Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P46821 (MAP1B_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Microtubule-associated protein 1B

Gene

MAP1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  • microtubule binding Source: ARUK-UCL
  • structural molecule activity Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • axon extension Source: ARUK-UCL
  • cellular process Source: DFLAT
  • dendrite development Source: Ensembl
  • establishment of monopolar cell polarity Source: Ensembl
  • microtubule bundle formation Source: Ensembl
  • mitochondrion transport along microtubule Source: Ensembl
  • negative regulation of intracellular transport Source: Ensembl
  • neuron migration Source: ARUK-UCL
  • positive regulation of axon extension Source: Ensembl
View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

SIGNORiP46821

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Cleaved into the following 2 chains:
MAP1B heavy chain
MAP1 light chain LC1
Gene namesi
Name:MAP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000131711.14
HGNCiHGNC:6836 MAP1B
MIMi157129 gene
neXtProtiNX_P46821

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

Pathology & Biotechi

Organism-specific databases

DisGeNETi4131
OpenTargetsiENSG00000131711
PharmGKBiPA30581

Chemistry databases

ChEMBLiCHEMBL3217382

Polymorphism and mutation databases

BioMutaiMAP1B
DMDMi317373388

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000186042 – 2468Microtubule-associated protein 1BAdd BLAST2467
ChainiPRO_00004183792 – 2206MAP1B heavy chainAdd BLAST2205
ChainiPRO_00000186052207 – 2468MAP1 light chain LC1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei336PhosphoserineCombined sources1
Modified residuei339PhosphoserineBy similarity1
Modified residuei343PhosphoserineCombined sources1
Modified residuei527PhosphothreonineBy similarity1
Modified residuei541PhosphoserineCombined sources1
Modified residuei544PhosphoserineBy similarity1
Modified residuei561PhosphoserineBy similarity1
Modified residuei614PhosphoserineCombined sources1
Modified residuei828PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei832PhosphoserineCombined sources1
Modified residuei891PhosphoserineBy similarity1
Modified residuei899PhosphothreonineBy similarity1
Modified residuei908PhosphothreonineBy similarity1
Modified residuei936PhosphoserineBy similarity1
Modified residuei937PhosphoserineCombined sources1
Modified residuei948PhosphothreonineCombined sources1
Modified residuei970PhosphoserineBy similarity1
Modified residuei977PhosphoserineBy similarity1
Modified residuei992PhosphoserineCombined sources1
Modified residuei995PhosphoserineCombined sources1
Modified residuei1016PhosphoserineCombined sources1
Modified residuei1144PhosphoserineCombined sources1
Modified residuei1154PhosphoserineCombined sources1
Modified residuei1156PhosphoserineCombined sources1
Modified residuei1187PhosphoserineBy similarity1
Modified residuei1190PhosphoserineBy similarity1
Modified residuei1208PhosphoserineCombined sources1
Modified residuei1211PhosphoserineBy similarity1
Modified residuei1212PhosphoserineBy similarity1
Modified residuei1229PhosphoserineBy similarity1
Modified residuei1247PhosphoserineBy similarity1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1256PhosphoserineCombined sources1
Modified residuei1258PhosphoserineBy similarity1
Modified residuei1260PhosphoserineCombined sources1
Modified residuei1262PhosphoserineCombined sources1
Modified residuei1265PhosphoserineCombined sources1
Modified residuei1276PhosphoserineCombined sources1
Modified residuei1280PhosphoserineCombined sources1
Modified residuei1282PhosphothreonineCombined sources1
Modified residuei1298PhosphoserineCombined sources1
Modified residuei1312PhosphoserineBy similarity1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1324PhosphoserineBy similarity1
Modified residuei1326PhosphoserineBy similarity1
Modified residuei1328PhosphothreonineBy similarity1
Modified residuei1330PhosphoserineBy similarity1
Modified residuei1339PhosphoserineBy similarity1
Modified residuei1376PhosphoserineBy similarity1
Modified residuei1378PhosphoserineCombined sources1
Modified residuei1387PhosphoserineCombined sources1
Modified residuei1389PhosphoserineCombined sources1
Modified residuei1396PhosphoserineCombined sources1
Modified residuei1400PhosphoserineCombined sources1
Modified residuei1408PhosphoserineBy similarity1
Modified residuei1410PhosphotyrosineBy similarity1
Modified residuei1427PhosphoserineCombined sources1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1443PhosphoserineCombined sources1
Modified residuei1501PhosphoserineCombined sources1
Modified residuei1512PhosphoserineBy similarity1
Modified residuei1520PhosphoserineBy similarity1
Modified residuei1522PhosphoserineBy similarity1
Modified residuei1525PhosphothreonineBy similarity1
Modified residuei1527PhosphoserineBy similarity1
Modified residuei1618PhosphoserineCombined sources1
Modified residuei1620PhosphoserineCombined sources1
Modified residuei1625PhosphoserineCombined sources1
Modified residuei1653PhosphoserineCombined sources1
Modified residuei1663PhosphoserineBy similarity1
Modified residuei1666PhosphoserineCombined sources1
Modified residuei1690PhosphoserineBy similarity1
Modified residuei1772PhosphoserineBy similarity1
Modified residuei1779PhosphoserineCombined sources1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1785PhosphoserineCombined sources1
Modified residuei1788PhosphothreonineCombined sources1
Modified residuei1792PhosphoserineBy similarity1
Modified residuei1793PhosphoserineCombined sources1
Modified residuei1796PhosphotyrosineBy similarity1
Modified residuei1797PhosphoserineCombined sources1
Modified residuei1801PhosphoserineBy similarity1
Modified residuei1819PhosphoserineBy similarity1
Modified residuei1881PhosphoserineBy similarity1
Modified residuei1899PhosphoserineCombined sources1
Modified residuei1915PhosphoserineCombined sources1
Modified residuei1917PhosphoserineCombined sources1
Modified residuei1919PhosphoserineCombined sources1
Modified residuei1932PhosphothreonineCombined sources1
Modified residuei1939PhosphoserineCombined sources1
Modified residuei1949PhosphothreonineCombined sources1
Modified residuei1965PhosphoserineCombined sources1
Modified residuei2034PhosphothreonineCombined sources1
Modified residuei2209PhosphoserineCombined sources1
Modified residuei2271PhosphoserineCombined sources1
Modified residuei2289PhosphoserineCombined sources1
Modified residuei2305PhosphothreonineCombined sources1
Modified residuei2414PhosphoserineBy similarity1
Modified residuei2464S-nitrosocysteineBy similarity1

Post-translational modificationi

LC1 is generated from MAP1B by proteolytic processing.1 Publication
S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP46821
MaxQBiP46821
PaxDbiP46821
PeptideAtlasiP46821
PRIDEiP46821
ProteomicsDBi55766

PTM databases

CarbonylDBiP46821
iPTMnetiP46821
PhosphoSitePlusiP46821

Expressioni

Gene expression databases

BgeeiENSG00000131711
CleanExiHS_MAP1B
ExpressionAtlasiP46821 baseline and differential
GenevisibleiP46821 HS

Organism-specific databases

HPAiCAB009792
HPA022275

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL (By similarity). Interacts (via C-terminus) with GAN (via Kelch domains) (PubMed:12147674, PubMed:16227972). Interacts (via N-terminus) with DAPK1 (PubMed:18195017). Interacts with TMEM185A (PubMed:15525354). Interacts with MAP1LC3B (PubMed:24089205). Interacts with KIRREL3 (PubMed:25902260).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi110304, 65 interactors
DIPiDIP-33474N
IntActiP46821, 37 interactors
MINTiP46821
STRINGi9606.ENSP00000296755

Structurei

3D structure databases

ProteinModelPortaliP46821
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1878 – 1894MAP1B 1Add BLAST17
Repeati1895 – 1911MAP1B 2Add BLAST17
Repeati1912 – 1928MAP1B 3Add BLAST17
Repeati1929 – 1945MAP1B 4Add BLAST17
Repeati1946 – 1962MAP1B 5Add BLAST17
Repeati1963 – 1979MAP1B 6Add BLAST17
Repeati1997 – 2013MAP1B 7Add BLAST17
Repeati2014 – 2030MAP1B 8Add BLAST17
Repeati2031 – 2047MAP1B 9Add BLAST17
Repeati2048 – 2064MAP1B 10Add BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2294 – 2468Mediates interaction with TMEM185A1 PublicationAdd BLAST175

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi589 – 790Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add BLAST202

Domaini

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3592 Eukaryota
ENOG410XRYM LUCA
GeneTreeiENSGT00550000074593
HOGENOMiHOG000063256
HOVERGENiHBG052409
InParanoidiP46821
KOiK10429
OMAiECPRPMS
OrthoDBiEOG091G12OH
PhylomeDBiP46821
TreeFamiTF350229

Family and domain databases

InterProiView protein in InterPro
IPR026074 MAP1
IPR027321 MAP1B
IPR000102 MAP1B_neuraxin
PANTHERiPTHR13843 PTHR13843, 1 hit
PTHR13843:SF5 PTHR13843:SF5, 1 hit
PfamiView protein in Pfam
PF00414 MAP1B_neuraxin, 5 hits
PROSITEiView protein in PROSITE
PS00230 MAP1B_NEURAXIN, 6 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE 
        60         70         80         90        100
HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL 
       110        120        130        140        150
HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL 
       160        170        180        190        200
ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN 
       210        220        230        240        250
LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT 
       260        270        280        290        300
SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 
       310        320        330        340        350
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI 
       360        370        380        390        400
SPDLGVVFLN VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR 
       410        420        430        440        450
SVGNTIDPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE 
       460        470        480        490        500
FILPNGQEVD LPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE 
       510        520        530        540        550
GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD SRESLKPAAK 
       560        570        580        590        600
PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 
       610        620        630        640        650
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK 
       660        670        680        690        700
EEKEKPKKEV AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV 
       710        720        730        740        750
KKETPPKEVK KEVKKEEKKE VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK 
       760        770        780        790        800
KPAALKPKVP KKEESVKKDS VAAGKPKEKG KIKVIKKEGK AAEAVAAAVG 
       810        820        830        840        850
TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF EELKAEEVDV 
       860        870        880        890        900
TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 
       910        920        930        940        950
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE 
       960        970        980        990       1000
AEEPEEDGEE HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA 
      1010       1020       1030       1040       1050
EEDMDEAIEK GEAEQSEEEA DEEDKAEDAR EEEYEPEKME AEDYVMAVVD 
      1060       1070       1080       1090       1100
KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE PASSIHDETL PGGSESEATA 
      1110       1120       1130       1140       1150
SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR DVMSDETNNE 
      1160       1170       1180       1190       1200
ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 
      1210       1220       1230       1240       1250
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK 
      1260       1270       1280       1290       1300
VSPSKSPSLS PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE 
      1310       1320       1330       1340       1350
VTQEVVEEHC ASPEDKTLEV VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT 
      1360       1370       1380       1390       1400
EVIEKPPAVP VSFEFSDAKD ENERASVSPM DEPVPDSESP IEKVLSPLRS 
      1410       1420       1430       1440       1450
PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD QVSPVSEMTS 
      1460       1470       1480       1490       1500
TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 
      1510       1520       1530       1540       1550
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA 
      1560       1570       1580       1590       1600
SVSTASVATS SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT 
      1610       1620       1630       1640       1650
FQETEMSPSK EECPRPMSIS PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG 
      1660       1670       1680       1690       1700
QESPEQSLAM DFSRQSPDHP TVGAGVLHIT ENGPTEVDYS PSDMQDSSLS 
      1710       1720       1730       1740       1750
HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ IASPLQEDTL 
      1760       1770       1780       1790       1800
SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 
      1810       1820       1830       1840       1850
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD 
      1860       1870       1880       1890       1900
LSTPGLEKDS GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD 
      1910       1920       1930       1940       1950
VGGYYYEKIE RTTKSPSDSG YSYETIGKTT KTPEDGDYSY EIIEKTTRTP 
      1960       1970       1980       1990       2000
EEGGYSYDIS EKTTSPPEVS GYSYEKTERS RRLLDDISNG YDDSEDGGHT 
      2010       2020       2030       2040       2050
LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY CYETAEKITR 
      2060       2070       2080       2090       2100
TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 
      2110       2120       2130       2140       2150
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV 
      2160       2170       2180       2190       2200
SESAPSQTDS DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP 
      2210       2220       2230       2240       2250
PPAPVQDRSP SPRHPDVSMV DPEALAIEQN LGKALKKDLK EKTKTKKPGT 
      2260       2270       2280       2290       2300
KTKSSSPVKK SDGKSKPLAA SPKPAGLKES SDKVSRVASP KKKESVEKAA 
      2310       2320       2330       2340       2350
KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG TTKTTKSSAV 
      2360       2370       2380       2390       2400
PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 
      2410       2420       2430       2440       2450
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS 
      2460 
SSTVVMQDES FPACKIEL
Length:2,468
Mass (Da):270,634
Last modified:January 11, 2011 - v2
Checksum:i3FFDCB2E20049A8A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036016326R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs766004582Ensembl.1
Natural variantiVAR_036017574V → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs369022142Ensembl.1
Natural variantiVAR_024530594I → V3 PublicationsCorresponds to variant dbSNP:rs1866374Ensembl.1
Natural variantiVAR_030347869E → G. Corresponds to variant dbSNP:rs16876070Ensembl.1
Natural variantiVAR_0341051296P → L. Corresponds to variant dbSNP:rs34093016Ensembl.1
Natural variantiVAR_0561231917S → R. Corresponds to variant dbSNP:rs13153166Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06237 mRNA Translation: AAA18904.1
BN001084 mRNA Translation: CAM06633.1
AC012609 Genomic DNA No translation available.
AC093218 Genomic DNA No translation available.
CH471084 Genomic DNA Translation: EAW95697.1
CCDSiCCDS4012.1
RefSeqiNP_005900.2, NM_005909.4
UniGeneiHs.335079

Genome annotation databases

EnsembliENST00000296755; ENSP00000296755; ENSG00000131711
GeneIDi4131
KEGGihsa:4131
UCSCiuc003kbw.5 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiMAP1B_HUMAN
AccessioniPrimary (citable) accession number: P46821
Secondary accession number(s): A2BDK5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 11, 2011
Last modified: June 20, 2018
This is version 166 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health