SRP14_HUMAN - dbPTM
SRP14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP14_HUMAN
UniProt AC P37108
Protein Name Signal recognition particle 14 kDa protein
Gene Name SRP14
Organism Homo sapiens (Human).
Sequence Length 136
Subcellular Localization Cytoplasm.
Protein Description Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding..
Protein Sequence MVLLESEQFLTELTRLFQKCRTSGSVYITLKKYDGRTKPIPKKGTVEGFEPADNKCLLRATDGKKKISTVVSSKEVNKFQMAYSNLLRANMDGLKKRDKKNKTKKTKAAAAAAAAAPAAAATAPTTAATTAATAAQ
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--MVLLESEQFLTEL
--CCCCCHHHHHHHH
36.3520071362
19UbiquitinationELTRLFQKCRTSGSV
HHHHHHHHHCCCCCE
20.5327667366
19AcetylationELTRLFQKCRTSGSV
HHHHHHHHHCCCCCE
20.5326051181
22PhosphorylationRLFQKCRTSGSVYIT
HHHHHHCCCCCEEEE
47.0828331001
23PhosphorylationLFQKCRTSGSVYITL
HHHHHCCCCCEEEEE
15.0928442448
25PhosphorylationQKCRTSGSVYITLKK
HHHCCCCCEEEEEEE
16.1228152594
26UbiquitinationKCRTSGSVYITLKKY
HHCCCCCEEEEEEEE
4.5823000965
27PhosphorylationCRTSGSVYITLKKYD
HCCCCCEEEEEEEEC
7.0125159151
29PhosphorylationTSGSVYITLKKYDGR
CCCCEEEEEEEECCC
18.1628152594
30UbiquitinationSGSVYITLKKYDGRT
CCCEEEEEEEECCCC
3.0623000965
31UbiquitinationGSVYITLKKYDGRTK
CCEEEEEEEECCCCC
40.4133845483
31AcetylationGSVYITLKKYDGRTK
CCEEEEEEEECCCCC
40.4125953088
312-HydroxyisobutyrylationGSVYITLKKYDGRTK
CCEEEEEEEECCCCC
40.41-
33PhosphorylationVYITLKKYDGRTKPI
EEEEEEEECCCCCCC
23.2624719451
37PhosphorylationLKKYDGRTKPIPKKG
EEEECCCCCCCCCCC
46.8624719451
38UbiquitinationKKYDGRTKPIPKKGT
EEECCCCCCCCCCCE
39.3222817900
42UbiquitinationGRTKPIPKKGTVEGF
CCCCCCCCCCEECCC
65.6322817900
43AcetylationRTKPIPKKGTVEGFE
CCCCCCCCCEECCCC
55.2326051181
43UbiquitinationRTKPIPKKGTVEGFE
CCCCCCCCCEECCCC
55.2321906983
45PhosphorylationKPIPKKGTVEGFEPA
CCCCCCCEECCCCCC
25.0228985074
47UbiquitinationIPKKGTVEGFEPADN
CCCCCEECCCCCCCC
58.9933845483
54UbiquitinationEGFEPADNKCLLRAT
CCCCCCCCEEEEEEC
38.7623503661
55AcetylationGFEPADNKCLLRATD
CCCCCCCEEEEEECC
27.1426822725
552-HydroxyisobutyrylationGFEPADNKCLLRATD
CCCCCCCEEEEEECC
27.14-
55MalonylationGFEPADNKCLLRATD
CCCCCCCEEEEEECC
27.1430639696
55UbiquitinationGFEPADNKCLLRATD
CCCCCCCEEEEEECC
27.1432015554
56GlutathionylationFEPADNKCLLRATDG
CCCCCCEEEEEECCC
5.6222555962
56UbiquitinationFEPADNKCLLRATDG
CCCCCCEEEEEECCC
5.6223503661
57UbiquitinationEPADNKCLLRATDGK
CCCCCEEEEEECCCC
3.7623503661
59UbiquitinationADNKCLLRATDGKKK
CCCEEEEEECCCCCE
23.6121963094
64UbiquitinationLLRATDGKKKISTVV
EEEECCCCCEEEEEE
54.4229967540
65UbiquitinationLRATDGKKKISTVVS
EEECCCCCEEEEEEC
61.9529967540
66UbiquitinationRATDGKKKISTVVSS
EECCCCCEEEEEECH
45.4333845483
68PhosphorylationTDGKKKISTVVSSKE
CCCCCEEEEEECHHH
24.8328674419
74MalonylationISTVVSSKEVNKFQM
EEEEECHHHHCHHHH
59.1726320211
74NeddylationISTVVSSKEVNKFQM
EEEEECHHHHCHHHH
59.1732015554
742-HydroxyisobutyrylationISTVVSSKEVNKFQM
EEEEECHHHHCHHHH
59.17-
74AcetylationISTVVSSKEVNKFQM
EEEEECHHHHCHHHH
59.1726051181
74UbiquitinationISTVVSSKEVNKFQM
EEEEECHHHHCHHHH
59.1723000965
78AcetylationVSSKEVNKFQMAYSN
ECHHHHCHHHHHHHH
41.9925953088
78UbiquitinationVSSKEVNKFQMAYSN
ECHHHHCHHHHHHHH
41.9923000965
81SulfoxidationKEVNKFQMAYSNLLR
HHHCHHHHHHHHHHH
4.2130846556
83PhosphorylationVNKFQMAYSNLLRAN
HCHHHHHHHHHHHHC
7.8629523821
84PhosphorylationNKFQMAYSNLLRANM
CHHHHHHHHHHHHCH
16.0929523821
95UbiquitinationRANMDGLKKRDKKNK
HHCHHHHHHHHHCCC
51.8233845483
102UbiquitinationKKRDKKNKTKKTKAA
HHHHHCCCCHHHHHH
71.2823503661
104UbiquitinationRDKKNKTKKTKAAAA
HHHCCCCHHHHHHHH
61.1223503661
105UbiquitinationDKKNKTKKTKAAAAA
HHCCCCHHHHHHHHH
61.5623503661
105MethylationDKKNKTKKTKAAAAA
HHCCCCHHHHHHHHH
61.56-
106PhosphorylationKKNKTKKTKAAAAAA
HCCCCHHHHHHHHHH
27.7222964224
107UbiquitinationKNKTKKTKAAAAAAA
CCCCHHHHHHHHHHH
44.9321963094
107MethylationKNKTKKTKAAAAAAA
CCCCHHHHHHHHHHH
44.9323644510
122PhosphorylationAAPAAAATAPTTAAT
HHHHHHHCCCCHHHH
28.5725332170
125PhosphorylationAAAATAPTTAATTAA
HHHHCCCCHHHHHHH
26.9725332170
126PhosphorylationAAATAPTTAATTAAT
HHHCCCCHHHHHHHH
17.1525332170
133O-linked_GlycosylationTAATTAATAAQ----
HHHHHHHHHHC----
21.7728510447
133PhosphorylationTAATTAATAAQ----
HHHHHHHHHHC----
21.7724532841

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 SRP14_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP14_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 SRP14_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRRM2_HUMANSRRM2physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
AN32A_HUMANANP32Aphysical
22863883
IF4A3_HUMANEIF4A3physical
22863883
IPO9_HUMANIPO9physical
22863883
PDLI5_HUMANPDLIM5physical
22863883
SAE1_HUMANSAE1physical
22863883
SAE2_HUMANUBA2physical
22863883
MK67I_HUMANNIFKphysical
26344197
NOLC1_HUMANNOLC1physical
26344197
SRP68_HUMANSRP68physical
26344197
SRP72_HUMANSRP72physical
26344197

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 SRP14_HUMAN

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Related Literatures of Post-Translational Modification

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