Q96Q42 (ALS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1657 AA.
Sequence status	Complete.
Protein existence	Evidence 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 diversity	Alternative splicing Polymorphism
Disease	Amyotrophic lateral sclerosis Neurodegeneration
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rac protein signal transduction Inferred from electronic annotation. Source: Compara axonogenesis Inferred from electronic annotation. Source: Compara behavioral fear response Inferred from electronic annotation. Source: Compara cell death Inferred from electronic annotation. Source: UniProtKB-KW endosomal transport Inferred from electronic annotation. Source: Compara endosome organization Non-traceable author statement PubMed 12837691. Source: UniProtKB in utero embryonic development Inferred from electronic annotation. Source: Compara locomotory behavior Inferred from electronic annotation. Source: Compara neuromuscular junction development Inferred from electronic annotation. Source: Compara 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 protein localization Inferred from electronic annotation. Source: Compara receptor recycling Inferred from electronic annotation. Source: Compara regulation of Rab GTPase activity Inferred from electronic annotation. Source: Compara regulation of endosome size Inferred from expression pattern PubMed 15247254. Source: UniProtKB response to oxidative stress Inferred from electronic annotation. Source: Compara synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara vesicle organization Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara centrosome 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 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 membrane Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara postsynaptic density Inferred from electronic annotation. Source: Compara 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_function	Rab 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 phospholipid binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activator activity Inferred from direct assay PubMed 16049005. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1657	1657	Alsin		PRO_0000080903
Regions
	Repeat	59 – 108	50	RCC1 1
	Repeat	109 – 167	59	RCC1 2
	Repeat	169 – 218	50	RCC1 3
	Repeat	525 – 576	52	RCC1 4
	Repeat	578 – 627	50	RCC1 5
	Domain	690 – 885	196	DH
	Domain	901 – 1007	107	PH
	Repeat	1049 – 1071	23	MORN 1
	Repeat	1072 – 1094	23	MORN 2
	Repeat	1100 – 1122	23	MORN 3
	Repeat	1123 – 1145	23	MORN 4
	Repeat	1151 – 1173	23	MORN 5
	Repeat	1175 – 1197	23	MORN 6
	Repeat	1198 – 1220	23	MORN 7
	Repeat	1221 – 1244	24	MORN 8
	Domain	1513 – 1657	145	VPS9
Amino acid modifications
	Modified residue	483	1	Phosphoserine Ref.12 Ref.13 Ref.15
	Modified residue	492	1	Phosphoserine Ref.12 Ref.13 Ref.15
	Modified residue	533	1	N6-acetyllysine Ref.14
Natural variations
	Alternative sequence	372 – 396	25	PLLEE…LNSLV → VPAQFYKIKVCLELNCMGFS LETLK in isoform 2. Ref.2		VSP_050521
	Alternative sequence	397 – 1657	1261	Missing in isoform 2. Ref.2		VSP_050522
	Alternative sequence	785 – 807	23	YCTSI…KPAID → QVSSPVSCSISAGLFCQGEQ LLN in isoform 3.		VSP_050523
	Alternative sequence	808 – 1657	850	Missing in isoform 3.		VSP_050524
	Natural variant	94	1	I → V. Corresponds to variant rs3219154 [ dbSNP | Ensembl ].		VAR_036747
	Natural variant	102	1	H → R. Ref.1		VAR_015655
	Natural variant	159	1	E → K. Corresponds to variant rs3219155 [ dbSNP | Ensembl ].		VAR_036748
	Natural variant	368	1	V → M. Ref.1 Ref.2 Ref.3 Ref.8 Corresponds to variant rs3219156 [ dbSNP | Ensembl ].		VAR_015656
	Natural variant	1255	1	S → F. Corresponds to variant rs10206276 [ dbSNP | Ensembl ].		VAR_036749
	Natural variant	1406	1	R → K. Ref.1		VAR_015657
Experimental info
	Sequence conflict	69	1	P → L in AAL14103. Ref.1
	Sequence conflict	69	1	P → L in BAB14362. Ref.5
	Sequence conflict	115	1	W → C in AAH29174. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 0DF8AC7B259F255A	FASTA	1,657	183,634
	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
	Isoform 2 [UniParc]. Checksum: 31073E4152B67E08	FASTA	396	42,629
	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 SEHGEKPVPS QVPAQFYKIK VCLELNCMGF SLETLK
	Isoform 3 [UniParc]. Checksum: 4F5438CF9A46844B	FASTA	807	86,782
	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 SYTEQVSSPV SCSISAGLFC QGEQLLN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[15]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00242146. IPI00295004. IPI00295005.
RefSeq	NP_001129217.1. NM_001135745.1. NP_065970.2. NM_020919.3.
UniGene	Hs.471096. Hs.621812.
3D structure databases
ProteinModelPortal	Q96Q42.
SMR	Q96Q42. Positions 41-218, 443-682.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1632128.
STRING	9606.ENSP00000264276.
PTM databases
PhosphoSite	Q96Q42.
Polymorphism databases
DMDM	296434394.
Proteomic databases
PaxDb	Q96Q42.
PRIDE	Q96Q42.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264276; ENSP00000264276; ENSG00000003393. ENST00000467448; ENSP00000429223; ENSG00000003393.
GeneID	57679.
KEGG	hsa:57679.
UCSC	uc002uyo.3. human. uc002uyq.3. human. uc002uyr.3. human.
Organism-specific databases
CTD	57679.
GeneCards	GC02M202564.
H-InvDB	HIX0200249.
HGNC	HGNC:443. ALS2.
HPA	HPA046588.
MIM	205100. phenotype. 606352. gene. 606353. phenotype. 607225. phenotype.
neXtProt	NX_Q96Q42.
Orphanet	803. Amyotrophic lateral sclerosis. 293168. Infantile-onset ascending hereditary spastic paralysis. 300605. Juvenile Amyotrophic lateral sclerosis. 247604. Juvenile primary lateral sclerosis.
PharmGKB	PA24732.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4642.
HOVERGEN	HBG037320.
InParanoid	Q96Q42.
KO	K04575.
OMA	AKPAIDF.
OrthoDB	EOG4FTVZP.
Gene expression databases
ArrayExpress	Q96Q42.
Bgee	Q96Q42.
CleanEx	HS_ALS2.
Genevestigator	Q96Q42.
GermOnline	ENSG00000003393. Homo sapiens.
Family and domain databases
Gene3D	1.20.900.10. 1 hit. 2.130.10.30. 2 hits. 2.30.29.30. 1 hit.
InterPro	IPR000219. DH-domain. IPR003409. MORN. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR009091. RCC1/BLIP-II. IPR000408. Reg_chr_condens. IPR003123. VPS9. [Graphical view]
Pfam	PF02493. MORN. 8 hits. PF00415. RCC1. 4 hits. PF00621. RhoGEF. 1 hit. PF02204. VPS9. 1 hit. [Graphical view]
PRINTS	PR00633. RCCNDNSATION.
SMART	SM00698. MORN. 8 hits. SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF48065. DH-domain. 1 hit. SSF50985. RCC1/BLIP-II. 2 hits.
PROSITE	PS00741. DH_1. False negative. PS50010. DH_2. 1 hit. PS50003. PH_DOMAIN. False negative. PS00625. RCC1_1. False negative. PS00626. RCC1_2. 2 hits. PS50012. RCC1_3. 5 hits. PS51205. VPS9. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ALS2. human.
GenomeRNAi	57679.
NextBio	64490.
SOURCE	Search...

Entry information

Entry name

ALS2_HUMAN

Accession

Primary (citable) accession number: Q96Q42
Secondary accession number(s): Q53TT1 , Q53TV2, Q8N1E0, Q96PC4, Q96Q41, Q9H973, Q9HCK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.