RFIP1_HUMAN - dbPTM
RFIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFIP1_HUMAN
UniProt AC Q6WKZ4
Protein Name Rab11 family-interacting protein 1
Gene Name RAB11FIP1
Organism Homo sapiens (Human).
Sequence Length 1283
Subcellular Localization Recycling endosome . Rab11A rather than Rab4A mediates localization in the endocytic recycling compartment (ERC).
Isoform 2: Cytoplasmic vesicle, phagosome membrane. Membrane-bound (isoform 2). Colocalizes with Rab11A at phagosomes (isoform 2).
Protein Description A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis..
Protein Sequence MSLMVSAGRGLGAVWSPTHVQVTVLQARGLRAKGPGGTSDAYAVIQVGKEKYATSVSERSLGAPVWREEATFELPSLLSSGPAAAATLQLTVLHRALLGLDKFLGRAEVDLRDLHRDQGRRKTQWYKLKSKPGKKDKERGEIEVDIQFMRNNMTASMFDLSMKDKSRNPFGKLKDKIKGKNKDSGSDTASAIIPSTTPSVDSDDESVVKDKKKKSKIKTLLSKSNLQKTPLSQSMSVLPTSKPEKVLLRPGDFQSQWDEDDNEDESSSASDVMSHKRTASTDLKQLNQVNFTLPKKEGLSFLGGLRSKNDVLSRSNVCINGNHVYLEQPEAKGEIKDSSPSSSPSPKGFRKKHLFSSTENLAAGSWKEPAEGGGLSSDRQLSESSTKDSLKSMTLPSYRPAPLVSGDLRENMAPANSEATKEAKESKKPESRRSSLLSLMTGKKDVAKGSEGENPLTVPGREKEGMLMGVKPGEDASGPAEDLVRRSEKDTAAVVSRQGSSLNLFEDVQITEPEAEPESKSEPRPPISSPRAPQTRAVKPRLEVSPEAQPTARLPSPTDSPSSLPPLPSSSGQASVPSELGHGADTQSSESPSVFSSLSSPIAAPISTSTPIESWPLVDRGQAKSEGPPLLPKAELQTESLTPVPNSGSSALGSLFKQPSFPANKGTEDSLMGRTRETGTEKNTSSLELEESLPEQPETGRQEEELPRFPCKKQDYSPSSGEAQEVPFALSLSSDGAVSPVGELAAGGDRDLESQAGSLVESKARDAAEEVAPPLPMGASVPSIDSMMRKLEEMGLNLRKDQKKTKKRVSFSEQLFTEEAVAGAALLVEGHSSCPQELNPAWSVAGNASDGEPPESPHAEDSERESVTTPGPATCGAPASPADHLLLPSQEESFSEVPMSEASSAKDTPLFRMEGEDALVTQYQSKASDHEGLLSDPLSDLQLVSDFKSPIMADLNLSLPSIPEVASDDERIDQVEDDGDQVEDDGETAKSSTLDIGALSLGLVVPCPERGKGPSGEADRLVLGEGLCDFRLQAPQASVTAPSEQTTEFGIHKPHLGKSSSLDKQLPGPSGGEEEKPMGNGSPSPPPGTSLDNPVPSPSPSEIFPVTHSFPSSAHSDTHHTSTAESQKKATAEGSAGRVENFGKRKPLLQAWVSPSETHPVSAQPGAGTGSAKHRLHPVKPMNAMATKVANCSLGTATIISENLNNEVMMKKYSPSDPAFAYAQLTHDELIQLVLKQKETISKKEFQVRELEDYIDNLLVRVMEETPNILRIPTQVGKKAGKM
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
6Phosphorylation--MSLMVSAGRGLGA
--CCCCCCCCCCCCC
15.8430108239
6 (in isoform 2)Phosphorylation-15.8429507054
8 (in isoform 2)Phosphorylation-19.3830153514
9MethylationSLMVSAGRGLGAVWS
CCCCCCCCCCCCCCC
36.56115387261
13 (in isoform 1)Phosphorylation-12.49-
13 (in isoform 2)Phosphorylation-12.4929507054
14 (in isoform 1)Phosphorylation-5.02-
15 (in isoform 1)Phosphorylation-9.69-
21 (in isoform 1)Phosphorylation-19.98-
512-HydroxyisobutyrylationVIQVGKEKYATSVSE
EEEECCCEEEECCCH
43.61-
83 (in isoform 1)Phosphorylation-17.17-
87 (in isoform 1)Phosphorylation-15.43-
129AcetylationKTQWYKLKSKPGKKD
CCCEEECCCCCCCCC
52.8918525541
131AcetylationQWYKLKSKPGKKDKE
CEEECCCCCCCCCCC
57.0918525549
154PhosphorylationQFMRNNMTASMFDLS
HHHHHCCCHHHHCCC
20.0830266825
156PhosphorylationMRNNMTASMFDLSMK
HHHCCCHHHHCCCCC
15.7129255136
161PhosphorylationTASMFDLSMKDKSRN
CHHHHCCCCCCCCCC
26.1530266825
184PhosphorylationIKGKNKDSGSDTASA
HCCCCCCCCCCCCCC
41.6330266825
186PhosphorylationGKNKDSGSDTASAII
CCCCCCCCCCCCCCC
35.4230266825
188PhosphorylationNKDSGSDTASAIIPS
CCCCCCCCCCCCCCC
24.9830266825
190PhosphorylationDSGSDTASAIIPSTT
CCCCCCCCCCCCCCC
23.3030266825
195PhosphorylationTASAIIPSTTPSVDS
CCCCCCCCCCCCCCC
34.2130266825
196PhosphorylationASAIIPSTTPSVDSD
CCCCCCCCCCCCCCC
37.0530266825
197PhosphorylationSAIIPSTTPSVDSDD
CCCCCCCCCCCCCCC
20.2230266825
199PhosphorylationIIPSTTPSVDSDDES
CCCCCCCCCCCCCCH
36.1429255136
202PhosphorylationSTTPSVDSDDESVVK
CCCCCCCCCCCHHHC
44.8229255136
206PhosphorylationSVDSDDESVVKDKKK
CCCCCCCHHHCCHHH
38.9229255136
218UbiquitinationKKKKSKIKTLLSKSN
HHHHHHHHHHHCCCC
36.5429967540
219PhosphorylationKKKSKIKTLLSKSNL
HHHHHHHHHHCCCCC
36.0821712546
222PhosphorylationSKIKTLLSKSNLQKT
HHHHHHHCCCCCCCC
36.8329978859
224PhosphorylationIKTLLSKSNLQKTPL
HHHHHCCCCCCCCCC
39.1229978859
229PhosphorylationSKSNLQKTPLSQSMS
CCCCCCCCCCHHHCC
19.2630266825
232PhosphorylationNLQKTPLSQSMSVLP
CCCCCCCHHHCCCCC
22.7823401153
234PhosphorylationQKTPLSQSMSVLPTS
CCCCCHHHCCCCCCC
15.0625159151
236PhosphorylationTPLSQSMSVLPTSKP
CCCHHHCCCCCCCCC
26.2530266825
240PhosphorylationQSMSVLPTSKPEKVL
HHCCCCCCCCCCEEE
45.2621955146
241PhosphorylationSMSVLPTSKPEKVLL
HCCCCCCCCCCEEEE
44.2525159151
266PhosphorylationEDDNEDESSSASDVM
CCCCCCCCCCHHHHH
41.7526471730
267PhosphorylationDDNEDESSSASDVMS
CCCCCCCCCHHHHHH
28.0730576142
268PhosphorylationDNEDESSSASDVMSH
CCCCCCCCHHHHHHC
40.8626471730
270PhosphorylationEDESSSASDVMSHKR
CCCCCCHHHHHHCCC
32.4626471730
274PhosphorylationSSASDVMSHKRTAST
CCHHHHHHCCCCCCC
26.2126471730
278PhosphorylationDVMSHKRTASTDLKQ
HHHHCCCCCCCCHHH
29.7527794612
280PhosphorylationMSHKRTASTDLKQLN
HHCCCCCCCCHHHHH
23.1123401153
281PhosphorylationSHKRTASTDLKQLNQ
HCCCCCCCCHHHHHC
42.7730266825
292PhosphorylationQLNQVNFTLPKKEGL
HHHCCCCCCCHHHCH
36.6325159151
2962-HydroxyisobutyrylationVNFTLPKKEGLSFLG
CCCCCCHHHCHHHHC
55.89-
296UbiquitinationVNFTLPKKEGLSFLG
CCCCCCHHHCHHHHC
55.8929967540
296 (in isoform 1)Phosphorylation-55.89-
300PhosphorylationLPKKEGLSFLGGLRS
CCHHHCHHHHCCCCC
29.3125159151
307PhosphorylationSFLGGLRSKNDVLSR
HHHCCCCCCCCCCCC
40.6323312004
313PhosphorylationRSKNDVLSRSNVCIN
CCCCCCCCCCCEEEC
33.2522496350
315PhosphorylationKNDVLSRSNVCINGN
CCCCCCCCCEEECCC
30.1821945579
325PhosphorylationCINGNHVYLEQPEAK
EECCCEEEECCCCCC
9.2921945579
338PhosphorylationAKGEIKDSSPSSSPS
CCCCCCCCCCCCCCC
38.8625159151
339PhosphorylationKGEIKDSSPSSSPSP
CCCCCCCCCCCCCCC
38.6529255136
341PhosphorylationEIKDSSPSSSPSPKG
CCCCCCCCCCCCCCC
45.4522617229
342PhosphorylationIKDSSPSSSPSPKGF
CCCCCCCCCCCCCCC
50.0529255136
343PhosphorylationKDSSPSSSPSPKGFR
CCCCCCCCCCCCCCC
33.4629255136
345PhosphorylationSSPSSSPSPKGFRKK
CCCCCCCCCCCCCHH
40.9929255136
352UbiquitinationSPKGFRKKHLFSSTE
CCCCCCHHHCCCCCC
41.0829967540
356PhosphorylationFRKKHLFSSTENLAA
CCHHHCCCCCCCCCC
42.5922167270
357PhosphorylationRKKHLFSSTENLAAG
CHHHCCCCCCCCCCC
32.1922167270
358PhosphorylationKKHLFSSTENLAAGS
HHHCCCCCCCCCCCC
27.9122167270
365PhosphorylationTENLAAGSWKEPAEG
CCCCCCCCCCCCCCC
30.1923927012
376PhosphorylationPAEGGGLSSDRQLSE
CCCCCCCCCCHHHCC
33.2023927012
377PhosphorylationAEGGGLSSDRQLSES
CCCCCCCCCHHHCCC
41.6823403867
380 (in isoform 2)Phosphorylation-55.0925159151
381 (in isoform 2)Phosphorylation-6.8125159151
382PhosphorylationLSSDRQLSESSTKDS
CCCCHHHCCCCCHHH
27.3921406692
384PhosphorylationSDRQLSESSTKDSLK
CCHHHCCCCCHHHHH
39.6728450419
385PhosphorylationDRQLSESSTKDSLKS
CHHHCCCCCHHHHHH
35.1126657352
386PhosphorylationRQLSESSTKDSLKSM
HHHCCCCCHHHHHHC
48.4228450419
387UbiquitinationQLSESSTKDSLKSMT
HHCCCCCHHHHHHCC
47.4727667366
389PhosphorylationSESSTKDSLKSMTLP
CCCCCHHHHHHCCCC
38.9725159151
391UbiquitinationSSTKDSLKSMTLPSY
CCCHHHHHHCCCCCC
41.9829967540
392PhosphorylationSTKDSLKSMTLPSYR
CCHHHHHHCCCCCCC
23.4625159151
394PhosphorylationKDSLKSMTLPSYRPA
HHHHHHCCCCCCCCC
42.4825159151
397PhosphorylationLKSMTLPSYRPAPLV
HHHCCCCCCCCCCCC
36.5729978859
398PhosphorylationKSMTLPSYRPAPLVS
HHCCCCCCCCCCCCC
20.7629978859
405PhosphorylationYRPAPLVSGDLRENM
CCCCCCCCCCHHHCC
33.9823186163
424UbiquitinationSEATKEAKESKKPES
HHHHHHHHHHCCCHH
64.7124816145
426PhosphorylationATKEAKESKKPESRR
HHHHHHHHCCCHHHH
45.3224719451
431PhosphorylationKESKKPESRRSSLLS
HHHCCCHHHHHHHHH
41.3324719451
434PhosphorylationKKPESRRSSLLSLMT
CCCHHHHHHHHHHHH
24.9929255136
435PhosphorylationKPESRRSSLLSLMTG
CCHHHHHHHHHHHHC
31.3629255136
438PhosphorylationSRRSSLLSLMTGKKD
HHHHHHHHHHHCCCC
22.7625159151
441PhosphorylationSSLLSLMTGKKDVAK
HHHHHHHHCCCCHHC
51.6623927012
4432-HydroxyisobutyrylationLLSLMTGKKDVAKGS
HHHHHHCCCCHHCCC
36.31-
443AcetylationLLSLMTGKKDVAKGS
HHHHHHCCCCHHCCC
36.3130591741
448UbiquitinationTGKKDVAKGSEGENP
HCCCCHHCCCCCCCC
63.9227667366
450PhosphorylationKKDVAKGSEGENPLT
CCCHHCCCCCCCCCC
41.5428348404
4632-HydroxyisobutyrylationLTVPGREKEGMLMGV
CCCCCCCCCCCEECC
59.20-
464 (in isoform 1)Phosphorylation-45.11-
466SulfoxidationPGREKEGMLMGVKPG
CCCCCCCCEECCCCC
2.1521406390
471UbiquitinationEGMLMGVKPGEDASG
CCCEECCCCCCCCCC
41.3924816145
477PhosphorylationVKPGEDASGPAEDLV
CCCCCCCCCCHHHHH
58.6025159151
483 (in isoform 1)Phosphorylation-2.13-
487PhosphorylationAEDLVRRSEKDTAAV
HHHHHHHCHHCHHEE
38.13-
4892-HydroxyisobutyrylationDLVRRSEKDTAAVVS
HHHHHCHHCHHEEEE
62.72-
489UbiquitinationDLVRRSEKDTAAVVS
HHHHHCHHCHHEEEE
62.7224816145
491PhosphorylationVRRSEKDTAAVVSRQ
HHHCHHCHHEEEECC
27.8128450419
496PhosphorylationKDTAAVVSRQGSSLN
HCHHEEEECCCCCCC
16.5829255136
500PhosphorylationAVVSRQGSSLNLFED
EEEECCCCCCCCEEC
24.2622617229
501PhosphorylationVVSRQGSSLNLFEDV
EEECCCCCCCCEECE
28.2730278072
511PhosphorylationLFEDVQITEPEAEPE
CEECEECCCCCCCCC
28.5322115753
519PhosphorylationEPEAEPESKSEPRPP
CCCCCCCCCCCCCCC
52.8022817900
521PhosphorylationEAEPESKSEPRPPIS
CCCCCCCCCCCCCCC
63.2125159151
528PhosphorylationSEPRPPISSPRAPQT
CCCCCCCCCCCCCCC
39.8123401153
528 (in isoform 3)Phosphorylation-39.8125159151
529PhosphorylationEPRPPISSPRAPQTR
CCCCCCCCCCCCCCC
21.0830266825
529 (in isoform 3)Phosphorylation-21.0825159151
535PhosphorylationSSPRAPQTRAVKPRL
CCCCCCCCCCCCCCE
21.3830619164
541 (in isoform 1)Ubiquitination-37.4521906983
545PhosphorylationVKPRLEVSPEAQPTA
CCCCEECCCCCCCCC
13.9825159151
551PhosphorylationVSPEAQPTARLPSPT
CCCCCCCCCCCCCCC
16.6027050516
565 (in isoform 1)Ubiquitination-30.26-
577UbiquitinationSSGQASVPSELGHGA
CCCCCCCCHHHCCCC
21.4223503661
578UbiquitinationSGQASVPSELGHGAD
CCCCCCCHHHCCCCC
43.2123503661
578 (in isoform 3)Ubiquitination-43.2121906983
602UbiquitinationFSSLSSPIAAPISTS
HHCCCCCCCCCCCCC
5.7323503661
604UbiquitinationSLSSPIAAPISTSTP
CCCCCCCCCCCCCCC
11.5923503661
625PhosphorylationVDRGQAKSEGPPLLP
CCCCCCCCCCCCCCC
53.2825159151
638PhosphorylationLPKAELQTESLTPVP
CCCHHEECCCCCCCC
39.9221406692
642PhosphorylationELQTESLTPVPNSGS
HEECCCCCCCCCCCC
31.3624719451
644UbiquitinationQTESLTPVPNSGSSA
ECCCCCCCCCCCCHH
6.2133845483
648UbiquitinationLTPVPNSGSSALGSL
CCCCCCCCCHHHHHH
30.4924816145
654PhosphorylationSGSSALGSLFKQPSF
CCCHHHHHHHCCCCC
26.8624719451
660PhosphorylationGSLFKQPSFPANKGT
HHHHCCCCCCCCCCC
41.1726657352
670PhosphorylationANKGTEDSLMGRTRE
CCCCCCCCCCCCCCC
17.6421815630
684PhosphorylationETGTEKNTSSLELEE
CCCCCCCCCCCCCHH
30.6617192257
685PhosphorylationTGTEKNTSSLELEES
CCCCCCCCCCCCHHH
42.1717192257
686PhosphorylationGTEKNTSSLELEESL
CCCCCCCCCCCHHHC
24.6717192257
692PhosphorylationSSLELEESLPEQPET
CCCCCHHHCCCCCCC
39.5917192257
717PhosphorylationPCKKQDYSPSSGEAQ
CCCCCCCCCCCCCCC
26.9625921289
719PhosphorylationKKQDYSPSSGEAQEV
CCCCCCCCCCCCCCC
45.0628348404
720PhosphorylationKQDYSPSSGEAQEVP
CCCCCCCCCCCCCCC
44.0028348404
731PhosphorylationQEVPFALSLSSDGAV
CCCCEEEEECCCCCC
23.8328122231
733PhosphorylationVPFALSLSSDGAVSP
CCEEEEECCCCCCCC
24.0228122231
734PhosphorylationPFALSLSSDGAVSPV
CEEEEECCCCCCCCH
45.4128122231
739PhosphorylationLSSDGAVSPVGELAA
ECCCCCCCCHHHHHC
17.2126657352
754PhosphorylationGGDRDLESQAGSLVE
CCCCCHHHHHHHHHH
32.4025159151
758PhosphorylationDLESQAGSLVESKAR
CHHHHHHHHHHHHHH
32.0525159151
762PhosphorylationQAGSLVESKARDAAE
HHHHHHHHHHHHHHH
24.9220873877
783PhosphorylationPMGASVPSIDSMMRK
CCCCCCCCHHHHHHH
36.5522210691
786PhosphorylationASVPSIDSMMRKLEE
CCCCCHHHHHHHHHH
16.8922210691
800AcetylationEMGLNLRKDQKKTKK
HHCCCCCCCHHHHHH
68.6220167786
803AcetylationLNLRKDQKKTKKRVS
CCCCCCHHHHHHCCC
72.9720167786
880PhosphorylationATCGAPASPADHLLL
CCCCCCCCHHCCCCC
21.40-
908PhosphorylationEASSAKDTPLFRMEG
HHHCCCCCCCEEEEC
22.6121815630
921PhosphorylationEGEDALVTQYQSKAS
ECCCEEHHHHHHCCC
23.5529978859
923PhosphorylationEDALVTQYQSKASDH
CCEEHHHHHHCCCCC
12.8529978859
925PhosphorylationALVTQYQSKASDHEG
EEHHHHHHCCCCCCC
25.8421815630
928PhosphorylationTQYQSKASDHEGLLS
HHHHHCCCCCCCCCC
43.1425159151
935PhosphorylationSDHEGLLSDPLSDLQ
CCCCCCCCCCHHHHH
42.0725159151
939PhosphorylationGLLSDPLSDLQLVSD
CCCCCCHHHHHHHHC
41.4824626860
945PhosphorylationLSDLQLVSDFKSPIM
HHHHHHHHCCCCCHH
46.0224626860
958PhosphorylationIMADLNLSLPSIPEV
HHHCCCCCCCCCHHC
36.8420873877
961PhosphorylationDLNLSLPSIPEVASD
CCCCCCCCCHHCCCC
56.9530278072
967PhosphorylationPSIPEVASDDERIDQ
CCCHHCCCCCHHCCC
51.2630278072
1038PhosphorylationRLQAPQASVTAPSEQ
EEECCCCCEECCCCC
18.1128555341
1070PhosphorylationDKQLPGPSGGEEEKP
CCCCCCCCCCCCCCC
66.4027794612
1131PhosphorylationAESQKKATAEGSAGR
HHHHHHHHHCCCCHH
33.8428555341
1135PhosphorylationKKATAEGSAGRVENF
HHHHHCCCCHHHHHC
21.0325159151
1154PhosphorylationPLLQAWVSPSETHPV
CCEEECCCCCCCCCC
16.4118691976
1156PhosphorylationLQAWVSPSETHPVSA
EEECCCCCCCCCCCC
47.8528348404
1158PhosphorylationAWVSPSETHPVSAQP
ECCCCCCCCCCCCCC
35.5026434776
1162PhosphorylationPSETHPVSAQPGAGT
CCCCCCCCCCCCCCC
26.1526434776
1169PhosphorylationSAQPGAGTGSAKHRL
CCCCCCCCCCCCCCC
27.6826434776
1171PhosphorylationQPGAGTGSAKHRLHP
CCCCCCCCCCCCCCC
33.7026434776
1187PhosphorylationKPMNAMATKVANCSL
CCCCHHHHHHHCCCC
16.99-
1193PhosphorylationATKVANCSLGTATII
HHHHHCCCCCCEEEE
29.6425159151
1196PhosphorylationVANCSLGTATIISEN
HHCCCCCCEEEEECC
26.3925159151
1198PhosphorylationNCSLGTATIISENLN
CCCCCCEEEEECCCC
20.7725627689
1211UbiquitinationLNNEVMMKKYSPSDP
CCCHHHHHCCCCCCH
30.3923503661
1212UbiquitinationNNEVMMKKYSPSDPA
CCHHHHHCCCCCCHH
32.822190698
1212 (in isoform 4)Ubiquitination-32.8221906983
1214PhosphorylationEVMMKKYSPSDPAFA
HHHHHCCCCCCHHHH
27.1425159151
1216PhosphorylationMMKKYSPSDPAFAYA
HHHCCCCCCHHHHHH
50.73-
1226PhosphorylationAFAYAQLTHDELIQL
HHHHHHCCHHHHHHH
18.39-
1236UbiquitinationELIQLVLKQKETISK
HHHHHHHHCCCCCCH
52.4223503661
1238UbiquitinationIQLVLKQKETISKKE
HHHHHHCCCCCCHHH
56.0623503661
1254PhosphorylationQVRELEDYIDNLLVR
CHHHHHHHHHHHHHH
10.7829978859
1274PhosphorylationPNILRIPTQVGKKAG
CCCEECCCHHHHHCC
33.2526657352
12782-HydroxyisobutyrylationRIPTQVGKKAGKM--
ECCCHHHHHCCCC--
40.36-
1278UbiquitinationRIPTQVGKKAGKM--
ECCCHHHHHCCCC--
40.3633845483
1282UbiquitinationQVGKKAGKM------
HHHHHCCCC------
46.4224816145

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
234SPhosphorylationKinaseMARK2Q7KZI7
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFIP1_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 RFIP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP1_HUMANRAB11FIP1physical
12364336
RFIP2_HUMANRAB11FIP2physical
12364336
RB11A_HUMANRAB11Aphysical
11495908
RAB14_HUMANRAB14physical
19702578
ASAP1_HUMANASAP1physical
18685082
NOLC1_HUMANNOLC1physical
28514442
1433Z_HUMANYWHAZphysical
28514442
1433G_HUMANYWHAGphysical
28514442
CBY1_HUMANCBY1physical
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 RFIP1_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-156; SER-357 ANDSER-545, AND MASS 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-199; SER-202; SER-338;SER-343; SER-345 AND SER-545, 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-202; SER-338; SER-339;SER-341; SER-342; SER-343; SER-345; SER-435; SER-477 AND SER-545, 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-300; SER-435; SER-477;SER-500; SER-501; SER-545; THR-684; SER-685; SER-686; SER-692;SER-754; SER-758 AND SER-1135, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND MASSSPECTROMETRY.
"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-357, AND MASSSPECTROMETRY.

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