SRP68_HUMAN - dbPTM
SRP68_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP68_HUMAN
UniProt AC Q9UHB9
Protein Name Signal recognition particle subunit SRP68
Gene Name SRP68
Organism Homo sapiens (Human).
Sequence Length 627
Subcellular Localization Cytoplasm. Nucleus, nucleolus.
Protein Description Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function..
Protein Sequence MAAEKQVPGGGGGGGSGGGGGSGGGGSGGGRGAGGEENKENERPSAGSKANKEFGDSLSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTLNFKMGNRHKFTGKKVTEELLTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSRLRKAVKHAEELERLCESNRVDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIYEKLASAFTEEQAVLYNQRVEEISPNIRYCAYNIGDQSAINELMQMRLRSGGTEGLLAEKLEALITQTRAKQAATMSEVEWRGRTVPVKIDKVRIFLLGLADNEAAIVQAESEETKERLFESMLSECRDAIQVVREELKPDQKQRDYILEGEPGKVSNLQYLHSYLTYIKLSTAIKRNENMAKGLQRALLQQQPEDDSKRSPRPQDLIRLYDIILQNLVELLQLPGLEEDKAFQKEIGLKTLVFKAYRCFFIAQSYVLVKKWSEALVLYDRVLKYANEVNSDAGAFKNSLKDLPDVQELITQVRSEKCSLQAAAILDANDAHQTETSSSQVKDNKPLVERFETFCLDPSLVTKQANLVHFPPGFQPIPCKPLFFDLALNHVAFPPLEDKLEQKTKSGLTGYIKGIFGFRS
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
5Acetylation---MAAEKQVPGGGG
---CCCCCCCCCCCC
52.4423236377
16PhosphorylationGGGGGGGSGGGGGSG
CCCCCCCCCCCCCCC
37.2229255136
17UbiquitinationGGGGGGSGGGGGSGG
CCCCCCCCCCCCCCC
41.8822817900
21UbiquitinationGGSGGGGGSGGGGSG
CCCCCCCCCCCCCCC
26.7922817900
22PhosphorylationGSGGGGGSGGGGSGG
CCCCCCCCCCCCCCC
37.2229255136
27PhosphorylationGGSGGGGSGGGRGAG
CCCCCCCCCCCCCCC
37.2229255136
31MethylationGGGSGGGRGAGGEEN
CCCCCCCCCCCCCCC
34.75115917793
33UbiquitinationGSGGGRGAGGEENKE
CCCCCCCCCCCCCCC
22.8122817900
39UbiquitinationGAGGEENKENERPSA
CCCCCCCCCCCCCCC
66.2622817900
39 (in isoform 1)Ubiquitination-66.2621890473
39 (in isoform 2)Ubiquitination-66.2621890473
48PhosphorylationNERPSAGSKANKEFG
CCCCCCCHHHHHHHH
28.4522817900
49UbiquitinationERPSAGSKANKEFGD
CCCCCCHHHHHHHHC
55.8721906983
49 (in isoform 1)Ubiquitination-55.8721890473
49 (in isoform 2)Ubiquitination-55.8721890473
52UbiquitinationSAGSKANKEFGDSLS
CCCHHHHHHHHCHHH
60.3222817900
61UbiquitinationFGDSLSLEILQIIKE
HHCHHHHHHHHHHHH
37.9724816145
67UbiquitinationLEILQIIKESQQQHG
HHHHHHHHHHHHHHC
53.60-
77UbiquitinationQQQHGLRHGDFQRYR
HHHHCCCCCCHHHHH
45.2621963094
96UbiquitinationRRQRRLRKTLNFKMG
HHHHHHHHHHCCCCC
63.0524816145
1012-HydroxyisobutyrylationLRKTLNFKMGNRHKF
HHHHHCCCCCCCCCC
44.84-
104UbiquitinationTLNFKMGNRHKFTGK
HHCCCCCCCCCCCCC
39.1121890473
107UbiquitinationFKMGNRHKFTGKKVT
CCCCCCCCCCCCCCH
41.1922817900
111UbiquitinationNRHKFTGKKVTEELL
CCCCCCCCCCHHHHH
40.8022817900
112UbiquitinationRHKFTGKKVTEELLT
CCCCCCCCCHHHHHC
56.5922817900
112 (in isoform 1)Ubiquitination-56.5921890473
112 (in isoform 2)Ubiquitination-56.5921890473
113AcetylationHKFTGKKVTEELLTD
CCCCCCCCHHHHHCC
10.4319608861
113UbiquitinationHKFTGKKVTEELLTD
CCCCCCCCHHHHHCC
10.4323000965
118UbiquitinationKKVTEELLTDNRYLL
CCCHHHHHCCCCEEE
6.8123000965
123UbiquitinationELLTDNRYLLLVLMD
HHHCCCCEEEHHHHC
14.1423000965
126UbiquitinationTDNRYLLLVLMDAER
CCCCEEEHHHHCHHH
2.2829967540
142UbiquitinationWSYAMQLKQEANTEP
HHHHHHHHHHHCCCH
29.2421890473
142UbiquitinationWSYAMQLKQEANTEP
HHHHHHHHHHHCCCH
29.2421890473
142UbiquitinationWSYAMQLKQEANTEP
HHHHHHHHHHHCCCH
29.2421963094
142 (in isoform 1)Ubiquitination-29.2421890473
142 (in isoform 2)Ubiquitination-29.2421890473
152UbiquitinationANTEPRKRFHLLSRL
HCCCHHHHHHHHHHH
26.0422817900
161UbiquitinationHLLSRLRKAVKHAEE
HHHHHHHHHHHHHHH
63.2224816145
164AcetylationSRLRKAVKHAEELER
HHHHHHHHHHHHHHH
41.7927452117
164UbiquitinationSRLRKAVKHAEELER
HHHHHHHHHHHHHHH
41.7929967540
165UbiquitinationRLRKAVKHAEELERL
HHHHHHHHHHHHHHH
31.6027667366
167UbiquitinationRKAVKHAEELERLCE
HHHHHHHHHHHHHHH
63.9321890473
169UbiquitinationAVKHAEELERLCESN
HHHHHHHHHHHHHHC
3.3232015554
177UbiquitinationERLCESNRVDAKTKL
HHHHHHCCCCHHHHH
36.6523000965
182UbiquitinationSNRVDAKTKLEAQAY
HCCCCHHHHHHHHHH
42.4523000965
185UbiquitinationVDAKTKLEAQAYTAY
CCHHHHHHHHHHHHH
40.0521963094
205UbiquitinationRFEHQEWKAAIEAFN
HCCCHHHHHHHHHHH
27.4721890473
205UbiquitinationRFEHQEWKAAIEAFN
HCCCHHHHHHHHHHH
27.4721890473
205AcetylationRFEHQEWKAAIEAFN
HCCCHHHHHHHHHHH
27.4725953088
205UbiquitinationRFEHQEWKAAIEAFN
HCCCHHHHHHHHHHH
27.4721963094
205 (in isoform 1)Ubiquitination-27.4721890473
205 (in isoform 2)Ubiquitination-27.4721890473
210UbiquitinationEWKAAIEAFNKCKTI
HHHHHHHHHHHHHHH
13.7529967540
2132-HydroxyisobutyrylationAAIEAFNKCKTIYEK
HHHHHHHHHHHHHHH
30.56-
213AcetylationAAIEAFNKCKTIYEK
HHHHHHHHHHHHHHH
30.5625953088
213UbiquitinationAAIEAFNKCKTIYEK
HHHHHHHHHHHHHHH
30.5621963094
215UbiquitinationIEAFNKCKTIYEKLA
HHHHHHHHHHHHHHH
39.3023000965
220UbiquitinationKCKTIYEKLASAFTE
HHHHHHHHHHHCCCH
32.1721890473
220UbiquitinationKCKTIYEKLASAFTE
HHHHHHHHHHHCCCH
32.1721890473
220UbiquitinationKCKTIYEKLASAFTE
HHHHHHHHHHHCCCH
32.1723000965
220 (in isoform 1)Ubiquitination-32.1721890473
220 (in isoform 2)Ubiquitination-32.1721890473
233PhosphorylationTEEQAVLYNQRVEEI
CHHHHHHHHHHHHHC
11.5828152594
239UbiquitinationLYNQRVEEISPNIRY
HHHHHHHHCCCCCCE
46.0023000965
241PhosphorylationNQRVEEISPNIRYCA
HHHHHHCCCCCCEEH
18.3825159151
247GlutathionylationISPNIRYCAYNIGDQ
CCCCCCEEHHHCCCH
2.0222555962
250UbiquitinationNIRYCAYNIGDQSAI
CCCEEHHHCCCHHHH
17.1622817900
267PhosphorylationLMQMRLRSGGTEGLL
HHHHHHHCCCCCHHH
46.2830266825
268UbiquitinationMQMRLRSGGTEGLLA
HHHHHHCCCCCHHHH
40.3829967540
270PhosphorylationMRLRSGGTEGLLAEK
HHHHCCCCCHHHHHH
30.3330266825
271UbiquitinationRLRSGGTEGLLAEKL
HHHCCCCCHHHHHHH
51.6324816145
273UbiquitinationRSGGTEGLLAEKLEA
HCCCCCHHHHHHHHH
3.1429967540
277UbiquitinationTEGLLAEKLEALITQ
CCHHHHHHHHHHHHH
46.1221890473
277UbiquitinationTEGLLAEKLEALITQ
CCHHHHHHHHHHHHH
46.1223000965
277 (in isoform 1)Ubiquitination-46.1221890473
283PhosphorylationEKLEALITQTRAKQA
HHHHHHHHHHHHHHC
25.4121406692
285PhosphorylationLEALITQTRAKQAAT
HHHHHHHHHHHHCCC
24.7621406692
288UbiquitinationLITQTRAKQAATMSE
HHHHHHHHHCCCCCC
36.8622817900
288 (in isoform 1)Ubiquitination-36.8621890473
294PhosphorylationAKQAATMSEVEWRGR
HHHCCCCCCCEECCC
33.85-
295UbiquitinationKQAATMSEVEWRGRT
HHCCCCCCCEECCCE
33.3622817900
302 (in isoform 2)Ubiquitination-31.8021890473
3062-HydroxyisobutyrylationRGRTVPVKIDKVRIF
CCCEECEEECEEEEE
38.83-
306UbiquitinationRGRTVPVKIDKVRIF
CCCEECEEECEEEEE
38.8329967540
309UbiquitinationTVPVKIDKVRIFLLG
EECEEECEEEEEEEE
36.5724816145
318UbiquitinationRIFLLGLADNEAAIV
EEEEEECCCCHHHHH
18.7822817900
322UbiquitinationLGLADNEAAIVQAES
EECCCCHHHHHHCCC
14.5622817900
329 (in isoform 2)Ubiquitination-43.6921890473
333UbiquitinationQAESEETKERLFESM
HCCCHHHHHHHHHHH
44.0821906983
333 (in isoform 1)Ubiquitination-44.0821890473
333 (in isoform 2)Phosphorylation-44.0827642862
334UbiquitinationAESEETKERLFESML
CCCHHHHHHHHHHHH
63.1322817900
339PhosphorylationTKERLFESMLSECRD
HHHHHHHHHHHHHHH
20.07-
341 (in isoform 2)Ubiquitination-5.6221890473
344GlutathionylationFESMLSECRDAIQVV
HHHHHHHHHHHHHHH
4.2422555962
356AcetylationQVVREELKPDQKQRD
HHHHHHCCCCHHHHC
50.2426051181
356UbiquitinationQVVREELKPDQKQRD
HHHHHHCCCCHHHHC
50.2422817900
360UbiquitinationEELKPDQKQRDYILE
HHCCCCHHHHCHHHC
55.4721906983
360 (in isoform 1)Ubiquitination-55.4721890473
362UbiquitinationLKPDQKQRDYILEGE
CCCCHHHHCHHHCCC
45.8224816145
364NitrationPDQKQRDYILEGEPG
CCHHHHCHHHCCCCC
15.03-
364PhosphorylationPDQKQRDYILEGEPG
CCHHHHCHHHCCCCC
15.0328796482
372UbiquitinationILEGEPGKVSNLQYL
HHCCCCCCCCCHHHH
53.8822817900
372 (in isoform 1)Ubiquitination-53.8821890473
378UbiquitinationGKVSNLQYLHSYLTY
CCCCCHHHHHHHHHH
15.0021963094
381PhosphorylationSNLQYLHSYLTYIKL
CCHHHHHHHHHHHHH
21.1728152594
382PhosphorylationNLQYLHSYLTYIKLS
CHHHHHHHHHHHHHH
7.7228152594
384PhosphorylationQYLHSYLTYIKLSTA
HHHHHHHHHHHHHHH
18.2428152594
385PhosphorylationYLHSYLTYIKLSTAI
HHHHHHHHHHHHHHH
8.0828152594
385 (in isoform 2)Ubiquitination-8.0821890473
400AcetylationKRNENMAKGLQRALL
HCCHHHHHHHHHHHH
49.7627452117
400UbiquitinationKRNENMAKGLQRALL
HCCHHHHHHHHHHHH
49.7624816145
414AcetylationLQQQPEDDSKRSPRP
HHCCCCCCCCCCCCH
55.1619608861
414UbiquitinationLQQQPEDDSKRSPRP
HHCCCCCCCCCCCCH
55.1623000965
415PhosphorylationQQQPEDDSKRSPRPQ
HCCCCCCCCCCCCHH
42.1429255136
416AcetylationQQPEDDSKRSPRPQD
CCCCCCCCCCCCHHH
64.98156451
416UbiquitinationQQPEDDSKRSPRPQD
CCCCCCCCCCCCHHH
64.9821906983
416 (in isoform 1)Ubiquitination-64.9821890473
418PhosphorylationPEDDSKRSPRPQDLI
CCCCCCCCCCHHHHH
29.0620873877
419UbiquitinationEDDSKRSPRPQDLIR
CCCCCCCCCHHHHHH
56.8823000965
424UbiquitinationRSPRPQDLIRLYDII
CCCCHHHHHHHHHHH
1.7523000965
426 (in isoform 2)Ubiquitination-34.2021890473
452AcetylationEEDKAFQKEIGLKTL
CCCHHHHHHHCHHHH
44.8619608861
452UbiquitinationEEDKAFQKEIGLKTL
CCCHHHHHHHCHHHH
44.8623000965
453UbiquitinationEDKAFQKEIGLKTLV
CCHHHHHHHCHHHHH
31.3522817900
4572-HydroxyisobutyrylationFQKEIGLKTLVFKAY
HHHHHCHHHHHHHHH
34.30-
457UbiquitinationFQKEIGLKTLVFKAY
HHHHHCHHHHHHHHH
34.3023000965
457 (in isoform 1)Ubiquitination-34.3021890473
460 (in isoform 2)Ubiquitination-5.8321890473
462UbiquitinationGLKTLVFKAYRCFFI
CHHHHHHHHHHHHHH
36.7123000965
466UbiquitinationLVFKAYRCFFIAQSY
HHHHHHHHHHHHHHH
1.8127667366
470UbiquitinationAYRCFFIAQSYVLVK
HHHHHHHHHHHHHHH
6.2632015554
473UbiquitinationCFFIAQSYVLVKKWS
HHHHHHHHHHHHHHH
5.9221890473
473 (in isoform 2)Ubiquitination-5.9221890473
477UbiquitinationAQSYVLVKKWSEALV
HHHHHHHHHHHHHHH
44.35-
477 (in isoform 2)Ubiquitination-44.3521890473
486UbiquitinationWSEALVLYDRVLKYA
HHHHHHHHHHHHHHH
8.3321963094
491AcetylationVLYDRVLKYANEVNS
HHHHHHHHHHHHHCC
39.1923236377
491MalonylationVLYDRVLKYANEVNS
HHHHHHHHHHHHHCC
39.1926320211
491UbiquitinationVLYDRVLKYANEVNS
HHHHHHHHHHHHHCC
39.1921906983
491 (in isoform 1)Ubiquitination-39.1921890473
504UbiquitinationNSDAGAFKNSLKDLP
CCCCHHHHHHHHCCC
45.1321890473
504UbiquitinationNSDAGAFKNSLKDLP
CCCCHHHHHHHHCCC
45.1327667366
504 (in isoform 1)Ubiquitination-45.1321890473
508AcetylationGAFKNSLKDLPDVQE
HHHHHHHHCCCCHHH
57.9726051181
508UbiquitinationGAFKNSLKDLPDVQE
HHHHHHHHCCCCHHH
57.9722817900
508 (in isoform 1)Ubiquitination-57.9721890473
511UbiquitinationKNSLKDLPDVQELIT
HHHHHCCCCHHHHHH
50.2729967540
514UbiquitinationLKDLPDVQELITQVR
HHCCCCHHHHHHHHH
47.3521963094
518PhosphorylationPDVQELITQVRSEKC
CCHHHHHHHHHHHCC
33.3720068231
524UbiquitinationITQVRSEKCSLQAAA
HHHHHHHCCCCCHHH
30.3021963094
541PhosphorylationDANDAHQTETSSSQV
CCCCCCCCCCCCHHC
31.2227251275
543PhosphorylationNDAHQTETSSSQVKD
CCCCCCCCCCHHCCC
36.9827251275
544PhosphorylationDAHQTETSSSQVKDN
CCCCCCCCCHHCCCC
23.0427251275
545PhosphorylationAHQTETSSSQVKDNK
CCCCCCCCHHCCCCC
32.0127251275
546PhosphorylationHQTETSSSQVKDNKP
CCCCCCCHHCCCCCC
38.4727251275
549AcetylationETSSSQVKDNKPLVE
CCCCHHCCCCCCHHH
48.2025953088
549UbiquitinationETSSSQVKDNKPLVE
CCCCHHCCCCCCHHH
48.2029967540
552UbiquitinationSSQVKDNKPLVERFE
CHHCCCCCCHHHHHH
50.2721963094
562S-nitrosocysteineVERFETFCLDPSLVT
HHHHHHEECCHHHCC
5.71-
562GlutathionylationVERFETFCLDPSLVT
HHHHHHEECCHHHCC
5.7122555962
562S-nitrosylationVERFETFCLDPSLVT
HHHHHHEECCHHHCC
5.7119483679
574UbiquitinationLVTKQANLVHFPPGF
HCCCCCCCCCCCCCC
3.3829967540
587 (in isoform 2)Phosphorylation-39.1327642862
611PhosphorylationEDKLEQKTKSGLTGY
HHHHHHHHHCCHHHH
30.0929978859
612UbiquitinationDKLEQKTKSGLTGYI
HHHHHHHHCCHHHHH
49.9529967540
613PhosphorylationKLEQKTKSGLTGYIK
HHHHHHHCCHHHHHH
44.2429978859
616PhosphorylationQKTKSGLTGYIKGIF
HHHHCCHHHHHHHHC
31.3129978859
618PhosphorylationTKSGLTGYIKGIFGF
HHCCHHHHHHHHCCC
8.3329978859
627PhosphorylationKGIFGFRS-------
HHHCCCCC-------
42.1722617229

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 SRP68_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP68_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 SRP68_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRP72_HUMANSRP72physical
22939629
KI21A_HUMANKIF21Aphysical
22863883
RL31_HUMANRPL31physical
26344197
SRP54_HUMANSRP54physical
28514442
SRP19_HUMANSRP19physical
28514442
SRP72_HUMANSRP72physical
28514442
FZR1_HUMANFZR1physical
28514442
SRP14_HUMANSRP14physical
28514442
RL26L_HUMANRPL26L1physical
28514442
CDC27_HUMANCDC27physical
28514442
PUM3_HUMANKIAA0020physical
28514442
NOG1_HUMANGTPBP4physical
28514442
NOP2_HUMANNOP2physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
RBM28_HUMANRBM28physical
28514442
RL3_HUMANRPL3physical
28514442
EBP2_HUMANEBNA1BP2physical
28514442
DDX31_HUMANDDX31physical
28514442
TRAP1_HUMANTRAP1physical
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 SRP68_HUMAN

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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-452, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-627, 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-241, 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-48, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-618, AND MASSSPECTROMETRY.

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