NEUL4_HUMAN - dbPTM
NEUL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEUL4_HUMAN
UniProt AC Q96JN8
Protein Name Neuralized-like protein 4
Gene Name NEURL4
Organism Homo sapiens (Human).
Sequence Length 1562
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localizes to procentriole and daughter centriole in growing and quiescent cells (PubMed:22441691). May loose association with centrosomes during mitosis (PubMed:22261722)
Protein Description Promotes CCP110 ubiquitination and proteasome-dependent degradation. By counteracting accumulation of CP110, maintains normal centriolar homeostasis and preventing formation of ectopic microtubular organizing centers..
Protein Sequence MAAGSGGSGGSGGGPGPGPGGGGGPSGSGSGPGSNGGLGSGGELHPRTGRLVSLSACGRTARRQQPGQEFNHGLVLSREPLRDGRVFTVRIDRKVNSWSGSIEIGVTALDPSVLDFPSSATGLKGGSWVVSGCSVLRDGRSVLEEYGQDLDQLGEGDRVGVERTVAGELRLWVNGRDCGVAATGLPPRVWAVVDLYGKCTQITVLPPEPGFSPPTPIPTPPLEPLAPTEDSALAEQGTSADEAFMVSPAQARPETFPNSLESHNDFANMELSEVVSNTILSAYNGGLLNVNLSSPPAGEGLGSSGAATSPILTSNDALLFHEKCGTLIKLSNNNKTAERRRPLDEFNNGVVMTNRPLRDNEMFEIRIDKLVDKWSGSIEIGVTTHNPNSLEYPATMTNLQSGTIMMSGCGILTNGKGTRREYCEFSLDELQEGDHIGLTRKSNSALHFFINGIDQGVATPLTPPVVYGVVDLYGMAVKVTIVHNNNHSDRLRRNNAILRALSPEGALRRAAPAAQAEPERLLFHPNCGQKAAITHEGRTALRPHATDDFNHGVVLSSRALRDGEVFQVRIDKMVDKWAGSIEIGVTTHNPAYLQLPSTMTNLRSGTWMMTGNGVMHNGTTILDEYGHNLDRLKAGDTVGVVRREDGTLHFFVNGMTQGPAAWNVPPGVYAVVDLYGQAAQATIVDDVEVAPVPEPLPEGNNQVSPSSPSSGAGGSDLRFHQLHGSNAVITNGGRTALRHNCRSEFNDAIVISNRALRDGELFEIVIQKMVDRWSGSIEAGVTAIRPEDLEFPNTMTDIDYDTWMLSGTAIMQDGNTMRNNYGCDLDALGTGARIGMMRTAKGDLHYFINGQDQGAACSGLPPGKEVYAVVDLYGQCVQVSITNATGPMDNSLATSNTATEKSFPLHSPVAGVAHRFHSTCGKNVTLEEDGTRAVRAAGYAHGLVFSTKELRAEEVFEVKVEELDEKWAGSLRLGLTTLAPGEMGPGAGGGGPGLPPSLPELRTKTTWMVSSCEVRRDGQLQRMNYGRNLERLGVGSRVGVRRGADDTMHILVDGEDMGPAATGIAKNVWAVLDLYGPVRGVSIVSSTRLEESEGTQPPSPSSDTGSEGEEDDEGEEHGLGGQNEVGIIPTTLEFLENHGKNILLSNGNRTATRVASYNQGIVVINQPLVPQLLVQVRIDFLNRQWTSSLVLGVITCAPERLNFPASACALKRAAWLLRGRGVFHNGLKICEKFGPNLDTCPEGTILGLRLDSSGGLHLHVNGVDQGVAVPDVPQPCHALVDLYGQCEQVTIVNPEPGAASGKSAGTQGDMEKADMVDGIKESVCWGPPPAASPLKSCEYHALCSRFQELLLLPEDYFMPPPKRSLCYCESCRKLRGDEAHRRRGEPPREYALPFGWCRFNLRVNPRLEAGTLTKKWHMAYHGSNVAAVRRVLDRGELGAGTASILSCRPLKGEPGVGFEEPGENCAPPREEQPPPVLLSPSLQYAGAETLASKVQFRDPKSQRTHQAQVAFQVCVRPGSYTPGPPSAALGEPPDPHFSPAELEWVTKEKGATLLCALLVRVE
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
5Phosphorylation---MAAGSGGSGGSG
---CCCCCCCCCCCC		34.9428111955
8PhosphorylationMAAGSGGSGGSGGGP
CCCCCCCCCCCCCCC		43.4322210691
11PhosphorylationGSGGSGGSGGGPGPG
CCCCCCCCCCCCCCC		37.4828111955
26PhosphorylationPGGGGGPSGSGSGPG
CCCCCCCCCCCCCCC		49.1928111955
28PhosphorylationGGGGPSGSGSGPGSN
CCCCCCCCCCCCCCC		33.8428111955
30PhosphorylationGGPSGSGSGPGSNGG
CCCCCCCCCCCCCCC		43.4428111955
34PhosphorylationGSGSGPGSNGGLGSG
CCCCCCCCCCCCCCC		35.1228857561
40PhosphorylationGSNGGLGSGGELHPR
CCCCCCCCCCCCCCC		48.9828857561
48PhosphorylationGGELHPRTGRLVSLS
CCCCCCCCCCEEEEE		30.9828111955
53PhosphorylationPRTGRLVSLSACGRT
CCCCCEEEEECCCCC		22.6223312004
77PhosphorylationFNHGLVLSREPLRDG
CCCCEEEECCCCCCC		27.4124719451
308PhosphorylationLGSSGAATSPILTSN
CCCCCCCCCCCCCCC		34.2126074081
309PhosphorylationGSSGAATSPILTSND
CCCCCCCCCCCCCCC		12.7626074081
488PhosphorylationIVHNNNHSDRLRRNN
EECCCCHHHHHHHCC		26.9220860994
502PhosphorylationNAILRALSPEGALRR
CHHHHHHCHHHHHHH		21.6623401153
530UbiquitinationFHPNCGQKAAITHEG
ECCCCCCCEEECCCC		25.6833845483
557PhosphorylationNHGVVLSSRALRDGE
CCCEEEECCCCCCCC		19.8824719451
586PhosphorylationGSIEIGVTTHNPAYL
CEEEEEECCCCCCEE		19.6822210691
587PhosphorylationSIEIGVTTHNPAYLQ
EEEEEECCCCCCEEE		19.7622210691
597PhosphorylationPAYLQLPSTMTNLRS
CCEEECCCCCCCCCC		39.1322210691
633UbiquitinationGHNLDRLKAGDTVGV
CCCHHHCCCCCEEEE		51.7433845483
768UbiquitinationLFEIVIQKMVDRWSG
HHHHHHHHHHHHCCC		29.7521963094
821PhosphorylationGNTMRNNYGCDLDAL
CCCCCCCCCCCHHHC		23.76-
841 (in isoform 1)Ubiquitination-52.9621890473
841UbiquitinationIGMMRTAKGDLHYFI
EEEEEECCCCEEEEE		52.9633845483
867PhosphorylationLPPGKEVYAVVDLYG
CCCCCEEEEEEECCC		8.5124043423
873PhosphorylationVYAVVDLYGQCVQVS
EEEEEECCCCEEEEE		10.7324043423
880PhosphorylationYGQCVQVSITNATGP
CCCEEEEEEECCCCC		13.4524043423
882PhosphorylationQCVQVSITNATGPMD
CEEEEEEECCCCCCC		15.9924043423
885PhosphorylationQVSITNATGPMDNSL
EEEEECCCCCCCCCC		43.8424043423
891PhosphorylationATGPMDNSLATSNTA
CCCCCCCCCCCCCCC		18.3424043423
894PhosphorylationPMDNSLATSNTATEK
CCCCCCCCCCCCCCC		28.0124043423
895PhosphorylationMDNSLATSNTATEKS
CCCCCCCCCCCCCCC		26.9524043423
897PhosphorylationNSLATSNTATEKSFP
CCCCCCCCCCCCCCC		34.4224043423
899PhosphorylationLATSNTATEKSFPLH
CCCCCCCCCCCCCCC		41.7424043423
900PhosphorylationATSNTATEKSFPLHS
CCCCCCCCCCCCCCC		44.2132142685
901UbiquitinationTSNTATEKSFPLHSP
CCCCCCCCCCCCCCC		53.71-
902PhosphorylationSNTATEKSFPLHSPV
CCCCCCCCCCCCCCC		26.3429255136
905PhosphorylationATEKSFPLHSPVAGV
CCCCCCCCCCCCCCC		6.1832142685
907PhosphorylationEKSFPLHSPVAGVAH
CCCCCCCCCCCCCHH		28.8429255136
920UbiquitinationAHRFHSTCGKNVTLE
HHHCCCCCCCCEEEC		9.0629967540
922UbiquitinationRFHSTCGKNVTLEED
HCCCCCCCCEEECCC		50.8529967540
946PhosphorylationYAHGLVFSTKELRAE
HCCCEEEECCCCCHH		30.9624719451
964UbiquitinationEVKVEELDEKWAGSL
EEEHHHCCHHHCCEE		59.7232015554
964 (in isoform 2)Ubiquitination-59.7221890473
966 (in isoform 1)Ubiquitination-41.8521890473
966UbiquitinationKVEELDEKWAGSLRL
EHHHCCHHHCCEEEE		41.8521906983
1036PhosphorylationLERLGVGSRVGVRRG
HHHHCCCCCCEEECC		22.7628985074
1047PhosphorylationVRRGADDTMHILVDG
EECCCCCCEEEEECC		15.9328857561
1062PhosphorylationEDMGPAATGIAKNVW
CCCCCCHHHHHHHHH		31.0928857561
1101PhosphorylationGTQPPSPSSDTGSEG
CCCCCCCCCCCCCCC		45.2225921289
1102PhosphorylationTQPPSPSSDTGSEGE
CCCCCCCCCCCCCCC		42.4425921289
1104PhosphorylationPPSPSSDTGSEGEED
CCCCCCCCCCCCCCC		44.5525921289
1145PhosphorylationHGKNILLSNGNRTAT
CCCCEEEECCCCCCE		38.9719007248
1206PhosphorylationERLNFPASACALKRA
HHCCCCHHHHHHHHH		24.90-
1230UbiquitinationFHNGLKICEKFGPNL
CCCCHHHHHHHCCCC		4.4422053931
1232UbiquitinationNGLKICEKFGPNLDT
CCHHHHHHHCCCCCC		51.7322053931
1310UbiquitinationSAGTQGDMEKADMVD
CCCCCCCHHHHHCCC		7.9232015554
1312UbiquitinationGTQGDMEKADMVDGI
CCCCCHHHHHCCCCC		42.9432015554
1318UbiquitinationEKADMVDGIKESVCW
HHHHCCCCCHHCCCC		22.8132015554
1320UbiquitinationADMVDGIKESVCWGP
HHCCCCCHHCCCCCC		49.8432015554
1332PhosphorylationWGPPPAASPLKSCEY
CCCCCCCCCCHHHHH		32.6325159151
1413 (in isoform 2)Ubiquitination-30.3421890473
1413UbiquitinationRLEAGTLTKKWHMAY
CCCCCCCCCCEEHHH		30.3421890473
1414AcetylationLEAGTLTKKWHMAYH
CCCCCCCCCEEHHHC		57.9125953088
1415 (in isoform 1)Ubiquitination-36.7821890473
1415UbiquitinationEAGTLTKKWHMAYHG
CCCCCCCCEEHHHCC		36.7821890473
1449UbiquitinationASILSCRPLKGEPGV
EEEEECCCCCCCCCC		42.6329901268
1451UbiquitinationILSCRPLKGEPGVGF
EEECCCCCCCCCCCC		65.0029901268
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
-KUbiquitinationE3 ubiquitin ligaseHERC2O95714
PMID:22261722
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

22261722
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 NEUL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CP110_HUMANCCP110physical
22441691
CEP76_HUMANCEP76physical
22441691
CP110_HUMANCCP110physical
22261722
CEP97_HUMANCEP97physical
22261722
HERC2_HUMANHERC2physical
22261722
G6PI_HUMANGPIphysical
22261722
SSA27_HUMANSSSCA1physical
22261722
KTN1_HUMANKTN1physical
22261722
ECI2_HUMANECI2physical
22261722
PCM1_HUMANPCM1physical
22261722
RFA3_HUMANRPA3physical
22261722
RFA1_HUMANRPA1physical
22261722
MA7D1_HUMANMAP7D1physical
22261722
CE170_HUMANCEP170physical
22261722
MK06_HUMANMAPK6physical
22261722
VAC14_HUMANVAC14physical
22261722
RFA2_HUMANRPA2physical
22261722
RPB1_HUMANPOLR2Aphysical
22261722
CE290_HUMANCEP290physical
22261722
CP110_HUMANCCP110physical
23486064
UBP20_HUMANUSP20physical
23486064
CEP97_HUMANCEP97physical
23486064
DLL1_RATDll1physical
26355680
RAB5A_HUMANRAB5Aphysical
26355680
RAB5B_HUMANRAB5Bphysical
26355680
SPAG5_HUMANSPAG5physical
27173435
MYCB2_HUMANMYCBP2physical
27173435
RFC4_HUMANRFC4physical
27173435
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 NEUL4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-907, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-1145, ANDMASS SPECTROMETRY.

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