CIRBP_HUMAN - dbPTM
CIRBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CIRBP_HUMAN
UniProt AC Q14011
Protein Name Cold-inducible RNA-binding protein
Gene Name CIRBP
Organism Homo sapiens (Human).
Sequence Length 172
Subcellular Localization Nucleus, nucleoplasm . Cytoplasm . Translocates from the nucleus to the cytoplasm after exposure to UV radiation. Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks.
Protein Description Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed..
Protein Sequence MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE
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
14PhosphorylationKLFVGGLSFDTNEQS
CEEECCEECCCCHHH
25.0927732954
17PhosphorylationVGGLSFDTNEQSLEQ
ECCEECCCCHHHHHH
38.3527732954
21PhosphorylationSFDTNEQSLEQVFSK
ECCCCHHHHHHHHHH
27.9127732954
27PhosphorylationQSLEQVFSKYGQISE
HHHHHHHHHHCCEEE
26.5528122231
29PhosphorylationLEQVFSKYGQISEVV
HHHHHHHHCCEEEEE
17.0528152594
31UbiquitinationQVFSKYGQISEVVVV
HHHHHHCCEEEEEEE
32.70-
33PhosphorylationFSKYGQISEVVVVKD
HHHHCCEEEEEEEEC
19.2228152594
43PhosphorylationVVVKDRETQRSRGFG
EEEECCCCCHHCCEE
30.12-
47MethylationDRETQRSRGFGFVTF
CCCCCHHCCEEEEEE
46.80-
70AcetylationAMMAMNGKSVDGRQI
HHHHHCCEECCCCEE
42.15-
70AcetylationAMMAMNGKSVDGRQI
HHHHHCCEECCCCEE
42.1526051181
71PhosphorylationMMAMNGKSVDGRQIR
HHHHCCEECCCCEEE
27.1720068231
84UbiquitinationIRVDQAGKSSDNRSR
EEEECCCCCCCCCCC
50.2121906983
94MethylationDNRSRGYRGGSAGGR
CCCCCCCCCCCCCCC
45.91-
94DimethylationDNRSRGYRGGSAGGR
CCCCCCCCCCCCCCC
45.91-
101MethylationRGGSAGGRGFFRGGR
CCCCCCCCCCCCCCC
37.52-
101DimethylationRGGSAGGRGFFRGGR
CCCCCCCCCCCCCCC
37.52-
105MethylationAGGRGFFRGGRGRGR
CCCCCCCCCCCCCCC
44.38-
105DimethylationAGGRGFFRGGRGRGR
CCCCCCCCCCCCCCC
44.38-
110 (in isoform 3)Phosphorylation-30.2121815630
116MethylationGRGRGFSRGGGDRGY
CCCCCCCCCCCCCCC
45.58-
121MethylationFSRGGGDRGYGGNRF
CCCCCCCCCCCCCCC
43.43-
123PhosphorylationRGGGDRGYGGNRFES
CCCCCCCCCCCCCCC
23.82-
127MethylationDRGYGGNRFESRSGG
CCCCCCCCCCCCCCC
39.73-
129 (in isoform 2)Phosphorylation-41.8421815630
130PhosphorylationYGGNRFESRSGGYGG
CCCCCCCCCCCCCCC
29.0924670416
131MethylationGGNRFESRSGGYGGS
CCCCCCCCCCCCCCC
31.93-
132PhosphorylationGNRFESRSGGYGGSR
CCCCCCCCCCCCCCC
45.9421945579
135PhosphorylationFESRSGGYGGSRDYY
CCCCCCCCCCCCCCC
23.1021945579
138PhosphorylationRSGGYGGSRDYYSSR
CCCCCCCCCCCCCCC
20.0221945579
139MethylationSGGYGGSRDYYSSRS
CCCCCCCCCCCCCCC
38.94-
141PhosphorylationGYGGSRDYYSSRSQS
CCCCCCCCCCCCCCC
12.2521945579
142PhosphorylationYGGSRDYYSSRSQSG
CCCCCCCCCCCCCCC
12.4021945579
143PhosphorylationGGSRDYYSSRSQSGG
CCCCCCCCCCCCCCC
17.0421945579
144PhosphorylationGSRDYYSSRSQSGGY
CCCCCCCCCCCCCCC
21.6021945579
145MethylationSRDYYSSRSQSGGYS
CCCCCCCCCCCCCCC
32.54-
146PhosphorylationRDYYSSRSQSGGYSD
CCCCCCCCCCCCCCC
30.5522617229
148PhosphorylationYYSSRSQSGGYSDRS
CCCCCCCCCCCCCCC
35.1222617229
151PhosphorylationSRSQSGGYSDRSSGG
CCCCCCCCCCCCCCC
15.7828450419
152PhosphorylationRSQSGGYSDRSSGGS
CCCCCCCCCCCCCCC
29.8028450419
154MethylationQSGGYSDRSSGGSYR
CCCCCCCCCCCCCCC
27.12-
155PhosphorylationSGGYSDRSSGGSYRD
CCCCCCCCCCCCCCC
38.0223401153
156PhosphorylationGGYSDRSSGGSYRDS
CCCCCCCCCCCCCCC
48.3321712546
159PhosphorylationSDRSSGGSYRDSYDS
CCCCCCCCCCCCCCC
22.1123401153
160PhosphorylationDRSSGGSYRDSYDSY
CCCCCCCCCCCCCCC
23.0130177828
163PhosphorylationSGGSYRDSYDSYATH
CCCCCCCCCCCCCCC
23.1122617229
164PhosphorylationGGSYRDSYDSYATHN
CCCCCCCCCCCCCCC
17.1330177828
166PhosphorylationSYRDSYDSYATHNE-
CCCCCCCCCCCCCC-
14.4023898821
167PhosphorylationYRDSYDSYATHNE--
CCCCCCCCCCCCC--
16.7827273156
169PhosphorylationDSYDSYATHNE----
CCCCCCCCCCC----
19.5928152594

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 CIRBP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CIRBP_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 CIRBP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBMX_HUMANRBMXphysical
16189514
A4_HUMANAPPphysical
21832049
SF01_HUMANSF1physical
22939629
RTN4_HUMANRTN4physical
22939629
CNOT3_HUMANCNOT3physical
22939629
KAP2_HUMANPRKAR2Aphysical
22939629
LS14A_HUMANLSM14Aphysical
22939629
TPR_HUMANTPRphysical
22939629
FUBP2_HUMANKHSRPphysical
22939629
T2FA_HUMANGTF2F1physical
22939629
NUP88_HUMANNUP88physical
22939629
LAP2A_HUMANTMPOphysical
22939629
LAP2B_HUMANTMPOphysical
22939629
HNRH2_HUMANHNRNPH2physical
22939629
RPAC1_HUMANPOLR1Cphysical
22939629
ROA0_HUMANHNRNPA0physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
KHDR1_HUMANKHDRBS1physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
SRF_HUMANSRFphysical
21988832
HNRPK_HUMANHNRNPKphysical
25416956
RBY1A_HUMANRBMY1A1physical
25416956
SNRPA_HUMANSNRPAphysical
25416956
RBMX_HUMANRBMXphysical
25416956
LNX1_HUMANLNX1physical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
CCNB2_HUMANCCNB2physical
26344197
NAA20_HUMANNAA20physical
26344197
SYNC_HUMANNARSphysical
26344197
HNRPK_HUMANHNRNPKphysical
21516116
ANM5_HUMANPRMT5physical
28514442
COPRS_HUMANCOPRSphysical
28514442
RIOK1_HUMANRIOK1physical
28514442
ANM1_HUMANPRMT1physical
28514442
SYYM_HUMANYARS2physical
28514442
NGRN_HUMANNGRNphysical
28514442
PAI2B_HUMANPAIP2Bphysical
28514442
ANM6_HUMANPRMT6physical
28514442
RM01_HUMANMRPL1physical
28514442
MEP50_HUMANWDR77physical
28514442
MASU1_HUMANMALSU1physical
28514442

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 CIRBP_HUMAN

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Related Literatures of Post-Translational Modification

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