGSSFILSSDD
CCCCCCCCEEECCCC		20.0420873877
747PhosphorylationTGSSFILSSDDDDDD
CCCCEEECCCCCCCC		27.2320068231
748PhosphorylationGSSFILSSDDDDDDI
CCCEEECCCCCCCCC		41.4325137130
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 HTSF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HTSF1_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 HTSF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FEZ1_HUMANFEZ1physical
16169070
T2FB_HUMANGTF2F2physical
10454543
RPB1_HUMANPOLR2Aphysical
10454543
SPT5H_HUMANSUPT5Hphysical
10454543
SF3A2_HUMANSF3A2physical
9710584
SRRM1_HUMANSRRM1physical
22939629
SFPQ_HUMANSFPQphysical
22939629
PTBP1_HUMANPTBP1physical
22939629
PGK1_HUMANPGK1physical
22939629
NIBL1_HUMANFAM129Bphysical
22939629
POP1_HUMANPOP1physical
22939629
KATL2_HUMANKATNAL2physical
22939629
NAF1_HUMANNAF1physical
22939629
SRSF4_HUMANSRSF4physical
22365833
PELP1_HUMANPELP1physical
26344197
SMD2_HUMANSNRPD2physical
26344197
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 HTSF1_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-642; SER-702; SER-713AND SER-714, 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-445; SER-557; SER-561;SER-642; SER-702; SER-713 AND SER-714, 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-579; SER-616; SER-624;SER-642 AND SER-676, 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-452; SER-453; SER-498;SER-642; SER-713 AND SER-714, 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-702, 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-445; SER-616 ANDSER-702, AND MASS SPECTROMETRY.
"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-481, 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-498; SER-597; SER-607;SER-616; SER-624; SER-642; SER-676 AND SER-702, 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-624 AND SER-702, 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-387; SER-494; SER-498;SER-557; SER-561; SER-579; SER-597; SER-600; SER-607; SER-616;SER-624; SER-642; SER-676; SER-702; SER-713; SER-714 AND SER-721, ANDMASS SPECTROMETRY.

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