CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012416
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear mitotic apparatus protein 1 
Protein Synonyms/Alias
 NuMA protein; SP-H antigen 
Gene Name
 NUMA1 
Gene Synonyms/Alias
 NUMA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54EEGQQILKQPVSERLubiquitination[1]
267RLALLNEKQAASPLEubiquitination[2, 3]
303LKQCQDLKTEKSQMDubiquitination[1]
326ENGDLSFKLREFASHubiquitination[1]
364EKQAQLEKELSAALQubiquitination[1]
379DKKCLEEKNEILQGKacetylation[4]
386KNEILQGKLSQLEEHubiquitination[1, 2]
419VLQLETLKQEAATLAubiquitination[1]
604RERDAALKQLEALEKubiquitination[1]
616LEKEKAAKLEILQQQubiquitination[1]
855ELQEAKEKVAGIESHubiquitination[1]
891ALQQVQEKEVRAQKLacetylation[4, 5, 6]
891ALQQVQEKEVRAQKLubiquitination[1, 2, 6]
897EKEVRAQKLADDLSTubiquitination[1]
908DLSTLQEKMAATSKEubiquitination[1, 2, 3, 6, 7]
914EKMAATSKEVARLETubiquitination[1]
1024QADLALEKAARAELEubiquitination[6]
1121RTEPTGPKLEALRAEacetylation[5, 6, 8, 9]
1330EELGQELKAWQEKFFubiquitination[1, 2]
1335ELKAWQEKFFQKEQAubiquitination[1]
1430AQQLRAEKASYAEQLubiquitination[1]
1442EQLSMLKKAHGLLAEubiquitination[3]
1475ELDQAREKYVQELAAubiquitination[1, 3]
1511ELEVMTAKYEGAKVKacetylation[4]
1511ELEVMTAKYEGAKVKubiquitination[1, 3]
1573KVQQQKLKAVQAQGGubiquitination[2, 3]
1699QQLRDLGKFQVATDAubiquitination[1, 3]
1708QVATDALKSREPQAKubiquitination[1, 2, 3]
1715KSREPQAKPQLDLSIubiquitination[6]
1766ISQRLPPKVESLESLsumoylation[10]
1766ISQRLPPKVESLESLubiquitination[1, 2]
1803VFLDSGRKTRSARRRmethylation[11]
1821IINITMTKKLDVEEPubiquitination[1]
1822INITMTKKLDVEEPDubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] 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]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [10] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [11] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837] 
Functional Description
 Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority if the nuclear volume. Required for maintenance and establishment of the mitotic spindle poles, functionning as a tether linking bulk microtubules of the spindle to centrosomes. May be involved in coordination of the alignment of the mitotic spindle to the cellular polarity axis, which is a prerequisite for asymmetric cell divisions. 
Sequence Annotation
 REGION 1 212 Head (Globular).
 REGION 1700 2115 Tail (Globular).
 REGION 1866 1936 Interaction with microtubules.
 MOTIF 1984 1989 Nuclear localization signal.
 MOD_RES 169 169 Phosphoserine.
 MOD_RES 203 203 Phosphoserine.
 MOD_RES 211 211 Phosphothreonine.
 MOD_RES 271 271 Phosphoserine.
 MOD_RES 379 379 N6-acetyllysine.
 MOD_RES 388 388 Phosphoserine.
 MOD_RES 395 395 Phosphoserine.
 MOD_RES 820 820 Phosphoserine.
 MOD_RES 891 891 N6-acetyllysine.
 MOD_RES 1187 1187 Phosphoserine.
 MOD_RES 1225 1225 Phosphoserine.
 MOD_RES 1511 1511 N6-acetyllysine.
 MOD_RES 1601 1601 Phosphoserine.
 MOD_RES 1721 1721 Phosphoserine.
 MOD_RES 1724 1724 Phosphoserine.
 MOD_RES 1728 1728 Phosphoserine.
 MOD_RES 1757 1757 Phosphoserine.
 MOD_RES 1760 1760 Phosphoserine.
 MOD_RES 1769 1769 Phosphoserine.
 MOD_RES 1772 1772 Phosphoserine.
 MOD_RES 1774 1774 Phosphotyrosine.
 MOD_RES 1776 1776 Phosphothreonine.
 MOD_RES 1788 1788 Phosphoserine.
 MOD_RES 1789 1789 Phosphoserine.
 MOD_RES 1792 1792 Phosphoserine.
 MOD_RES 1800 1800 Phosphoserine.
 MOD_RES 1804 1804 Phosphothreonine.
 MOD_RES 1830 1830 Phosphoserine.
 MOD_RES 1833 1833 Phosphoserine.
 MOD_RES 1834 1834 Phosphoserine.
 MOD_RES 1836 1836 Phosphotyrosine.
 MOD_RES 1840 1840 Phosphoserine.
 MOD_RES 1862 1862 Phosphoserine.
 MOD_RES 1887 1887 Phosphoserine.
 MOD_RES 1969 1969 Phosphoserine.
 MOD_RES 1991 1991 Phosphoserine.
 MOD_RES 2000 2000 Phosphothreonine.
 MOD_RES 2003 2003 Phosphoserine.
 MOD_RES 2015 2015 Phosphothreonine; by CDK1.
 MOD_RES 2055 2055 Phosphothreonine; by CDK1.
 MOD_RES 2077 2077 Phosphoserine.
 MOD_RES 2087 2087 Phosphoserine; by CDK1.
 MOD_RES 2106 2106 Phosphothreonine; by CDK1.  
Keyword
 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2115 AA 
Protein Sequence
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ QILKQPVSER 60
LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM LLLYHSTMSS KSPRDWEQFE 120
YKIQAELAVI LKFVLDHEDG LNLNEDLENF LQKAPVPSTC SSTFPEELSP PSHQAKREIR 180
FLELQKVASS SSGNNFLSGS PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN 240
RKLLTEKDAQ IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ 300
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK ATQEWLEKQA 360
QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN PPQEKGEVLG DVLQLETLKQ 420
EAATLAANNT QLQARVEMLE TERGQQEAKL LAERGHFEEE KQQLSSLITD LQSSISNLSQ 480
AKEELEQASQ AHGARLTAQV ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ 540
QQEQASQGLR HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD 600
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR KVEELQACVE 660
TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL QEQLQALKES LKVTKGSLEE 720
EKRRAADALE EQQRCISELK AETRSLVEQH KRERKELEEE RAGRKGLEAR LQQLGEAHQA 780
ETEVLRRELA EAMAAQHTAE SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE 840
ECEKARQELQ EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD 900
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE WLEEQQGRQF 960
CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG QQEREVARLT QERGRAQADL 1020
ALEKAARAEL EMRLQNALNE QRVEFATLQE ALAHALTEKE GKDQELAKLR GLEAAQIKEL 1080
EELRQTVKQL KEQLAKKEKE HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ 1140
EQADSLERSL EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ 1200
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE LKRLVMAESE 1260
KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE AEKQRVASEN LRQELTSQAE 1320
RAEELGQELK AWQEKFFQKE QALSTLQLEH TSTQALVSEL LPAKHLCQQL QAEQAAAEKR 1380
HREELEQSKQ AAGGLRAELL RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML 1440
KKAHGLLAEE NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS 1500
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ VEELSKKLAD 1560
SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL SQKEQAAEHY KLQMEKAKTH 1620
YDAKKQQNQE LQEQLRSLEQ LQKENKELRA EAERLGHELQ QAGLKTKEAE QTCRHLTAQV 1680
RSLEAQVAHA DQQLRDLGKF QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK 1740
LPRTQPDGTS VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS 1800
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA TSSTQSLARL 1860
GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN SFYMGTCQDE PEQLDDWNRI 1920
AELQQRNRVC PPHLKTCYPL ESRPSLSLGT ITDEEMKTGD PQETLRRASM QPIQIAEGTG 1980
ITTRQQRKRV SLEPHQGPGT PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK 2040
QADRRQSMAF SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA 2100
AAIGATPRAK GKAKH 2115 
Gene Ontology
 GO:0045177; C:apical part of cell; IEA:Compara.
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005876; C:spindle microtubule; TAS:ProtInc.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000132; P:establishment of mitotic spindle orientation; IEA:Compara.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0060487; P:lung epithelial cell differentiation; IEA:Compara.
 GO:0000090; P:mitotic anaphase; TAS:ProtInc.
 GO:0006997; P:nucleus organization; TAS:ProtInc. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS