CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019549
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alsin 
Protein Synonyms/Alias
 Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 6 protein; Amyotrophic lateral sclerosis 2 protein 
Gene Name
 ALS2 
Gene Synonyms/Alias
 ALS2CR6; KIAA1563 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41RLPGWGGKTVLQAALubiquitination[1]
533TEVWTWGKGKEGQLGacetylation[2, 3]
849RRLHNYAKVLLKLATubiquitination[4]
1281DRPKVFRKLGNLAVPacetylation[5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 May act as a GTPase regulator. Controls survival and growth of spinal motoneurons (By similarity). 
Sequence Annotation
 REPEAT 59 108 RCC1 1.
 REPEAT 109 167 RCC1 2.
 REPEAT 169 218 RCC1 3.
 REPEAT 525 576 RCC1 4.
 REPEAT 578 627 RCC1 5.
 DOMAIN 690 885 DH.
 DOMAIN 901 1007 PH.
 REPEAT 1049 1071 MORN 1.
 REPEAT 1072 1094 MORN 2.
 REPEAT 1100 1122 MORN 3.
 REPEAT 1123 1145 MORN 4.
 REPEAT 1151 1173 MORN 5.
 REPEAT 1175 1197 MORN 6.
 REPEAT 1198 1220 MORN 7.
 REPEAT 1221 1244 MORN 8.
 DOMAIN 1513 1657 VPS9.
 MOD_RES 483 483 Phosphoserine.
 MOD_RES 492 492 Phosphoserine.
 MOD_RES 533 533 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Amyotrophic lateral sclerosis; Complete proteome; Guanine-nucleotide releasing factor; Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1657 AA 
Protein Sequence
MDSKKRSSTE AEGSKERGLV HIWQAGSFPI TPERLPGWGG KTVLQAALGV KHGVLLTEDG 60
EVYSFGTLPW RSGPVEICPS SPILENALVG QYVITVATGS FHSGAVTDNG VAYMWGENSA 120
GQCAVANQQY VPEPNPVSIA DSEASPLLAV RILQLACGEE HTLALSISRE IWAWGTGCQL 180
GLITTAFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PSQDLKPVPE RCNQCSQLLI 240
TMTDKEDHVI ISDSHCCPLG VTLTESQAEN HASTALSPST ETLDRQEEVF ENTLVANDQS 300
VATELNAVSA QITSSDAMSS QQNVMGTTEI SSARNIPSYP DTQAVNEYLR KLSDHSVRED 360
SEHGEKPVPS QPLLEEAIPN LHSPPTTSTS ALNSLVVSCA SAVGVRVAAT YEAGALSLKK 420
VMNFYSTTPC ETGAQAGSSA IGPEGLKDSR EEQVKQESMQ GKKSSSLVDI REEETEGGSR 480
RLSLPGLLSQ VSPRLLRKAA RVKTRTVVLT PTYSGEADAL LPSLRTEVWT WGKGKEGQLG 540
HGDVLPRLQP LCVKCLDGKE VIHLEAGGYH SLALTAKSQV YSWGSNTFGQ LGHSDFPTTV 600
PRLAKISSEN GVWSIAAGRD YSLFLVDTED FQPGLYYSGR QDPTEGDNLP ENHSGSKTPV 660
LLSCSKLGYI SRVTAGKDSY LALVDKNIMG YIASLHELAT TERRFYSKLS DIKSQILRPL 720
LSLENLGTTT TVQLLQEVAS RFSKLCYLIG QHGASLSSFL HGVKEARSLV ILKHSSLFLD 780
SYTEYCTSIT NFLVMGGFQL LAKPAIDFLN KNQELLQDLS EVNDENTQLM EILNTLFFLP 840
IRRLHNYAKV LLKLATCFEV ASPEYQKLQD SSSCYECLAL HLGRKRKEAE YTLGFWKTFP 900
GKMTDSLRKP ERRLLCESSN RALSLQHAGR FSVNWFILFN DALVHAQFST HHVFPLATLW 960
AEPLSEEAGG VNGLKITTPE EQFTLISSTP QEKTKWLRAI SQAVDQALRG MSDLPPYGSG 1020
SSVQRQEPPI SRSAKYTFYK DPRLKDATYD GRWLSGKPHG RGVLKWPDGK MYSGMFRNGL 1080
EDGYGEYRIP NKAMNKEDHY VGHWKEGKMC GQGVYSYASG EVFEGCFQDN MRHGHGLLRS 1140
GKLTSSSPSM FIGQWVMDKK AGYGVFDDIT RGEKYMGMWQ DDVCQGNGVV VTQFGLYYEG 1200
NFHLNKMMGN GVLLSEDDTI YEGEFSDDWT LSGKGTLTMP NGDYIEGYFS GEWGSGIKIT 1260
GTYFKPSLYE SDKDRPKVFR KLGNLAVPAD EKWKAVFDEC WRQLGCEGPG QGEVWKAWDN 1320
IAVALTTSRR QHRDSPEILS RSQTQTLESL EFIPQHVGAF SVEKYDDIRK YLIKACDTPL 1380
HPLGRLVETL VAVYRMTYVG VGANRRLLQE AVKEIKSYLK RIFQLVRFLF PELPEEGSTI 1440
PLSAPLPTER KSFCTGKSDS RSESPEPGYV VTSSGLLLPV LLPRLYPPLF MLYALDNDRE 1500
EDIYWECVLR LNKQPDIALL GFLGVQRKFW PATLSILGES KKVLPTTKDA CFASAVECLQ 1560
QISTTFTPSD KLKVIQQTFE EISQSVLASL HEDFLWSMDD LFPVFLYVVL RARIRNLGSE 1620
VHLIEDLMDP YLQHGEQGIM FTTLKACYYQ IQREKLN 1657 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0030425; C:dendrite; IDA:UniProtKB.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0030426; C:growth cone; ISS:UniProtKB.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0016020; C:membrane; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0014069; C:postsynaptic density; IEA:Compara.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0031982; C:vesicle; IDA:UniProtKB.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
 GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
 GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; NAS:UniProtKB.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0001662; P:behavioral fear response; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0016197; P:endosomal transport; IEA:Compara.
 GO:0007032; P:endosome organization; NAS:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0007626; P:locomotory behavior; IEA:Compara.
 GO:0007528; P:neuromuscular junction development; IEA:Compara.
 GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
 GO:0032855; P:positive regulation of Rac GTPase activity; IDA:UniProtKB.
 GO:0035022; P:positive regulation of Rac protein signal transduction; IC:UniProtKB.
 GO:0008104; P:protein localization; IEA:Compara.
 GO:0016601; P:Rac protein signal transduction; IEA:Compara.
 GO:0001881; P:receptor recycling; IEA:Compara.
 GO:0051036; P:regulation of endosome size; IEP:UniProtKB.
 GO:0032313; P:regulation of Rab GTPase activity; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IEA:Compara.
 GO:0035249; P:synaptic transmission, glutamatergic; IEA:Compara.
 GO:0016050; P:vesicle organization; IEA:Compara. 
Interpro
 IPR000219; DH-domain.
 IPR003409; MORN.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR009091; RCC1/BLIP-II.
 IPR000408; Reg_chr_condens.
 IPR003123; VPS9. 
Pfam
 PF02493; MORN
 PF00415; RCC1
 PF00621; RhoGEF
 PF02204; VPS9 
SMART
 SM00698; MORN
 SM00233; PH 
PROSITE
 PS00741; DH_1
 PS50010; DH_2
 PS50003; PH_DOMAIN
 PS00625; RCC1_1
 PS00626; RCC1_2
 PS50012; RCC1_3
 PS51205; VPS9 
PRINTS
 PR00633; RCCNDNSATION.