AAAS_HUMAN - dbPTM
AAAS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAAS_HUMAN
UniProt AC Q9NRG9
Protein Name Aladin
Gene Name AAAS
Organism Homo sapiens (Human).
Sequence Length 546
Subcellular Localization Nucleus, nuclear pore complex .
Protein Description Plays a role in the normal development of the peripheral and central nervous system..
Protein Sequence MCSLGLFPPPPPRGQVTLYEHNNELVTGSSYESPPPDFRGQWINLPVLQLTKDPLKTPGRLDHGTRTAFIHHREQVWKRCINIWRDVGLFGVLNEIANSEEEVFEWVKTASGWALALCRWASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVASLAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWTCERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGKPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIAHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL
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
2Acetylation------MCSLGLFPP
------CCCCCCCCC		4.6522223895
27PhosphorylationEHNNELVTGSSYESP
ECCCEEECCCCCCCC		43.9328348404
29PhosphorylationNNELVTGSSYESPPP
CCEEECCCCCCCCCC		22.0026471730
30PhosphorylationNELVTGSSYESPPPD
CEEECCCCCCCCCCC		33.9727251275
31PhosphorylationELVTGSSYESPPPDF
EEECCCCCCCCCCCC		23.3227251275
33PhosphorylationVTGSSYESPPPDFRG
ECCCCCCCCCCCCCC		34.1825159151
52UbiquitinationLPVLQLTKDPLKTPG
CCEEEECCCCCCCCC		66.9821890473
52UbiquitinationLPVLQLTKDPLKTPG
CCEEEECCCCCCCCC		66.9821906983
56UbiquitinationQLTKDPLKTPGRLDH
EECCCCCCCCCCCCC		59.0521906983
57PhosphorylationLTKDPLKTPGRLDHG
ECCCCCCCCCCCCCC		38.3625334437
78UbiquitinationHHREQVWKRCINIWR
HCHHHHHHHHHHHHH		38.24-
133PhosphorylationGSLFPHLSLRSEDLI
CCCCCCCCCCCHHHH		20.7824719451
156UbiquitinationWSSCCLRVFAWHPHT
HHHHHHHHHEECCCC		2.1821963094
156 (in isoform 2)Ubiquitination-2.18-
165UbiquitinationAWHPHTNKFAVALLD
EECCCCCCEEEEEEC		35.54-
178PhosphorylationLDDSVRVYNASSTIV
ECCCEEEECCCCCHH		8.4120068231
181PhosphorylationSVRVYNASSTIVPSL
CEEEECCCCCHHHHH		25.1120068231
182PhosphorylationVRVYNASSTIVPSLK
EEEECCCCCHHHHHH		21.5328509920
183PhosphorylationRVYNASSTIVPSLKH
EEECCCCCHHHHHHH		24.4128509920
187PhosphorylationASSTIVPSLKHRLQR
CCCCHHHHHHHHHHH		38.8720068231
189UbiquitinationSTIVPSLKHRLQRNV
CCHHHHHHHHHHHHH		30.8923503661
189AcetylationSTIVPSLKHRLQRNV
CCHHHHHHHHHHHHH		30.8926051181
261PhosphorylationPSGGRLLSASPVDAA
CCCCCEECCCCCCCE		31.15110758977
263PhosphorylationGGRLLSASPVDAAIR
CCCEECCCCCCCEEE		23.2925884760
268UbiquitinationSASPVDAAIRVWDVS
CCCCCCCEEEEEECC		5.9021963094
268UbiquitinationSASPVDAAIRVWDVS
CCCCCCCEEEEEECC		5.9021890473
291PhosphorylationWFRGGGVTNLLWSPD
CCCCCCEEEEEECCC		24.3520068231
296PhosphorylationGVTNLLWSPDGSKIL
CEEEEEECCCCCCEE		17.0620068231
301UbiquitinationLWSPDGSKILATTPS
EECCCCCCEEEECHH		47.4721963094
305PhosphorylationDGSKILATTPSAVFR
CCCCEEEECHHHHHH		35.4825002506
306PhosphorylationGSKILATTPSAVFRV
CCCEEEECHHHHHHH		15.05110758985
308PhosphorylationKILATTPSAVFRVWE
CEEEECHHHHHHHHE		34.6725002506
333PhosphorylationTLSGRCQTGCWSPDG
CCCCCCCCCCCCCCC		37.6246156117
333UbiquitinationTLSGRCQTGCWSPDG
CCCCCCCCCCCCCCC		37.6222505724
337PhosphorylationRCQTGCWSPDGSRLL
CCCCCCCCCCCCEEE		19.7268728231
340UbiquitinationTGCWSPDGSRLLFTV
CCCCCCCCCEEEEEE		20.3221963094
341PhosphorylationGCWSPDGSRLLFTVL
CCCCCCCCEEEEEEC		27.4368728237
366UbiquitinationPERCGEGKGCVGGAK
CCHHCCCCCCCCCCC		44.8522505724
373UbiquitinationKGCVGGAKSATIVAD
CCCCCCCCCEEEEEE		43.8521963094
383UbiquitinationTIVADLSETTIQTPD
EEEEECCCCEEECCC		58.2127667366
385UbiquitinationVADLSETTIQTPDGE
EEECCCCEEECCCCC		13.6721963094
392UbiquitinationTIQTPDGEERLGGEA
EEECCCCCCCCCCCC		47.5321890473
392UbiquitinationTIQTPDGEERLGGEA
EEECCCCCCCCCCCC		47.5321963094
416UbiquitinationERLAVLMKGKPRVQD
CEEEEEECCCCCCCC		60.6727667366
418UbiquitinationLAVLMKGKPRVQDGK
EEEEECCCCCCCCCC		24.9221963094
425UbiquitinationKPRVQDGKPVILLFR
CCCCCCCCEEEEEEE		44.3821906983
462PhosphorylationPQLITFHPSFNKGAL
CEEEEECCCCCCCCE		36.1032645325
485PhosphorylationRIAHIPLYFVNAQFP
CEECCEEEEECCCCC		10.5026434776
495PhosphorylationNAQFPRFSPVLGRAQ
CCCCCCCCCCCCCCC		18.5122167270
511PhosphorylationPPAGGGGSIHDLPLF
CCCCCCCCCCCCCCC		21.7422115753
519PhosphorylationIHDLPLFTETSPTSA
CCCCCCCCCCCCCCC		46.1422115753
521PhosphorylationDLPLFTETSPTSAPW
CCCCCCCCCCCCCCC		36.6322115753
522PhosphorylationLPLFTETSPTSAPWD
CCCCCCCCCCCCCCC		21.6822115753
524PhosphorylationLFTETSPTSAPWDPL
CCCCCCCCCCCCCCC		36.9722115753
525PhosphorylationFTETSPTSAPWDPLP
CCCCCCCCCCCCCCC		35.4022115753
541PhosphorylationPPPVLPHSPHSHL--
CCCCCCCCCCCCC--		23.5122115753
544PhosphorylationVLPHSPHSHL-----
CCCCCCCCCC-----		29.8422115753
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 AAAS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAAS_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 AAAS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REL_HUMANRELphysical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
231550Achalasia-addisonianism-alacrima syndrome (AAAS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AAAS_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-495, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, 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-33 AND SER-495, 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-495, 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-495, AND MASSSPECTROMETRY.

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