dbPTM

KI13B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KI13B_HUMAN
UniProt AC	Q9NQT8
Protein Name	Kinesin-like protein KIF13B
Gene Name	KIF13B
Organism	Homo sapiens (Human).
Sequence Length	1826
Subcellular Localization	Cytoplasm, cytoskeleton . Cell projection, axon . accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites.
Protein Description	Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes..
Protein Sequence	MGDSKVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNPVNTNLSKGDARGQPKVFAYDHCFWSMDESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEDQDPSMKNENSSEQLDVDGDSSSEVSSEVNFNYEYAQMEVTMKALGSNDPMQSILNSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPEKQNCRSMDRFSFHSPSAQQRLRQWAEEREATLNNSLMRLREQIVKANLLVREANYIAEELDKRTEYKVTLQIPASSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLDNRLLDMRDLYQEWKECEEDNPVIRSYFKRADPFYDEQENHSLIGVANVFLESLFYDVKLQYAVPIINQKGEVAGRLHVEVMRLSGDVGERIAGGDEVAEVSFEKETQENKLVCMVKILQATGLPQHLSHFVFCKYSFWDQQEPVIVAPEVDTSSSSVSKEPHCMVVFDHCNEFSVNITEDFIEHLSEGALAIEVYGHKINDPRKNPALWDLGIIQAKTRSLRDRWSEVTRKLEFWVQILEQNENGEYCPVEVISAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRAPRTHETFHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKRDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMETHIPVIFLDLNADDFSSQDNLDDPEAGGWDATLTGEEEEEFFELQIVKQHDGEVKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQLSHPADMQLVLRKRICVNVHGRQGFAQSLLKKMSHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENPASADSEAYIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLSRRSISSPNVNRLSGSRQDLIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSWAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21 (in isoform 2)	Phosphorylation	-	31.53	25627689
42	Phosphorylation	VILNPVNTNLSKGDA EEECCCCCCCCCCCC	37.46	21406692
45	Phosphorylation	NPVNTNLSKGDARGQ CCCCCCCCCCCCCCC	36.34	21406692
46	Ubiquitination	PVNTNLSKGDARGQP CCCCCCCCCCCCCCC	65.07	32015554
58	Phosphorylation	GQPKVFAYDHCFWSM CCCCEEEEEEEECCC	5.98	29978859
64	Phosphorylation	AYDHCFWSMDESVKE EEEEEECCCCHHHHH	8.98	29978859
68	Phosphorylation	CFWSMDESVKEKYAG EECCCCHHHHHHHCC	33.94	29978859
107	Phosphorylation	FAYGQTGSGKSYTMM EEEECCCCCCCEEEC	46.57	-
128	Phosphorylation	GLIPRLCSGLFERTQ CHHHHHHHHHHHHCC	43.02	-
134	Phosphorylation	CSGLFERTQKEENEE HHHHHHHCCCHHCHH	36.47	-
154	Phosphorylation	EVSYMEIYNEKVRDL EEEEHHHHCHHHHHH	12.17	27762562
177	Phosphorylation	TLKVREHSVLGPYVD CEEEEECCCHHHHCC	17.81	22210691
193	Phosphorylation	LSKLAVTSYKDIESL HHHEEECCHHHHHHH	26.01	22210691
195	Ubiquitination	KLAVTSYKDIESLMS HEEECCHHHHHHHHH	52.58	29967540
199	Phosphorylation	TSYKDIESLMSEGNK CCHHHHHHHHHCCCH	29.70	20068231
202	Phosphorylation	KDIESLMSEGNKSRT HHHHHHHHCCCHHCC	47.87	22210691
207	Phosphorylation	LMSEGNKSRTVAATN HHHCCCHHCCEEEEC	36.86	20068231
209	Phosphorylation	SEGNKSRTVAATNMN HCCCHHCCEEEECCC	22.91	20068231
213	Phosphorylation	KSRTVAATNMNEESS HHCCEEEECCCHHHH	25.84	20068231
219	Phosphorylation	ATNMNEESSRSHAVF EECCCHHHHHCCEEE	25.52	20068231
220	Phosphorylation	TNMNEESSRSHAVFK ECCCHHHHHCCEEEE	40.87	20068231
222	Phosphorylation	MNEESSRSHAVFKIT CCHHHHHCCEEEEEE	20.11	22468782
233	Phosphorylation	FKITLTHTLYDVKSG EEEEEEEEEEECCCC	23.06	22468782
241	Phosphorylation	LYDVKSGTSGEKVGK EEECCCCCCCCEEEE	40.42	22468782
245	Sumoylation	KSGTSGEKVGKLSLV CCCCCCCEEEEEEEE	60.87	-
250	Phosphorylation	GEKVGKLSLVDLAGS CCEEEEEEEEECCCC	29.81	20873877
257	Phosphorylation	SLVDLAGSERATKTG EEEECCCCCCCCCCC	20.50	20873877
261	Phosphorylation	LAGSERATKTGAAGD CCCCCCCCCCCCCCC	35.05	20873877
263	Phosphorylation	GSERATKTGAAGDRL CCCCCCCCCCCCCHH	27.91	20873877
271	Ubiquitination	GAAGDRLKEGSNINK CCCCCHHCCCCCCCH	62.01	-
279	Phosphorylation	EGSNINKSLTTLGLV CCCCCCHHHHHHHHH	26.91	-
281	Phosphorylation	SNINKSLTTLGLVIS CCCCHHHHHHHHHHH	29.29	-
282	Phosphorylation	NINKSLTTLGLVISA CCCHHHHHHHHHHHH	24.91	-
308	Phosphorylation	KFVPYRDSVLTWLLK CCCCCHHHHHHHHHH	15.27	27251275
311	Phosphorylation	PYRDSVLTWLLKDSL CCHHHHHHHHHHCCC	16.35	27251275
324	Phosphorylation	SLGGNSKTAMVATVS CCCCCCCEEEEEEEC	21.58	18510355
329	Phosphorylation	SKTAMVATVSPAADN CCEEEEEEECCCCCC	15.31	25954137
331	Phosphorylation	TAMVATVSPAADNYD EEEEEEECCCCCCCH	12.41	18510355
337	Phosphorylation	VSPAADNYDETLSTL ECCCCCCCHHHHHHH	18.72	25954137
340	Phosphorylation	AADNYDETLSTLRYA CCCCCHHHHHHHHHH	24.10	27251275
342	Phosphorylation	DNYDETLSTLRYADR CCCHHHHHHHHHHHH	32.58	18510355
343	Phosphorylation	NYDETLSTLRYADRA CCHHHHHHHHHHHHH	20.54	25954137
390	Phosphorylation	TKAEAMKSPELKDRL HHHHHHCCHHHHHHH	15.55	24719451
408	Phosphorylation	EKLIQEMTVTWEEKL HHHHHHHHCCHHHHH	17.65	21955146
410	Phosphorylation	LIQEMTVTWEEKLRK HHHHHHCCHHHHHHH	20.28	21955146
431	Phosphorylation	ERQKQLESLGISLQS HHHHHHHHCCCCHHC	40.25	-
435	Phosphorylation	QLESLGISLQSSGIK HHHHCCCCHHCCCCE	20.68	23917254
438	Phosphorylation	SLGISLQSSGIKVGD HCCCCHHCCCCEECC	35.51	23186163
439	Phosphorylation	LGISLQSSGIKVGDD CCCCHHCCCCEECCC	31.41	23186163
506	Phosphorylation	SEGQVMLTPQKNTRT CCCEEEECCCCCCEE	12.94	24719451
513	Phosphorylation	TPQKNTRTFVNGSSV CCCCCCEEEECCCCC	29.87	28270605
518	Phosphorylation	TRTFVNGSSVSSPIQ CEEEECCCCCCCCEE	23.51	28555341
519	Phosphorylation	RTFVNGSSVSSPIQL EEEECCCCCCCCEEE	27.67	28270605
521	Phosphorylation	FVNGSSVSSPIQLHH EECCCCCCCCEEEEC	32.14	28270605
522	Phosphorylation	VNGSSVSSPIQLHHG ECCCCCCCCEEEECC	24.70	28270605
603	Phosphorylation	VTMKALGSNDPMQSI EHHHHHCCCCHHHHH	38.62	29978859
609	Phosphorylation	GSNDPMQSILNSLEQ CCCCHHHHHHHHHHH	23.85	29978859
622	Acetylation	EQQHEEEKRSALERQ HHHHHHHHHHHHHHH	55.74	11922857
622	Ubiquitination	EQQHEEEKRSALERQ HHHHHHHHHHHHHHH	55.74	29967540
633	Phosphorylation	LERQRLMYEHELEQL HHHHHHHHHHHHHHH	20.80	27642862
645	Phosphorylation	EQLRRRLSPEKQNCR HHHHHHHCHHHHHCC	29.24	29496963
645	Ubiquitination	EQLRRRLSPEKQNCR HHHHHHHCHHHHHCC	29.24	24816145
653	Phosphorylation	PEKQNCRSMDRFSFH HHHHHCCCCCCCCCC	27.51	24505115
658	Phosphorylation	CRSMDRFSFHSPSAQ CCCCCCCCCCCHHHH	23.97	29396449
661	Phosphorylation	MDRFSFHSPSAQQRL CCCCCCCCHHHHHHH	20.66	25159151
663	Phosphorylation	RFSFHSPSAQQRLRQ CCCCCCHHHHHHHHH	41.55	21712546
702	Phosphorylation	LLVREANYIAEELDK HHHHHHHHHHHHHHH	14.46	20071362
709	Ubiquitination	YIAEELDKRTEYKVT HHHHHHHHCCEEEEE	74.06	24816145
722	Phosphorylation	VTLQIPASSLDANRK EEEEECHHHCCCCCC	26.53	22617229
723	Phosphorylation	TLQIPASSLDANRKR EEEECHHHCCCCCCC	32.16	22617229
732	Phosphorylation	DANRKRGSLLSEPAI CCCCCCCCCCCCCEE	30.12	23927012
735	Phosphorylation	RKRGSLLSEPAIQVR CCCCCCCCCCEEEEE	46.99	23927012
767	Phosphorylation	LLDMRDLYQEWKECE HHCHHHHHHHHHHHH	14.53	-
858	Phosphorylation	GDEVAEVSFEKETQE CCCEEEEEEECCCCC	24.16	26657352
1053	O-linked_Glycosylation	LMEECILSVGIGCVK HHHHHHHHCCCCEEE	9.82	29351928
1284	Phosphorylation	GRQGFAQSLLKKMSH CCCCHHHHHHHHHHC	32.04	24719451
1293	Phosphorylation	LKKMSHRSSIPGCGV HHHHHCCCCCCCCCE	27.48	28348404
1294	Phosphorylation	KKMSHRSSIPGCGVT HHHHCCCCCCCCCEE	32.53	26657352
1379	Phosphorylation	KGKLSRRSISSPNVN CCCCCCCCCCCCCCH	26.22	30266825
1381	Phosphorylation	KLSRRSISSPNVNRL CCCCCCCCCCCCHHC	40.78	29255136
1382	Phosphorylation	LSRRSISSPNVNRLS CCCCCCCCCCCHHCC	20.87	30266825
1389	Phosphorylation	SPNVNRLSGSRQDLI CCCCHHCCCCCCCCC	31.33	25159151
1391	Phosphorylation	NVNRLSGSRQDLIPS CCHHCCCCCCCCCCH	24.32	23401153
1398	Phosphorylation	SRQDLIPSYSLGSNK CCCCCCCHHCCCCCC	21.99	23403867
1399	Phosphorylation	RQDLIPSYSLGSNKG CCCCCCHHCCCCCCC	11.54	23403867
1400	Phosphorylation	QDLIPSYSLGSNKGR CCCCCHHCCCCCCCC	30.50	23403867
1403	Phosphorylation	IPSYSLGSNKGRWES CCHHCCCCCCCCCCC	40.43	23403867
1410	Phosphorylation	SNKGRWESQQDVSQT CCCCCCCCCCCHHHC	26.61	19664994
1415	Phosphorylation	WESQQDVSQTTVSRG CCCCCCHHHCCCCCC	30.05	23403867
1417	Phosphorylation	SQQDVSQTTVSRGIA CCCCHHHCCCCCCCC	22.97	23403867
1418	Phosphorylation	QQDVSQTTVSRGIAP CCCHHHCCCCCCCCC	14.62	23403867
1420	Phosphorylation	DVSQTTVSRGIAPAP CHHHCCCCCCCCCCC	23.77	23403867
1430	Phosphorylation	IAPAPALSVSPQNNH CCCCCCCCCCCCCCC	23.74	22199227
1432	Phosphorylation	PAPALSVSPQNNHSP CCCCCCCCCCCCCCC	19.86	26055452
1438	Phosphorylation	VSPQNNHSPDPGLSN CCCCCCCCCCCCHHH	32.87	26055452
1444	Phosphorylation	HSPDPGLSNLAASYL CCCCCCHHHHHHHHH	35.39	26657352
1449	Phosphorylation	GLSNLAASYLNPVKS CHHHHHHHHHCCHHH	25.25	23879269
1450	Phosphorylation	LSNLAASYLNPVKSF HHHHHHHHHCCHHHH	13.03	22199227
1481	Phosphorylation	EKRGKRPSPLAHQPV CCCCCCCCCCCCCCC	36.26	29255136
1492	Sulfoxidation	HQPVPRIMVQSASPD CCCCCEEEEECCCCC	2.07	21406390
1495	Phosphorylation	VPRIMVQSASPDIRV CCEEEEECCCCCCEE	21.21	29255136
1497	Phosphorylation	RIMVQSASPDIRVTR EEEEECCCCCCEEEE	28.49	29255136
1503	Phosphorylation	ASPDIRVTRMEEAQP CCCCCEEEEHHHCCC	17.91	22210691
1537	Phosphorylation	DKPAKVPSPPPVIAV CCCCCCCCCCCEEEE	53.69	26657352
1545	Phosphorylation	PPPVIAVTAVTPAPE CCCEEEEEEEECCCC	13.34	26074081
1548	Phosphorylation	VIAVTAVTPAPEAQD EEEEEEEECCCCCCC	15.98	26074081
1559	Phosphorylation	EAQDGPPSPLSEASS CCCCCCCCCCHHCCC	41.42	26657352
1562	Phosphorylation	DGPPSPLSEASSGYF CCCCCCCHHCCCCCC	34.20	26657352
1644	Phosphorylation	LEAPAPGSPFRVRRV CCCCCCCCCCEEEEE	21.58	29255136
1654	Phosphorylation	RVRRVRASELRSFSR EEEEECHHHHHHHHH	26.97	28857561
1658	Phosphorylation	VRASELRSFSRMLAG ECHHHHHHHHHHHCC	39.95	27251275
1660	Phosphorylation	ASELRSFSRMLAGDP HHHHHHHHHHHCCCC	20.30	17081983
1670	Phosphorylation	LAGDPGCSPGAEGNA HCCCCCCCCCCCCCC	32.08	26552605
1689	Phosphorylation	AGGQALASDSEEADE CCCCCCCCCCHHHHC	42.38	30278072
1691	Phosphorylation	GQALASDSEEADEVP CCCCCCCCHHHHCCC	34.54	30278072
1739	Phosphorylation	GVELDLPSGKNDGSI EEEEECCCCCCCCCC	70.47	24719451
1771	Phosphorylation	PSRVRRATGPVRRRS HHHHHHCCCCCCCCC	39.96	17322306
1778	Phosphorylation	TGPVRRRSTGLRLGA CCCCCCCCCCCCCCC	25.64	27273156
1779	Phosphorylation	GPVRRRSTGLRLGAP CCCCCCCCCCCCCCH	38.12	22199227
1782	Methylation	RRRSTGLRLGAPEAR CCCCCCCCCCCHHHH	32.21	115388851
1791	Phosphorylation	GAPEARRSATLSGSA CCHHHHHCCCCCCHH	21.76	28176443
1793	Phosphorylation	PEARRSATLSGSATN HHHHHCCCCCCHHHH	23.78	27273156
1795	Phosphorylation	ARRSATLSGSATNLA HHHCCCCCCHHHHHH	26.75	28176443
1797	Phosphorylation	RSATLSGSATNLASL HCCCCCCHHHHHHHH	28.66	28176443
1799	Phosphorylation	ATLSGSATNLASLTA CCCCCHHHHHHHHHH	32.25	28176443
1803	Phosphorylation	GSATNLASLTAALAK CHHHHHHHHHHHHHH	29.44	28176443
1805	Phosphorylation	ATNLASLTAALAKAD HHHHHHHHHHHHHHH	13.85	23403867
1814	Phosphorylation	ALAKADRSHKNPENR HHHHHHHHCCCCCHH	39.08	23403867
1823	Phosphorylation	KNPENRKSWAS---- CCCCHHHHCCC----	25.33	23312004
1826	Phosphorylation	ENRKSWAS------- CHHHHCCC-------	34.20	23312004

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
1381	S	Phosphorylation	Kinase	MARK2	Q7KZI7	Uniprot
1410	S	Phosphorylation	Kinase	MARK2	Q7KZI7	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1381	S	Phosphorylation	20194617
Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting interaction with 14-3-3 and inhibiting microtubule-dependent accumulation and formation of axons.
1410	S	Phosphorylation	19690332
Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting interaction with 14-3-3 and inhibiting microtubule-dependent accumulation and formation of axons.

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 KI13B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG1_HUMAN	DLG1	physical	10859302
PP1A_HUMAN	PPP1CA	physical	19094064
MARK2_HUMAN	MARK2	physical	20194617
1433B_HUMAN	YWHAB	physical	20194617
CING_HUMAN	CGN	physical	27173435
MAGI1_HUMAN	MAGI1	physical	27173435
TESK2_HUMAN	TESK2	physical	27173435
HDAC4_HUMAN	HDAC4	physical	27173435
SYDE1_HUMAN	SYDE1	physical	27173435
NGAP_HUMAN	RASAL2	physical	27173435
F110B_HUMAN	FAM110B	physical	27173435
KIF1C_HUMAN	KIF1C	physical	27173435
NAV1_HUMAN	NAV1	physical	27173435
F110A_HUMAN	FAM110A	physical	27173435
MFR1L_HUMAN	MTFR1L	physical	27173435
HDAC7_HUMAN	HDAC7	physical	27173435
HDAC5_HUMAN	HDAC5	physical	27173435
KIF1B_HUMAN	KIF1B	physical	27173435
CRTC3_HUMAN	CRTC3	physical	27173435
REEP3_HUMAN	REEP3	physical	27173435
CRTC2_HUMAN	CRTC2	physical	27173435
DCP1A_HUMAN	DCP1A	physical	27173435
DCP1B_HUMAN	DCP1B	physical	27173435
CRTC1_HUMAN	CRTC1	physical	27173435
SH3B4_HUMAN	SH3BP4	physical	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 KI13B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B toregulate axon formation."; Yoshimura Y., Terabayashi T., Miki H.; Mol. Cell. Biol. 30:2206-2219(2010). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESISOF SER-1381 AND SER-1410, AND PHOSPHORYLATION AT SER-1381 ANDSER-1410.	20194617 [Abstract]
"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-1410, AND MASSSPECTROMETRY.	19690332 [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-1379; SER-1382; SER-1432AND SER-1438, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-1644, AND MASSSPECTROMETRY.	18088087 [Abstract]
"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-1410, AND MASSSPECTROMETRY.	17525332 [Abstract]

show

show