ALS2_HUMAN - dbPTM
ALS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALS2_HUMAN
UniProt AC Q96Q42
Protein Name Alsin
Gene Name ALS2
Organism Homo sapiens (Human).
Sequence Length 1657
Subcellular Localization
Protein Description May act as a GTPase regulator. Controls survival and growth of spinal motoneurons (By similarity)..
Protein Sequence MDSKKRSSTEAEGSKERGLVHIWQAGSFPITPERLPGWGGKTVLQAALGVKHGVLLTEDGEVYSFGTLPWRSGPVEICPSSPILENALVGQYVITVATGSFHSGAVTDNGVAYMWGENSAGQCAVANQQYVPEPNPVSIADSEASPLLAVRILQLACGEEHTLALSISREIWAWGTGCQLGLITTAFPVTKPQKVEHLAGRVVLQVACGAFHSLALVQCLPSQDLKPVPERCNQCSQLLITMTDKEDHVIISDSHCCPLGVTLTESQAENHASTALSPSTETLDRQEEVFENTLVANDQSVATELNAVSAQITSSDAMSSQQNVMGTTEISSARNIPSYPDTQAVNEYLRKLSDHSVREDSEHGEKPVPSQPLLEEAIPNLHSPPTTSTSALNSLVVSCASAVGVRVAATYEAGALSLKKVMNFYSTTPCETGAQAGSSAIGPEGLKDSREEQVKQESMQGKKSSSLVDIREEETEGGSRRLSLPGLLSQVSPRLLRKAARVKTRTVVLTPTYSGEADALLPSLRTEVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGYHSLALTAKSQVYSWGSNTFGQLGHSDFPTTVPRLAKISSENGVWSIAAGRDYSLFLVDTEDFQPGLYYSGRQDPTEGDNLPENHSGSKTPVLLSCSKLGYISRVTAGKDSYLALVDKNIMGYIASLHELATTERRFYSKLSDIKSQILRPLLSLENLGTTTTVQLLQEVASRFSKLCYLIGQHGASLSSFLHGVKEARSLVILKHSSLFLDSYTEYCTSITNFLVMGGFQLLAKPAIDFLNKNQELLQDLSEVNDENTQLMEILNTLFFLPIRRLHNYAKVLLKLATCFEVASPEYQKLQDSSSCYECLALHLGRKRKEAEYTLGFWKTFPGKMTDSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGGVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQALRGMSDLPPYGSGSSVQRQEPPISRSAKYTFYKDPRLKDATYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKAMNKEDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHGLLRSGKLTSSSPSMFIGQWVMDKKAGYGVFDDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDWTLSGKGTLTMPNGDYIEGYFSGEWGSGIKITGTYFKPSLYESDKDRPKVFRKLGNLAVPADEKWKAVFDECWRQLGCEGPGQGEVWKAWDNIAVALTTSRRQHRDSPEILSRSQTQTLESLEFIPQHVGAFSVEKYDDIRKYLIKACDTPLHPLGRLVETLVAVYRMTYVGVGANRRLLQEAVKEIKSYLKRIFQLVRFLFPELPEEGSTIPLSAPLPTERKSFCTGKSDSRSESPEPGYVVTSSGLLLPVLLPRLYPPLFMLYALDNDREEDIYWECVLRLNKQPDIALLGFLGVQRKFWPATLSILGESKKVLPTTKDACFASAVECLQQISTTFTPSDKLKVIQQTFEEISQSVLASLHEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPYLQHGEQGIMFTTLKACYYQIQREKLN
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
9PhosphorylationDSKKRSSTEAEGSKE
CCCCCCCCCCCCCCC		40.2228985074
31PhosphorylationQAGSFPITPERLPGW
ECCCCCCCCCCCCCC		21.2346162777
41UbiquitinationRLPGWGGKTVLQAAL
CCCCCCHHHHHHHHH		31.36-
166PhosphorylationEEHTLALSISREIWA
CCCEEHHEEEHHHHH		16.9524719451
353PhosphorylationNEYLRKLSDHSVRED
HHHHHHHCCCCCCCC		35.9926657352
356PhosphorylationLRKLSDHSVREDSEH
HHHHCCCCCCCCCCC		28.0629449344
361PhosphorylationDHSVREDSEHGEKPV
CCCCCCCCCCCCCCC		27.0969013021
417PhosphorylationTYEAGALSLKKVMNF
EEECCCCCHHHHHCC		37.2924719451
425PhosphorylationLKKVMNFYSTTPCET
HHHHHCCCCCCCCCC		10.4923879269
426PhosphorylationKKVMNFYSTTPCETG
HHHHCCCCCCCCCCC		22.9723879269
464PhosphorylationESMQGKKSSSLVDIR
HHHCCCCCCCCEECC		28.7530266825
465PhosphorylationSMQGKKSSSLVDIRE
HHCCCCCCCCEECCH		36.2530266825
466PhosphorylationMQGKKSSSLVDIREE
HCCCCCCCCEECCHH		39.2319664994
475PhosphorylationVDIREEETEGGSRRL
EECCHHHCCCCCCCC		43.1223403867
479PhosphorylationEEETEGGSRRLSLPG
HHHCCCCCCCCCHHH		25.6923403867
481MethylationETEGGSRRLSLPGLL
HCCCCCCCCCHHHHH		30.26-
483PhosphorylationEGGSRRLSLPGLLSQ
CCCCCCCCHHHHHHH		30.6119664994
489PhosphorylationLSLPGLLSQVSPRLL
CCHHHHHHHCCHHHH		33.3130266825
492PhosphorylationPGLLSQVSPRLLRKA
HHHHHHCCHHHHHHH		9.1819664994
506PhosphorylationAARVKTRTVVLTPTY
HCCCCCCEEEECCCC		21.8725850435
510PhosphorylationKTRTVVLTPTYSGEA
CCCEEEECCCCCCCH		11.2825850435
512PhosphorylationRTVVLTPTYSGEADA
CEEEECCCCCCCHHH		25.6925850435
513PhosphorylationTVVLTPTYSGEADAL
EEEECCCCCCCHHHH		18.8425954137
514PhosphorylationVVLTPTYSGEADALL
EEECCCCCCCHHHHC		32.4125850435
523PhosphorylationEADALLPSLRTEVWT
CHHHHCHHHEEEEEE		30.3824719451
526PhosphorylationALLPSLRTEVWTWGK
HHCHHHEEEEEEECC		39.9446162783
530PhosphorylationSLRTEVWTWGKGKEG
HHEEEEEEECCCCCC		29.5246162789
533MalonylationTEVWTWGKGKEGQLG
EEEEEECCCCCCCCC		59.3726320211
533AcetylationTEVWTWGKGKEGQLG
EEEEEECCCCCCCCC		59.3719608861
644PhosphorylationYSGRQDPTEGDNLPE
ECCCCCCCCCCCCCC		61.9722210691
656PhosphorylationLPENHSGSKTPVLLS
CCCCCCCCCCCEEEE		36.0522210691
658PhosphorylationENHSGSKTPVLLSCS
CCCCCCCCCEEEEEC		21.9622210691
677UbiquitinationISRVTAGKDSYLALV
EEEEECCCCCEEEEE		40.83-
714PhosphorylationSKLSDIKSQILRPLL
HHHHHHHHHHHHHHH		23.8446162771
849 (in isoform 1)Ubiquitination-24.0521890473
849UbiquitinationRRLHNYAKVLLKLAT
HHHHHHHHHHHHHHH		24.0521890473
849UbiquitinationRRLHNYAKVLLKLAT
HHHHHHHHHHHHHHH		24.0521890473
906PhosphorylationFPGKMTDSLRKPERR
CCCCCCCCCCCHHHH		22.4026091039
993UbiquitinationISSTPQEKTKWLRAI
ECCCHHHHHHHHHHH		50.59-
1036PhosphorylationPISRSAKYTFYKDPR
CCCCCCCEEEECCCC		11.2028152594
1037PhosphorylationISRSAKYTFYKDPRL
CCCCCCEEEECCCCC		21.5628152594
1039PhosphorylationRSAKYTFYKDPRLKD
CCCCEEEECCCCCCC		13.4928152594
1055PhosphorylationTYDGRWLSGKPHGRG
EECCCCCCCCCCCCC		37.50108417795
1057UbiquitinationDGRWLSGKPHGRGVL
CCCCCCCCCCCCCCE		30.39-
1084PhosphorylationRNGLEDGYGEYRIPN
CCCCCCCCCCCCCCC		21.077067023
1144PhosphorylationLLRSGKLTSSSPSMF
CCCCCCCCCCCCCCC		30.0127251275
1145PhosphorylationLRSGKLTSSSPSMFI
CCCCCCCCCCCCCCC		38.9828348404
1146PhosphorylationRSGKLTSSSPSMFIG
CCCCCCCCCCCCCCE		40.8228348404
1147PhosphorylationSGKLTSSSPSMFIGQ
CCCCCCCCCCCCCEE		22.2924719451
1149PhosphorylationKLTSSSPSMFIGQWV
CCCCCCCCCCCEEEH		28.4228348404
1160UbiquitinationGQWVMDKKAGYGVFD
EEEHHCCCCCCCCCC		42.66-
1281AcetylationDRPKVFRKLGNLAVP
CCCHHHHHHCCCCCC		49.6420167786
1292AcetylationLAVPADEKWKAVFDE
CCCCCCHHHHHHHHH		55.327696719
1335PhosphorylationSRRQHRDSPEILSRS
CCCCCCCCHHHHCCH		25.1223401153
1340PhosphorylationRDSPEILSRSQTQTL
CCCHHHHCCHHCCCH		35.2323403867
1342PhosphorylationSPEILSRSQTQTLES
CHHHHCCHHCCCHHH		33.9228857561
1344PhosphorylationEILSRSQTQTLESLE
HHHCCHHCCCHHHHC		25.4317525332
1346PhosphorylationLSRSQTQTLESLEFI
HCCHHCCCHHHHCCC		35.5627251275
1349PhosphorylationSQTQTLESLEFIPQH
HHCCCHHHHCCCHHH		35.99113332709
1394PhosphorylationVETLVAVYRMTYVGV
HHHHHHHHHHHHCCC		5.7322817900
1398PhosphorylationVAVYRMTYVGVGANR
HHHHHHHHCCCCHHH		5.9522817900
1417PhosphorylationEAVKEIKSYLKRIFQ
HHHHHHHHHHHHHHH		41.1628851738
1452PhosphorylationPLPTERKSFCTGKSD
CCCCCCCCCCCCCCC		31.6024719451
1458PhosphorylationKSFCTGKSDSRSESP
CCCCCCCCCCCCCCC		42.0122115753
1460PhosphorylationFCTGKSDSRSESPEP
CCCCCCCCCCCCCCC		44.8130278072
1462PhosphorylationTGKSDSRSESPEPGY
CCCCCCCCCCCCCCE		46.5122167270
1464PhosphorylationKSDSRSESPEPGYVV
CCCCCCCCCCCCEEE		35.4922167270
1469PhosphorylationSESPEPGYVVTSSGL
CCCCCCCEEEECCCC		11.4922167270
1472PhosphorylationPEPGYVVTSSGLLLP
CCCCEEEECCCCCHH		13.7128176443
1473PhosphorylationEPGYVVTSSGLLLPV
CCCEEEECCCCCHHH		15.7028176443
1474PhosphorylationPGYVVTSSGLLLPVL
CCEEEECCCCCHHHH		24.8828176443
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 ALS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALS2_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 ALS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEK1_HUMANNEK1physical
28514442
CU002_HUMANC21orf2physical
28514442
RBM6_HUMANRBM6physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
205100Amyotrophic lateral sclerosis 2 (ALS2)
606353Juvenile primary lateral sclerosis (JPLS)
607225Infantile-onset ascending spastic paralysis (IAHSP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALS2_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-533, AND MASS SPECTROMETRY.
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-483 AND SER-492, ANDMASS SPECTROMETRY.
"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-1464, 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-483 AND SER-492, ANDMASS SPECTROMETRY.
"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-483 AND SER-492, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1464, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1344, AND MASSSPECTROMETRY.

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