RBCC1_HUMAN - dbPTM
RBCC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBCC1_HUMAN
UniProt AC Q8TDY2
Protein Name RB1-inducible coiled-coil protein 1
Gene Name RB1CC1
Organism Homo sapiens (Human).
Sequence Length 1594
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytosol . Preautophagosomal structure . Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formati
Protein Description Involved in autophagy. [PubMed: 21775823 Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1]
Protein Sequence MKLYVFLVNTGTTLTFDTELTVQTVADLKHAIQSKYKIAIQHQVLVVNGGECMAADRRVCTYSAGTDTNPIFLFNKEMILCDRPPAIPKTTFSTENDMEIKVEESLMMPAVFHTVASRTQLALEMYEVAKKLCSFCEGLVHDEHLQHQGWAAIMANLEDCSNSYQKLLFKFESIYSNYLQSIEDIKLKLTHLGTAVSVMAKIPLLECLTRHSYRECLGRLDSLPEHEDSEKAEMKRSTELVLSPDMPRTTNESLLTSFPKSVEHVSPDTADAESGKEIRESCQSTVHQQDETTIDTKDGDLPFFNVSLLDWINVQDRPNDVESLVRKCFDSMSRLDPRIIRPFIAECRQTIAKLDNQNMKAIKGLEDRLYALDQMIASCGRLVNEQKELAQGFLANQKRAENLKDASVLPDLCLSHANQLMIMLQNHRKLLDIKQKCTTAKQELANNLHVRLKWCCFVMLHADQDGEKLQALLRLVIELLERVKIVEALSTVPQMYCLAVVEVVRRKMFIKHYREWAGALVKDGKRLYEAEKSKRESFGKLFRKSFLRNRLFRGLDSWPPSFCTQKPRKFDCELPDISLKDLQFLQSFCPSEVQPFLRVPLLCDFEPLHQHVLALHNLVKAAQSLDEMSQTITDLLSEQKASVSQTSPQSASSPRMESTAGITTTTSPRTPPPLTVQDPLCPAVCPLEELSPDSIDAHTFDFETIPHPNIEQTIHQVSLDLDSLAESPESDFMSAVNEFVIEENLSSPNPISDPQSPEMMVESLYSSVINAIDSRRMQDTNVCGKEDFGDHTSLNVQLERCRVVAQDSHFSIQTIKEDLCHFRTFVQKEQCDFSNSLKCTAVEIRNIIEKVKCSLEITLKEKHQKELLSLKNEYEGKLDGLIKETEENENKIKKLKGELVCLEEVLQNKDNEFALVKHEKEAVICLQNEKDQKLLEMENIMHSQNCEIKELKQSREIVLEDLKKLHVENDEKLQLLRAELQSLEQSHLKELEDTLQVRHIQEFEKVMTDHRVSLEELKKENQQIINQIQESHAEIIQEKEKQLQELKLKVSDLSDTRCKLEVELALKEAETDEIKILLEESRAQQKETLKSLLEQETENLRTEISKLNQKIQDNNENYQVGLAELRTLMTIEKDQCISELISRHEEESNILKAELNKVTSLHNQAFEIEKNLKEQIIELQSKLDSELSALERQKDEKITQQEEKYEAIIQNLEKDRQKLVSSQEQDREQLIQKLNCEKDEAIQTALKEFKLEREVVEKELLEKVKHLENQIAKSPAIDSTRGDSSSLVAELQEKLQEEKAKFLEQLEEQEKRKNEEMQNVRTSLIAEQQTNFNTVLTREKMRKENIINDLSDKLKSTMQQQERDKDLIESLSEDRARLLEEKKKLEEEVSKLRSSSFVPSPYVATAPELYGACAPELPGESDRSAVETADEGRVDSAMETSMMSVQENIHMLSEEKQRIMLLERTLQLKEEENKRLNQRLMSQSMSSVSSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV
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
35UbiquitinationLKHAIQSKYKIAIQH
HHHHHHHCCCEEEEC
33.9029967540
61PhosphorylationAADRRVCTYSAGTDT
ECCCEEEEEECCCCC
20.0429759185
62PhosphorylationADRRVCTYSAGTDTN
CCCEEEEEECCCCCC
7.4429759185
63PhosphorylationDRRVCTYSAGTDTNP
CCEEEEEECCCCCCC
11.3229759185
68PhosphorylationTYSAGTDTNPIFLFN
EEECCCCCCCEEEEC
42.6129759185
105PhosphorylationMEIKVEESLMMPAVF
CEEEHHHHHCCCHHH
14.20-
134PhosphorylationEVAKKLCSFCEGLVH
HHHHHHHHHHHCCCC
43.28-
209PhosphorylationIPLLECLTRHSYREC
CHHHHHHHHCCHHHH
37.6926434776
210DimethylationPLLECLTRHSYRECL
HHHHHHHHCCHHHHH
12.10-
210MethylationPLLECLTRHSYRECL
HHHHHHHHCCHHHHH
12.10115372781
212PhosphorylationLECLTRHSYRECLGR
HHHHHHCCHHHHHCC
23.6917081983
213PhosphorylationECLTRHSYRECLGRL
HHHHHCCHHHHHCCH
12.3326434776
214DimethylationCLTRHSYRECLGRLD
HHHHCCHHHHHCCHH
31.03-
214MethylationCLTRHSYRECLGRLD
HHHHCCHHHHHCCHH
31.03115372787
222PhosphorylationECLGRLDSLPEHEDS
HHHCCHHCCCCCCCH
50.8723401153
229PhosphorylationSLPEHEDSEKAEMKR
CCCCCCCHHHHHHHH
37.7030266825
237PhosphorylationEKAEMKRSTELVLSP
HHHHHHHHCEEEECC
22.2529255136
238PhosphorylationKAEMKRSTELVLSPD
HHHHHHHCEEEECCC
37.0529255136
243PhosphorylationRSTELVLSPDMPRTT
HHCEEEECCCCCCCC
16.0429255136
249PhosphorylationLSPDMPRTTNESLLT
ECCCCCCCCCHHHHH
28.2723403867
250PhosphorylationSPDMPRTTNESLLTS
CCCCCCCCCHHHHHC
37.9623403867
253PhosphorylationMPRTTNESLLTSFPK
CCCCCCHHHHHCCCC
30.6525159151
256PhosphorylationTTNESLLTSFPKSVE
CCCHHHHHCCCCCCC
33.3530266825
257PhosphorylationTNESLLTSFPKSVEH
CCHHHHHCCCCCCCC
39.2519664994
260UbiquitinationSLLTSFPKSVEHVSP
HHHHCCCCCCCCCCC
66.1929967540
261PhosphorylationLLTSFPKSVEHVSPD
HHHCCCCCCCCCCCC
32.7329255136
266PhosphorylationPKSVEHVSPDTADAE
CCCCCCCCCCCCCCC
20.9729255136
269PhosphorylationVEHVSPDTADAESGK
CCCCCCCCCCCCCHH
29.8029255136
274PhosphorylationPDTADAESGKEIRES
CCCCCCCCHHHHHHH
57.8123927012
276AcetylationTADAESGKEIRESCQ
CCCCCCHHHHHHHHH
60.2823236377
281PhosphorylationSGKEIRESCQSTVHQ
CHHHHHHHHHHHCCC
13.9625849741
284PhosphorylationEIRESCQSTVHQQDE
HHHHHHHHHCCCCCC
36.4025849741
285PhosphorylationIRESCQSTVHQQDET
HHHHHHHHCCCCCCC
8.9823312004
292PhosphorylationTVHQQDETTIDTKDG
HCCCCCCCEECCCCC
37.0223312004
293PhosphorylationVHQQDETTIDTKDGD
CCCCCCCEECCCCCC
18.1423312004
296PhosphorylationQDETTIDTKDGDLPF
CCCCEECCCCCCCCC
27.4723312004
387UbiquitinationGRLVNEQKELAQGFL
HHHHHHHHHHHHHHH
48.8229967540
434UbiquitinationHRKLLDIKQKCTTAK
HHHHHHHHHHCHHHH
43.2929967540
480UbiquitinationLRLVIELLERVKIVE
HHHHHHHHHHCCHHH
2.2824816145
490PhosphorylationVKIVEALSTVPQMYC
CCHHHHHHCCCHHHH
34.1124719451
491PhosphorylationKIVEALSTVPQMYCL
CHHHHHHCCCHHHHH
36.7424719451
496PhosphorylationLSTVPQMYCLAVVEV
HHCCCHHHHHHHHHH
4.5024719451
522UbiquitinationEWAGALVKDGKRLYE
HHHHHHHHCCHHHHH
62.7129967540
532UbiquitinationKRLYEAEKSKRESFG
HHHHHHHHHHHHHHH
69.2224816145
537PhosphorylationAEKSKRESFGKLFRK
HHHHHHHHHHHHHHH
43.2522817900
545PhosphorylationFGKLFRKSFLRNRLF
HHHHHHHHHHHHHHH
25.8424719451
569AcetylationFCTQKPRKFDCELPD
HHCCCCCCCCCCCCC
54.8225953088
624PhosphorylationNLVKAAQSLDEMSQT
HHHHHHHHHHHHHHH
32.8230278072
629PhosphorylationAQSLDEMSQTITDLL
HHHHHHHHHHHHHHH
23.3230278072
631PhosphorylationSLDEMSQTITDLLSE
HHHHHHHHHHHHHHH
20.6623403867
633PhosphorylationDEMSQTITDLLSEQK
HHHHHHHHHHHHHHH
24.7923403867
637PhosphorylationQTITDLLSEQKASVS
HHHHHHHHHHHCCCC
45.3223403867
642PhosphorylationLLSEQKASVSQTSPQ
HHHHHHCCCCCCCCC
29.3629255136
644PhosphorylationSEQKASVSQTSPQSA
HHHHCCCCCCCCCCC
25.8329255136
646PhosphorylationQKASVSQTSPQSASS
HHCCCCCCCCCCCCC
34.5629255136
647PhosphorylationKASVSQTSPQSASSP
HCCCCCCCCCCCCCC
17.1929255136
650PhosphorylationVSQTSPQSASSPRME
CCCCCCCCCCCCCCE
33.2426055452
652PhosphorylationQTSPQSASSPRMEST
CCCCCCCCCCCCEEC
46.2329255136
653PhosphorylationTSPQSASSPRMESTA
CCCCCCCCCCCEECC
19.0829255136
658PhosphorylationASSPRMESTAGITTT
CCCCCCEECCCCCCC
17.7627251275
659PhosphorylationSSPRMESTAGITTTT
CCCCCEECCCCCCCC
18.6527251275
663PhosphorylationMESTAGITTTTSPRT
CEECCCCCCCCCCCC
19.7129978859
664PhosphorylationESTAGITTTTSPRTP
EECCCCCCCCCCCCC
26.5929255136
665PhosphorylationSTAGITTTTSPRTPP
ECCCCCCCCCCCCCC
19.3429255136
666PhosphorylationTAGITTTTSPRTPPP
CCCCCCCCCCCCCCC
34.3429255136
667PhosphorylationAGITTTTSPRTPPPL
CCCCCCCCCCCCCCC
15.4229255136
670PhosphorylationTTTTSPRTPPPLTVQ
CCCCCCCCCCCCCCC
43.4626074081
691PhosphorylationVCPLEELSPDSIDAH
CCCHHHCCCCCCCCC
29.9126074081
694PhosphorylationLEELSPDSIDAHTFD
HHHCCCCCCCCCCCC
26.2526074081
767PhosphorylationMVESLYSSVINAIDS
HHHHHHHHHHHHHHH
17.2922468782
792PhosphorylationKEDFGDHTSLNVQLE
CCCCCCCCCHHHEEE
39.3827732954
793PhosphorylationEDFGDHTSLNVQLER
CCCCCCCCHHHEEEE
17.9627732954
828UbiquitinationHFRTFVQKEQCDFSN
CHHHHCCHHHCCCCC
44.4429967540
836PhosphorylationEQCDFSNSLKCTAVE
HHCCCCCCCCEEEHH
28.1823312004
850MalonylationEIRNIIEKVKCSLEI
HHHHHHHHHCCCEEE
36.2632601280
865UbiquitinationTLKEKHQKELLSLKN
EECHHHHHHHHHCCH
50.4729967540
869PhosphorylationKHQKELLSLKNEYEG
HHHHHHHHCCHHHHC
50.3424719451
871UbiquitinationQKELLSLKNEYEGKL
HHHHHHCCHHHHCCH
44.3429967540
877UbiquitinationLKNEYEGKLDGLIKE
CCHHHHCCHHHHCHH
31.3129967540
883AcetylationGKLDGLIKETEENEN
CCHHHHCHHCHHCHH
64.7220167786
891AcetylationETEENENKIKKLKGE
HCHHCHHHHHHHHHH
50.1220167786
896UbiquitinationENKIKKLKGELVCLE
HHHHHHHHHHEECHH
60.2532015554
917UbiquitinationDNEFALVKHEKEAVI
CCCEEEEECCCEEEE
47.0729967540
931UbiquitinationICLQNEKDQKLLEME
EEECCHHHHHHHHHH
44.6724816145
938UbiquitinationDQKLLEMENIMHSQN
HHHHHHHHHHHHHCC
33.9424816145
943PhosphorylationEMENIMHSQNCEIKE
HHHHHHHHCCCCHHH
13.0028355574
963SumoylationEIVLEDLKKLHVEND
HHHHHHHHHHCCCCH
66.66-
963SumoylationEIVLEDLKKLHVEND
HHHHHHHHHHCCCCH
66.66-
963UbiquitinationEIVLEDLKKLHVEND
HHHHHHHHHHCCCCH
66.6629967540
982PhosphorylationLLRAELQSLEQSHLK
HHHHHHHHHHHHHHH
46.6423312004
986PhosphorylationELQSLEQSHLKELED
HHHHHHHHHHHHHHH
22.7825849741
989UbiquitinationSLEQSHLKELEDTLQ
HHHHHHHHHHHHHHH
55.6329967540
994PhosphorylationHLKELEDTLQVRHIQ
HHHHHHHHHHHHHHH
15.0923312004
1041AcetylationEIIQEKEKQLQELKL
HHHHHHHHHHHHHCH
68.3323236377
1051PhosphorylationQELKLKVSDLSDTRC
HHHCHHHHHCCCCHH
31.1128857561
1090UbiquitinationAQQKETLKSLLEQET
HHHHHHHHHHHHHHH
46.6129967540
1091PhosphorylationQQKETLKSLLEQETE
HHHHHHHHHHHHHHH
41.10-
1110UbiquitinationEISKLNQKIQDNNEN
HHHHHHHHHHHCCCC
41.0629967540
1142PhosphorylationQCISELISRHEEESN
HHHHHHHHHCHHHHH
39.9624719451
1159PhosphorylationKAELNKVTSLHNQAF
HHHHHHHHHHHHHHH
27.4728348404
1160PhosphorylationAELNKVTSLHNQAFE
HHHHHHHHHHHHHHH
30.5325849741
1188PhosphorylationSKLDSELSALERQKD
HHHHHHHHHHHHHHH
27.1028509920
1199PhosphorylationRQKDEKITQQEEKYE
HHHHHHCCHHHHHHH
34.9623532336
1204UbiquitinationKITQQEEKYEAIIQN
HCCHHHHHHHHHHHH
47.8729967540
1205PhosphorylationITQQEEKYEAIIQNL
CCHHHHHHHHHHHHH
17.55-
1221PhosphorylationKDRQKLVSSQEQDRE
HHHHHHHCCHHHHHH
36.4229255136
1222PhosphorylationDRQKLVSSQEQDREQ
HHHHHHCCHHHHHHH
30.2029255136
1233UbiquitinationDREQLIQKLNCEKDE
HHHHHHHHHCCCHHH
34.3729967540
12382-HydroxyisobutyrylationIQKLNCEKDEAIQTA
HHHHCCCHHHHHHHH
64.17-
1247UbiquitinationEAIQTALKEFKLERE
HHHHHHHHHHCHHHH
59.6529967540
1263AcetylationVEKELLEKVKHLENQ
HHHHHHHHHHHHHHH
57.4620167786
1274PhosphorylationLENQIAKSPAIDSTR
HHHHHHCCCCCCCCC
15.5626307563
1279PhosphorylationAKSPAIDSTRGDSSS
HCCCCCCCCCCCCHH
17.5626307563
1280PhosphorylationKSPAIDSTRGDSSSL
CCCCCCCCCCCCHHH
34.6226307563
1284PhosphorylationIDSTRGDSSSLVAEL
CCCCCCCCHHHHHHH
25.3430266825
1285PhosphorylationDSTRGDSSSLVAELQ
CCCCCCCHHHHHHHH
32.2230266825
1286PhosphorylationSTRGDSSSLVAELQE
CCCCCCHHHHHHHHH
30.7126657352
1322PhosphorylationEEMQNVRTSLIAEQQ
HHHHHHHHHHHHHHH
24.4927251275
1323PhosphorylationEMQNVRTSLIAEQQT
HHHHHHHHHHHHHHC
13.7627251275
1330PhosphorylationSLIAEQQTNFNTVLT
HHHHHHHCCHHHHHC
41.2827251275
1334PhosphorylationEQQTNFNTVLTREKM
HHHCCHHHHHCHHHH
16.8627251275
1353AcetylationIINDLSDKLKSTMQQ
HHHHHHHHHHHHHHH
55.2126051181
1370PhosphorylationRDKDLIESLSEDRAR
HHHHHHHHHHHHHHH
30.1525159151
1372PhosphorylationKDLIESLSEDRARLL
HHHHHHHHHHHHHHH
46.8929514088
1400PhosphorylationRSSSFVPSPYVATAP
HHCCCCCCCCCCCCH
24.4627251275
1402PhosphorylationSSFVPSPYVATAPEL
CCCCCCCCCCCCHHH
13.6827251275
1422UbiquitinationPELPGESDRSAVETA
CCCCCCCCCCHHHHC
44.2324816145
1424PhosphorylationLPGESDRSAVETADE
CCCCCCCCHHHHCCC
41.4721815630
1429UbiquitinationDRSAVETADEGRVDS
CCCHHHHCCCCCCCC
10.1924816145
1440PhosphorylationRVDSAMETSMMSVQE
CCCCHHHHHHHHHHH
14.6118452278
1441PhosphorylationVDSAMETSMMSVQEN
CCCHHHHHHHHHHHH
10.1318452278
1460SulfoxidationSEEKQRIMLLERTLQ
CHHHHHHHHHHHHHH
3.6821406390
1474UbiquitinationQLKEEENKRLNQRLM
HHHHHHHHHHHHHHH
62.6424816145
1481UbiquitinationKRLNQRLMSQSMSSV
HHHHHHHHHHHHHHH
3.5924816145
1482PhosphorylationRLNQRLMSQSMSSVS
HHHHHHHHHHHHHHH
24.5627732954
1484PhosphorylationNQRLMSQSMSSVSSR
HHHHHHHHHHHHHHH
17.2122617229
1486PhosphorylationRLMSQSMSSVSSRHS
HHHHHHHHHHHHHCC
32.6027732954
1487PhosphorylationLMSQSMSSVSSRHSE
HHHHHHHHHHHHCCC
19.8528857561
1578UbiquitinationQNRFKVPLGTKFYRV
HHCCCCCCCCCEEEE
17.8132015554
1581UbiquitinationFKVPLGTKFYRVKAV
CCCCCCCCEEEEEEE
38.3032015554

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
943SPhosphorylationKinaseULK1O75385
PSP
986SPhosphorylationKinaseULK1O75385
PSP
1323SPhosphorylationKinaseULK1O75385
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBCC1_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 RBCC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K5_HUMANMAP3K5physical
17015619
FAK2_HUMANPTK2Bphysical
10769033
FAK1_HUMANPTK2physical
10769033
SMCR8_HUMANSMCR8physical
20562859
HSBP1_HUMANHSBP1physical
20562859
ATG13_HUMANATG13physical
20562859
ATGA1_HUMANATG101physical
20562859
TBK1_HUMANTBK1physical
20562859
RFA1_HUMANRPA1physical
20562859
SAFB2_HUMANSAFB2physical
20562859
SAFB1_HUMANSAFBphysical
20562859
RFA2_HUMANRPA2physical
20562859
RBMX_HUMANRBMXphysical
20562859
YLPM1_HUMANYLPM1physical
20562859
SNF5_HUMANSMARCB1physical
20614030
P53_HUMANTP53physical
20614030
RN111_HUMANRNF111physical
21795712
SKI_HUMANSKIphysical
21795712
SKIL_HUMANSKILphysical
21795712
CTNB1_HUMANCTNNB1physical
22751121
UBC_HUMANUBCphysical
22751121
RFWD2_HUMANRFWD2physical
23289756
A16L1_HUMANATG16L1physical
24100292
ATG5_HUMANATG5physical
23262492
A16L1_HUMANATG16L1physical
23262492
SESN2_HUMANSESN2physical
25040165
ATGA1_HUMANATG101physical
19597335
BAP1_HUMANBAP1physical
25640309
BLID_HUMANBLIDphysical
25640309
ESIP1_HUMANEPSTI1physical
25640309
ERRFI_HUMANERRFI1physical
25640309
GLCE_HUMANGLCEphysical
25640309
GREB1_HUMANGREB1physical
25640309
I13R2_HUMANIL13RA2physical
25640309
IL24_HUMANIL24physical
25640309
ITIH5_HUMANITIH5physical
25640309
LYPD3_HUMANLYPD3physical
25640309
MRC2_HUMANMRC2physical
25640309
HOP2_HUMANPSMC3IPphysical
25640309
BRE1A_HUMANRNF20physical
25640309
THRSP_HUMANTHRSPphysical
25640309
VPS45_HUMANVPS45physical
25640309
NSD3_HUMANWHSC1L1physical
25640309
WIF1_HUMANWIF1physical
25640309
HBP1_HUMANHBP1physical
25640309
MADD_HUMANMADDphysical
25640309
SYN1_HUMANSYN1physical
25640309
UMPS_HUMANUMPSphysical
25640309
TBK1_HUMANTBK1genetic
28877469

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 RBCC1_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-243 AND SER-257, ANDMASS 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-647; SER-650; SER-652AND SER-653, 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-237; SER-624; SER-647AND SER-653, AND MASS 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-537, AND MASSSPECTROMETRY.

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