CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004269
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein 1B 
Protein Synonyms/Alias
 MAP-1B; MAP1(X); MAP1.2; MAP1B heavy chain; MAP1 light chain LC1 
Gene Name
 Map1b 
Gene Synonyms/Alias
 Mtap1b; Mtap5 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
327INSMLQRKIAELEEEubiquitination[1]
366LNVPENLKDPEPNIKubiquitination[1]
394YLNKLSMKPEPLFRSubiquitination[1]
429MYVLNPVKSSKEMQYubiquitination[1]
432LNPVKSSKEMQYFMQubiquitination[1]
446QQWTGTNKDKAELILubiquitination[1]
504NILEGLEKLKHLDFLubiquitination[1]
519KQPLATQKDLTGQVPubiquitination[1]
841TKDFEELKAEEIDVAubiquitination[1]
852IDVAKDIKPQLELIEubiquitination[1]
863ELIEDEEKLKETQPGubiquitination[1]
865IEDEEKLKETQPGEAubiquitination[1]
877GEAYVIQKETEVSKGubiquitination[1]
1464STGFIPIKEDFGPEKubiquitination[1]
1777EGEKLSPKSDISPLTubiquitination[1]
1904VGGYYYEKTERTIKSubiquitination[1]
1941YTCEITEKTTRTPEEubiquitination[1]
1958YSYEISEKTTRTPEVubiquitination[1]
1972VSGYTYEKTERSRRLacetylation[2]
1972VSGYTYEKTERSRRLubiquitination[1]
2026YSYETSTKTTRSPDTubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 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 (By similarity). Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation. 
Sequence Annotation
 REPEAT 1874 1890 MAP1B 1.
 REPEAT 1891 1907 MAP1B 2.
 REPEAT 1908 1924 MAP1B 3.
 REPEAT 1925 1941 MAP1B 4.
 REPEAT 1942 1958 MAP1B 5.
 REPEAT 1959 1975 MAP1B 6.
 REPEAT 1993 2009 MAP1B 7.
 REPEAT 2010 2026 MAP1B 8.
 REPEAT 2027 2043 MAP1B 9.
 REPEAT 2044 2060 MAP1B 10.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 336 336 Phosphoserine (By similarity).
 MOD_RES 527 527 Phosphothreonine.
 MOD_RES 541 541 Phosphoserine.
 MOD_RES 544 544 Phosphoserine.
 MOD_RES 561 561 Phosphoserine.
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 828 828 Phosphoserine.
 MOD_RES 829 829 Phosphoserine.
 MOD_RES 934 934 Phosphoserine.
 MOD_RES 989 989 Phosphoserine.
 MOD_RES 992 992 Phosphoserine.
 MOD_RES 1013 1013 Phosphoserine.
 MOD_RES 1141 1141 Phosphoserine (By similarity).
 MOD_RES 1151 1151 Phosphoserine.
 MOD_RES 1153 1153 Phosphoserine (By similarity).
 MOD_RES 1204 1204 Phosphoserine.
 MOD_RES 1247 1247 Phosphoserine.
 MOD_RES 1251 1251 Phosphoserine.
 MOD_RES 1255 1255 Phosphoserine.
 MOD_RES 1260 1260 Phosphoserine.
 MOD_RES 1271 1271 Phosphoserine (By similarity).
 MOD_RES 1275 1275 Phosphoserine (By similarity).
 MOD_RES 1277 1277 Phosphothreonine.
 MOD_RES 1307 1307 Phosphoserine.
 MOD_RES 1317 1317 Phosphoserine.
 MOD_RES 1319 1319 Phosphoserine.
 MOD_RES 1331 1331 Phosphotyrosine.
 MOD_RES 1332 1332 Phosphotyrosine.
 MOD_RES 1334 1334 Phosphoserine.
 MOD_RES 1371 1371 Phosphoserine.
 MOD_RES 1373 1373 Phosphoserine.
 MOD_RES 1382 1382 Phosphoserine.
 MOD_RES 1384 1384 Phosphoserine.
 MOD_RES 1391 1391 Phosphoserine.
 MOD_RES 1395 1395 Phosphoserine.
 MOD_RES 1403 1403 Phosphoserine.
 MOD_RES 1422 1422 Phosphoserine.
 MOD_RES 1438 1438 Phosphoserine.
 MOD_RES 1497 1497 Phosphoserine.
 MOD_RES 1614 1614 Phosphoserine (By similarity).
 MOD_RES 1616 1616 Phosphoserine.
 MOD_RES 1621 1621 Phosphoserine.
 MOD_RES 1649 1649 Phosphoserine (By similarity).
 MOD_RES 1768 1768 Phosphoserine.
 MOD_RES 1775 1775 Phosphoserine.
 MOD_RES 1778 1778 Phosphoserine.
 MOD_RES 1781 1781 Phosphoserine.
 MOD_RES 1784 1784 Phosphothreonine.
 MOD_RES 1789 1789 Phosphoserine.
 MOD_RES 1792 1792 Phosphotyrosine.
 MOD_RES 1793 1793 Phosphoserine.
 MOD_RES 1806 1806 Phosphothreonine.
 MOD_RES 1813 1813 Phosphoserine.
 MOD_RES 1815 1815 Phosphoserine.
 MOD_RES 1877 1877 Phosphoserine.
 MOD_RES 1911 1911 Phosphoserine.
 MOD_RES 1928 1928 Phosphothreonine.
 MOD_RES 1945 1945 Phosphothreonine.
 MOD_RES 2030 2030 Phosphoserine.
 MOD_RES 2068 2068 Phosphoserine.
 MOD_RES 2094 2094 Phosphoserine.
 MOD_RES 2267 2267 Phosphoserine (By similarity).
 MOD_RES 2285 2285 Phosphoserine (By similarity).
 MOD_RES 2460 2460 S-nitrosocysteine.  
Keyword
 Acetylation; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2464 AA 
Protein Sequence
MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE 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 LEEERSQGST SNSDWMKNLI SPDLGVVFLN 360
VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIEPVI LFQKMGVGKL 420
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE LILPNGQEVD IPISYLTSVS SLIVWHPANP 480
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD 540
SRESLKPATK PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP 600
SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK EEKPKKEVVK 660
KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK ETPLKDAKKE VKKEEKKEVK 720
KEEKEPKKEI KKISKDIKKS TPLSDTKKPS ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK 780
VIKKEGKTTE AAATAVGTAA TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL 840
KAEEIDVAKD IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG 900
ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE PEEDGEDNAS 960
GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED MDDVLEKGEA EQSEEEGEEE 1020
DKAEDAREEG YEPDKTEAED YVMAVADKAA EAGVTEEQYG YLGTSAKQPG IQSPSREPAS 1080
SIHDETLPGG SESEATASDE ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM 1140
SDETNNEETE SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA 1200
STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK SPSLSPSPPS 1260
PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV VEEHCASPEE KTLEVVSPSQ 1320
SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK PQAVPVSFEF SEAKDENERA SLSPMDEPVP 1380
DSESPVEKVL SPLRSPPLLG SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV 1440
SDLTSTGLYQ DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ 1500
IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST ASVATSSFPE 1560
PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET EMSPSKEECP RPMSISPPDF 1620
SPKTAKSRTP VQDHRSEQSS MSIEFGQESP EHSLAMDFSR QSPDHPTLGA SVLHITENGP 1680
TEVDYSPSDI QDSSLSHKIP PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP 1740
LQEDTLSDVV PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST 1800
SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS SVEKDSGGKT 1860
PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY YYEKTERTIK SPCDSGYSYE 1920
TIEKTIKTPE DGGYTCEITE KTTRTPEEGG YSYEISEKTT RTPEVSGYTY EKTERSRRLL 1980
DDISNGYDDT EDGGHTLGDC SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET 2040
MEKITKTPQA STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP 2100
NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA PSQTDSDVPP 2160
ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP MQDRSPSPRH PDVSMVDPDA 2220
LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS SSPVKKGDGK SKPLAASPKP GALKESSDKV 2280
SRVASPKKKE SVEKATKTTT TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT 2340
AKSSTVPPGL PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA 2400
LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV VMQDESFPAC 2460
KIEL 2464 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; TAS:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
 GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI.
 GO:0016787; F:hydrolase activity; IEA:InterPro.
 GO:0048675; P:axon extension; IMP:MGI.
 GO:0016358; P:dendrite development; IMP:MGI.
 GO:0061162; P:establishment of monopolar cell polarity; IMP:MGI.
 GO:0001578; P:microtubule bundle formation; IMP:MGI.
 GO:0047497; P:mitochondrion transport along microtubule; IMP:MGI.
 GO:0032387; P:negative regulation of intracellular transport; IMP:MGI.
 GO:0045773; P:positive regulation of axon extension; IMP:MGI. 
Interpro
 IPR001279; Beta-lactamas-like.
 IPR026074; MAP1.
 IPR027321; MAP1B.
 IPR000102; MAP1B_neuraxin. 
Pfam
 PF00414; MAP1B_neuraxin 
SMART
  
PROSITE
 PS00230; MAP1B_NEURAXIN 
PRINTS