CIR1_HUMAN - dbPTM
CIR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CIR1_HUMAN
UniProt AC Q86X95
Protein Name Corepressor interacting with RBPJ 1
Gene Name CIR1
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Nucleus speckle. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Colocalizes with NEK6 in the centrosome.
Protein Description May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription..
Protein Sequence MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGAKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVASEGEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKDRKKKKFQKSRSKHKKHKSSSSSSSSSSSSSSTETSESSSESESNNKEKKIQRKKRKKNKCSGHNNSDSEEKDKSKKRKLHEELSSSHHNREKAKEKPRFLKHESSREDSKWSHSDSDKKSRTHKHSPEKRGSERKEGSSRSHGREERSRRSRSRSPGSYKQRETRKRAQRNPGEEQSRRNDSRSHGTDLYRGEKMYREHPGGTHTKVTQRE
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
3Methylation-----MGKSFANFMC
-----CCCCHHHHHH		40.89-
4Phosphorylation----MGKSFANFMCK
----CCCCHHHHHHC		24.7028555341
12UbiquitinationFANFMCKKDFHPASK
HHHHHHCCCCCCCCH		61.7829967540
18PhosphorylationKKDFHPASKSNIKKV
CCCCCCCCHHHHHHH		40.86-
19UbiquitinationKDFHPASKSNIKKVW
CCCCCCCHHHHHHHH		50.0229967540
24UbiquitinationASKSNIKKVWMAEQK
CCHHHHHHHHHHCHH		37.0129967540
38UbiquitinationKISYDKKKQEELMQQ
HCCCCHHHHHHHHHH		69.5529967540
48UbiquitinationELMQQYLKEQESYDN
HHHHHHHHHHHCCCC		53.0329967540
65UbiquitinationLMGDERVKNGLNFMY
CCCCHHHHCCCCCCC		52.0629967540
72PhosphorylationKNGLNFMYEAPPGAK
HCCCCCCCCCCCCCC		12.5621945579
79SumoylationYEAPPGAKKENKEKE
CCCCCCCCCCCCCHH		67.5428112733
88PhosphorylationENKEKEETEGETEYK
CCCCHHCCCCCCCCC		50.8325159151
100UbiquitinationEYKFEWQKGAPREKY
CCCCEECCCCCHHHH		59.1029967540
182AcetylationRNSGFALKRNVLGRN
HHCCCCCCCCCCCCC		38.2025953088
182MethylationRNSGFALKRNVLGRN
HHCCCCCCCCCCCCC		38.20-
182UbiquitinationRNSGFALKRNVLGRN
HHCCCCCCCCCCCCC		38.20-
191PhosphorylationNVLGRNLTANDPSQE
CCCCCCCCCCCCCCH		27.2828464451
196PhosphorylationNLTANDPSQEYVASE
CCCCCCCCCHHHCCC		38.2130266825
199PhosphorylationANDPSQEYVASEGEE
CCCCCCHHHCCCCCC		8.1530266825
202PhosphorylationPSQEYVASEGEEDPE
CCCHHHCCCCCCCHH		35.7729255136
258PhosphorylationKHKKHKSSSSSSSSS
HHHHCCCCCCCCCCC		38.76-
259PhosphorylationHKKHKSSSSSSSSSS
HHHCCCCCCCCCCCC		41.13-
260PhosphorylationKKHKSSSSSSSSSSS
HHCCCCCCCCCCCCC		35.87-
261PhosphorylationKHKSSSSSSSSSSSS
HCCCCCCCCCCCCCC		35.87-
262PhosphorylationHKSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
263PhosphorylationKSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
264PhosphorylationSSSSSSSSSSSSSST
CCCCCCCCCCCCCCC		35.87-
265PhosphorylationSSSSSSSSSSSSSTE
CCCCCCCCCCCCCCC		35.87-
266PhosphorylationSSSSSSSSSSSSTET
CCCCCCCCCCCCCCC		35.87-
267PhosphorylationSSSSSSSSSSSTETS
CCCCCCCCCCCCCCC		35.87-
268PhosphorylationSSSSSSSSSSTETSE
CCCCCCCCCCCCCCC		30.20-
269PhosphorylationSSSSSSSSSTETSES
CCCCCCCCCCCCCCC		43.13-
270PhosphorylationSSSSSSSSTETSESS
CCCCCCCCCCCCCCC		32.01-
271PhosphorylationSSSSSSSTETSESSS
CCCCCCCCCCCCCCC		45.27-
273PhosphorylationSSSSSTETSESSSES
CCCCCCCCCCCCCCC		37.57-
276PhosphorylationSSTETSESSSESESN
CCCCCCCCCCCCCCC		38.64-
280PhosphorylationTSESSSESESNNKEK
CCCCCCCCCCCHHHH		48.55-
282PhosphorylationESSSESESNNKEKKI
CCCCCCCCCHHHHHH		55.79-
305PhosphorylationKCSGHNNSDSEEKDK
CCCCCCCCCHHHHHH		48.0730576142
307PhosphorylationSGHNNSDSEEKDKSK
CCCCCCCHHHHHHHH		47.6930576142
323PhosphorylationRKLHEELSSSHHNRE
HHHHHHHHHHHHHHH		32.8330108239
324PhosphorylationKLHEELSSSHHNREK
HHHHHHHHHHHHHHH		46.4430108239
325PhosphorylationLHEELSSSHHNREKA
HHHHHHHHHHHHHHH		25.9530108239
340SumoylationKEKPRFLKHESSRED
HHCCCCCCCCCCCCC		42.48-
340SumoylationKEKPRFLKHESSRED
HHCCCCCCCCCCCCC		42.4828112733
343PhosphorylationPRFLKHESSREDSKW
CCCCCCCCCCCCCCC		34.1223532336
344PhosphorylationRFLKHESSREDSKWS
CCCCCCCCCCCCCCC		36.38-
351PhosphorylationSREDSKWSHSDSDKK
CCCCCCCCCCCCCHH		19.4928985074
353PhosphorylationEDSKWSHSDSDKKSR
CCCCCCCCCCCHHHC		33.0430576142
355PhosphorylationSKWSHSDSDKKSRTH
CCCCCCCCCHHHCCC		55.1129514088
361PhosphorylationDSDKKSRTHKHSPEK
CCCHHHCCCCCCCCC		42.2224144214
365PhosphorylationKSRTHKHSPEKRGSE
HHCCCCCCCCCCCCC		39.2926657352
377PhosphorylationGSERKEGSSRSHGRE
CCCCCCCCCCCCCHH		24.54-
380PhosphorylationRKEGSSRSHGREERS
CCCCCCCCCCHHHHH		32.04-
390PhosphorylationREERSRRSRSRSPGS
HHHHHHHHHCCCCCC		33.2330576142
392PhosphorylationERSRRSRSRSPGSYK
HHHHHHHCCCCCCHH		38.0530266825
394PhosphorylationSRRSRSRSPGSYKQR
HHHHHCCCCCCHHHH		34.5530266825
397PhosphorylationSRSRSPGSYKQRETR
HHCCCCCCHHHHHHH		32.3223663014
398PhosphorylationRSRSPGSYKQRETRK
HCCCCCCHHHHHHHH		19.6330242111
423PhosphorylationSRRNDSRSHGTDLYR
HHHHCCCCCCCCCHH		30.1628555341
429PhosphorylationRSHGTDLYRGEKMYR
CCCCCCCHHCCCCHH		21.27-
435PhosphorylationLYRGEKMYREHPGGT
CHHCCCCHHCCCCCC		24.74-
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 CIR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CIR1_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 CIR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNW1_HUMANSNW1physical
10644367
SAP30_HUMANSAP30physical
9874765
HDAC2_MOUSEHdac2physical
9874765
NCOR2_HUMANNCOR2physical
11509665
RP9_HUMANRP9physical
15652350
SRSF2_HUMANSRSF2physical
15652350
SRSF1_HUMANSRSF1physical
15652350
U2AF1_HUMANU2AF1physical
15652350
CEP76_HUMANCEP76physical
25416956
CCYL1_HUMANCCNYL1physical
28514442
UBR3_HUMANUBR3physical
28514442
GRAN_HUMANGCAphysical
28514442
BTBD1_HUMANBTBD1physical
28514442
DCA10_HUMANDCAF10physical
28514442
CDCA3_HUMANCDCA3physical
28514442
RBM12_HUMANRBM12physical
28514442
CTNA2_HUMANCTNNA2physical
28514442
EPHA2_HUMANEPHA2physical
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 CIR1_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-202, AND MASSSPECTROMETRY.
"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, 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-202, AND MASSSPECTROMETRY.

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