CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007838
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein 1B 
Protein Synonyms/Alias
 MAP-1B; MAP1B heavy chain; MAP1 light chain LC1 
Gene Name
 MAP1B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
327INSMLQRKIAELEEEubiquitination[1]
366LNVPENLKNPEPNIKubiquitination[1]
504NILEGLEKLKHLDFLubiquitination[1]
506LEGLEKLKHLDFLKQacetylation[2]
519KQPLATQKDLTGQVPubiquitination[1]
531QVPTPVVKQTKLKQRubiquitination[1, 3]
562KSVRKESKEETPEVTubiquitination[1]
1810STSAVKEKTATCHSSubiquitination[1]
1863LEKDSGGKTPGDFSYubiquitination[1]
1894YDYESYEKTTRTSDVubiquitination[1]
1908VGGYYYEKIERTTKSubiquitination[1, 3, 4]
1914EKIERTTKSPSDSGYubiquitination[1]
1928YSYETIGKTTKTPEDubiquitination[1, 3]
1931ETIGKTTKTPEDGDYubiquitination[1]
1945YSYEIIEKTTRTPEEubiquitination[1]
1962YSYDISEKTTSPPEVubiquitination[1]
1976VSGYSYEKTERSRRLubiquitination[1, 3]
2030YSYETSTKTTRTPDTubiquitination[1, 4]
2047YCYETAEKITRTPQAubiquitination[4]
Reference
 [1] 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]
 [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] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Facilitates tyrosination of alpha-tubulin in neuronal microtubules (By similarity). Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B Binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. 
Sequence Annotation
 REPEAT 1878 1894 MAP1B 1.
 REPEAT 1895 1911 MAP1B 2.
 REPEAT 1912 1928 MAP1B 3.
 REPEAT 1929 1945 MAP1B 4.
 REPEAT 1946 1962 MAP1B 5.
 REPEAT 1963 1979 MAP1B 6.
 REPEAT 1997 2013 MAP1B 7.
 REPEAT 2014 2030 MAP1B 8.
 REPEAT 2031 2047 MAP1B 9.
 REPEAT 2048 2064 MAP1B 10.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 336 336 Phosphoserine.
 MOD_RES 527 527 Phosphothreonine (By similarity).
 MOD_RES 541 541 Phosphoserine (By similarity).
 MOD_RES 544 544 Phosphoserine (By similarity).
 MOD_RES 561 561 Phosphoserine (By similarity).
 MOD_RES 614 614 Phosphoserine (By similarity).
 MOD_RES 828 828 Phosphoserine.
 MOD_RES 831 831 Phosphoserine.
 MOD_RES 832 832 Phosphoserine.
 MOD_RES 937 937 Phosphoserine.
 MOD_RES 992 992 Phosphoserine.
 MOD_RES 995 995 Phosphoserine.
 MOD_RES 1016 1016 Phosphoserine.
 MOD_RES 1144 1144 Phosphoserine.
 MOD_RES 1154 1154 Phosphoserine.
 MOD_RES 1156 1156 Phosphoserine.
 MOD_RES 1208 1208 Phosphoserine.
 MOD_RES 1252 1252 Phosphoserine.
 MOD_RES 1256 1256 Phosphoserine.
 MOD_RES 1260 1260 Phosphoserine.
 MOD_RES 1265 1265 Phosphoserine.
 MOD_RES 1276 1276 Phosphoserine.
 MOD_RES 1280 1280 Phosphoserine.
 MOD_RES 1282 1282 Phosphothreonine.
 MOD_RES 1312 1312 Phosphoserine (By similarity).
 MOD_RES 1322 1322 Phosphoserine (By similarity).
 MOD_RES 1324 1324 Phosphoserine (By similarity).
 MOD_RES 1336 1336 Phosphotyrosine (By similarity).
 MOD_RES 1337 1337 Phosphotyrosine (By similarity).
 MOD_RES 1339 1339 Phosphoserine (By similarity).
 MOD_RES 1376 1376 Phosphoserine (By similarity).
 MOD_RES 1378 1378 Phosphoserine.
 MOD_RES 1387 1387 Phosphoserine.
 MOD_RES 1389 1389 Phosphoserine.
 MOD_RES 1396 1396 Phosphoserine.
 MOD_RES 1400 1400 Phosphoserine.
 MOD_RES 1408 1408 Phosphoserine (By similarity).
 MOD_RES 1427 1427 Phosphoserine.
 MOD_RES 1438 1438 Phosphoserine.
 MOD_RES 1443 1443 Phosphoserine.
 MOD_RES 1501 1501 Phosphoserine.
 MOD_RES 1618 1618 Phosphoserine.
 MOD_RES 1620 1620 Phosphoserine.
 MOD_RES 1625 1625 Phosphoserine.
 MOD_RES 1653 1653 Phosphoserine.
 MOD_RES 1772 1772 Phosphoserine (By similarity).
 MOD_RES 1779 1779 Phosphoserine.
 MOD_RES 1782 1782 Phosphoserine.
 MOD_RES 1785 1785 Phosphoserine.
 MOD_RES 1788 1788 Phosphothreonine.
 MOD_RES 1793 1793 Phosphoserine (By similarity).
 MOD_RES 1796 1796 Phosphotyrosine (By similarity).
 MOD_RES 1797 1797 Phosphoserine.
 MOD_RES 1817 1817 Phosphoserine (By similarity).
 MOD_RES 1819 1819 Phosphoserine (By similarity).
 MOD_RES 1881 1881 Phosphoserine (By similarity).
 MOD_RES 1915 1915 Phosphoserine.
 MOD_RES 1917 1917 Phosphoserine.
 MOD_RES 1932 1932 Phosphothreonine (By similarity).
 MOD_RES 1949 1949 Phosphothreonine (By similarity).
 MOD_RES 1965 1965 Phosphoserine.
 MOD_RES 2072 2072 Phosphoserine (By similarity).
 MOD_RES 2098 2098 Phosphoserine (By similarity).
 MOD_RES 2271 2271 Phosphoserine.
 MOD_RES 2289 2289 Phosphoserine.
 MOD_RES 2464 2464 S-nitrosocysteine (By similarity).  
Keyword
 Acetylation; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Repeat; S-nitrosylation; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2468 AA 
Protein Sequence
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE HLRRAIGNIE 60
LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV 120
STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP 180
ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP 240
SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 300
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI SPDLGVVFLN 360
VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIDPVI LFQKMGVGKL 420
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE FILPNGQEVD LPISYLTSVS SLIVWHPANP 480
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD 540
SRESLKPAAK PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 600
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK EEKEKPKKEV 660
AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV KKETPPKEVK KEVKKEEKKE 720
VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK KPAALKPKVP KKEESVKKDS VAAGKPKEKG 780
KIKVIKKEGK AAEAVAAAVG TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF 840
EELKAEEVDV TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 900
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE AEEPEEDGEE 960
HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA EEDMDEAIEK GEAEQSEEEA 1020
DEEDKAEDAR EEEYEPEKME AEDYVMAVVD KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE 1080
PASSIHDETL PGGSESEATA SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR 1140
DVMSDETNNE ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 1200
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK VSPSKSPSLS 1260
PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE VTQEVVEEHC ASPEDKTLEV 1320
VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT EVIEKPPAVP VSFEFSDAKD ENERASVSPM 1380
DEPVPDSESP IEKVLSPLRS PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD 1440
QVSPVSEMTS TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 1500
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA SVSTASVATS 1560
SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT FQETEMSPSK EECPRPMSIS 1620
PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG QESPEQSLAM DFSRQSPDHP TVGAGVLHIT 1680
ENGPTEVDYS PSDMQDSSLS HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ 1740
IASPLQEDTL SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 1800
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD LSTPGLEKDS 1860
GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD VGGYYYEKIE RTTKSPSDSG 1920
YSYETIGKTT KTPEDGDYSY EIIEKTTRTP EEGGYSYDIS EKTTSPPEVS GYSYEKTERS 1980
RRLLDDISNG YDDSEDGGHT LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY 2040
CYETAEKITR TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 2100
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV SESAPSQTDS 2160
DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP PPAPVQDRSP SPRHPDVSMV 2220
DPEALAIEQN LGKALKKDLK EKTKTKKPGT KTKSSSPVKK SDGKSKPLAA SPKPAGLKES 2280
SDKVSRVASP KKKESVEKAA KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG 2340
TTKTTKSSAV PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 2400
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS SSTVVMQDES 2460
FPACKIEL 2468 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; TAS:ProtInc.
 GO:0005886; C:plasma membrane; IDA:DFLAT.
 GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
 GO:0016787; F:hydrolase activity; IEA:InterPro.
 GO:0005198; F:structural molecule activity; NAS:ProtInc.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0009987; P:cellular process; IDA:DFLAT.
 GO:0016358; P:dendrite development; IEA:Compara.
 GO:0061162; P:establishment of monopolar cell polarity; IEA:Compara.
 GO:0001578; P:microtubule bundle formation; IEA:Compara.
 GO:0047497; P:mitochondrion transport along microtubule; IEA:Compara.
 GO:0032387; P:negative regulation of intracellular transport; IEA:Compara.
 GO:0045773; P:positive regulation of axon extension; IEA:Compara. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR026074; MAP1.
 IPR027321; MAP1B.
 IPR000102; MAP1B_neuraxin. 
Pfam
 PF00414; MAP1B_neuraxin 
SMART
  
PROSITE
 PS00230; MAP1B_NEURAXIN 
PRINTS