CRNL1_HUMAN - dbPTM
CRNL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRNL1_HUMAN
UniProt AC Q9BZJ0
Protein Name Crooked neck-like protein 1
Gene Name CRNKL1
Organism Homo sapiens (Human).
Sequence Length 848
Subcellular Localization Nucleus . Nucleus speckle . Colocalizes with core spliceosomal snRNP proteins (PubMed:12084575).
Protein Description Involved in pre-mRNA splicing process..
Protein Sequence MTATVENLTFQKDTLGNAVDKNTSRLELRSYSLAGRHGSTEPLVLAWSSQFRRLTWGCALDALHRSPCVAASQHGVTHLIRSSRTPHSTRCRKEDAQPGHHGNGAASVTAQARGQRSVLQVPLPVPRSCLFSESFVVSVSSQSRFLASVPGTGVQRSTAADMAASTAAGKQRIPKVAKVKNKAPAEVQITAEQLLREAKERELELLPPPPQQKITDEEELNDYKLRKRKTFEDNIRKNRTVISNWIKYAQWEESLKEIQRARSIYERALDVDYRNITLWLKYAEMEMKNRQVNHARNIWDRAITTLPRVNQFWYKYTYMEEMLGNVAGARQVFERWMEWQPEEQAWHSYINFELRYKEVDRARTIYERFVLVHPDVKNWIKYARFEEKHAYFAHARKVYERAVEFFGDEHMDEHLYVAFAKFEENQKEFERVRVIYKYALDRISKQDAQELFKNYTIFEKKFGDRRGIEDIIVSKRRFQYEEEVKANPHNYDAWFDYLRLVESDAEAEAVREVYERAIANVPPIQEKRHWKRYIYLWINYALYEELEAKDPERTRQVYQASLELIPHKKFTFAKMWILYAQFEIRQKNLSLARRALGTSIGKCPKNKLFKVYIELELQLREFDRCRKLYEKFLEFGPENCTSWIKFAELETILGDIDRARAIYELAISQPRLDMPEVLWKSYIDFEIEQEETERTRNLYRRLLQRTQHVKVWISFAQFELSSGKEGSLTKCRQIYEEANKTMRNCEEKEERLMLLESWRSFEEEFGTASDKERVDKLMPEKVKKRRKVQTDDGSDAGWEEYFDYIFPEDAANQPNLKLLAMAKLWKKQQQEKEDAEHHPDEDVDESES
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
2 (in isoform 2)Acetylation-30.9122814378
2Phosphorylation------MTATVENLT
------CCCEEECCE		30.91-
24PhosphorylationNAVDKNTSRLELRSY
CCCCCCCCCCEEEHH		44.24-
30PhosphorylationTSRLELRSYSLAGRH
CCCCEEEHHCCCCCC		31.5325690035
31PhosphorylationSRLELRSYSLAGRHG
CCCEEEHHCCCCCCC		10.9825690035
32PhosphorylationRLELRSYSLAGRHGS
CCEEEHHCCCCCCCC		17.0025690035
141PhosphorylationSFVVSVSSQSRFLAS
CEEEEECCCCCEEEC		29.98-
143PhosphorylationVVSVSSQSRFLASVP
EEEECCCCCEEECCC		27.26-
166PhosphorylationAADMAASTAAGKQRI
HHHHHHHHHHHHCCC		18.7930576142
170SumoylationAASTAAGKQRIPKVA
HHHHHHHHCCCCCCH		31.51-
170AcetylationAASTAAGKQRIPKVA
HHHHHHHHCCCCCCH		31.5125953088
170SumoylationAASTAAGKQRIPKVA
HHHHHHHHCCCCCCH		31.51-
199UbiquitinationEQLLREAKERELELL
HHHHHHHHHHHHHCC		53.18-
213UbiquitinationLPPPPQQKITDEEEL
CCCCCCCCCCCHHHH		42.18-
224AcetylationEEELNDYKLRKRKTF
HHHHHHHHHHCCCCH		44.6826051181
224UbiquitinationEEELNDYKLRKRKTF
HHHHHHHHHHCCCCH		44.68-
229"N6,N6-dimethyllysine"DYKLRKRKTFEDNIR
HHHHHCCCCHHHHHH		61.68-
229MethylationDYKLRKRKTFEDNIR
HHHHHCCCCHHHHHH		61.68-
240PhosphorylationDNIRKNRTVISNWIK
HHHHHCHHHHHHHHH		31.4229978859
243PhosphorylationRKNRTVISNWIKYAQ
HHCHHHHHHHHHHHH		23.0629978859
256UbiquitinationAQWEESLKEIQRARS
HHHHHHHHHHHHHHH		63.15-
265PhosphorylationIQRARSIYERALDVD
HHHHHHHHHHHHCCC		10.70-
381AcetylationPDVKNWIKYARFEEK
CCHHHHHHHHHHHHH		25.1919608861
388UbiquitinationKYARFEEKHAYFAHA
HHHHHHHHHHHHHHH		26.74-
427AcetylationAKFEENQKEFERVRV
HHHHHCHHHHHHHHH		75.7827452117
438PhosphorylationRVRVIYKYALDRISK
HHHHHHHHHHHHCCH		8.7421712546
442MethylationIYKYALDRISKQDAQ
HHHHHHHHCCHHHHH		35.61-
444PhosphorylationKYALDRISKQDAQEL
HHHHHHCCHHHHHHH		25.7621712546
453UbiquitinationQDAQELFKNYTIFEK
HHHHHHHHCCCHHHH		62.76-
461UbiquitinationNYTIFEKKFGDRRGI
CCCHHHHHHCCCCCH		47.59-
475AcetylationIEDIIVSKRRFQYEE
HHHEEEECCCCCCHH		36.3825953088
475UbiquitinationIEDIIVSKRRFQYEE
HHHEEEECCCCCCHH		36.38-
503PhosphorylationDYLRLVESDAEAEAV
HHHHHHHCHHHHHHH		34.3414702039
514PhosphorylationAEAVREVYERAIANV
HHHHHHHHHHHHHCC		8.5725884760
598PhosphorylationLARRALGTSIGKCPK
HHHHHHCCCCCCCCC		20.3020068231
599PhosphorylationARRALGTSIGKCPKN
HHHHHCCCCCCCCCC		27.7820068231
602AcetylationALGTSIGKCPKNKLF
HHCCCCCCCCCCCCE		45.7725953088
602UbiquitinationALGTSIGKCPKNKLF
HHCCCCCCCCCCCCE		45.77-
631UbiquitinationRCRKLYEKFLEFGPE
HHHHHHHHHHHHCCC		41.51-
721PhosphorylationSFAQFELSSGKEGSL
EEEEEECCCCCCCCH		29.82-
727PhosphorylationLSSGKEGSLTKCRQI
CCCCCCCCHHHHHHH		33.6824719451
740AcetylationQIYEEANKTMRNCEE
HHHHHHHHHHHCCHH		51.2325953088
740UbiquitinationQIYEEANKTMRNCEE
HHHHHHHHHHHCCHH		51.23-
748AcetylationTMRNCEEKEERLMLL
HHHCCHHHHHHHHHH		42.4526051181
767PhosphorylationSFEEEFGTASDKERV
HHHHHHCCCCCHHHH		28.4523312004
769PhosphorylationEEEFGTASDKERVDK
HHHHCCCCCHHHHHH		49.4023312004
771UbiquitinationEFGTASDKERVDKLM
HHCCCCCHHHHHHHC		44.95-
823AcetylationLKLLAMAKLWKKQQQ
HHHHHHHHHHHHHHH		41.6225953088
823UbiquitinationLKLLAMAKLWKKQQQ
HHHHHHHHHHHHHHH		41.62-
846PhosphorylationPDEDVDESES-----
CCCCCCCCCC-----		38.3830576142
848PhosphorylationEDVDESES-------
CCCCCCCC-------		55.5930576142
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 CRNL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRNL1_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 CRNL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP8_HUMANPRPF8physical
22939629
DHX8_HUMANDHX8physical
22939629
U520_HUMANSNRNP200physical
22939629
SMRD3_HUMANSMARCD3physical
22939629
CCD12_HUMANCCDC12physical
22365833
AQR_HUMANAQRphysical
26344197
CCD12_HUMANCCDC12physical
26344197
U5S1_HUMANEFTUD2physical
26344197
PPIE_HUMANPPIEphysical
26344197
SNUT1_HUMANSART1physical
26344197
RU17_HUMANSNRNP70physical
26344197
SMD2_HUMANSNRPD2physical
26344197
SNW1_HUMANSNW1physical
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 CRNL1_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-381, AND MASS SPECTROMETRY.

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