WAPL_MOUSE - dbPTM
WAPL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WAPL_MOUSE
UniProt AC Q65Z40
Protein Name Wings apart-like protein homolog
Gene Name Wapl {ECO:0000312|MGI:MGI:2675859}
Organism Mus musculus (Mouse).
Sequence Length 1200
Subcellular Localization Nucleus. Chromosome. Cytoplasm. Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase (By similarity)..
Protein Description Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity)..
Protein Sequence MTSRFGKTYSRKGGNGSSKFDEVFSNKRTTLSTKWGETTFMAKLGQKRPNFKPDIQEIPKKPKVEEEDTGDPFGFDSDDESLPVSSKNLAQGKGSSYSESSEAAQLEEVTSVFEANSKCSHVVGEDSFASDRCLLVEDTLIGKEKSISRIPEDNANKSSCTKLLTSDKVENFSEEHEKNSHHFHKNAEDSTKKPNAETAVASEYKADETKETNDTWNSQSGKRTESPSESCPVKGSVRTGLYEWDNDFEDIRSEDCILSLDNESLLEMKDEDLKNRIGGLENLNETFEEDIIQSVLRPSNCRTYCRANKARSSQGASNFDKLMDGTSQSLAKANSESSKDGLNQAKKGSASCGTSFRGTVGRTRDYTVLHPSCLSVCNVTIQDTMERSMDEFTASTPADLGEAGRLRKKADIATSKTTTRFRPSNTKSKKDVKLEFFGFEDHDETGGDEGGSGSSNYKIKYFGFDDLSESEDDDDDDCQVERKKDKKRTKTAPSPSQQPPPESSDNSQDSQSSTNNAENLDFTEDLPGVPESVKKPISKQGDKSKENTRKIFSGPKRSPTKAVYNARHWNHPDSEELPGPPIAKPQRVTVRLSSKEPNQKDDGVFKAPAPPLKVIKTVTIPTQPYQEIVTALKCRKEDKELYTVVQHVKHFNDVVEFGENQEFTDDIEYLLSGLKSTQPLNTRCLSVISLATKCAMPSFRMHLRAHGMVAMVFKTLDDSQHHQNLSLCTAALMYILSRDRLNMDLDRASLDLMIRLLELEQDASSAKLLNEKDMNKIKEKIRRLCETVHNKHLDLENITTGHLAMETLLSLTSKRAGDWFKEELRLLGGLDHIVDKVKECVDHLSRDDEDEEKLVASLWGAERCLRVLESVTVHNPENQSYLIAYKDSQLIISSAKALQHCEDLIQQYNRAENSICVADSNPLPYQNVTNHVGKAVEDCMRAIIGVLLNLTNDNEWGSTKTGEQEGLIGTAMNCVLQVPKYLPQEQRFDIRVLGLGLLINLVEYSARNRHCLVNMQTSCSFDSSFSSGEGDHSLRLAGQVHAVQALVQLFLERERAAQLAESKTDELIKDAPTTQHDKSGEWQETSGEIQWVSTEKTDGAEEKQKKEEEDEELDLNKALQHAGKHMEDCIVASYTALLLGCLCQESPINVTTVREYLPEGDFSIMTEMLKKFLSFMNLTCAVGTTGQKSISRVIEYLEHC
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
17PhosphorylationSRKGGNGSSKFDEVF
CCCCCCCCCCHHHHH		34.0629472430
18PhosphorylationRKGGNGSSKFDEVFS
CCCCCCCCCHHHHHC		38.4529472430
52AcetylationGQKRPNFKPDIQEIP
CCCCCCCCCCHHHCC		48.7123806337
69PhosphorylationPKVEEEDTGDPFGFD
CCCCCCCCCCCCCCC		46.9225619855
77PhosphorylationGDPFGFDSDDESLPV
CCCCCCCCCCCCCCC		44.7024925903
81PhosphorylationGFDSDDESLPVSSKN
CCCCCCCCCCCCCCC		44.9924925903
85PhosphorylationDDESLPVSSKNLAQG
CCCCCCCCCCCCCCC		33.3925619855
86PhosphorylationDESLPVSSKNLAQGK
CCCCCCCCCCCCCCC		26.2925619855
95PhosphorylationNLAQGKGSSYSESSE
CCCCCCCCCCCCCCH		29.5928833060
96PhosphorylationLAQGKGSSYSESSEA
CCCCCCCCCCCCCHH		41.1528833060
97PhosphorylationAQGKGSSYSESSEAA
CCCCCCCCCCCCHHH		20.3928833060
98PhosphorylationQGKGSSYSESSEAAQ
CCCCCCCCCCCHHHH		32.7128833060
100PhosphorylationKGSSYSESSEAAQLE
CCCCCCCCCHHHHHH		27.7728833060
101PhosphorylationGSSYSESSEAAQLEE
CCCCCCCCHHHHHHH		27.4828833060
110PhosphorylationAAQLEEVTSVFEANS
HHHHHHHHHHHHHCC		23.5828833060
127PhosphorylationSHVVGEDSFASDRCL
CEECCCCCCCCCCEE		20.5725266776
168AcetylationTKLLTSDKVENFSEE
HHHHCCHHHHCCCHH		51.7423806337
173PhosphorylationSDKVENFSEEHEKNS
CHHHHCCCHHHHHCC		54.3727841257
222AcetylationTWNSQSGKRTESPSE
CCCCCCCCCCCCCCC		62.4830988501
224PhosphorylationNSQSGKRTESPSESC
CCCCCCCCCCCCCCC		44.2827087446
226PhosphorylationQSGKRTESPSESCPV
CCCCCCCCCCCCCCC		32.8727087446
228PhosphorylationGKRTESPSESCPVKG
CCCCCCCCCCCCCCC		51.9626824392
230PhosphorylationRTESPSESCPVKGSV
CCCCCCCCCCCCCEE		28.2328833060
264PhosphorylationILSLDNESLLEMKDE
EEEECCHHHHHCCCH		44.5021149613
286PhosphorylationGLENLNETFEEDIIQ
CHHHHHHHCHHHHHH		34.9621149613
312PhosphorylationCRANKARSSQGASNF
HHHCCHHCCCCCCCH		31.6930635358
313PhosphorylationRANKARSSQGASNFD
HHCCHHCCCCCCCHH		27.3825266776
321AcetylationQGASNFDKLMDGTSQ
CCCCCHHHHHCCCHH		41.3922826441
321UbiquitinationQGASNFDKLMDGTSQ
CCCCCHHHHHCCCHH		41.3922790023
326PhosphorylationFDKLMDGTSQSLAKA
HHHHHCCCHHHHHHH		21.2323140645
327PhosphorylationDKLMDGTSQSLAKAN
HHHHCCCHHHHHHHC		24.2523140645
329PhosphorylationLMDGTSQSLAKANSE
HHCCCHHHHHHHCCC		30.0223140645
335PhosphorylationQSLAKANSESSKDGL
HHHHHHCCCCCHHHH		43.6523140645
337PhosphorylationLAKANSESSKDGLNQ
HHHHCCCCCHHHHHH		42.3723140645
338PhosphorylationAKANSESSKDGLNQA
HHHCCCCCHHHHHHH		30.6223140645
339AcetylationKANSESSKDGLNQAK
HHCCCCCHHHHHHHH		66.1619865887
355PhosphorylationGSASCGTSFRGTVGR
CCCCCCCCCCCCCCC		9.76-
363PhosphorylationFRGTVGRTRDYTVLH
CCCCCCCCCCCEEEC		23.2022668510
380PhosphorylationCLSVCNVTIQDTMER
HHHHHCEEHHHHHHH		10.0322668510
384PhosphorylationCNVTIQDTMERSMDE
HCEEHHHHHHHHHHH		12.4522668510
388PhosphorylationIQDTMERSMDEFTAS
HHHHHHHHHHHHHCC		19.7821149613
393PhosphorylationERSMDEFTASTPADL
HHHHHHHHCCCCHHH		20.0421149613
424PhosphorylationTTTRFRPSNTKSKKD
CCCCCCCCCCCCCCC		53.5325338131
424O-linked_GlycosylationTTTRFRPSNTKSKKD
CCCCCCCCCCCCCCC		53.5330059200
426O-linked_GlycosylationTRFRPSNTKSKKDVK
CCCCCCCCCCCCCEE		40.8230059200
445PhosphorylationGFEDHDETGGDEGGS
EEECCCCCCCCCCCC		53.1528285833
452PhosphorylationTGGDEGGSGSSNYKI
CCCCCCCCCCCCCEE		46.4928833060
454PhosphorylationGDEGGSGSSNYKIKY
CCCCCCCCCCCEEEE		19.6728833060
461PhosphorylationSSNYKIKYFGFDDLS
CCCCEEEEEEECCCC		16.6528833060
468PhosphorylationYFGFDDLSESEDDDD
EEEECCCCCCCCCCC		46.1827087446
470PhosphorylationGFDDLSESEDDDDDD
EECCCCCCCCCCCCC		42.8427087446
491PhosphorylationKDKKRTKTAPSPSQQ
HCCCCCCCCCCCCCC		43.0928973931
494PhosphorylationKRTKTAPSPSQQPPP
CCCCCCCCCCCCCCC		34.4225338131
496PhosphorylationTKTAPSPSQQPPPES
CCCCCCCCCCCCCCC		45.8722942356
514PhosphorylationSQDSQSSTNNAENLD
CCCCHHHCCCHHHCC		37.4322668510
553PhosphorylationENTRKIFSGPKRSPT
CCCCHHHCCCCCCCC		58.6226643407
558PhosphorylationIFSGPKRSPTKAVYN
HHCCCCCCCCHHHHC		42.9426745281
560PhosphorylationSGPKRSPTKAVYNAR
CCCCCCCCHHHHCCC		32.6518779572
564PhosphorylationRSPTKAVYNARHWNH
CCCCHHHHCCCCCCC		14.15-
594PhosphorylationRVTVRLSSKEPNQKD
EEEEEECCCCCCCCC		45.70-
633UbiquitinationQEIVTALKCRKEDKE
HHHHHHHHCCCCHHH		29.5422790023
764PhosphorylationLELEQDASSAKLLNE
HHHHCCHHHHHHCCH		38.8325338131
767UbiquitinationEQDASSAKLLNEKDM
HCCHHHHHHCCHHHH		56.2922790023
914PhosphorylationQYNRAENSICVADSN
HHHHHCCCEEEECCC		14.6322817900
1079PhosphorylationPTTQHDKSGEWQETS
CCCCCCCCCCCEECC		48.2627600695
1106UbiquitinationGAEEKQKKEEEDEEL
CHHHHHHHHHHHHHC		68.79-
1124UbiquitinationKALQHAGKHMEDCIV
HHHHHHHHCHHHHHH		40.33-
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 WAPL_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WAPL_MOUSE !!
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 WAPL_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WAPL_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WAPL_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASSSPECTROMETRY.

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