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Q96Q42 (ALS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alsin
Alternative name(s):
Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 6 protein
Amyotrophic lateral sclerosis 2 protein
Gene names
Name:ALS2
Synonyms:ALS2CR6, KIAA1563
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a GTPase regulator. Controls survival and growth of spinal motoneurons By similarity. Ref.2

Subunit structure

Forms a heteromeric complex with ALS2CL. Interacts with ALS2CL. Ref.9

Involvement in disease

Amyotrophic lateral sclerosis 2 (ALS2) [MIM:205100]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9

Juvenile primary lateral sclerosis (JPLS) [MIM:606353]: A neurodegenerative disorder which is closely related to but clinically distinct from amyotrophic lateral sclerosis. It is a progressive paralytic disorder which results from dysfunction of the upper motor neurons while the lower neurons are unaffected.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Infantile-onset ascending spastic paralysis (IAHSP) [MIM:607225]: Characterized by progressive spasticity and weakness of limbs.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 8 MORN repeats.

Contains 1 PH domain.

Contains 5 RCC1 repeats.

Contains 1 VPS9 domain.

Sequence caution

The sequence BAB13389.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAmyotrophic lateral sclerosis
Neurodegeneration
   DomainRepeat
   Molecular functionGuanine-nucleotide releasing factor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

endosomal transport

Inferred from electronic annotation. Source: Ensembl

endosome organization

Non-traceable author statement PubMed 12837691. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from direct assay PubMed 16049005. Source: UniProtKB

positive regulation of Rac GTPase activity

Inferred from direct assay PubMed 16049005. Source: UniProtKB

positive regulation of Rac protein signal transduction

Inferred by curator PubMed 16049005. Source: UniProtKB

positive regulation of protein kinase activity

Inferred from direct assay PubMed 16049005. Source: UniProtKB

positive regulation of protein serine/threonine kinase activity

Inferred from direct assay PubMed 16049005. Source: GOC

protein localization

Inferred from electronic annotation. Source: Ensembl

receptor recycling

Inferred from electronic annotation. Source: Ensembl

regulation of Rac GTPase activity

Inferred from direct assay PubMed 16049005. Source: GOC

regulation of Ran GTPase activity

Non-traceable author statement Ref.2. Source: GOC

regulation of endosome size

Inferred from expression pattern PubMed 15247254. Source: UniProtKB

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

vesicle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay PubMed 16085057. Source: MGI

cytosol

Inferred from direct assay PubMed 12837691. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 15371724. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from direct assay PubMed 12837691. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 15247254. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle

Inferred from direct assay PubMed 12837691. Source: UniProtKB

   Molecular_functionRab GTPase binding

Inferred from direct assay PubMed 15247254. Source: UniProtKB

Rab guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 12837691. Source: UniProtKB

Rac guanyl-nucleotide exchange factor activity

Inferred from direct assay PubMed 16049005. Source: UniProtKB

Ran guanyl-nucleotide exchange factor activity

Non-traceable author statement Ref.2. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 15247254. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from direct assay PubMed 16049005. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAB5AP203392EBI-1044902,EBI-399437

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.2 (identifier: Q96Q42-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.2 (identifier: Q96Q42-2)

The sequence of this isoform differs from the canonical sequence as follows:
     372-396: PLLEEAIPNLHSPPTTSTSALNSLV → VPAQFYKIKVCLELNCMGFSLETLK
     397-1657: Missing.
Isoform 3 (identifier: Q96Q42-3)

The sequence of this isoform differs from the canonical sequence as follows:
     785-807: YCTSITNFLVMGGFQLLAKPAID → QVSSPVSCSISAGLFCQGEQLLN
     808-1657: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16571657Alsin
PRO_0000080903

Regions

Repeat59 – 10850RCC1 1
Repeat109 – 16759RCC1 2
Repeat169 – 21850RCC1 3
Repeat525 – 57652RCC1 4
Repeat578 – 62750RCC1 5
Domain690 – 885196DH
Domain901 – 1007107PH
Repeat1049 – 107123MORN 1
Repeat1072 – 109423MORN 2
Repeat1100 – 112223MORN 3
Repeat1123 – 114523MORN 4
Repeat1151 – 117323MORN 5
Repeat1175 – 119723MORN 6
Repeat1198 – 122023MORN 7
Repeat1221 – 124424MORN 8
Domain1513 – 1657145VPS9

Amino acid modifications

Modified residue4831Phosphoserine Ref.12 Ref.14 Ref.16
Modified residue4921Phosphoserine Ref.12 Ref.14 Ref.16
Modified residue5331N6-acetyllysine Ref.15

Natural variations

Alternative sequence372 – 39625PLLEE…LNSLV → VPAQFYKIKVCLELNCMGFS LETLK in isoform 2. Ref.2
VSP_050521
Alternative sequence397 – 16571261Missing in isoform 2. Ref.2
VSP_050522
Alternative sequence785 – 80723YCTSI…KPAID → QVSSPVSCSISAGLFCQGEQ LLN in isoform 3.
VSP_050523
Alternative sequence808 – 1657850Missing in isoform 3.
VSP_050524
Natural variant941I → V.
Corresponds to variant rs3219154 [ dbSNP | Ensembl ].
VAR_036747
Natural variant1021H → R. Ref.1
VAR_015655
Natural variant1591E → K.
Corresponds to variant rs3219155 [ dbSNP | Ensembl ].
VAR_036748
Natural variant3681V → M. Ref.1 Ref.2 Ref.3 Ref.8
Corresponds to variant rs3219156 [ dbSNP | Ensembl ].
VAR_015656
Natural variant12551S → F.
Corresponds to variant rs10206276 [ dbSNP | Ensembl ].
VAR_036749
Natural variant14061R → K. Ref.1
VAR_015657

Experimental info

Sequence conflict691P → L in AAL14103. Ref.1
Sequence conflict691P → L in BAB14362. Ref.5
Sequence conflict1151W → C in AAH29174. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 0DF8AC7B259F255A

FASTA1,657183,634
        10         20         30         40         50         60 
MDSKKRSSTE AEGSKERGLV HIWQAGSFPI TPERLPGWGG KTVLQAALGV KHGVLLTEDG 

        70         80         90        100        110        120 
EVYSFGTLPW RSGPVEICPS SPILENALVG QYVITVATGS FHSGAVTDNG VAYMWGENSA 

       130        140        150        160        170        180 
GQCAVANQQY VPEPNPVSIA DSEASPLLAV RILQLACGEE HTLALSISRE IWAWGTGCQL 

       190        200        210        220        230        240 
GLITTAFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PSQDLKPVPE RCNQCSQLLI 

       250        260        270        280        290        300 
TMTDKEDHVI ISDSHCCPLG VTLTESQAEN HASTALSPST ETLDRQEEVF ENTLVANDQS 

       310        320        330        340        350        360 
VATELNAVSA QITSSDAMSS QQNVMGTTEI SSARNIPSYP DTQAVNEYLR KLSDHSVRED 

       370        380        390        400        410        420 
SEHGEKPVPS QPLLEEAIPN LHSPPTTSTS ALNSLVVSCA SAVGVRVAAT YEAGALSLKK 

       430        440        450        460        470        480 
VMNFYSTTPC ETGAQAGSSA IGPEGLKDSR EEQVKQESMQ GKKSSSLVDI REEETEGGSR 

       490        500        510        520        530        540 
RLSLPGLLSQ VSPRLLRKAA RVKTRTVVLT PTYSGEADAL LPSLRTEVWT WGKGKEGQLG 

       550        560        570        580        590        600 
HGDVLPRLQP LCVKCLDGKE VIHLEAGGYH SLALTAKSQV YSWGSNTFGQ LGHSDFPTTV 

       610        620        630        640        650        660 
PRLAKISSEN GVWSIAAGRD YSLFLVDTED FQPGLYYSGR QDPTEGDNLP ENHSGSKTPV 

       670        680        690        700        710        720 
LLSCSKLGYI SRVTAGKDSY LALVDKNIMG YIASLHELAT TERRFYSKLS DIKSQILRPL 

       730        740        750        760        770        780 
LSLENLGTTT TVQLLQEVAS RFSKLCYLIG QHGASLSSFL HGVKEARSLV ILKHSSLFLD 

       790        800        810        820        830        840 
SYTEYCTSIT NFLVMGGFQL LAKPAIDFLN KNQELLQDLS EVNDENTQLM EILNTLFFLP 

       850        860        870        880        890        900 
IRRLHNYAKV LLKLATCFEV ASPEYQKLQD SSSCYECLAL HLGRKRKEAE YTLGFWKTFP 

       910        920        930        940        950        960 
GKMTDSLRKP ERRLLCESSN RALSLQHAGR FSVNWFILFN DALVHAQFST HHVFPLATLW 

       970        980        990       1000       1010       1020 
AEPLSEEAGG VNGLKITTPE EQFTLISSTP QEKTKWLRAI SQAVDQALRG MSDLPPYGSG 

      1030       1040       1050       1060       1070       1080 
SSVQRQEPPI SRSAKYTFYK DPRLKDATYD GRWLSGKPHG RGVLKWPDGK MYSGMFRNGL 

      1090       1100       1110       1120       1130       1140 
EDGYGEYRIP NKAMNKEDHY VGHWKEGKMC GQGVYSYASG EVFEGCFQDN MRHGHGLLRS 

      1150       1160       1170       1180       1190       1200 
GKLTSSSPSM FIGQWVMDKK AGYGVFDDIT RGEKYMGMWQ DDVCQGNGVV VTQFGLYYEG 

      1210       1220       1230       1240       1250       1260 
NFHLNKMMGN GVLLSEDDTI YEGEFSDDWT LSGKGTLTMP NGDYIEGYFS GEWGSGIKIT 

      1270       1280       1290       1300       1310       1320 
GTYFKPSLYE SDKDRPKVFR KLGNLAVPAD EKWKAVFDEC WRQLGCEGPG QGEVWKAWDN 

      1330       1340       1350       1360       1370       1380 
IAVALTTSRR QHRDSPEILS RSQTQTLESL EFIPQHVGAF SVEKYDDIRK YLIKACDTPL 

      1390       1400       1410       1420       1430       1440 
HPLGRLVETL VAVYRMTYVG VGANRRLLQE AVKEIKSYLK RIFQLVRFLF PELPEEGSTI 

      1450       1460       1470       1480       1490       1500 
PLSAPLPTER KSFCTGKSDS RSESPEPGYV VTSSGLLLPV LLPRLYPPLF MLYALDNDRE 

      1510       1520       1530       1540       1550       1560 
EDIYWECVLR LNKQPDIALL GFLGVQRKFW PATLSILGES KKVLPTTKDA CFASAVECLQ 

      1570       1580       1590       1600       1610       1620 
QISTTFTPSD KLKVIQQTFE EISQSVLASL HEDFLWSMDD LFPVFLYVVL RARIRNLGSE 

      1630       1640       1650 
VHLIEDLMDP YLQHGEQGIM FTTLKACYYQ IQREKLN 

« Hide

Isoform 2 [UniParc].

Checksum: 31073E4152B67E08
Show »

FASTA39642,629
Isoform 3 [UniParc].

Checksum: 4F5438CF9A46844B
Show »

FASTA80786,782

References

« Hide 'large scale' references
[1]"The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis."
Yang Y., Hentati A., Deng H.-X., Dabbagh O., Sasaki T., Hirano M., Hung W.-Y., Ouahchi K., Yan J., Azim A.C., Cole N., Gascon G., Yagmour A., Ben-Hamida M., Pericak-Vance M., Hentati F., Siddique T.
Nat. Genet. 29:160-165(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-102 AND LYS-1406, INVOLVEMENT IN JPLS.
[2]"A gene encoding a putative GTPase regulator is mutated in familial amyotrophic lateral sclerosis 2."
Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S., Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A., Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr., Scherer S.W. expand/collapse author list , Rouleau G.A., Hayden M.R., Ikeda J.-E.
Nat. Genet. 29:166-173(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INVOLVEMENT IN ALS2, VARIANT MET-368.
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-368.
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 303-304.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT MET-368.
Tissue: Colon and Kidney.
[9]"ALS2CL, a novel ALS2-interactor, modulates ALS2-mediated endosome dynamics."
Suzuki-Utsunomiya K., Hadano S., Otomo A., Kunita R., Mizumura H., Osuga H., Ikeda J.-E.
Biochem. Biophys. Res. Commun. 354:491-497(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH ALS2CL.
[10]"Infantile-onset ascending hereditary spastic paralysis is associated with mutations in the alsin gene."
Eymard-Pierre E., Lesca G., Dollet S., Santorelli F.M., di Capua M., Bertini E., Boespflug-Tanguy O.
Am. J. Hum. Genet. 71:518-527(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IAHSP.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483 AND SER-492, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Alsod

ALS genetic mutations db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF391100 mRNA. Translation: AAL14103.1.
AB053305 mRNA. Translation: BAB69014.1.
AB053306 mRNA. Translation: BAB69015.1.
AB046783 mRNA. Translation: BAB13389.2. Different initiation.
AK023024 mRNA. Translation: BAB14362.1.
AC007242 Genomic DNA. Translation: AAX93181.1.
AC007279 Genomic DNA. Translation: AAY15058.1.
CH471063 Genomic DNA. Translation: EAW70291.1.
BC029174 mRNA. Translation: AAH29174.1.
RefSeqNP_001129217.1. NM_001135745.1.
NP_065970.2. NM_020919.3.
UniGeneHs.471096.
Hs.621812.

3D structure databases

ProteinModelPortalQ96Q42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121708. 3 interactions.
IntActQ96Q42. 3 interactions.
MINTMINT-1632128.
STRING9606.ENSP00000264276.

PTM databases

PhosphoSiteQ96Q42.

Polymorphism databases

DMDM296434394.

Proteomic databases

PaxDbQ96Q42.
PRIDEQ96Q42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264276; ENSP00000264276; ENSG00000003393. [Q96Q42-1]
ENST00000467448; ENSP00000429223; ENSG00000003393. [Q96Q42-2]
GeneID57679.
KEGGhsa:57679.
UCSCuc002uyo.3. human. [Q96Q42-1]
uc002uyq.3. human. [Q96Q42-3]
uc002uyr.3. human. [Q96Q42-2]

Organism-specific databases

CTD57679.
GeneCardsGC02M202564.
H-InvDBHIX0200249.
HGNCHGNC:443. ALS2.
HPAHPA046588.
MIM205100. phenotype.
606352. gene.
606353. phenotype.
607225. phenotype.
neXtProtNX_Q96Q42.
Orphanet293168. Infantile-onset ascending hereditary spastic paralysis.
300605. Juvenile amyotrophic lateral sclerosis.
247604. Juvenile primary lateral sclerosis.
PharmGKBPA24732.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4642.
HOVERGENHBG037320.
InParanoidQ96Q42.
KOK04575.
OMAKLATCFE.
OrthoDBEOG7C5M7B.
PhylomeDBQ96Q42.
TreeFamTF331793.

Gene expression databases

ArrayExpressQ96Q42.
BgeeQ96Q42.
CleanExHS_ALS2.
GenevestigatorQ96Q42.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.130.10.30. 2 hits.
2.30.29.30. 1 hit.
InterProIPR000219. DH-domain.
IPR003409. MORN.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR003123. VPS9.
[Graphical view]
PfamPF02493. MORN. 8 hits.
PF00415. RCC1. 4 hits.
PF00621. RhoGEF. 1 hit.
PF02204. VPS9. 1 hit.
[Graphical view]
PRINTSPR00633. RCCNDNSATION.
SMARTSM00698. MORN. 8 hits.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF50985. SSF50985. 2 hits.
PROSITEPS50010. DH_2. 1 hit.
PS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 5 hits.
PS51205. VPS9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALS2. human.
GeneWikiALS2.
GenomeRNAi57679.
NextBio64490.
PROQ96Q42.
SOURCESearch...

Entry information

Entry nameALS2_HUMAN
AccessionPrimary (citable) accession number: Q96Q42
Secondary accession number(s): Q53TT1 expand/collapse secondary AC list , Q53TV2, Q8N1E0, Q96PC4, Q96Q41, Q9H973, Q9HCK9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM