RACK1_HUMAN - dbPTM
RACK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RACK1_HUMAN
UniProt AC P63244
Protein Name Receptor of activated protein C kinase 1
Gene Name RACK1 {ECO:0000312|HGNC:HGNC:4399}
Organism Homo sapiens (Human).
Sequence Length 317
Subcellular Localization Cell membrane
Peripheral membrane protein. Cytoplasm . Cytoplasm, perinuclear region . Nucleus . Perikaryon . Cell projection, dendrite . Cell projection, phagocytic cup . Recruited to the plasma membrane through interaction with KRT1 which binds t
Protein Description Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. [PubMed: 23636399 Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits]
Protein Sequence MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
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
1Acetylation-------MTEQMTLR
-------CCCEEEEC
22814378
2Acetylation------MTEQMTLRG
------CCCEEEECE
21406692
2Phosphorylation------MTEQMTLRG
------CCCEEEECE
20363803
6Phosphorylation--MTEQMTLRGTLKG
--CCCEEEECEEEEC
25159151
8MethylationMTEQMTLRGTLKGHN
CCCEEEECEEEECCC
115490059
10PhosphorylationEQMTLRGTLKGHNGW
CEEEECEEEECCCCC
21406692
12AcetylationMTLRGTLKGHNGWVT
EEECEEEECCCCCEE
26051181
12MethylationMTLRGTLKGHNGWVT
EEECEEEECCCCCEE
24633395
12UbiquitinationMTLRGTLKGHNGWVT
EEECEEEECCCCCEE
21906983
19PhosphorylationKGHNGWVTQIATTPQ
ECCCCCEEEEEECCC
21406692
23PhosphorylationGWVTQIATTPQFPDM
CCEEEEEECCCCCHH
21406692
24PhosphorylationWVTQIATTPQFPDMI
CEEEEEECCCCCHHH
21406692
30SulfoxidationTTPQFPDMILSASRD
ECCCCCHHHEECCCC
28465586
33PhosphorylationQFPDMILSASRDKTI
CCCHHHEECCCCCEE
21406692
35PhosphorylationPDMILSASRDKTIIM
CHHHEECCCCCEEEE
21406692
382-HydroxyisobutyrylationILSASRDKTIIMWKL
HEECCCCCEEEEEEE
-
38AcetylationILSASRDKTIIMWKL
HEECCCCCEEEEEEE
25953088
38UbiquitinationILSASRDKTIIMWKL
HEECCCCCEEEEEEE
21906983
39O-linked_GlycosylationLSASRDKTIIMWKLT
EECCCCCEEEEEEEC
23301498
39PhosphorylationLSASRDKTIIMWKLT
EECCCCCEEEEEEEC
20068231
44AcetylationDKTIIMWKLTRDETN
CCEEEEEEECCCCCC
26051181
44UbiquitinationDKTIIMWKLTRDETN
CCEEEEEEECCCCCC
21906983
46PhosphorylationTIIMWKLTRDETNYG
EEEEEEECCCCCCCC
28152594
47MethylationIIMWKLTRDETNYGI
EEEEEECCCCCCCCC
115490051
50PhosphorylationWKLTRDETNYGIPQR
EEECCCCCCCCCCHH
28796482
52NitrationLTRDETNYGIPQRAL
ECCCCCCCCCCHHHH
-
52PhosphorylationLTRDETNYGIPQRAL
ECCCCCCCCCCHHHH
28796482
63PhosphorylationQRALRGHSHFVSDVV
HHHHCCCCCEEEEEE
-
93PhosphorylationTLRLWDLTTGTTTRR
EEEEEECCCCCCEEE
23312004
94PhosphorylationLRLWDLTTGTTTRRF
EEEEECCCCCCEEEE
23312004
96PhosphorylationLWDLTTGTTTRRFVG
EEECCCCCCEEEECC
23403867
97PhosphorylationWDLTTGTTTRRFVGH
EECCCCCCEEEECCC
23403867
98PhosphorylationDLTTGTTTRRFVGHT
ECCCCCCEEEECCCC
24275569
105PhosphorylationTRRFVGHTKDVLSVA
EEEECCCCCCEEEEE
24275569
1062-HydroxyisobutyrylationRRFVGHTKDVLSVAF
EEECCCCCCEEEEEE
-
106AcetylationRRFVGHTKDVLSVAF
EEECCCCCCEEEEEE
26051181
106UbiquitinationRRFVGHTKDVLSVAF
EEECCCCCCEEEEEE
21906983
110PhosphorylationGHTKDVLSVAFSSDN
CCCCCEEEEEECCCC
21406692
114PhosphorylationDVLSVAFSSDNRQIV
CEEEEEECCCCCEEE
21406692
115PhosphorylationVLSVAFSSDNRQIVS
EEEEEECCCCCEEEC
21406692
122PhosphorylationSDNRQIVSGSRDKTI
CCCCEEECCCCCHHE
21406692
124O-linked_GlycosylationNRQIVSGSRDKTIKL
CCEEECCCCCHHEEH
23301498
124PhosphorylationNRQIVSGSRDKTIKL
CCEEECCCCCHHEEH
21406692
128PhosphorylationVSGSRDKTIKLWNTL
ECCCCCHHEEHHHHC
-
130SumoylationGSRDKTIKLWNTLGV
CCCCHHEEHHHHCCC
-
130AcetylationGSRDKTIKLWNTLGV
CCCCHHEEHHHHCCC
19608861
130MalonylationGSRDKTIKLWNTLGV
CCCCHHEEHHHHCCC
26320211
130SumoylationGSRDKTIKLWNTLGV
CCCCHHEEHHHHCCC
19608861
130UbiquitinationGSRDKTIKLWNTLGV
CCCCHHEEHHHHCCC
20639865
134PhosphorylationKTIKLWNTLGVCKYT
HHEEHHHHCCCCEEE
23312004
138S-nitrosocysteineLWNTLGVCKYTVQDE
HHHHCCCCEEEECCC
-
138S-palmitoylationLWNTLGVCKYTVQDE
HHHHCCCCEEEECCC
29575903
139AcetylationWNTLGVCKYTVQDES
HHHCCCCEEEECCCC
25953088
139UbiquitinationWNTLGVCKYTVQDES
HHHCCCCEEEECCCC
21906983
140PhosphorylationNTLGVCKYTVQDESH
HHCCCCEEEECCCCC
28152594
141PhosphorylationTLGVCKYTVQDESHS
HCCCCEEEECCCCCC
28152594
146PhosphorylationKYTVQDESHSEWVSC
EEEECCCCCCCCEEE
28152594
157PhosphorylationWVSCVRFSPNSSNPI
CEEEEEECCCCCCCE
20873877
160PhosphorylationCVRFSPNSSNPIIVS
EEEECCCCCCCEEEE
25850435
161PhosphorylationVRFSPNSSNPIIVSC
EEECCCCCCCEEEEE
25850435
167PhosphorylationSSNPIIVSCGWDKLV
CCCCEEEEECHHHHH
21712546
168S-nitrosocysteineSNPIIVSCGWDKLVK
CCCEEEEECHHHHHH
-
1722-HydroxyisobutyrylationIVSCGWDKLVKVWNL
EEEECHHHHHHHHHH
-
172AcetylationIVSCGWDKLVKVWNL
EEEECHHHHHHHHHH
25953088
172MethylationIVSCGWDKLVKVWNL
EEEECHHHHHHHHHH
70595
172UbiquitinationIVSCGWDKLVKVWNL
EEEECHHHHHHHHHH
21906983
175AcetylationCGWDKLVKVWNLANC
ECHHHHHHHHHHCCC
26051181
175UbiquitinationCGWDKLVKVWNLANC
ECHHHHHHHHHHCCC
21906983
182S-nitrosocysteineKVWNLANCKLKTNHI
HHHHHCCCEEECCCC
-
183AcetylationVWNLANCKLKTNHIG
HHHHCCCEEECCCCC
23954790
183MalonylationVWNLANCKLKTNHIG
HHHHCCCEEECCCCC
26320211
183UbiquitinationVWNLANCKLKTNHIG
HHHHCCCEEECCCCC
21890473
1852-HydroxyisobutyrylationNLANCKLKTNHIGHT
HHCCCEEECCCCCCC
-
185AcetylationNLANCKLKTNHIGHT
HHCCCEEECCCCCCC
26051181
185UbiquitinationNLANCKLKTNHIGHT
HHCCCEEECCCCCCC
20639865
186PhosphorylationLANCKLKTNHIGHTG
HCCCEEECCCCCCCC
28442448
192PhosphorylationKTNHIGHTGYLNTVT
ECCCCCCCCEEEEEE
28442448
194PhosphorylationNHIGHTGYLNTVTVS
CCCCCCCEEEEEEEC
15240704
197PhosphorylationGHTGYLNTVTVSPDG
CCCCEEEEEEECCCC
28442448
199PhosphorylationTGYLNTVTVSPDGSL
CCEEEEEEECCCCCC
28442448
201PhosphorylationYLNTVTVSPDGSLCA
EEEEEEECCCCCCCC
28442448
205PhosphorylationVTVSPDGSLCASGGK
EEECCCCCCCCCCCC
25693802
209PhosphorylationPDGSLCASGGKDGQA
CCCCCCCCCCCCCCE
25693802
2122-HydroxyisobutyrylationSLCASGGKDGQAMLW
CCCCCCCCCCCEEEE
-
212AcetylationSLCASGGKDGQAMLW
CCCCCCCCCCCEEEE
26051181
212UbiquitinationSLCASGGKDGQAMLW
CCCCCCCCCCCEEEE
-
217SulfoxidationGGKDGQAMLWDLNEG
CCCCCCEEEEECCCC
30846556
225AcetylationLWDLNEGKHLYTLDG
EEECCCCCEEEEECC
26051181
225UbiquitinationLWDLNEGKHLYTLDG
EEECCCCCEEEEECC
-
228PhosphorylationLNEGKHLYTLDGGDI
CCCCCEEEEECCCCC
12400005
229PhosphorylationNEGKHLYTLDGGDII
CCCCEEEEECCCCCE
28152594
240S-palmitoylationGDIINALCFSPNRYW
CCCEEEEEECCCCEE
29575903
242PhosphorylationIINALCFSPNRYWLC
CEEEEEECCCCEEEE
20873877
245MethylationALCFSPNRYWLCAAT
EEEECCCCEEEEEEC
115490043
246PhosphorylationLCFSPNRYWLCAATG
EEECCCCEEEEEECC
12400005
249S-nitrosocysteineSPNRYWLCAATGPSI
CCCCEEEEEECCCEE
-
255PhosphorylationLCAATGPSIKIWDLE
EEEECCCEEEEEECC
21712546
257AcetylationAATGPSIKIWDLEGK
EECCCEEEEEECCCC
26051181
257UbiquitinationAATGPSIKIWDLEGK
EECCCEEEEEECCCC
21906983
2642-HydroxyisobutyrylationKIWDLEGKIIVDELK
EEEECCCCEEHHHHH
-
264UbiquitinationKIWDLEGKIIVDELK
EEEECCCCEEHHHHH
21906983
271SumoylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
-
2712-HydroxyisobutyrylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
-
271AcetylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
26822725
271MethylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
66701141
271SuccinylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
23954790
271SumoylationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
-
271UbiquitinationKIIVDELKQEVISTS
CEEHHHHHHHHHCCC
21890473
276PhosphorylationELKQEVISTSSKAEP
HHHHHHHCCCCCCCC
25159151
277O-linked_GlycosylationLKQEVISTSSKAEPP
HHHHHHCCCCCCCCC
23301498
277PhosphorylationLKQEVISTSSKAEPP
HHHHHHCCCCCCCCC
25849741
278PhosphorylationKQEVISTSSKAEPPQ
HHHHHCCCCCCCCCC
29632367
279O-linked_GlycosylationQEVISTSSKAEPPQC
HHHHCCCCCCCCCCC
23301498
279PhosphorylationQEVISTSSKAEPPQC
HHHHCCCCCCCCCCC
29632367
280MethylationEVISTSSKAEPPQCT
HHHCCCCCCCCCCCC
-
280UbiquitinationEVISTSSKAEPPQCT
HHHCCCCCCCCCCCC
-
302PhosphorylationGQTLFAGYTDNLVRV
CCEEEEEECCCEEEE
18567578
313PhosphorylationLVRVWQVTIGTR---
EEEEEEEEECCC---
28102081
316PhosphorylationVWQVTIGTR------
EEEEEECCC------
25159151
317MethylationWQVTIGTR-------
EEEEECCC-------
115490067

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
50TPhosphorylationKinasePRKAA1Q13131
GPS
52YPhosphorylationKinaseABLP00519
PSP
52YPhosphorylationKinaseSRCP12931
PSP
52YPhosphorylationKinaseABL-FAMILY-GPS
194YPhosphorylationKinaseTYK2P29597
PSP
228YPhosphorylationKinaseSRCP12931
PSP
228YPhosphorylationKinaseSRC64-PhosphoELM
246YPhosphorylationKinaseSRCP12931
PSP
246YPhosphorylationKinaseSRC64-PhosphoELM
276SPhosphorylationKinaseVIRAL VACV B1 KINASE-Uniprot
277TPhosphorylationKinaseVIRAL VACV B1 KINASE-Uniprot
278SPhosphorylationKinaseVIRAL VACV B1 KINASE-Uniprot
279SPhosphorylationKinaseVIRAL VACV B1 KINASE-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RACK1_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 RACK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HABP4_HUMANHABP4physical
14699138
FAN_HUMANNSMAFphysical
12391233
T22D4_HUMANTSC22D4physical
16189514
PTPRM_HUMANPTPRMphysical
11801604
IF6_HUMANEIF6physical
14654845
TYK2_HUMANTYK2physical
12960323
JAK1_HUMANJAK1physical
12960323
STAT1_HUMANSTAT1physical
12960323
IL4RA_HUMANIL4Rphysical
12960323
IL2RB_HUMANIL2RBphysical
12960323
EPOR_HUMANEPORphysical
12960323
P73_HUMANTP73physical
12761493
RB_HUMANRB1physical
12761493
PTN_HUMANPTNphysical
16169070
KPCB_HUMANPRKCBphysical
10480917
KPCE_HUMANPRKCEphysical
11956211
NHRF1_HUMANSLC9A3R1physical
11956211
PTPRM_HUMANPTPRMphysical
11278757
PDE4D_HUMANPDE4Dphysical
10329691
FYN_HUMANFYNphysical
12524444
NMDE2_HUMANGRIN2Bphysical
12524444
PLCG1_HUMANPLCG1physical
8290562
STAT1_HUMANSTAT1physical
11301323
LAR4B_HUMANLARP4Bphysical
12388589
PABP1_HUMANPABPC1physical
12388589
ATRAP_HUMANAGTRAPphysical
11733189
SRC_HUMANSRCphysical
9584165
PDE4D_HUMANPDE4Dphysical
11516626
RASA3_HUMANRASA3physical
11350068
RASA1_HUMANRASA1physical
11350068
SAT1_HUMANSAT1physical
17875644
H31_HUMANHIST1H3Aphysical
20410295
RACK1_HUMANGNB2L1physical
17965024
ELOC_HUMANTCEB1physical
19855191
FEM1B_HUMANFEM1Bphysical
19855191
ELOC_HUMANTCEB1physical
17244529
ELOB_HUMANTCEB2physical
17244529
HIF1A_HUMANHIF1Aphysical
17244529
VHL_HUMANVHLphysical
20871634
IGF1R_HUMANIGF1Rphysical
20871634
P63_HUMANTP63physical
15467455
GBB1_HUMANGNB1physical
22065575
GBG2_HUMANGNG2physical
22065575
DYL1_HUMANDYNLL1physical
18420585
B2L11_HUMANBCL2L11physical
18420585
CUL2_HUMANCUL2physical
18420585
GBB1_HUMANGNB1physical
18596232
SRC_HUMANSRCphysical
18596232
KPCB_HUMANPRKCBphysical
18596232
KCAB1_HUMANKCNAB1physical
22547057
KCNA5_HUMANKCNA5physical
22547057
RL13_HUMANRPL13physical
22939629
RL4_HUMANRPL4physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RL27A_HUMANRPL27Aphysical
22939629
RL15_HUMANRPL15physical
22939629
RL21_HUMANRPL21physical
22939629
RL19_HUMANRPL19physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RS2_HUMANRPS2physical
22939629
TIAR_HUMANTIAL1physical
22939629
RS25_HUMANRPS25physical
22939629
CHERP_HUMANCHERPphysical
22365833
PRP31_HUMANPRPF31physical
22365833
RED_HUMANIKphysical
22365833
WDR83_HUMANWDR83physical
22365833
DGC14_HUMANDGCR14physical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
FBXW2_HUMANFBXW2physical
23651062
LAR4B_HUMANLARP4Bphysical
21988832
RHOA_HUMANRHOAphysical
21988832
PTOV1_HUMANPTOV1physical
23455324
RS6_HUMANRPS6physical
23455324
EIF3E_HUMANEIF3Ephysical
22863883
RSSA_HUMANRPSAphysical
22863883
RS12_HUMANRPS12physical
22863883
RS13_HUMANRPS13physical
22863883
RS16_HUMANRPS16physical
22863883
RS18_HUMANRPS18physical
22863883
RS20_HUMANRPS20physical
22863883
RS27_HUMANRPS27physical
22863883
RS3A_HUMANRPS3Aphysical
22863883
RS3_HUMANRPS3physical
22863883
RS8_HUMANRPS8physical
22863883
RS9_HUMANRPS9physical
22863883
HNRPQ_HUMANSYNCRIPphysical
22863883
TRI45_HUMANTRIM45physical
24681954
KPCB_HUMANPRKCBphysical
24681954
LAR4B_HUMANLARP4Bphysical
25416956
MKRN2_HUMANMKRN2physical
25416956
SYN2_HUMANSYN2physical
22558273
JAK1_HUMANJAK1physical
22558273
LARP4_HUMANLARP4physical
26186194
TNR6C_HUMANTNRC6Cphysical
26186194
LAR4B_HUMANLARP4Bphysical
26186194
KI67_HUMANMKI67physical
26186194
ZCHC3_HUMANZCCHC3physical
26186194
RIOK3_HUMANRIOK3physical
26186194
CAB39_HUMANCAB39physical
26344197
CCD58_HUMANCCDC58physical
26344197
FUBP1_HUMANFUBP1physical
26344197
LSM12_HUMANLSM12physical
26344197
PCBP1_HUMANPCBP1physical
26344197
PCBP2_HUMANPCBP2physical
26344197
INAR1_HUMANIFNAR1physical
12960323
TNR6C_HUMANTNRC6Cphysical
28514442
LAR4B_HUMANLARP4Bphysical
28514442
KI67_HUMANMKI67physical
28514442
ZCHC3_HUMANZCCHC3physical
28514442
PDE4D_HUMANPDE4Dphysical
12193273
EED_HUMANEEDphysical
20080539

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RACK1_HUMAN

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Related Literatures of Post-Translational Modification

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