POGZ_MOUSE - dbPTM
POGZ_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POGZ_MOUSE
UniProt AC Q8BZH4
Protein Name Pogo transposable element with ZNF domain
Gene Name Pogz
Organism Mus musculus (Mouse).
Sequence Length 1409
Subcellular Localization Nucleus . Chromosome. Cytoplasm. Recruited to trimethylated 'Lys-9' of histone H3 (H3K9me3)..
Protein Description Plays a role in mitotic cell cycle progression and is involved in kinetochore assembly and mitotic sister chromatid cohesion. Probably through its association with CBX5 plays a role in mitotic chromosome segregation by regulating aurora kinase B/AURKB activation and AURKB and CBX5 dissociation from chromosome arms (By similarity)..
Protein Sequence MADTDLFMECEEEELEPWQKISDVIEDSVVEDYNSVDKTTSVSVSQQPVSAPVPIAAHASVAGHLSTSTTVSNSGAQNSDSTKKTLVTLIANNNAGNTLVQQGGQPLILTQNPAPGLGTMVTQPVLRPVQVMQNANHVTSSPVASQPIFITTQGFPVRNVRPVQNAMNQVGIVLNVQQGQTVRPITLVPAPGTQFVKPTVGVPQVFSQMTPVRPGSTMPVRPTTNTFTTVIPATLTIRSTVPQSQSQQTKSTPSTSTTPTATQPTSLGQLAGQPPGQSNQTSNPKLAPSFPSPPAVSIASFVTVKRPGVTGENSNEVAKLVNTLNTVPSLGQSPGPVVVSNNSSAQRTSGPESSVKVTSSIPVFDLQDGGRKICPRCNAQFRVTEALRGHMCYCCPEMVEYQKKGKSLDAEPSVPSAAKPSSPEKTAPVTSTPSSTPIPALSPPTKVPEPNENAGDAVQTKLIMLVDDFYYGRDGGKAAQLTSFPKVATSFRCPHCTKRLKNNIRFMNHMKHHVELDQQNGEVDGHTICQHCYRQFSTPFQLQCHLENVHSPYESTTKCKICEWAFESEPLFLQHMKDTHKPGEMPYVCQVCQYRSSLYSEVDVHFRMIHEDTRHLLCPYCLKVFKNGNAFQQHYMRHQKRNVYHCNKCRLQFLFAKDKIEHKLQHHKTFRKPKQLEGLKPGTKVTIRASRGQPRTVPVSSNDAPSGTLQEAAALTSTDPLPVFLYPPVQRNIQKRAVRKMSVMGRQTCLECSFEIPDFPNHFPTYVHCSLCRYSTCCSRAYANHMINNHVPRKSPKYLALFKNSVSGIKLACTSCTFATSVGDAMAKHLVFNPSHRSSNILPRGLSWMSHLRPGQASERVFDWSMKNTYLPPPLVPNKAATVKPVGVTPAEPQELAGPVLQALPSPASTATPPATPTHPQPSALPPSATEGTECLNVSEQEEGSPVTQDPEPASGGGGGSGVGKKEQLSVKKLRVVLFALCCNTEQAAEHFRNPQRRIRRWLRRFQASQGENLEGKYLSFEAEEKLAEWVLIQREQQLPVNEETLFQKATKIGRSLEGGFKISYEWAVRFMLRHHLTPHARRAVAHTLPKHVAENAGLFIEFVQRQIHNQDLPLSMIVAIDEISLFLDTEVLSSDDRKENALQTVGTGEPWCDVVLAILADGTVLPTLVFFRGQANRFANVPDSILLEAKDSGYSDDEIMELWSTRVWKKHTACQHSKSMLVMDCHRTHLSEEVLALLSASSTLPAVVPAGCSSKIQPLDVCIKRTVKNFLHKKWKEQAREMADAACDSDVLLQLVLVWLGEVLGVIGDSPELVQRSFLVASVLPGPDGNVNSPTRNADMQEELIASLEEQLKLNGEQSEEHSASAPRPRSSPEETVEPESLHQLFEGESETESFYGFEEADLDLMEI
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
28PhosphorylationISDVIEDSVVEDYNS
HHHHHHHHHCCCCCC		18.4428066266
35PhosphorylationSVVEDYNSVDKTTSV
HHCCCCCCCCCCCEE		26.0128066266
251PhosphorylationSQSQQTKSTPSTSTT
CCCCCCCCCCCCCCC		49.2726745281
252PhosphorylationQSQQTKSTPSTSTTP
CCCCCCCCCCCCCCC		23.8625777480
254PhosphorylationQQTKSTPSTSTTPTA
CCCCCCCCCCCCCCC		34.7725777480
255PhosphorylationQTKSTPSTSTTPTAT
CCCCCCCCCCCCCCC		31.1525777480
256PhosphorylationTKSTPSTSTTPTATQ
CCCCCCCCCCCCCCC		34.3225777480
257PhosphorylationKSTPSTSTTPTATQP
CCCCCCCCCCCCCCC		36.5625777480
258PhosphorylationSTPSTSTTPTATQPT
CCCCCCCCCCCCCCC		20.5724453211
260PhosphorylationPSTSTTPTATQPTSL
CCCCCCCCCCCCCCH		40.0025777480
262PhosphorylationTSTTPTATQPTSLGQ
CCCCCCCCCCCCHHH		37.2425777480
265PhosphorylationTPTATQPTSLGQLAG
CCCCCCCCCHHHHCC		27.1125777480
266PhosphorylationPTATQPTSLGQLAGQ
CCCCCCCCHHHHCCC		36.8725777480
278PhosphorylationAGQPPGQSNQTSNPK
CCCCCCCCCCCCCCC		36.5025777480
281PhosphorylationPPGQSNQTSNPKLAP
CCCCCCCCCCCCCCC		34.4225777480
282PhosphorylationPGQSNQTSNPKLAPS
CCCCCCCCCCCCCCC		41.1725777480
292PhosphorylationKLAPSFPSPPAVSIA
CCCCCCCCCCCEEEE		41.3226643407
297PhosphorylationFPSPPAVSIASFVTV
CCCCCCEEEEEEEEE		17.9726745281
310O-linked_GlycosylationTVKRPGVTGENSNEV
EEECCCCCCCCHHHH		44.7021606357
323PhosphorylationEVAKLVNTLNTVPSL
HHHHHHHHHHCCCCC		17.5725619855
326PhosphorylationKLVNTLNTVPSLGQS
HHHHHHHCCCCCCCC		36.5925619855
329PhosphorylationNTLNTVPSLGQSPGP
HHHHCCCCCCCCCCC		40.5725619855
333PhosphorylationTVPSLGQSPGPVVVS
CCCCCCCCCCCEEEE		29.9925619855
340PhosphorylationSPGPVVVSNNSSAQR
CCCCEEEECCCCCCC		20.7725619855
343PhosphorylationPVVVSNNSSAQRTSG
CEEEECCCCCCCCCC		31.1625619855
344PhosphorylationVVVSNNSSAQRTSGP
EEEECCCCCCCCCCC		30.4625619855
358O-linked_GlycosylationPESSVKVTSSIPVFD
CCCCCEEEECCCEEE		15.8421606357
360PhosphorylationSSVKVTSSIPVFDLQ
CCCEEEECCCEEECC		22.88-
407PhosphorylationEYQKKGKSLDAEPSV
HHHHCCCCCCCCCCC		39.9025619855
413PhosphorylationKSLDAEPSVPSAAKP
CCCCCCCCCCCCCCC		37.8624925903
416PhosphorylationDAEPSVPSAAKPSSP
CCCCCCCCCCCCCCC		38.4124925903
421PhosphorylationVPSAAKPSSPEKTAP
CCCCCCCCCCCCCCC		58.7924925903
422PhosphorylationPSAAKPSSPEKTAPV
CCCCCCCCCCCCCCC		45.6824925903
426PhosphorylationKPSSPEKTAPVTSTP
CCCCCCCCCCCCCCC		34.2325619855
430PhosphorylationPEKTAPVTSTPSSTP
CCCCCCCCCCCCCCC		26.3125619855
431PhosphorylationEKTAPVTSTPSSTPI
CCCCCCCCCCCCCCC		38.2625619855
432PhosphorylationKTAPVTSTPSSTPIP
CCCCCCCCCCCCCCC		20.1625619855
434PhosphorylationAPVTSTPSSTPIPAL
CCCCCCCCCCCCCCC		47.1025619855
435PhosphorylationPVTSTPSSTPIPALS
CCCCCCCCCCCCCCC		39.1325619855
436PhosphorylationVTSTPSSTPIPALSP
CCCCCCCCCCCCCCC		29.5825619855
442PhosphorylationSTPIPALSPPTKVPE
CCCCCCCCCCCCCCC		30.8222942356
445PhosphorylationIPALSPPTKVPEPNE
CCCCCCCCCCCCCCC		48.3225619855
460PhosphorylationNAGDAVQTKLIMLVD
CCCHHHHHHEEEEEC		22.6325619855
635PhosphorylationGNAFQQHYMRHQKRN
CCHHHHHHHHHHCCC		7.4822802335
683PhosphorylationLEGLKPGTKVTIRAS
CCCCCCCCEEEEEEC		30.7627149854
742PhosphorylationKRAVRKMSVMGRQTC
HHHHHHHCCCCCCCH		16.4025521595
1009PhosphorylationWLRRFQASQGENLEG
HHHHHHHHCCCCCCC		28.12-
1049UbiquitinationNEETLFQKATKIGRS
CHHHHHHHHHHHCHH		51.17-
1195PhosphorylationLEAKDSGYSDDEIME
EEEHHCCCCHHHHHH		16.9322807455
1206PhosphorylationEIMELWSTRVWKKHT
HHHHHHHHHHHHHCC		20.0522807455
1318PhosphorylationSPELVQRSFLVASVL
CHHHHHHHHEEEECC		13.0725777480
1323PhosphorylationQRSFLVASVLPGPDG
HHHHEEEECCCCCCC		19.3925159016
1334PhosphorylationGPDGNVNSPTRNADM
CCCCCCCCCCCCHHH		24.3025521595
1336PhosphorylationDGNVNSPTRNADMQE
CCCCCCCCCCHHHHH		36.0525159016
1348PhosphorylationMQEELIASLEEQLKL
HHHHHHHHHHHHHHH		29.3526745281
1360PhosphorylationLKLNGEQSEEHSASA
HHHCCCCCCCCCCCC		40.4225266776
1364PhosphorylationGEQSEEHSASAPRPR
CCCCCCCCCCCCCCC		27.4825266776
1366PhosphorylationQSEEHSASAPRPRSS
CCCCCCCCCCCCCCC		41.65-
1372PhosphorylationASAPRPRSSPEETVE
CCCCCCCCCCCCCCC		53.58-
1373PhosphorylationSAPRPRSSPEETVEP
CCCCCCCCCCCCCCH		37.30-
1377PhosphorylationPRSSPEETVEPESLH
CCCCCCCCCCHHHHH		28.62-
1391PhosphorylationHQLFEGESETESFYG
HHHHCCCCCCCCCCC		61.75-
1393PhosphorylationLFEGESETESFYGFE
HHCCCCCCCCCCCCC		46.32-
1395PhosphorylationEGESETESFYGFEEA
CCCCCCCCCCCCCHH		31.05-
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 POGZ_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-421 AND SER-422, ANDMASS SPECTROMETRY.

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