dbPTM

UBP37_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP37_HUMAN
UniProt AC	Q86T82
Protein Name	Ubiquitin carboxyl-terminal hydrolase 37
Gene Name	USP37
Organism	Homo sapiens (Human).
Sequence Length	979
Subcellular Localization
Protein Description	Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). [PubMed: 21596315 Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1]
Protein Sequence	MSPLKIHGPIRIRSMQTGITKWKEGSFEIVEKENKVSLVVHYNTGGIPRIFQLSHNIKNVVLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLPAAMKPSQGSGSFGAILGSRTSQKETSRQLSYSDNQASAKRGSLETKDDIPFRKVLGNPGRGSIKTVAGSGIARTIPSLTSTSTPLRSGLLENRTEKRKRMISTGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRSLGFLPQPVPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVSGEENSPDISATRAYTCPVITNLEFEVQHSIICKACGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFTLGWSAHMAISRPLKASQMVNSCITSPSTPSKKFTFKSKSSLALCLDSDSEDELKRSVALSQRLCEMLGNEQQQEDLEKDSKLCPIEPDKSELENSGFDRMSEEELLAAVLEISKRDASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFVDALGSDEDSGNEDVFDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKNSQSLSTEVGKTTRQAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSPLKIHGP ------CCCCCCCCC	38.65	23186163
68	Acetylation	VLRPSGAKQSRLMLT EECCCCCCCCEEEEE	52.94	25953088
68	Ubiquitination	VLRPSGAKQSRLMLT EECCCCCCCCEEEEE	52.94	-
75	Phosphorylation	KQSRLMLTLQDNSFL CCCEEEEEECCCCCE	14.38	24043423
80	Phosphorylation	MLTLQDNSFLSIDKV EEEECCCCCEEEECC	35.53	24043423
83	Phosphorylation	LQDNSFLSIDKVPSK ECCCCCEEEECCCCC	27.08	28450419
114	Phosphorylation	LPAAMKPSQGSGSFG CCCCCCCCCCCCCHH	41.47	-
138	Phosphorylation	KETSRQLSYSDNQAS CHHHCCCCCCCCHHH	17.79	28450419
139	Phosphorylation	ETSRQLSYSDNQASA HHHCCCCCCCCHHHH	28.74	22210691
140	Phosphorylation	TSRQLSYSDNQASAK HHCCCCCCCCHHHHH	27.06	22210691
147	Ubiquitination	SDNQASAKRGSLETK CCCHHHHHCCCCCCC	55.59	-
150	Phosphorylation	QASAKRGSLETKDDI HHHHHCCCCCCCCCC	27.37	24719451
161	Ubiquitination	KDDIPFRKVLGNPGR CCCCCHHHHCCCCCC	42.04	-
168	Methylation	KVLGNPGRGSIKTVA HHCCCCCCCCCEEEC	36.62	82954869
170	Phosphorylation	LGNPGRGSIKTVAGS CCCCCCCCCEEECCC	21.39	28450419
172	Acetylation	NPGRGSIKTVAGSGI CCCCCCCEEECCCCH	38.35	25953088
187	Phosphorylation	ARTIPSLTSTSTPLR HHCCCCCCCCCCCCC	34.01	24719451
188	Phosphorylation	RTIPSLTSTSTPLRS HCCCCCCCCCCCCCC	26.17	29978859
189	Phosphorylation	TIPSLTSTSTPLRSG CCCCCCCCCCCCCCC	31.24	29978859
190	Phosphorylation	IPSLTSTSTPLRSGL CCCCCCCCCCCCCCC	28.00	24719451
191	Phosphorylation	PSLTSTSTPLRSGLL CCCCCCCCCCCCCCC	26.82	25159151
210	Phosphorylation	EKRKRMISTGSELNE HHHHHHHHCCCCCCC	19.85	29255136
211	Phosphorylation	KRKRMISTGSELNED HHHHHHHCCCCCCCC	33.53	27273156
213	Phosphorylation	KRMISTGSELNEDYP HHHHHCCCCCCCCCC	38.71	29255136
219	Phosphorylation	GSELNEDYPKENDSS CCCCCCCCCCCCCCC	15.27	23186163
227	Phosphorylation	PKENDSSSNNKAMTD CCCCCCCCCCCCCCC	48.66	-
233	Phosphorylation	SSNNKAMTDPSRKYL CCCCCCCCCHHHHHH	50.01	29116813
236	Phosphorylation	NKAMTDPSRKYLTSS CCCCCCHHHHHHCCH	44.19	29116813
241	Phosphorylation	DPSRKYLTSSREKQL CHHHHHHCCHHHHHH	22.90	29116813
242	Phosphorylation	PSRKYLTSSREKQLS HHHHHHCCHHHHHHC	25.46	29116813
243	Phosphorylation	SRKYLTSSREKQLSL HHHHHCCHHHHHHCH	38.94	29116813
246	Ubiquitination	YLTSSREKQLSLKQS HHCCHHHHHHCHHHC	56.26	-
251	Ubiquitination	REKQLSLKQSEENRT HHHHHCHHHCHHHCC	48.69	-
266	Phosphorylation	SGLLPLQSSSFYGSR CCCEECCCCCCCCCC	35.32	28555341
267	Phosphorylation	GLLPLQSSSFYGSRA CCEECCCCCCCCCCC	16.11	23186163
268	Phosphorylation	LLPLQSSSFYGSRAG CEECCCCCCCCCCCC	27.95	23917254
277	Ubiquitination	YGSRAGSKEHSSGGT CCCCCCCCCCCCCCC	59.53	-
288	Methylation	SGGTNLDRTNVSSQT CCCCCCCCCCCCCCC	31.22	115919621
293	Phosphorylation	LDRTNVSSQTPSAKR CCCCCCCCCCCCCCH	33.52	29396449
295	Phosphorylation	RTNVSSQTPSAKRSL CCCCCCCCCCCCHHC	22.59	29396449
299	Ubiquitination	SSQTPSAKRSLGFLP CCCCCCCCHHCCCCC	47.02	-
301	Phosphorylation	QTPSAKRSLGFLPQP CCCCCCHHCCCCCCC	31.94	25159151
312	Phosphorylation	LPQPVPLSVKKLRCN CCCCCCCEEEECCCC	26.31	25159151
314	Acetylation	QPVPLSVKKLRCNQD CCCCCEEEECCCCCC	42.59	25953088
315	Ubiquitination	PVPLSVKKLRCNQDY CCCCEEEECCCCCCC	38.72	-
327	Ubiquitination	QDYTGWNKPRVPLSS CCCCCCCCCCCCCCH	27.91	-
378	Ubiquitination	KQGIPWKKIPLNALI HCCCCHHCCCHHHHH	45.76	-
411	Ubiquitination	KDLLKKVKNAISATA HHHHHHHHHHHHHHH	49.93	-
415	Phosphorylation	KKVKNAISATAERFS HHHHHHHHHHHHHHC	19.70	-
417	Phosphorylation	VKNAISATAERFSGY HHHHHHHHHHHHCHH	23.43	-
422	Phosphorylation	SATAERFSGYMQNDA HHHHHHHCHHCCCHH	34.92	29759185
424	Phosphorylation	TAERFSGYMQNDAHE HHHHHCHHCCCHHHH	8.37	29759185
446	Acetylation	QLKEDMEKLNKTWKT HHHHHHHHHHHHCCC	51.20	90625
452	Sumoylation	EKLNKTWKTEPVSGE HHHHHHCCCCCCCCC	48.52	-
452	Sumoylation	EKLNKTWKTEPVSGE HHHHHHCCCCCCCCC	48.52	-
452	Ubiquitination	EKLNKTWKTEPVSGE HHHHHHCCCCCCCCC	48.52	21906983
453	Phosphorylation	KLNKTWKTEPVSGEE HHHHHCCCCCCCCCC	36.76	24114839
457	Phosphorylation	TWKTEPVSGEENSPD HCCCCCCCCCCCCCC	51.72	28450419
462	Phosphorylation	PVSGEENSPDISATR CCCCCCCCCCCCCCE	27.51	28450419
466	Phosphorylation	EENSPDISATRAYTC CCCCCCCCCCEEEEC	30.85	28450419
468	Phosphorylation	NSPDISATRAYTCPV CCCCCCCCEEEECCE	14.72	28450419
498	Ubiquitination	ACGEIIPKREQFNDL HCCCCCCCHHHHCCC	59.15	-
540	Ubiquitination	ELEYSCEKCGGKCAL HHHHHHHHHCCEEHH	42.37	-
544	Ubiquitination	SCEKCGGKCALVRHK HHHHHCCEEHHHHHH	11.13	-
573	Phosphorylation	YSFNVALSLNNKIGQ CEEEEEEECCCCCCC	21.22	25159151
619	Phosphorylation	ISRPLKASQMVNSCI HCCCCCHHHHHHHHC	19.74	26074081
624	Phosphorylation	KASQMVNSCITSPST CHHHHHHHHCCCCCC	8.76	30576142
627	Phosphorylation	QMVNSCITSPSTPSK HHHHHHCCCCCCCCC	38.62	28450419
628	Phosphorylation	MVNSCITSPSTPSKK HHHHHCCCCCCCCCC	9.28	25159151
630	Phosphorylation	NSCITSPSTPSKKFT HHHCCCCCCCCCCEE	53.36	28450419
631	Phosphorylation	SCITSPSTPSKKFTF HHCCCCCCCCCCEEE	34.66	25159151
633	Phosphorylation	ITSPSTPSKKFTFKS CCCCCCCCCCEEECC	48.87	28450419
635	Ubiquitination	SPSTPSKKFTFKSKS CCCCCCCCEEECCCC	54.71	-
642	Phosphorylation	KFTFKSKSSLALCLD CEEECCCCEEEEEEC	37.36	23663014
643	Phosphorylation	FTFKSKSSLALCLDS EEECCCCEEEEEECC	22.77	23663014
650	Phosphorylation	SLALCLDSDSEDELK EEEEEECCCCHHHHH	30.04	25159151
652	Phosphorylation	ALCLDSDSEDELKRS EEEECCCCHHHHHHH	51.39	25159151
681	Ubiquitination	QQQEDLEKDSKLCPI HHHHHHHHHCCCCCC	74.69	-
683	Phosphorylation	QEDLEKDSKLCPIEP HHHHHHHCCCCCCCC	38.30	-
684	Ubiquitination	EDLEKDSKLCPIEPD HHHHHHCCCCCCCCC	65.33	-
692	Ubiquitination	LCPIEPDKSELENSG CCCCCCCHHHHHCCC	57.45	-
693	Phosphorylation	CPIEPDKSELENSGF CCCCCCHHHHHCCCC	55.59	29978859
698	Phosphorylation	DKSELENSGFDRMSE CHHHHHCCCCCCCCH	31.31	25159151
716	Phosphorylation	LAAVLEISKRDASPS HHHHHHHHCCCCCCC	16.56	27690223
717	Ubiquitination	AAVLEISKRDASPSL HHHHHHHCCCCCCCC	61.02	-
733	Phosphorylation	HEDDDKPTSSPDTGF CCCCCCCCCCCCCCC	47.80	28348404
734	Phosphorylation	EDDDKPTSSPDTGFA CCCCCCCCCCCCCCC	48.69	28348404
735	Phosphorylation	DDDKPTSSPDTGFAE CCCCCCCCCCCCCCH	29.31	30576142
738	Phosphorylation	KPTSSPDTGFAEDDI CCCCCCCCCCCHHHH	37.27	30576142
757	Phosphorylation	ENPDTMETEKPKTIT CCCCCCCCCCCCCCC	38.19	30576142
770	Phosphorylation	ITELDPASFTEITKD CCCCCHHHHCHHCCC	37.78	10997877
772	Phosphorylation	ELDPASFTEITKDCD CCCHHHHCHHCCCCC	24.79	22199227
775	Phosphorylation	PASFTEITKDCDENK HHHHCHHCCCCCCCC	18.01	26074081
776	Ubiquitination	ASFTEITKDCDENKE HHHCHHCCCCCCCCC	63.12	-
782	Ubiquitination	TKDCDENKENKTPEG CCCCCCCCCCCCCCC	61.69	PubMed
785	Ubiquitination	CDENKENKTPEGSQG CCCCCCCCCCCCCHH	67.55	-
786	Phosphorylation	DENKENKTPEGSQGE CCCCCCCCCCCCHHH	37.85	28348404
790	Phosphorylation	ENKTPEGSQGEVDWL CCCCCCCCHHHHHHH	33.09	28348404
915	Ubiquitination	ISDVYDIKKQAWFTY CCCCEECHHCEEEEE	35.62	-
916	Ubiquitination	SDVYDIKKQAWFTYN CCCEECHHCEEEEEC	45.65	-
962	Ubiquitination	DELLETEKNSQSLST HHHHHHHHHCCCCCH	70.13	21906983
973	Ubiquitination	SLSTEVGKTTRQAL- CCCHHCCHHHHHHC-	52.47	21906983

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
628	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:23027877

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
628	S	Phosphorylation	21596315
Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity.
628	S	ubiquitylation	21596315
Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity.

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 UBP37_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ALBU_HUMAN	ALB	physical	19615732
KRT84_HUMAN	KRT84	physical	19615732
FBW1B_HUMAN	FBXW11	physical	19615732
FZR1_HUMAN	FZR1	physical	21596315
APC5_HUMAN	ANAPC5	physical	21596315
APC7_HUMAN	ANAPC7	physical	21596315
CDC27_HUMAN	CDC27	physical	21596315
CDC20_HUMAN	CDC20	physical	21596315
CCNA2_HUMAN	CCNA2	physical	21596315
CCNB1_HUMAN	CCNB1	physical	21596315
UBP37_HUMAN	USP37	physical	21596315
CUL1_HUMAN	CUL1	physical	23027877
SKP1_HUMAN	SKP1	physical	23027877
FBW1A_HUMAN	BTRC	physical	23027877
PLK1_HUMAN	PLK1	physical	23027877
UBC_HUMAN	UBC	physical	23287719
UBC_HUMAN	UBC	physical	24324262
MYC_HUMAN	MYC	physical	25284584
1433G_HUMAN	YWHAG	physical	26427597
SMC3_HUMAN	SMC3	physical	26299517
SMC1A_HUMAN	SMC1A	physical	26299517
SIN3B_HUMAN	SIN3B	physical	26299517
TBA1A_HUMAN	TUBA1A	physical	26299517
ADNP_HUMAN	ADNP	physical	26299517
STAG2_HUMAN	STAG2	physical	26299517
SK2L2_HUMAN	SKIV2L2	physical	26299517
RAD21_HUMAN	RAD21	physical	26299517
U520_HUMAN	SNRNP200	physical	26299517
FBW1B_HUMAN	FBXW11	physical	26299517
DHX15_HUMAN	DHX15	physical	26299517
CDC27_HUMAN	CDC27	physical	26299517
HDAC2_HUMAN	HDAC2	physical	26299517
HDAC1_HUMAN	HDAC1	physical	26299517
STAG1_HUMAN	STAG1	physical	26299517
U5S1_HUMAN	EFTUD2	physical	26299517
WAPL_HUMAN	WAPAL	physical	26299517
APC4_HUMAN	ANAPC4	physical	26299517
WDHD1_HUMAN	WDHD1	physical	26299517
CHERP_HUMAN	CHERP	physical	26299517
APC1_HUMAN	ANAPC1	physical	26299517
TF3C4_HUMAN	GTF3C4	physical	26299517
SUGP2_HUMAN	SUGP2	physical	26299517
WDR82_HUMAN	WDR82	physical	26299517
HNRPC_HUMAN	HNRNPC	physical	26299517
RIF1_HUMAN	RIF1	physical	26299517
CDC23_HUMAN	CDC23	physical	26299517
CBX3_HUMAN	CBX3	physical	26299517
PRP19_HUMAN	PRPF19	physical	26299517
APC7_HUMAN	ANAPC7	physical	26299517
H2AZ_HUMAN	H2AFZ	physical	26299517
APC5_HUMAN	ANAPC5	physical	26299517
FBW1A_HUMAN	BTRC	physical	26299517
MCM4_HUMAN	MCM4	physical	26299517
CDC16_HUMAN	CDC16	physical	26299517
WRIP1_HUMAN	WRNIP1	physical	26299517
ROA3_HUMAN	HNRNPA3	physical	26299517
PININ_HUMAN	PNN	physical	26299517
CHD8_HUMAN	CHD8	physical	26299517
RFA1_HUMAN	RPA1	physical	26299517
PP1B_HUMAN	PPP1CB	physical	26299517
MCM6_HUMAN	MCM6	physical	26299517
GTF2I_HUMAN	GTF2I	physical	26299517
TAF1_HUMAN	TAF1	physical	26299517
SIR1_HUMAN	SIRT1	physical	26299517
RNPS1_HUMAN	RNPS1	physical	26299517
NIPBL_HUMAN	NIPBL	physical	26299517
FANCJ_HUMAN	BRIP1	physical	26299517
TAF9B_HUMAN	TAF9B	physical	26299517
PRI2_HUMAN	PRIM2	physical	26299517
SKP1_HUMAN	SKP1	physical	26299517
POGZ_HUMAN	POGZ	physical	26299517
SF3B5_HUMAN	SF3B5	physical	26299517
CDK2_HUMAN	CDK2	physical	26299517
PAXB1_HUMAN	PAXBP1	physical	26299517
TAF6_HUMAN	TAF6	physical	26299517
TASOR_HUMAN	FAM208A	physical	26299517
TRIM4_HUMAN	TRIM4	physical	26299517
MINT_HUMAN	SPEN	physical	26299517
PHF3_HUMAN	PHF3	physical	26299517
RFA3_HUMAN	RPA3	physical	26299517
APC15_HUMAN	ANAPC15	physical	26299517
APC16_HUMAN	ANAPC16	physical	26299517
SAP18_HUMAN	SAP18	physical	26299517
INT12_HUMAN	INTS12	physical	26299517
TF3C3_HUMAN	GTF3C3	physical	26299517
EXOS9_HUMAN	EXOSC9	physical	26299517
ECH1_HUMAN	ECH1	physical	26299517
RPAB3_HUMAN	POLR2H	physical	26299517
DPY30_HUMAN	DPY30	physical	26299517
NH2L1_HUMAN	NHP2L1	physical	26299517
IPO9_HUMAN	IPO9	physical	26299517
RFA2_HUMAN	RPA2	physical	26299517
MCM10_HUMAN	MCM10	physical	26299517
SNR40_HUMAN	SNRNP40	physical	26299517
TIF1A_HUMAN	TRIM24	physical	26299517
Z280C_HUMAN	ZNF280C	physical	26299517
ZN326_HUMAN	ZNF326	physical	26299517
APC13_HUMAN	ANAPC13	physical	26299517
BRCA1_HUMAN	BRCA1	physical	26299517
MS18A_HUMAN	MIS18A	physical	26299517
PHF2_HUMAN	PHF2	physical	26299517
CDC26_HUMAN	CDC26	physical	26299517
CDT1_HUMAN	CDT1	physical	27296872
UBC_HUMAN	UBC	physical	28327663

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 UBP37_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) andpromote S phase entry."; Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.; Mol. Cell 42:511-523(2011). Cited for: FUNCTION, UBIQUITINATION, PHOSPHORYLATION AT SER-628 BY CDK2, DOMAINKEN BOX 3, DEVELOPMENTAL STAGE, INDUCTION, INTERACTION WITH FZR1, ANDMUTAGENESIS OF 32-LYS--ASN-34; 71-ARG-LEU-74; 96-ARG-LEU-99;160-ARG-LEU-163; 221-LYS--ASN-223; CYS-350; 782-LYS--ASN-784 ANDSER-628.	21596315 [Abstract]
"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-650, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-650 AND SER-652, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-652, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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-650 AND SER-652, ANDMASS SPECTROMETRY.	17081983 [Abstract]

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