UBP32_HUMAN - dbPTM
UBP32_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP32_HUMAN
UniProt AC Q8NFA0
Protein Name Ubiquitin carboxyl-terminal hydrolase 32
Gene Name USP32
Organism Homo sapiens (Human).
Sequence Length 1604
Subcellular Localization Membrane
Lipid-anchor . Golgi apparatus .
Protein Description
Protein Sequence MGAKESRIGFLSYEEALRRVTDVELKRLKDAFKRTCGLSYYMGQHCFIREVLGDGVPPKVAEVIYCSFGGTSKGLHFNNLIVGLVLLTRGKDEEKAKYIFSLFSSESGNYVIREEMERMLHVVDGKVPDTLRKCFSEGEKVNYEKFRNWLFLNKDAFTFSRWLLSGGVYVTLTDDSDTPTFYQTLAGVTHLEESDIIDLEKRYWLLKAQSRTGRFDLETFGPLVSPPIRPSLSEGLFNAFDENRDNHIDFKEISCGLSACCRGPLAERQKFCFKVFDVDRDGVLSRVELRDMVVALLEVWKDNRTDDIPELHMDLSDIVEGILNAHDTTKMGHLTLEDYQIWSVKNVLANEFLNLLFQVCHIVLGLRPATPEEEGQIIRGWLERESRYGLQAGHNWFIISMQWWQQWKEYVKYDANPVVIEPSSVLNGGKYSFGTAAHPMEQVEDRIGSSLSYVNTTEEKFSDNISTASEASETAGSGFLYSATPGADVCFARQHNTSDNNNQCLLGANGNILLHLNPQKPGAIDNQPLVTQEPVKATSLTLEGGRLKRTPQLIHGRDYEMVPEPVWRALYHWYGANLALPRPVIKNSKTDIPELELFPRYLLFLRQQPATRTQQSNIWVNMGNVPSPNAPLKRVLAYTGCFSRMQTIKEIHEYLSQRLRIKEEDMRLWLYNSENYLTLLDDEDHKLEYLKIQDEQHLVIEVRNKDMSWPEEMSFIANSSKIDRHKVPTEKGATGLSNLGNTCFMNSSIQCVSNTQPLTQYFISGRHLYELNRTNPIGMKGHMAKCYGDLVQELWSGTQKNVAPLKLRWTIAKYAPRFNGFQQQDSQELLAFLLDGLHEDLNRVHEKPYVELKDSDGRPDWEVAAEAWDNHLRRNRSIVVDLFHGQLRSQVKCKTCGHISVRFDPFNFLSLPLPMDSYMHLEITVIKLDGTTPVRYGLRLNMDEKYTGLKKQLSDLCGLNSEQILLAEVHGSNIKNFPQDNQKVRLSVSGFLCAFEIPVPVSPISASSPTQTDFSSSPSTNEMFTLTTNGDLPRPIFIPNGMPNTVVPCGTEKNFTNGMVNGHMPSLPDSPFTGYIIAVHRKMMRTELYFLSSQKNRPSLFGMPLIVPCTVHTRKKDLYDAVWIQVSRLASPLPPQEASNHAQDCDDSMGYQYPFTLRVVQKDGNSCAWCPWYRFCRGCKIDCGEDRAFIGNAYIAVDWDPTALHLRYQTSQERVVDEHESVEQSRRAQAEPINLDSCLRAFTSEEELGENEMYYCSKCKTHCLATKKLDLWRLPPILIIHLKRFQFVNGRWIKSQKIVKFPRESFDPSAFLVPRDPALCQHKPLTPQGDELSEPRILAREVKKVDAQSSAGEEDVLLSKSPSSLSANIISSPKGSPSSSRKSGTSCPSSKNSSPNSSPRTLGRSKGRLRLPQIGSKNKLSSSKENLDASKENGAGQICELADALSRGHVLGGSQPELVTPQDHEVALANGFLYEHEACGNGYSNGQLGNHSEEDSTDDQREDTRIKPIYNLYAISCHSGILGGGHYVTYAKNPNCKWYCYNDSSCKELHPDEIDTDSAYILFYEQQGIDYAQFLPKTDGKKMADTSSMDEDFESDYKKYCVLQ
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
16UbiquitinationGFLSYEEALRRVTDV
CCCCHHHHHHHCCHH
8.4024816145
23UbiquitinationALRRVTDVELKRLKD
HHHHCCHHHHHHHHH
7.2924816145
26UbiquitinationRVTDVELKRLKDAFK
HCCHHHHHHHHHHHH
42.0224816145
35PhosphorylationLKDAFKRTCGLSYYM
HHHHHHHHHCCHHHH
16.1224043423
39PhosphorylationFKRTCGLSYYMGQHC
HHHHHCCHHHHCCCE
10.2524043423
40PhosphorylationKRTCGLSYYMGQHCF
HHHHCCHHHHCCCEE
11.5224043423
41PhosphorylationRTCGLSYYMGQHCFI
HHHCCHHHHCCCEEH
7.4424043423
42UbiquitinationTCGLSYYMGQHCFIR
HHCCHHHHCCCEEHH
2.9424816145
98PhosphorylationKDEEKAKYIFSLFSS
CCHHHHHHHHHHHCC
16.4422115753
101PhosphorylationEKAKYIFSLFSSESG
HHHHHHHHHHCCCCC
20.9522115753
104PhosphorylationKYIFSLFSSESGNYV
HHHHHHHCCCCCCEE
38.1922115753
105PhosphorylationYIFSLFSSESGNYVI
HHHHHHCCCCCCEEE
28.5722115753
107PhosphorylationFSLFSSESGNYVIRE
HHHHCCCCCCEEEHH
34.0022115753
110PhosphorylationFSSESGNYVIREEME
HCCCCCCEEEHHHHH
10.7722115753
145AcetylationGEKVNYEKFRNWLFL
CCCCCHHHHHCCCCC
38.988242893
145UbiquitinationGEKVNYEKFRNWLFL
CCCCCHHHHHCCCCC
38.9829967540
203PhosphorylationIIDLEKRYWLLKAQS
CEEHHHHHHHHHHHC
16.1030576142
256UbiquitinationDFKEISCGLSACCRG
CHHHHCCCCHHHHCC
18.8427667366
259UbiquitinationEISCGLSACCRGPLA
HHCCCCHHHHCCCHH
11.0627667366
274"N6,N6-dimethyllysine"ERQKFCFKVFDVDRD
HHCCEEEEEEEECCC
43.08-
274MethylationERQKFCFKVFDVDRD
HHCCEEEEEEEECCC
43.0823644510
285PhosphorylationVDRDGVLSRVELRDM
ECCCCCCCHHHHHHH
31.6924719451
295UbiquitinationELRDMVVALLEVWKD
HHHHHHHHHHHHHHH
8.6027667366
298UbiquitinationDMVVALLEVWKDNRT
HHHHHHHHHHHHCCC
47.3727667366
410PhosphorylationWWQQWKEYVKYDANP
HHHHHHHHHCCCCCC
9.87-
431PhosphorylationSVLNGGKYSFGTAAH
HHCCCCCEECCCCCC
16.7127174698
432PhosphorylationVLNGGKYSFGTAAHP
HCCCCCEECCCCCCC
22.2327174698
435PhosphorylationGGKYSFGTAAHPMEQ
CCCEECCCCCCCHHH
20.7527174698
449PhosphorylationQVEDRIGSSLSYVNT
HHHHHHHCCCCCCCC
26.2428796482
450PhosphorylationVEDRIGSSLSYVNTT
HHHHHHCCCCCCCCC
19.0028796482
452PhosphorylationDRIGSSLSYVNTTEE
HHHHCCCCCCCCCCH
29.0528796482
453PhosphorylationRIGSSLSYVNTTEEK
HHHCCCCCCCCCCHH
11.7428796482
456PhosphorylationSSLSYVNTTEEKFSD
CCCCCCCCCCHHHCC
26.0728796482
457PhosphorylationSLSYVNTTEEKFSDN
CCCCCCCCCHHHCCC
36.6229978859
539PhosphorylationQEPVKATSLTLEGGR
CCCEECEEEEEECCE
24.9815302935
540UbiquitinationEPVKATSLTLEGGRL
CCEECEEEEEECCEE
5.7127667366
543UbiquitinationKATSLTLEGGRLKRT
ECEEEEEECCEECCC
55.1327667366
559PhosphorylationQLIHGRDYEMVPEPV
CEECCCCCCCCCHHH
12.4527642862
576UbiquitinationALYHWYGANLALPRP
HHHHHHCCCCCCCCC
7.6827667366
579UbiquitinationHWYGANLALPRPVIK
HHHCCCCCCCCCCCC
18.4827667366
583UbiquitinationANLALPRPVIKNSKT
CCCCCCCCCCCCCCC
30.1927667366
586UbiquitinationALPRPVIKNSKTDIP
CCCCCCCCCCCCCCH
56.2427667366
589UbiquitinationRPVIKNSKTDIPELE
CCCCCCCCCCCHHHH
60.6621906983
602UbiquitinationLELFPRYLLFLRQQP
HHHHHHHHHHHHCCC
2.6227667366
605UbiquitinationFPRYLLFLRQQPATR
HHHHHHHHHCCCCCC
4.9527667366
627PhosphorylationVNMGNVPSPNAPLKR
EECCCCCCCCCCHHH
26.8921712546
635UbiquitinationPNAPLKRVLAYTGCF
CCCCHHHHHHHHCHH
3.2421890473
674UbiquitinationRLWLYNSENYLTLLD
HHEEECCCCCEEEEC
46.3821890473
676PhosphorylationWLYNSENYLTLLDDE
EEECCCCCEEEECCC
9.3027642862
705AcetylationLVIEVRNKDMSWPEE
EEEEEECCCCCCCHH
44.2223236377
764PhosphorylationPLTQYFISGRHLYEL
CCEEEEECCCCEEEC
21.6324719451
806UbiquitinationQKNVAPLKLRWTIAK
CCCCCCEEHHHHHHH
34.6429967540
847UbiquitinationDLNRVHEKPYVELKD
HHHHHHCCCCEEEEC
27.1129967540
849PhosphorylationNRVHEKPYVELKDSD
HHHHCCCCEEEECCC
20.0227642862
877PhosphorylationNHLRRNRSIVVDLFH
HHHHHCCEEEEECCC
24.2324247654
905UbiquitinationHISVRFDPFNFLSLP
CEEEEECCCCCCCCC
24.3021890473
919UbiquitinationPLPMDSYMHLEITVI
CCCCCCCEEEEEEEE
3.1721890473
936PhosphorylationDGTTPVRYGLRLNMD
CCCCCCEEEEECCCC
22.2718083107
946PhosphorylationRLNMDEKYTGLKKQL
ECCCCHHHHCHHHHH
12.1823403867
947PhosphorylationLNMDEKYTGLKKQLS
CCCCHHHHCHHHHHH
47.2924719451
948UbiquitinationNMDEKYTGLKKQLSD
CCCHHHHCHHHHHHH
32.2021890473
951UbiquitinationEKYTGLKKQLSDLCG
HHHHCHHHHHHHHCC
62.6121890473
955UbiquitinationGLKKQLSDLCGLNSE
CHHHHHHHHCCCCHH
55.3521890473
962UbiquitinationDLCGLNSEQILLAEV
HHCCCCHHHEEEEEC
40.3321890473
965UbiquitinationGLNSEQILLAEVHGS
CCCHHHEEEEECCCC
3.5621890473
967UbiquitinationNSEQILLAEVHGSNI
CHHHEEEEECCCCCC
17.2021890473
981UbiquitinationIKNFPQDNQKVRLSV
CCCCCCCCCEEEEEE
38.0221890473
1005PhosphorylationPVPVSPISASSPTQT
CCCCCCCCCCCCCCC
26.0326074081
1007PhosphorylationPVSPISASSPTQTDF
CCCCCCCCCCCCCCC
30.0226074081
1008PhosphorylationVSPISASSPTQTDFS
CCCCCCCCCCCCCCC
31.5126074081
1010PhosphorylationPISASSPTQTDFSSS
CCCCCCCCCCCCCCC
46.1526074081
1012PhosphorylationSASSPTQTDFSSSPS
CCCCCCCCCCCCCCC
41.3026074081
1089PhosphorylationKMMRTELYFLSSQKN
HHHHHHHHHHHCCCC
9.0227642862
1119PhosphorylationHTRKKDLYDAVWIQV
CCCCCHHHHHHEEEH
16.4029507054
1127PhosphorylationDAVWIQVSRLASPLP
HHHEEEHHHCCCCCC
12.76-
1156PhosphorylationMGYQYPFTLRVVQKD
CCCCCCEEEEEEEEC
14.7824719451
1162UbiquitinationFTLRVVQKDGNSCAW
EEEEEEEECCCCCEE
56.87-
1173PhosphorylationSCAWCPWYRFCRGCK
CCEECCHHHHCCCCC
4.4818669648
1216UbiquitinationQTSQERVVDEHESVE
CCCCCHHCCCHHHHH
10.0223503661
1221UbiquitinationRVVDEHESVEQSRRA
HHCCCHHHHHHHHHH
32.6323503661
1243PhosphorylationDSCLRAFTSEEELGE
HHHHHHCCCHHHHCC
33.95-
1255UbiquitinationLGENEMYYCSKCKTH
HCCCCEEEHHHHHCC
6.7423503661
1260UbiquitinationMYYCSKCKTHCLATK
EEEHHHHHCCEEECC
45.0723503661
1323UbiquitinationDPALCQHKPLTPQGD
CHHHHCCCCCCCCCC
18.8229967540
1326PhosphorylationLCQHKPLTPQGDELS
HHCCCCCCCCCCCCC
23.3023401153
1333PhosphorylationTPQGDELSEPRILAR
CCCCCCCCCCHHHHH
43.4330108239
1349PhosphorylationVKKVDAQSSAGEEDV
EEECCCCCCCCCCCE
24.7123401153
1350PhosphorylationKKVDAQSSAGEEDVL
EECCCCCCCCCCCEE
28.3630266825
1359PhosphorylationGEEDVLLSKSPSSLS
CCCCEEEECCCCCCC
27.2524144214
1361PhosphorylationEDVLLSKSPSSLSAN
CCEEEECCCCCCCCC
27.0023927012
1363PhosphorylationVLLSKSPSSLSANII
EEEECCCCCCCCCEE
51.5123927012
1364PhosphorylationLLSKSPSSLSANIIS
EEECCCCCCCCCEEE
29.7223927012
1366PhosphorylationSKSPSSLSANIISSP
ECCCCCCCCCEEECC
22.6323927012
1371PhosphorylationSLSANIISSPKGSPS
CCCCCEEECCCCCCC
36.4730266825
1372PhosphorylationLSANIISSPKGSPSS
CCCCEEECCCCCCCC
21.8823927012
1376PhosphorylationIISSPKGSPSSSRKS
EEECCCCCCCCCCCC
27.9523401153
1378PhosphorylationSSPKGSPSSSRKSGT
ECCCCCCCCCCCCCC
42.5123927012
1379PhosphorylationSPKGSPSSSRKSGTS
CCCCCCCCCCCCCCC
37.2323927012
1380PhosphorylationPKGSPSSSRKSGTSC
CCCCCCCCCCCCCCC
48.3323927012
1383PhosphorylationSPSSSRKSGTSCPSS
CCCCCCCCCCCCCCC
46.3128985074
1385PhosphorylationSSSRKSGTSCPSSKN
CCCCCCCCCCCCCCC
33.9630576142
1386PhosphorylationSSRKSGTSCPSSKNS
CCCCCCCCCCCCCCC
27.7925849741
1389PhosphorylationKSGTSCPSSKNSSPN
CCCCCCCCCCCCCCC
59.2723090842
1390PhosphorylationSGTSCPSSKNSSPNS
CCCCCCCCCCCCCCC
22.4623090842
1393PhosphorylationSCPSSKNSSPNSSPR
CCCCCCCCCCCCCCC
51.4125849741
1394PhosphorylationCPSSKNSSPNSSPRT
CCCCCCCCCCCCCCC
37.1825159151
1397PhosphorylationSKNSSPNSSPRTLGR
CCCCCCCCCCCCCCC
45.1422199227
1398PhosphorylationKNSSPNSSPRTLGRS
CCCCCCCCCCCCCCC
25.6625159151
1401PhosphorylationSPNSSPRTLGRSKGR
CCCCCCCCCCCCCCC
36.6322199227
1405PhosphorylationSPRTLGRSKGRLRLP
CCCCCCCCCCCCCCC
37.3529514088
1416PhosphorylationLRLPQIGSKNKLSSS
CCCCCCCCCCCCCCC
34.3822617229
1421PhosphorylationIGSKNKLSSSKENLD
CCCCCCCCCCHHHHH
33.8923401153
1422PhosphorylationGSKNKLSSSKENLDA
CCCCCCCCCHHHHHH
56.7330266825
1423PhosphorylationSKNKLSSSKENLDAS
CCCCCCCCHHHHHHH
40.3823401153
1430PhosphorylationSKENLDASKENGAGQ
CHHHHHHHHHCCHHH
39.9223403867
1446PhosphorylationCELADALSRGHVLGG
HHHHHHHHCCCCCCC
37.6326074081
1454PhosphorylationRGHVLGGSQPELVTP
CCCCCCCCCCCCCCC
40.5426074081
1460PhosphorylationGSQPELVTPQDHEVA
CCCCCCCCCCCHHHH
28.0526074081
1486UbiquitinationCGNGYSNGQLGNHSE
CCCCCCCCCCCCCCC
20.3923503661
1491UbiquitinationSNGQLGNHSEEDSTD
CCCCCCCCCCCCCCC
34.4923503661
1500UbiquitinationEEDSTDDQREDTRIK
CCCCCCCCCHHHCCC
54.1723503661
1505UbiquitinationDDQREDTRIKPIYNL
CCCCHHHCCCHHHEE
47.4523503661
1529UbiquitinationLGGGHYVTYAKNPNC
CCCCCEEEEECCCCC
15.5923503661
1532UbiquitinationGHYVTYAKNPNCKWY
CCEEEEECCCCCEEE
63.6223503661
1534UbiquitinationYVTYAKNPNCKWYCY
EEEEECCCCCEEEEE
47.0623503661
1536UbiquitinationTYAKNPNCKWYCYND
EEECCCCCEEEEECC
3.2723503661
1537UbiquitinationYAKNPNCKWYCYNDS
EECCCCCEEEEECCC
48.082190698
1539PhosphorylationKNPNCKWYCYNDSSC
CCCCCEEEEECCCCC
3.16-
1541PhosphorylationPNCKWYCYNDSSCKE
CCCEEEEECCCCCCC
13.30-
1541UbiquitinationPNCKWYCYNDSSCKE
CCCEEEEECCCCCCC
13.3023503661
1543UbiquitinationCKWYCYNDSSCKELH
CEEEEECCCCCCCCC
18.5623503661
1544PhosphorylationKWYCYNDSSCKELHP
EEEEECCCCCCCCCC
33.72-
1545PhosphorylationWYCYNDSSCKELHPD
EEEECCCCCCCCCCC
31.88-
1546UbiquitinationYCYNDSSCKELHPDE
EEECCCCCCCCCCCC
4.6123503661
1548UbiquitinationYNDSSCKELHPDEID
ECCCCCCCCCCCCCC
57.5523503661
1551UbiquitinationSSCKELHPDEIDTDS
CCCCCCCCCCCCCCC
54.2623503661
1553UbiquitinationCKELHPDEIDTDSAY
CCCCCCCCCCCCCEE
47.4123503661
1562UbiquitinationDTDSAYILFYEQQGI
CCCCEEEEEEEECCC
2.1423503661
1567UbiquitinationYILFYEQQGIDYAQF
EEEEEEECCCCHHEE
38.5823503661
1586PhosphorylationDGKKMADTSSMDEDF
CCCCCCCCCCCCCCH
17.1123927012
1587PhosphorylationGKKMADTSSMDEDFE
CCCCCCCCCCCCCHH
24.9823927012
1588PhosphorylationKKMADTSSMDEDFES
CCCCCCCCCCCCHHH
32.1425159151
1595PhosphorylationSMDEDFESDYKKYCV
CCCCCHHHHHHHHEE
46.3523403867
1597PhosphorylationDEDFESDYKKYCVLQ
CCCHHHHHHHHEECC
20.7523403867
1600PhosphorylationFESDYKKYCVLQ---
HHHHHHHHEECC---
5.4424719451
1601FarnesylationESDYKKYCVLQ----
HHHHHHHEECC----
3.19-
1601MethylationESDYKKYCVLQ----
HHHHHHHEECC----
3.19-

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 UBP32_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP32_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 UBP32_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK1_HUMANCDK1physical
19615732
SYFA_HUMANFARSAphysical
19615732
K2C8_HUMANKRT8physical
19615732
K1C18_HUMANKRT18physical
19615732
K1C19_HUMANKRT19physical
19615732
ABCD3_HUMANABCD3physical
19615732
1433B_HUMANYWHABphysical
19615732
TBA1A_HUMANTUBA1Aphysical
19615732
SMC1A_HUMANSMC1Aphysical
19615732
UBP6_HUMANUSP6physical
19615732
PCH2_HUMANTRIP13physical
19615732
ERP44_HUMANERP44physical
19615732
UBXN1_HUMANUBXN1physical
19615732
RM39_HUMANMRPL39physical
19615732
VPS35_HUMANVPS35physical
19615732
LRC47_HUMANLRRC47physical
19615732
HOIL1_HUMANRBCK1physical
23105109
TRI46_HUMANTRIM46physical
23105109
R144A_HUMANRNF144Aphysical
23105109
TRI74_HUMANTRIM74physical
23105109
NDKM_HUMANNME4physical
28514442
HS12A_HUMANHSPA12Aphysical
28514442

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 UBP32_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-1372, AND MASSSPECTROMETRY.
"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-1372 AND SER-1376, 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-1361 AND SER-1372, 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 TYR-1173, AND MASSSPECTROMETRY.

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