Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transitional endoplasmic reticulum ATPase  

UniProtKB / Swiss-Prot ID :  TERA_HUMAN

Gene Name (Synonyms) : 
VCP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus. Note=Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parki 

Protein Function :  Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. 

Protein Sequence MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCI...
Predicted Secondary Structure CCCCCCCCHHHHHHHHHHHCCCCCHHHHHHHHCCCCCEEEECHHHHHHHCCCCCCEEEEECCCCCEEEEE...
Protein Variant
LocationDescription
95R -> G (in IBMPFD; cultured cellsexpressing the mutant protein show a
155R -> C (in IBMPFD; also in one patientwithout evidence of Paget disease of the
155R -> H (in ALS14 and IBMPFD; ALS14patients do not manifest frontotemporal
155R -> P (in IBMPFD). VAR_033019
159R -> G (in ALS14). VAR_065910
159R -> H (in IBMPFD; without frontotemporaldementia).
191R -> Q (in ALS14 and IBMPFD). VAR_033021
232A -> E (in IBMPFD). VAR_033022
592D -> N (in ALS14; ALS14 patients do notshow frontotemporal dementia).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASGAD
---CCCCCC
19.37UniProtKB
Link-
3Phosphoserine--MASGADS
--CCCCCCC
32.96HPRD
Link-
3Phosphoserine--MASGADS
--CCCCCCC
32.96Phosphositeplus
Link-
3Phosphoserine--MASGADS
--CCCCCCC
32.96SysPTM
Link-
3Phosphoserine.--MASGADS
--CCCCCCC
32.96UniProtKB
Link-
7PhosphoserineSGADSKGDD
CCCCCCHHH
37.69Phosphositeplus
Link-
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GADSKGDDL
CCCCCHHHH
67.89Phosphositeplus
Link-
8N6-acetyllysineGADSKGDDL
CCCCCHHHH
67.89Phosphositeplus
Link-
13PhosphoserineGDDLSTAIL
HHHHHHHHH
23.84Phosphositeplus
Link-
14PhosphothreonineDDLSTAILK
HHHHHHHHH
25.64Phosphositeplus
Link-
18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TAILKQKNR
HHHHHHCCC
53.78Phosphositeplus
Link-
18N6-acetyllysineTAILKQKNR
HHHHHHCCC
53.78Phosphositeplus
Link-
37PhosphoserineNEDNSVVSL
CCCCCEEEE
35.90Phosphositeplus
Link-
37Phosphoserine.NEDNSVVSL
CCCCCEEEE
35.90UniProtKB
Link-
45Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSQPKMDEL
ECHHHHHHH
51.88Phosphositeplus
Link-
56PhosphothreonineFRGDTVLLK
CCCCEEEEE
18.84Phosphositeplus
Link-
60N6-acetyllysineTVLLKGKKR
EEEEECCCC
65.60Phosphositeplus
Link-
73PhosphoserineCIVLSDDTC
EEEECCCCC
23.65Phosphositeplus
Link-
81N6-acetyllysineCSDEKIRMN
CCCCEEEEH
40.37Phosphositeplus
Link-
101PhosphoserineGDVISIQPC
CCCEEEEEC
18.28Phosphositeplus
Link-
105S-nitrosocysteineSIQPCPDVK
EEEECCCCC
2.29dbSNO
Link-
109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CPDVKYGKR
CCCCCCCCE
56.52Phosphositeplus
Link-
110PhosphotyrosinePDVKYGKRI
CCCCCCCEE
27.94Phosphositeplus
Link-
138PhosphotyrosineYLKPYFLEA
HHHHHHHHC
21.14Phosphositeplus
Link-
143PhosphotyrosineFLEAYRPIR
HHHCCCHHH
13.93Phosphositeplus
Link-
164N6-acetyllysineAVEFKVVET
HHHHHHHHH
31.68Phosphositeplus
Link-
168PhosphothreonineKVVETDPSP
HHHHHCCCC
41.42Phosphositeplus
Link-
197PhosphoserineDEEESLNEV
HHHHCCCCC
39.51Phosphositeplus
Link-
211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGCRKQLAQ
CCHHHHHHH
54.46Phosphositeplus
Link-
217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LAQIKEMVE
HHHHHHHHH
27.90Phosphositeplus
Link-
231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PALFKAIGV
CHHHHHCCC
39.69Phosphositeplus
Link-
236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AIGVKPPRG
HCCCCCCCC
44.05Phosphositeplus
Link-
244PhosphotyrosineGILLYGPPG
CEEEECCCC
24.92Phosphositeplus
Link-
249PhosphothreonineGPPGTGKTL
CCCCCCHHH
41.08Phosphositeplus
Link-
251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PGTGKTLIA
CCCCHHHHH
39.74Phosphositeplus
Link-
251N6-acetyllysinePGTGKTLIA
CCCCHHHHH
39.74Phosphositeplus
Link-
276PhosphoserinePEIMSKLAG
HHHHHHHHC
30.13Phosphositeplus
Link-
282PhosphoserineLAGESESNL
HHCCCHHHH
45.46Phosphositeplus
Link-
282Phosphoserine.LAGESESNL
HHCCCHHHH
45.46UniProtKB
Link-
284PhosphoserineGESESNLRK
CCCHHHHHH
50.90Phosphositeplus
Link-
284Phosphoserine.GESESNLRK
CCCHHHHHH
50.90UniProtKB
Link-
288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SNLRKAFEE
HHHHHHHHH
61.67Phosphositeplus
Link-
295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEAEKNAPA
HHHHHCCCC
66.51Phosphositeplus
Link-
312Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AIAPKREKT
HHCCCCCCC
65.25Phosphositeplus
Link-
315N6-acetyllysinePKREKTHGE
CCCCCCCCH
50.26Phosphositeplus
Link-
316PhosphothreonineKREKTHGEV
CCCCCCCHH
30.29Phosphositeplus
Link-
326PhosphoserineRRIVSQLLT
HHHHHHHHH
16.85Phosphositeplus
Link-
330PhosphothreonineSQLLTLMDG
HHHHHHHCC
28.73Phosphositeplus
Link-
336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MDGLKQRAH
HCCCCCCCC
43.18Phosphositeplus
Link-
336N6-acetyllysineMDGLKQRAH
HCCCCCCCC
43.18Phosphositeplus
Link-
347PhosphothreonineVMAATNRPN
EEEEECCHH
23.40Phosphositeplus
Link-
352PhosphoserineNRPNSIDPA
CCHHHCCHH
30.93PhosphoELM
Link-
352PhosphoserineNRPNSIDPA
CCHHHCCHH
30.93Phosphositeplus
Link-
375PhosphothreonineIPDATGRLE
CCCHHHHHH
30.16Phosphositeplus
Link-
385PhosphothreonineLQIHTKNMK
HHHHHHCCC
26.24Phosphositeplus
Link-
386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QIHTKNMKL
HHHHHCCCC
40.66Phosphositeplus
Link-
386N6-acetyllysineQIHTKNMKL
HHHHHCCCC
40.66Phosphositeplus
Link-
436PhosphothreonineLEDETIDAE
HHHHHHHHH
36.16HPRD
Link-
436PhosphothreonineLEDETIDAE
HHHHHHHHH
36.16Phosphositeplus
Link-
436PhosphothreonineLEDETIDAE
HHHHHHHHH
36.16SysPTM
Link-
436Phosphothreonine.LEDETIDAE
HHHHHHHHH
36.16UniProtKB
Link-
457PhosphoserineRWALSQSNP
CCCCCCCCC
24.66Phosphositeplus
Link-
457Phosphoserine.RWALSQSNP
CCCCCCCCC
24.66UniProtKB
Link-
459PhosphoserineALSQSNPSA
CCCCCCCCC
47.54Phosphositeplus
Link-
486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEDVKRELQ
HHHHHHHHH
53.10Phosphositeplus
Link-
502Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EHPDKFLKF
HHHHHHHHC
57.98Phosphositeplus
Link-
505Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DKFLKFGMT
HHHHHCCCC
42.90Phosphositeplus
Link-
505N6-acetyllysineDKFLKFGMT
HHHHHCCCC
42.90Phosphositeplus
Link-
509PhosphothreonineKFGMTPSKG
HCCCCCCCC
25.45HPRD
Link-
509PhosphothreonineKFGMTPSKG
HCCCCCCCC
25.45Phosphositeplus
Link-
509PhosphothreonineKFGMTPSKG
HCCCCCCCC
25.45SysPTM
Link-
509Phosphothreonine.KFGMTPSKG
HCCCCCCCC
25.45UniProtKB
Link-
511PhosphoserineGMTPSKGVL
CCCCCCCEE
32.64Phosphositeplus
Link-
512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MTPSKGVLF
CCCCCCEEE
55.00Phosphositeplus
Link-
512N6-acetyllysineMTPSKGVLF
CCCCCCEEE
55.00Phosphositeplus
Link-
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PGCGKTLLA
CCCCHHHHH
39.82Phosphositeplus
Link-
524N6-acetyllysinePGCGKTLLA
CCCCHHHHH
39.82Phosphositeplus
Link-
525PhosphothreonineGCGKTLLAK
CCCHHHHHH
16.58Phosphositeplus
Link-
529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TLLAKAIAN
HHHHHHHHH
40.05Phosphositeplus
Link-
529N6-acetyllysineTLLAKAIAN
HHHHHHHHH
40.05Phosphositeplus
Link-
535S-nitrosocysteineIANECQANF
HHHHCCCCE
4.67dbSNO
Link-
541PhosphoserineANFISIKGP
CCEEEEEHH
17.70Phosphositeplus
Link-
555PhosphoserineWFGESEANV
CCCCCHHHH
42.25Phosphositeplus
Link-
565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIFDKARQA
HHHHHHHHC
34.42Phosphositeplus
Link-
572S-nitrosocysteineQAAPCVLFF
HCCCCEEEE
3.40dbSNO
Link-
584Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSIAKARGG
HHHCCCCCC
36.63Phosphositeplus
Link-
606PhosphothreonineNQILTEMDG
HHHHHHHCC
30.78Phosphositeplus
Link-
612PhosphoserineMDGMSTKKN
HCCCCCCCC
42.47Phosphositeplus
Link-
613PhosphothreonineDGMSTKKNV
CCCCCCCCE
36.83HPRD
Link-
613PhosphothreonineDGMSTKKNV
CCCCCCCCE
36.83Phosphositeplus
Link-
614Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GMSTKKNVF
CCCCCCCEE
34.74Phosphositeplus
Link-
614N6-acetyllysineGMSTKKNVF
CCCCCCCEE
34.74Phosphositeplus
Link-
623PhosphothreonineIIGATNRPD
EEEECCCHH
26.92Phosphositeplus
Link-
644PhosphotyrosineDQLIYIPLP
CEEEEECCC
12.70Phosphositeplus
Link-
651Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPDEKSRVA
CCCHHHHHH
51.44Phosphositeplus
Link-
652PhosphoserinePDEKSRVAI
CCHHHHHHH
29.91Phosphositeplus
Link-
658Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VAILKANLR
HHHHHHHHH
29.17Phosphositeplus
Link-
658N6-acetyllysineVAILKANLR
HHHHHHHHH
29.17Phosphositeplus
Link-
663Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ANLRKSPVA
HHHHHCCCC
63.38Phosphositeplus
Link-
663N6-acetyllysineANLRKSPVA
HHHHHCCCC
63.38Phosphositeplus
Link-
664PhosphoserineNLRKSPVAK
HHHHCCCCC
20.41Phosphositeplus
Link-
668Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SPVAKDVDL
CCCCCCCCH
59.52Phosphositeplus
Link-
668N6-acetyllysineSPVAKDVDL
CCCCCCCCH
59.52Phosphositeplus
Link-
677N6-acetyllysineEFLAKMTNG
HHHHHHCCC
48.69Phosphositeplus
Link-
679PhosphothreonineLAKMTNGFS
HHHHCCCCC
31.33Phosphositeplus
Link-
683PhosphoserineTNGFSGADL
CCCCCHHHH
34.17Phosphositeplus
Link-
688PhosphothreonineGADLTEICQ
HHHHHHHHH
24.69Phosphositeplus
Link-
696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QRACKLAIR
HHHHHHHHH
39.71Phosphositeplus
Link-
696N6-acetyllysineQRACKLAIR
HHHHHHHHH
39.71Phosphositeplus
Link-
702PhosphoserineAIRESIESE
HHHHHHHHH
23.08Phosphositeplus
Link-
702Phosphoserine.AIRESIESE
HHHHHHHHH
23.08UniProtKB
Link-
705PhosphoserineESIESEIRR
HHHHHHHHH
36.33Phosphositeplus
Link-
705Phosphoserine.ESIESEIRR
HHHHHHHHH
36.33UniProtKB
Link-
746PhosphoserineFARRSVSDN
HHHHCCCHH
22.03PhosphoELM
Link-
746PhosphoserineFARRSVSDN
HHHHCCCHH
22.03Phosphositeplus
Link-
746Phosphoserine.FARRSVSDN
HHHHCCCHH
22.03UniProtKB
Link-
748PhosphoserineRRSVSDNDI
HHCCCHHHH
31.76PhosphoELM
Link-
748PhosphoserineRRSVSDNDI
HHCCCHHHH
31.76Phosphositeplus
Link-
748Phosphoserine.RRSVSDNDI
HHCCCHHHH
31.76UniProtKB
Link-
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NDIRKYEMF
HHHHHHHHH
45.99Phosphositeplus
Link-
754N6-acetyllysineNDIRKYEMF
HHHHHHHHH
45.99Phosphositeplus
Link-
755PhosphotyrosineDIRKYEMFA
HHHHHHHHH
11.63Phosphositeplus
Link-
761PhosphothreonineMFAQTLQQS
HHHHHHHHH
24.09Phosphositeplus
Link-
765PhosphoserineTLQQSRGFG
HHHHHHCCC
22.78Phosphositeplus
Link-
770PhosphoserineRGFGSFRFP
HCCCCCCCC
15.81Phosphositeplus
Link-
770Phosphoserine.RGFGSFRFP
HCCCCCCCC
15.81UniProtKB
Link-
775PhosphoserineFRFPSGNQG
CCCCCCCCC
47.89HPRD
Link-
775PhosphoserineFRFPSGNQG
CCCCCCCCC
47.89Phosphositeplus
Link-
775Phosphoserine.FRFPSGNQG
CCCCCCCCC
47.89UniProtKB
Link-
784PhosphoserineGAGPSQGSG
CCCCHHCCC
46.38HPRD
Link-
784PhosphoserineGAGPSQGSG
CCCCHHCCC
46.38PhosphoELM
Link-
784PhosphoserineGAGPSQGSG
CCCCHHCCC
46.38Phosphositeplus
Link-
784Phosphoserine.GAGPSQGSG
CCCCHHCCC
46.38UniProtKB
Link-
787PhosphoserinePSQGSGGGT
CHHCCCCCC
26.99HPRD
Link-
787PhosphoserinePSQGSGGGT
CHHCCCCCC
26.99Phosphositeplus
Link-
787PhosphoserinePSQGSGGGT
CHHCCCCCC
26.99SysPTM
Link-
787Phosphoserine.PSQGSGGGT
CHHCCCCCC
26.99UniProtKB
Link-
796DePhosphotyrosineGGSVYTEDN
CCCCCCCCC
13.20HPRD
Link-
805DePhosphotyrosineDDDLYG
CCCCCC
27.99HPRD
Link-
805PhosphotyrosineDDDLYG
CCCCCC
27.99HPRD
Link-
805PhosphotyrosineDDDLYG
CCCCCC
27.99PhosphoELM
Link-
805PhosphotyrosineDDDLYG
CCCCCC
27.99Phosphositeplus
Link-
805Phosphotyrosine.DDDLYG
CCCCCC
27.99UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATX3_HUMANcolocalizationMINT-2837835MINT16525503
ATX3_HUMANphysical interactionMINT-50299MINT12944474
ATX3_HUMANdirect interactionMINT-2837662MINT16525503
ATX3_HUMANdirect interactionMINT-2837891MINT16525503
ATX3_HUMANdirect interactionMINT-2838443MINT16525503
UFD1_HUMANdirect interactionMINT-2837686MINT16525503
BRCA1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03013HPRD10855792
JAK2_HUMANin vitro
in vivo
HPRD:03013HPRD11087817
HDAC6_HUMANin vitro
in vivo
HPRD:03013HPRD11689694
TERA_HUMANin vitroHPRD:03013HPRD12807884
IKBA_HUMANin vitro
in vivo
HPRD:03013HPRD9452483
UFD1_HUMANin vitroHPRD:03013HPRD16525503
WRN_HUMANin vitro
in vivo
HPRD:03013HPRD15037256
NSF1C_HUMANENSP00000351777STRING
DERL1_HUMANENSP00000351777STRING
PTN3_HUMANENSP00000351777STRING
AMFR2_HUMANENSP00000351777STRING
WRN_HUMANENSP00000351777STRING
PSMD2_HUMANENSP00000351777STRING
NPL4_HUMANENSP00000351777STRING
RN19A_HUMANENSP00000351777STRING
RN19A_HUMANENSP00000351777STRING
UBE4B_HUMANENSP00000351777STRING
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Disease Reference
Kegg disease
OMIM disease
167320Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 1 (IBMPFD1)
613954Amyotrophic lateral sclerosis 14, with or without frontotemporal dementia (ALS14)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC).";
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
J. Proteome Res. 4:1661-1671(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, AND MASSSPECTROMETRY.
"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-784, AND MASSSPECTROMETRY.
"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 SER-705, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-436; THR-509 ANDSER-787, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-37; SER-282;SER-284; SER-457; SER-746 AND SER-748, AND MASS SPECTROMETRY.
"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-770 AND SER-775, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures