CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014712
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein 1S 
Protein Synonyms/Alias
 MAP-1S; BPY2-interacting protein 1; Microtubule-associated protein 8; Variable charge Y chromosome 2-interacting protein 1; VCY2-interacting protein 1; VCY2IP-1; MAP1S heavy chain; MAP1S light chain 
Gene Name
 MAP1S 
Gene Synonyms/Alias
 BPY2IP1; C19orf5; MAP8; VCY2IP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73ATFSSIVKGQRSLHHubiquitination[1, 2]
96VLLNPSDKSLYDELRubiquitination[2, 3, 4]
277NPKSSFWKLVRHLDRubiquitination[2]
380SRGPVPAKPTVLFEKubiquitination[2, 3]
387KPTVLFEKMGVGRLDubiquitination[2, 3, 4]
520RKTEKEAKTPRELKKacetylation[5]
1000LDALLASKQHWDRDLubiquitination[2, 3, 6, 7]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [6] 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]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity). 
Sequence Annotation
 REGION 1 797 Necessary for the microtubule-organizing
 REGION 666 1059 Necessary for interaction with RASSF1
 REGION 714 966 Necessary for association with
 REGION 960 1059 Necessary for association with actin (By
 REGION 967 991 Necessary for the mitochondrial
 MOD_RES 472 472 Phosphoserine.
 MOD_RES 640 640 Phosphoserine.
 MOD_RES 657 657 Phosphoserine.
 MOD_RES 759 759 Phosphoserine.
 MOD_RES 809 809 Phosphoserine.
 MOD_RES 919 919 Phosphoserine (By similarity).  
Keyword
 Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1059 AA 
Protein Sequence
MAAVAGSGAA AAPSSLLLVV GSEFGSPGLL TYVLEELERG IRSWDVDPGV CNLDEQLKVF 60
VSRHSATFSS IVKGQRSLHH RGDNLETLVL LNPSDKSLYD ELRNLLLDPA SHKLLVLAGP 120
CLEETGELLL QTGGFSPHHF LQVLKDREIR DILATTPPPV QPPILTITCP TFGDWAQLAP 180
AVPGLQGALR LQLRLNPPAQ LPNSEGLCEF LEYVAESLEP PSPFELLEPP TSGGFLRLGR 240
PCCYIFPGGL GDAAFFAVNG FTVLVNGGSN PKSSFWKLVR HLDRVDAVLV THPGADSLPG 300
LNSLLRRKLA ERSEVAAGGG SWDDRLRRLI SPNLGVVFFN ACEAASRLAR GEDEAELALS 360
LLAQLGITPL PLSRGPVPAK PTVLFEKMGV GRLDMYVLHP PSAGAERTLA SVCALLVWHP 420
AGPGEKVVRV LFPGCTPPAC LLDGLVRLQH LRFLREPVVT PQDLEGPGRA ESKESVGSRD 480
SSKREGLLAT HPRPGQERPG VARKEPARAE APRKTEKEAK TPRELKKDPK PSVSRTQPRE 540
VRRAASSVPN LKKTNAQAAP KPRKAPSTSH SGFPPVANGP RSPPSLRCGE ASPPSAACGS 600
PASQLVATPS LELGPIPAGE EKALELPLAA SSIPRPRTPS PESHRSPAEG SERLSLSPLR 660
GGEAGPDASP TVTTPTVTTP SLPAEVGSPH STEVDESLSV SFEQVLPPSA PTSEAGLSLP 720
LRGPRARRSA SPHDVDLCLV SPCEFEHRKA VPMAPAPASP GSSNDSSARS QERAGGLGAE 780
ETPPTSVSES LPTLSDSDPV PLAPGAADSD EDTEGFGVPR HDPLPDPLKV PPPLPDPSSI 840
CMVDPEMLPP KTARQTENVS RTRKPLARPN SRAAAPKATP VAAAKTKGLA GGDRASRPLS 900
ARSEPSEKGG RAPLSRKSST PKTATRGPSG SASSRPGVSA TPPKSPVYLD LAYLPSGSSA 960
HLVDEEFFQR VRALCYVISG QDQRKEEGMR AVLDALLASK QHWDRDLQVT LIPTFDSVAM 1020
HTWYAETHAR HQALGITVLG SNSMVSMQDD AFPACKVEF 1059 
Gene Ontology
 GO:0005829; C:cytosol; IDA:HGNC.
 GO:0030425; C:dendrite; ISS:HGNC.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; ISS:HGNC.
 GO:0005634; C:nucleus; IDA:HGNC.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0045202; C:synapse; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:HGNC.
 GO:0048487; F:beta-tubulin binding; IDA:HGNC.
 GO:0003677; F:DNA binding; IDA:HGNC.
 GO:0016787; F:hydrolase activity; IEA:InterPro.
 GO:0008017; F:microtubule binding; IDA:HGNC.
 GO:0006309; P:apoptotic DNA fragmentation; TAS:BHF-UCL.
 GO:0007420; P:brain development; ISS:HGNC.
 GO:0001578; P:microtubule bundle formation; IMP:HGNC.
 GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
 GO:0048812; P:neuron projection morphogenesis; IEP:HGNC. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR026074; MAP1.
 IPR027322; MAP1S. 
Pfam
  
SMART
  
PROSITE
  
PRINTS