RABX5_HUMAN - dbPTM
RABX5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RABX5_HUMAN
UniProt AC Q9UJ41
Protein Name Rab5 GDP/GTP exchange factor
Gene Name RABGEF1
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Cytoplasm . Early endosome . Recycling endosome .
Protein Description Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity)..
Protein Sequence MVVVTGREPDSRRQDGAMSSSDAEDDFLEPATPTATQAGHALPLLPQERCAEFPALRGPPTQGACSSCVQRGPVLCHRAPPGAAGEHAATEGREGAPSVSGTHALLQRPLGADCGDRPAACGPAEGPLCQAQVVSRKKMSLKSERRGIHVDQSDLLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERVLLCCPGWSAMVQFQLTATSASWAQVILLLQPPKWLGLQKLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGSKKEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEGMHYKRDLSIEEQSECAQDFYHNVAERMQTRGKERRFHHVGQAGLELLTSGDPPASASQSAGNTGVEPPHPAVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALRWVTPQMLCVPVNEDIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQEAESWSPDACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAREVQDIVEKYPLEIKPPNQPLAAIDSENVENDKLPPPLQPQVYAG
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
5Phosphorylation---MVVVTGREPDSR
---CEEEECCCCCCC		20.9321406692
5 (in isoform 2)Phosphorylation-20.9324719451
11PhosphorylationVTGREPDSRRQDGAM
EECCCCCCCCCCCCC		39.8321406692
19PhosphorylationRRQDGAMSSSDAEDD
CCCCCCCCCCHHCCC		26.5922210691
20PhosphorylationRQDGAMSSSDAEDDF
CCCCCCCCCHHCCCC		21.1022210691
36PhosphorylationEPATPTATQAGHALP
CCCCCCCCCCCCCCC		22.7922210691
63UbiquitinationLRGPPTQGACSSCVQ
HCCCCCCCCCHHHHH		30.91-
85 (in isoform 2)Ubiquitination-27.0421890473
89 (in isoform 2)Ubiquitination-14.2121890473
99UbiquitinationGREGAPSVSGTHALL
CCCCCCCCCCCHHHH		6.2721890473
99UbiquitinationGREGAPSVSGTHALL
CCCCCCCCCCCHHHH		6.27-
100 (in isoform 2)Phosphorylation-42.1624719451
102 (in isoform 2)Ubiquitination-9.1121890473
103UbiquitinationAPSVSGTHALLQRPL
CCCCCCCHHHHCCCC		20.22-
103UbiquitinationAPSVSGTHALLQRPL
CCCCCCCHHHHCCCC		20.22-
103 (in isoform 2)Ubiquitination-20.2221890473
104UbiquitinationPSVSGTHALLQRPLG
CCCCCCHHHHCCCCC		15.14-
106 (in isoform 2)Phosphorylation-4.1624719451
108 (in isoform 2)Phosphorylation-28.5124719451
109 (in isoform 2)Phosphorylation-23.3724719451
113 (in isoform 2)Phosphorylation-34.8224719451
116UbiquitinationPLGADCGDRPAACGP
CCCCCCCCCCCCCCC		60.77-
116UbiquitinationPLGADCGDRPAACGP
CCCCCCCCCCCCCCC		60.77-
117UbiquitinationLGADCGDRPAACGPA
CCCCCCCCCCCCCCC		14.1921890473
117SumoylationLGADCGDRPAACGPA
CCCCCCCCCCCCCCC		14.19-
117UbiquitinationLGADCGDRPAACGPA
CCCCCCCCCCCCCCC		14.19-
120PhosphorylationDCGDRPAACGPAEGP
CCCCCCCCCCCCCCC		11.07-
121 (in isoform 2)Ubiquitination-7.9321890473
122PhosphorylationGDRPAACGPAEGPLC
CCCCCCCCCCCCCCH		21.52-
124PhosphorylationRPAACGPAEGPLCQA
CCCCCCCCCCCCHHH		21.4723186163
124 (in isoform 2)Phosphorylation-21.4724719451
125 (in isoform 3)Ubiquitination-65.5621890473
127PhosphorylationACGPAEGPLCQAQVV
CCCCCCCCCHHHHHH		22.82-
129SumoylationGPAEGPLCQAQVVSR
CCCCCCCHHHHHHCC		3.38-
129 (in isoform 3)Ubiquitination-3.3821890473
131 (in isoform 2)Phosphorylation-11.7924719451
132PhosphorylationEGPLCQAQVVSRKKM
CCCCHHHHHHCCCCC		15.4024275569
132 (in isoform 2)Phosphorylation-15.40-
135UbiquitinationLCQAQVVSRKKMSLK
CHHHHHHCCCCCCCC		39.25-
135UbiquitinationLCQAQVVSRKKMSLK
CHHHHHHCCCCCCCC		39.25-
135 (in isoform 2)Phosphorylation-39.25-
138PhosphorylationAQVVSRKKMSLKSER
HHHHCCCCCCCCCCC		32.3918669648
140 (in isoform 2)Ubiquitination-41.3421890473
142 (in isoform 3)Ubiquitination-42.8521890473
143PhosphorylationRKKMSLKSERRGIHV
CCCCCCCCCCCCCCC		41.4524719451
143 (in isoform 3)Ubiquitination-41.4521890473
145PhosphorylationKMSLKSERRGIHVDQ
CCCCCCCCCCCCCCH		49.57-
146PhosphorylationMSLKSERRGIHVDQS
CCCCCCCCCCCCCHH		44.3532645325
147 (in isoform 2)Ubiquitination-22.1521890473
149PhosphorylationKSERRGIHVDQSDLL
CCCCCCCCCCHHHHH		21.67-
151AcetylationERRGIHVDQSDLLCK
CCCCCCCCHHHHHCC		28.2719608861
151 (in isoform 2)Acetylation-28.27-
151 (in isoform 2)Ubiquitination-28.2721890473
154UbiquitinationGIHVDQSDLLCKKGC
CCCCCHHHHHCCCCC		37.7221890473
154UbiquitinationGIHVDQSDLLCKKGC
CCCCCHHHHHCCCCC		37.72-
158 (in isoform 2)Ubiquitination-52.77-
161UbiquitinationDLLCKKGCGYYGNPA
HHHCCCCCCCCCCHH		4.3221890473
161UbiquitinationDLLCKKGCGYYGNPA
HHHCCCCCCCCCCHH		4.32-
161 (in isoform 2)Ubiquitination-4.3221890473
161 (in isoform 3)Ubiquitination-4.3221890473
165UbiquitinationKKGCGYYGNPAWQGF
CCCCCCCCCHHHHHH		25.7621890473
165AcetylationKKGCGYYGNPAWQGF
CCCCCCCCCHHHHHH		25.76-
165UbiquitinationKKGCGYYGNPAWQGF
CCCCCCCCCHHHHHH		25.76-
170AcetylationYYGNPAWQGFCSKCW
CCCCHHHHHHHHHHH		36.8719608861
170 (in isoform 2)Acetylation-36.87-
170 (in isoform 2)Ubiquitination-36.8721890473
172UbiquitinationGNPAWQGFCSKCWRE
CCHHHHHHHHHHHHH		2.26-
172UbiquitinationGNPAWQGFCSKCWRE
CCHHHHHHHHHHHHH		2.26-
174PhosphorylationPAWQGFCSKCWREEY
HHHHHHHHHHHHHHH		28.7028857561
175UbiquitinationAWQGFCSKCWREEYH
HHHHHHHHHHHHHHH		38.71-
175UbiquitinationAWQGFCSKCWREEYH
HHHHHHHHHHHHHHH		38.71-
180 (in isoform 3)Ubiquitination-44.3521890473
184UbiquitinationWREEYHKARQKQIQE
HHHHHHHHHHHHHHH		13.0621890473
184AcetylationWREEYHKARQKQIQE
HHHHHHHHHHHHHHH		13.06-
184UbiquitinationWREEYHKARQKQIQE
HHHHHHHHHHHHHHH		13.06-
187 (in isoform 3)Ubiquitination-43.7621890473
191 (in isoform 3)Ubiquitination-67.7221890473
201 (in isoform 3)Ubiquitination-2.3021890473
206 (in isoform 2)Ubiquitination-2.8421890473
210 (in isoform 3)Ubiquitination-5.2921890473
213 (in isoform 2)Acetylation-22.32-
220UbiquitinationQLTATSASWAQVILL
ECCCCCCCHHHHHHH		23.7821890473
220UbiquitinationQLTATSASWAQVILL
ECCCCCCCHHHHHHH		23.78-
227AcetylationSWAQVILLLQPPKWL
CHHHHHHHHCCCCCC		2.61-
235UbiquitinationLQPPKWLGLQKLQRE
HCCCCCCCHHHHHHH		25.58-
246 (in isoform 3)Ubiquitination-14.4821890473
248UbiquitinationREEEEAFASSQSSQG
HHHHHHHHHCCCCCC		18.47-
254UbiquitinationFASSQSSQGAQSLTF
HHHCCCCCCCHHCCC		57.39-
254UbiquitinationFASSQSSQGAQSLTF
HHHCCCCCCCHHCCC		57.39-
258PhosphorylationQSSQGAQSLTFSKFE
CCCCCCHHCCCHHHC		28.9228555341
263UbiquitinationAQSLTFSKFEEKKTN
CHHCCCHHHCHHHCC		53.2422053931
263 (in isoform 1)Ubiquitination-53.2421890473
267UbiquitinationTFSKFEEKKTNEKTR
CCHHHCHHHCCCCCC		58.6721906983
267 (in isoform 1)Ubiquitination-58.6721890473
268UbiquitinationFSKFEEKKTNEKTRK
CHHHCHHHCCCCCCC		60.92-
277PhosphorylationNEKTRKVTTVKKFFS
CCCCCCCHHHHHHHC		28.9826503514
278PhosphorylationEKTRKVTTVKKFFSA
CCCCCCHHHHHHHCC		33.0624719451
280UbiquitinationTRKVTTVKKFFSASS
CCCCHHHHHHHCCCC		41.5921906983
280 (in isoform 1)Ubiquitination-41.5921890473
281UbiquitinationRKVTTVKKFFSASSR
CCCHHHHHHHCCCCC		47.5122053931
281 (in isoform 1)Ubiquitination-47.5121890473
284PhosphorylationTTVKKFFSASSRVGS
HHHHHHHCCCCCCCC		30.3029514088
286PhosphorylationVKKFFSASSRVGSKK
HHHHHCCCCCCCCHH		19.9229514088
287PhosphorylationKKFFSASSRVGSKKE
HHHHCCCCCCCCHHH		30.6029514088
291PhosphorylationSASSRVGSKKEIQEA
CCCCCCCCHHHHHHC		37.3823403867
295UbiquitinationRVGSKKEIQEAKAPS
CCCCHHHHHHCCCCC		6.52-
299UbiquitinationKKEIQEAKAPSPSIN
HHHHHHCCCCCCCCC		61.1421906983
299 (in isoform 1)Ubiquitination-61.1421890473
301UbiquitinationEIQEAKAPSPSINRQ
HHHHCCCCCCCCCCC		46.17-
302PhosphorylationIQEAKAPSPSINRQT
HHHCCCCCCCCCCCC		35.8229255136
303 (in isoform 2)Ubiquitination-37.8621890473
304PhosphorylationEAKAPSPSINRQTSI
HCCCCCCCCCCCCCC		36.5130266825
307UbiquitinationAPSPSINRQTSIETD
CCCCCCCCCCCCCHH		39.21-
309PhosphorylationSPSINRQTSIETDRV
CCCCCCCCCCCHHHH		28.5629255136
310PhosphorylationPSINRQTSIETDRVS
CCCCCCCCCCHHHHH		15.3023401153
313PhosphorylationNRQTSIETDRVSKEF
CCCCCCCHHHHHHHH		27.6928176443
317UbiquitinationSIETDRVSKEFIEFL
CCCHHHHHHHHHHHH		27.6221890473
317PhosphorylationSIETDRVSKEFIEFL
CCCHHHHHHHHHHHH		27.6223403867
317SumoylationSIETDRVSKEFIEFL
CCCHHHHHHHHHHHH		27.62-
317UbiquitinationSIETDRVSKEFIEFL
CCCHHHHHHHHHHHH		27.62-
318UbiquitinationIETDRVSKEFIEFLK
CCHHHHHHHHHHHHH		54.5121890473
318 (in isoform 1)Ubiquitination-54.5121890473
325UbiquitinationKEFIEFLKTFHKTGQ
HHHHHHHHHHHHHHH		55.2421890473
325 (in isoform 1)Ubiquitination-55.2421890473
329AcetylationEFLKTFHKTGQEIYK
HHHHHHHHHHHHHHH		50.5919608861
329UbiquitinationEFLKTFHKTGQEIYK
HHHHHHHHHHHHHHH		50.5921890473
329 (in isoform 1)Ubiquitination-50.5921890473
330PhosphorylationFLKTFHKTGQEIYKQ
HHHHHHHHHHHHHHH		35.2128102081
335PhosphorylationHKTGQEIYKQTKLFL
HHHHHHHHHHHHHHH		9.0428102081
336AcetylationKTGQEIYKQTKLFLE
HHHHHHHHHHHHHHH		58.0925953088
336UbiquitinationKTGQEIYKQTKLFLE
HHHHHHHHHHHHHHH		58.09-
339AcetylationQEIYKQTKLFLEGMH
HHHHHHHHHHHHHCH		34.4525953088
339UbiquitinationQEIYKQTKLFLEGMH
HHHHHHHHHHHHHCH		34.4521906983
339 (in isoform 1)Ubiquitination-34.4521890473
343 (in isoform 3)Ubiquitination-47.3221890473
348AcetylationFLEGMHYKRDLSIEE
HHHHCHHCCCCCHHH		25.4319608861
348UbiquitinationFLEGMHYKRDLSIEE
HHHHCHHCCCCCHHH		25.4321890473
348 (in isoform 1)Ubiquitination-25.4321890473
373PhosphorylationNVAERMQTRGKERRF
HHHHHHHHCCCHHHC		31.8520068231
373 (in isoform 2)Phosphorylation-31.85-
377PhosphorylationRMQTRGKERRFHHVG
HHHHCCCHHHCCCHH		52.4920068231
377 (in isoform 2)Phosphorylation-52.49-
384 (in isoform 2)Phosphorylation-13.78-
386 (in isoform 2)Phosphorylation-20.7124719451
387PhosphorylationFHHVGQAGLELLTSG
CCCHHHHHHHHHHCC		16.28-
389 (in isoform 2)Phosphorylation-40.59-
390PhosphorylationVGQAGLELLTSGDPP
HHHHHHHHHHCCCCC		8.32-
390 (in isoform 2)Phosphorylation-8.3227251275
391PhosphorylationGQAGLELLTSGDPPA
HHHHHHHHHCCCCCC		2.33-
398PhosphorylationLTSGDPPASASQSAG
HHCCCCCCCCCCCCC		24.1018669648
398 (in isoform 2)Phosphorylation-24.1027251275
400PhosphorylationSGDPPASASQSAGNT
CCCCCCCCCCCCCCC		17.4423186163
400 (in isoform 2)Phosphorylation-17.4424719451
403PhosphorylationPPASASQSAGNTGVE
CCCCCCCCCCCCCCC		35.3318669648
404PhosphorylationPASASQSAGNTGVEP
CCCCCCCCCCCCCCC		13.9718669648
407UbiquitinationASQSAGNTGVEPPHP
CCCCCCCCCCCCCCC		41.51-
412PhosphorylationGNTGVEPPHPAVPPE
CCCCCCCCCCCCCHH		32.37-
412 (in isoform 2)Ubiquitination-32.3721890473
414PhosphorylationTGVEPPHPAVPPERV
CCCCCCCCCCCHHHH		40.50-
422UbiquitinationAVPPERVEKIMDQIE
CCCHHHHHHHHHHHH		42.98-
422UbiquitinationAVPPERVEKIMDQIE
CCCHHHHHHHHHHHH		42.98-
423AcetylationVPPERVEKIMDQIEK
CCHHHHHHHHHHHHH		40.2425953088
423UbiquitinationVPPERVEKIMDQIEK
CCHHHHHHHHHHHHH		40.2421890473
423 (in isoform 1)Ubiquitination-40.2421890473
426UbiquitinationERVEKIMDQIEKYIM
HHHHHHHHHHHHHHH		50.1821890473
426UbiquitinationERVEKIMDQIEKYIM
HHHHHHHHHHHHHHH		50.18-
430AcetylationKIMDQIEKYIMTRLY
HHHHHHHHHHHHHHH		41.5325129629
431PhosphorylationIMDQIEKYIMTRLYK
HHHHHHHHHHHHHHH		5.3228509920
434PhosphorylationQIEKYIMTRLYKYVF
HHHHHHHHHHHHHHC		14.1528509920
437PhosphorylationKYIMTRLYKYVFCPE
HHHHHHHHHHHCCCC		9.2928509920
439PhosphorylationIMTRLYKYVFCPETT
HHHHHHHHHCCCCCC		5.7928270605
445PhosphorylationKYVFCPETTDDEKKD
HHHCCCCCCCHHHHH		22.2228270605
446PhosphorylationYVFCPETTDDEKKDL
HHCCCCCCCHHHHHH		39.5328270605
447UbiquitinationVFCPETTDDEKKDLA
HCCCCCCCHHHHHHH		70.28-
450UbiquitinationPETTDDEKKDLAIQK
CCCCCHHHHHHHHHH		59.59-
452 (in isoform 3)Ubiquitination-53.0221890473
470PhosphorylationRWVTPQMLCVPVNED
HCCCCHHEEEECCCC		1.93-
497PhosphorylationTDIIEMDSKRVPRDK
HHHHHHCCCCCCHHH		22.5022210691
512PhosphorylationLACITKCSKHIFNAI
HHHHHHHHHHHHHHH		28.9130631047
520SumoylationKHIFNAIKITKNEPA
HHHHHHHHCCCCCCC		41.74-
520UbiquitinationKHIFNAIKITKNEPA
HHHHHHHHCCCCCCC		41.7421890473
520 (in isoform 1)Ubiquitination-41.7421890473
562PhosphorylationITRFCNPSRLMTGED
HHHHCCHHHCCCCCC		24.85-
590PhosphorylationIEKLDAQSLNLSQED
HHHHCHHHCCCCHHH		22.4228176443
594PhosphorylationDAQSLNLSQEDFDRY
CHHHCCCCHHHHHHH		30.3728176443
601PhosphorylationSQEDFDRYMSGQTSP
CHHHHHHHHCCCCCC		9.4728176443
603PhosphorylationEDFDRYMSGQTSPRK
HHHHHHHCCCCCCCH		20.8623401153
606PhosphorylationDRYMSGQTSPRKQEA
HHHHCCCCCCCHHHH		44.2030266825
607PhosphorylationRYMSGQTSPRKQEAE
HHHCCCCCCCHHHHH		18.1529255136
615PhosphorylationPRKQEAESWSPDACL
CCHHHHHHCCHHHHH		39.6430266825
617PhosphorylationKQEAESWSPDACLGV
HHHHHHCCHHHHHHH		23.3716499958
629UbiquitinationLGVKQMYKNLDLLSQ
HHHHHHHHHHHHHHH		45.7721890473
629 (in isoform 1)Ubiquitination-45.7721890473
650UbiquitinationRIMNEAKKLEKDLID
HHHHHHHHHHHHHHH		69.77-
673PhosphorylationVQDIVEKYPLEIKPP
HHHHHHHCCCCCCCC		10.2725159151
706PhosphorylationPPLQPQVYAG-----
CCCCCCCCCC-----		10.6027642862
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 RABX5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RABX5_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 RABX5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KXDL1_HUMANKXD1physical
16189514
GGA1_HUMANGGA1physical
15143060
RASH_HUMANHRASphysical
20655225
MK01_HUMANMAPK1physical
20655225
RB22A_HUMANRAB22Aphysical
19759177
RAB5A_HUMANRAB5Aphysical
19759177
ESR1_HUMANESR1physical
21356307
UBC_HUMANUBCphysical
21356307
RABX5_HUMANRABGEF1physical
17341663
UBC_HUMANUBCphysical
17341663
RABE1_HUMANRABEP1physical
17341663
UBC_BOVINUBCphysical
16499958
EGFR_HUMANEGFRphysical
16499958
UBC_HUMANUBCphysical
16499958
RAB5A_HUMANRAB5Aphysical
23048039
L1CAM_HUMANL1CAMphysical
23048039
RAB21_HUMANRAB21physical
17450153
UB2D3_HUMANUBE2D3physical
20655225
UB2D1_HUMANUBE2D1physical
17341663
RABX5_HUMANRABGEF1physical
25416956
TRI54_HUMANTRIM54physical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
CIPC_HUMANCIPCphysical
25416956
TRI15_HUMANTRIM15physical
25416956
UBC_HUMANUBCphysical
16407276
RABE1_HUMANRABEP1physical
24957337
RABE1_HUMANRABEP1physical
26430212
RABE1_HUMANRABEP1physical
28514442
RABE2_HUMANRABEP2physical
28514442
HOIL1_HUMANRBCK1physical
28514442
OTUD5_HUMANOTUD5physical
28514442
SHRPN_HUMANSHARPINphysical
28514442
SLMAP_HUMANSLMAPphysical
28514442
RNF31_HUMANRNF31physical
28514442
BIRC2_HUMANBIRC2physical
28514442
GAK_HUMANGAKphysical
28514442
TAXB1_HUMANTAX1BP1physical
28514442
HGFA_HUMANHGFACphysical
28514442
CYHR1_HUMANCYHR1physical
28514442
VTI1B_HUMANVTI1Bphysical
28514442
RAB21_HUMANRAB21physical
28514442
TRAF2_HUMANTRAF2physical
28514442
UBR1_HUMANUBR1physical
28514442
EPN4_HUMANCLINT1physical
28514442
BACD3_HUMANKCTD10physical
28514442
HERC1_HUMANHERC1physical
28514442
PKN3_HUMANPKN3physical
27173435
CAVN1_HUMANPTRFphysical
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 RABX5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329 AND LYS-348, AND MASSSPECTROMETRY.
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.
"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-302, AND MASSSPECTROMETRY.
"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-302, AND MASSSPECTROMETRY.
"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-310, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory