UniProtKB - P46821 (MAP1B_HUMAN)

BLAST

>sp|P46821|MAP1B_HUMAN Microtubule-associated protein 1B OS=Homo sapiens OX=9606 GN=MAP1B PE=1 SV=2
MATVVVEATEPEPSGSIANPAASTSPSLSHRFLDSKFYLLVVVGEIVTEEHLRRAIGNIE
LGIRSWDTNLIECNLDQELKLFVSRHSARFSPEVPGQKILHHRSDVLETVVLINPSDEAV
STEVRLMITDAARHKLLVLTGQCFENTGELILQSGSFSFQNFIEIFTDQEIGELLSTTHP
ANKASLTLFCPEEGDWKNSNLDRHNLQDFINIKLNSASILPEMEGLSEFTEYLSESVEVP
SPFDILEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNMLINGGSERKSCFWKLIRH
LDRVDSILLTHIGDDNLPGINSMLQRKIAELEEEQSQGSTTNSDWMKNLISPDLGVVFLN
VPENLKNPEPNIKMKRSIEEACFTLQYLNKLSMKPEPLFRSVGNTIDPVILFQKMGVGKL
EMYVLNPVKSSKEMQYFMQQWTGTNKDKAEFILPNGQEVDLPISYLTSVSSLIVWHPANP
AEKIIRVLFPGNSTQYNILEGLEKLKHLDFLKQPLATQKDLTGQVPTPVVKQTKLKQRAD
SRESLKPAAKPLPSKSVRKESKEETPEVTKVNHVEKPPKVESKEKVMVKKDKPIKTETKP
SVTEKEVPSKEEPSPVKAEVAEKQATDVKPKAAKEKTVKKETKVKPEDKKEEKEKPKKEV
AKKEDKTPIKKEEKPKKEEVKKEVKKEIKKEEKKEPKKEVKKETPPKEVKKEVKKEEKKE
VKKEEKEPKKEIKKLPKDAKKSSTPLSEAKKPAALKPKVPKKEESVKKDSVAAGKPKEKG
KIKVIKKEGKAAEAVAAAVGTGATTAAVMAAAGIAAIGPAKELEAERSLMSSPEDLTKDF
EELKAEEVDVTKDIKPQLELIEDEEKLKETEPVEAYVIQKEREVTKGPAESPDEGITTTE
GEGECEQTPEELEPVEKQGVDDIEKFEDEGAGFEESSETGDYEEKAETEEAEEPEEDGEE
HVCVSASKHSPTEDEESAKAEADAYIREKRESVASGDDRAEEDMDEAIEKGEAEQSEEEA
DEEDKAEDAREEEYEPEKMEAEDYVMAVVDKAAEAGGAEEQYGFLTTPTKQLGAQSPGRE
PASSIHDETLPGGSESEATASDEENREDQPEEFTATSGYTQSTIEISSEPTPMDEMSTPR
DVMSDETNNEETESPSQEFVNITKYESSLYSQEYSKPADVTPLNGFSEGSKTDATDGKDY
NASASTISPPSSMEEDKFSRSALRDAYCSEVKASTTLDIKDSISAVSSEKVSPSKSPSLS
PSPPSPLEKTPLGERSVNFSLTPNEIKVSAEAEVAPVSPEVTQEVVEEHCASPEDKTLEV
VSPSQSVTGSAGHTPYYQSPTDEKSSHLPTEVIEKPPAVPVSFEFSDAKDENERASVSPM
DEPVPDSESPIEKVLSPLRSPPLIGSESAYESFLSADDKASGRGAESPFEEKSGKQGSPD
QVSPVSEMTSTSLYQDKQEGKSTDFAPIKEDFGQEKKTDDVEAMSSQPALALDERKLGDV
SPTQIDVSQFGSFKEDTKMSISEGTVSDKSATPVDEGVAEDTYSHMEGVASVSTASVATS
SFPEPTTDDVSPSLHAEVGSPHSTEVDDSLSVSVVQTPTTFQETEMSPSKEECPRPMSIS
PPDFSPKTAKSRTPVQDHRSEQSSMSIEFGQESPEQSLAMDFSRQSPDHPTVGAGVLHIT
ENGPTEVDYSPSDMQDSSLSHKIPPMEEPSYTQDNDLSELISVSQVEASPSTSSAHTPSQ
IASPLQEDTLSDVAPPRDMSLYASLTSEKVQSLEGEKLSPKSDISPLTPRESSPLYSPTF
SDSTSAVKEKTATCHSSSSPPIDAASAEPYGFRASVLFDTMQHHLALNRDLSTPGLEKDS
GGKTPGDFSYAYQKPEETTRSPDEEDYDYESYEKTTRTSDVGGYYYEKIERTTKSPSDSG
YSYETIGKTTKTPEDGDYSYEIIEKTTRTPEEGGYSYDISEKTTSPPEVSGYSYEKTERS
RRLLDDISNGYDDSEDGGHTLGDPSYSYETTEKITSFPESEGYSYETSTKTTRTPDTSTY
CYETAEKITRTPQASTYSYETSDLCYTAEKKSPSEARQDVDLCLVSSCEYKHPKTELSPS
FINPNPLEWFASEEPTEESEKPLTQSGGAPPPPGGKQQGRQCDETPPTSVSESAPSQTDS
DVPPETEECPSITADANIDSEDESETIPTDKTVTYKHMDPPPAPVQDRSPSPRHPDVSMV
DPEALAIEQNLGKALKKDLKEKTKTKKPGTKTKSSSPVKKSDGKSKPLAASPKPAGLKES
SDKVSRVASPKKKESVEKAAKPTTTPEVKAARGEEKDKETKNAANASASKSAKTATAGPG
TTKTTKSSAVPPGLPVYLDLCYIPNHSNSKNVDVEFFKRVRSSYYVVSGNDPAAEEPSRA
VLDALLEGKAQWGSNMQVTLIPTHDSEVMREWYQETHEKQQDLNIMVLASSSTVVMQDES
FPACKIEL

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History
Entry version 170 (07 Nov 2018)
Sequence version 2 (11 Jan 2011)
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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

actin binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
microtubule binding Source: ARUK-UCL
structural molecule activity
Source: ProtInc
Non-traceable author statementⁱ
- 1881920
tubulin binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

axon extension
Source: ARUK-UCL
Traceable author statementⁱ
- 26609151
axonogenesis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cellular process
Source: DFLAT
Inferred from direct assayⁱ
- 19567321
dendrite development
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
establishment of monopolar cell polarity Source: Ensembl
microtubule bundle formation Source: Ensembl
microtubule cytoskeleton organization
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
mitochondrion transport along microtubule Source: Ensembl
negative regulation of intracellular transport Source: Ensembl
neuron migration
Source: ARUK-UCL
Traceable author statementⁱ
- 26609151
positive regulation of axon extension Source: Ensembl

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

SIGNORⁱ	P46821

SIGNORⁱ

P46821

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000131711.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6836 MAP1B
MIMⁱ	157129 gene
neXtProtⁱ	NX_P46821

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4131
Open Targets More...OpenTargetsⁱ	ENSG00000131711
PharmGKBⁱ	PA30581

Chemistry databases

ChEMBLⁱ	CHEMBL3217382

ChEMBLⁱ

CHEMBL3217382

Polymorphism and mutation databases

BioMutaⁱ	MAP1B
DMDMⁱ	317373388

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Initiator methionineⁱ		RemovedCombined sources1 Publication
ChainⁱPRO_0000018604	2 – 2468	Microtubule-associated protein 1BAdd BLAST	2467
ChainⁱPRO_0000418379	2 – 2206	MAP1B heavy chainAdd BLAST	2205
ChainⁱPRO_0000018605	2207 – 2468	MAP1 light chain LC1Add BLAST	262

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylalanineCombined sources1 Publication	1
Modified residueⁱ	336	PhosphoserineCombined sources	1
Modified residueⁱ	339	PhosphoserineBy similarity	1
Modified residueⁱ	343	PhosphoserineCombined sources	1
Modified residueⁱ	527	PhosphothreonineBy similarity	1
Modified residueⁱ	541	PhosphoserineCombined sources	1
Modified residueⁱ	544	PhosphoserineBy similarity	1
Modified residueⁱ	561	PhosphoserineBy similarity	1
Modified residueⁱ	614	PhosphoserineCombined sources	1
Modified residueⁱ	828	PhosphoserineCombined sources	1
Modified residueⁱ	831	PhosphoserineCombined sources	1
Modified residueⁱ	832	PhosphoserineCombined sources	1
Modified residueⁱ	891	PhosphoserineBy similarity	1
Modified residueⁱ	899	PhosphothreonineBy similarity	1
Modified residueⁱ	908	PhosphothreonineBy similarity	1
Modified residueⁱ	936	PhosphoserineBy similarity	1
Modified residueⁱ	937	PhosphoserineCombined sources	1
Modified residueⁱ	948	PhosphothreonineCombined sources	1
Modified residueⁱ	970	PhosphoserineBy similarity	1
Modified residueⁱ	977	PhosphoserineBy similarity	1
Modified residueⁱ	992	PhosphoserineCombined sources	1
Modified residueⁱ	995	PhosphoserineCombined sources	1
Modified residueⁱ	1016	PhosphoserineCombined sources	1
Modified residueⁱ	1144	PhosphoserineCombined sources	1
Modified residueⁱ	1154	PhosphoserineCombined sources	1
Modified residueⁱ	1156	PhosphoserineCombined sources	1
Modified residueⁱ	1187	PhosphoserineBy similarity	1
Modified residueⁱ	1190	PhosphoserineBy similarity	1
Modified residueⁱ	1208	PhosphoserineCombined sources	1
Modified residueⁱ	1211	PhosphoserineBy similarity	1
Modified residueⁱ	1212	PhosphoserineBy similarity	1
Modified residueⁱ	1229	PhosphoserineBy similarity	1
Modified residueⁱ	1247	PhosphoserineBy similarity	1
Modified residueⁱ	1252	PhosphoserineCombined sources	1
Modified residueⁱ	1256	PhosphoserineCombined sources	1
Modified residueⁱ	1258	PhosphoserineBy similarity	1
Modified residueⁱ	1260	PhosphoserineCombined sources	1
Modified residueⁱ	1262	PhosphoserineCombined sources	1
Modified residueⁱ	1265	PhosphoserineCombined sources	1
Modified residueⁱ	1276	PhosphoserineCombined sources	1
Modified residueⁱ	1280	PhosphoserineCombined sources	1
Modified residueⁱ	1282	PhosphothreonineCombined sources	1
Modified residueⁱ	1298	PhosphoserineCombined sources	1
Modified residueⁱ	1312	PhosphoserineBy similarity	1
Modified residueⁱ	1322	PhosphoserineCombined sources	1
Modified residueⁱ	1324	PhosphoserineBy similarity	1
Modified residueⁱ	1326	PhosphoserineBy similarity	1
Modified residueⁱ	1328	PhosphothreonineBy similarity	1
Modified residueⁱ	1330	PhosphoserineBy similarity	1
Modified residueⁱ	1339	PhosphoserineBy similarity	1
Modified residueⁱ	1376	PhosphoserineBy similarity	1
Modified residueⁱ	1378	PhosphoserineCombined sources	1
Modified residueⁱ	1387	PhosphoserineCombined sources	1
Modified residueⁱ	1389	PhosphoserineCombined sources	1
Modified residueⁱ	1396	PhosphoserineCombined sources	1
Modified residueⁱ	1400	PhosphoserineCombined sources	1
Modified residueⁱ	1408	PhosphoserineBy similarity	1
Modified residueⁱ	1410	PhosphotyrosineBy similarity	1
Modified residueⁱ	1427	PhosphoserineCombined sources	1
Modified residueⁱ	1438	PhosphoserineCombined sources	1
Modified residueⁱ	1443	PhosphoserineCombined sources	1
Modified residueⁱ	1501	PhosphoserineCombined sources	1
Modified residueⁱ	1512	PhosphoserineBy similarity	1
Modified residueⁱ	1520	PhosphoserineBy similarity	1
Modified residueⁱ	1522	PhosphoserineBy similarity	1
Modified residueⁱ	1525	PhosphothreonineBy similarity	1
Modified residueⁱ	1527	PhosphoserineBy similarity	1
Modified residueⁱ	1618	PhosphoserineCombined sources	1
Modified residueⁱ	1620	PhosphoserineCombined sources	1
Modified residueⁱ	1625	PhosphoserineCombined sources	1
Modified residueⁱ	1653	PhosphoserineCombined sources	1
Modified residueⁱ	1663	PhosphoserineBy similarity	1
Modified residueⁱ	1666	PhosphoserineCombined sources	1
Modified residueⁱ	1690	PhosphoserineBy similarity	1
Modified residueⁱ	1772	PhosphoserineBy similarity	1
Modified residueⁱ	1779	PhosphoserineCombined sources	1
Modified residueⁱ	1782	PhosphoserineCombined sources	1
Modified residueⁱ	1785	PhosphoserineCombined sources	1
Modified residueⁱ	1788	PhosphothreonineCombined sources	1
Modified residueⁱ	1792	PhosphoserineBy similarity	1
Modified residueⁱ	1793	PhosphoserineCombined sources	1
Modified residueⁱ	1796	PhosphotyrosineBy similarity	1
Modified residueⁱ	1797	PhosphoserineCombined sources	1
Modified residueⁱ	1801	PhosphoserineBy similarity	1
Modified residueⁱ	1819	PhosphoserineBy similarity	1
Modified residueⁱ	1881	PhosphoserineBy similarity	1
Modified residueⁱ	1899	PhosphoserineCombined sources	1
Modified residueⁱ	1915	PhosphoserineCombined sources	1
Modified residueⁱ	1917	PhosphoserineCombined sources	1
Modified residueⁱ	1919	PhosphoserineCombined sources	1
Modified residueⁱ	1932	PhosphothreonineCombined sources	1
Modified residueⁱ	1939	PhosphoserineCombined sources	1
Modified residueⁱ	1949	PhosphothreonineCombined sources	1
Modified residueⁱ	1965	PhosphoserineCombined sources	1
Modified residueⁱ	2034	PhosphothreonineCombined sources	1
Modified residueⁱ	2209	PhosphoserineCombined sources	1
Modified residueⁱ	2271	PhosphoserineCombined sources	1
Modified residueⁱ	2289	PhosphoserineCombined sources	1
Modified residueⁱ	2305	PhosphothreonineCombined sources	1
Modified residueⁱ	2414	PhosphoserineBy similarity	1
Modified residueⁱ	2464	S-nitrosocysteineBy similarity	1

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

EPDⁱ	P46821
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P46821
PaxDbⁱ	P46821
PeptideAtlas More...PeptideAtlasⁱ	P46821
PRIDEⁱ	P46821
ProteomicsDBⁱ	55766

PTM databases

CarbonylDBⁱ	P46821
iPTMnetⁱ	P46821
PhosphoSitePlusⁱ	P46821

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000131711 Expressed in 243 organ(s), highest expression level in entorhinal cortex
CleanExⁱ	HS_MAP1B
ExpressionAtlasⁱ	P46821 baseline and differential
Genevisibleⁱ	P46821 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB009792 HPA022275

HPAⁱ

CAB009792
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

With	Entry	#Exp.	IntAct
GAN	Q9H2C0	3	EBI-764611,EBI-764342
KIRREL3	Q8IZU9	4	EBI-9517186,EBI-16427312
LRRK2	Q5S007	5	EBI-9517186,EBI-5323863
TP53	P04637	6	EBI-764611,EBI-366083

GO - Molecular functionⁱ

actin binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
microtubule binding Source: ARUK-UCL
tubulin binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110304, 67 interactors
Database of interacting proteins More...DIPⁱ	DIP-33474N
IntActⁱ	P46821, 38 interactors
Molecular INTeraction database More...MINTⁱ	P46821
STRINGⁱ	9606.ENSP00000296755

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P46821
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	1878 – 1894	MAP1B 1Add BLAST	17
Repeatⁱ	1895 – 1911	MAP1B 2Add BLAST	17
Repeatⁱ	1912 – 1928	MAP1B 3Add BLAST	17
Repeatⁱ	1929 – 1945	MAP1B 4Add BLAST	17
Repeatⁱ	1946 – 1962	MAP1B 5Add BLAST	17
Repeatⁱ	1963 – 1979	MAP1B 6Add BLAST	17
Repeatⁱ	1997 – 2013	MAP1B 7Add BLAST	17
Repeatⁱ	2014 – 2030	MAP1B 8Add BLAST	17
Repeatⁱ	2031 – 2047	MAP1B 9Add BLAST	17
Repeatⁱ	2048 – 2064	MAP1B 10Add BLAST	17

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	2294 – 2468	Mediates interaction with TMEM185A1 PublicationAdd BLAST		175

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	589 – 790	Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add BLAST		202

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

eggNOGⁱ	KOG3592 Eukaryota ENOG410XRYM LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074593
HOGENOMⁱ	HOG000063256
HOVERGENⁱ	HBG052409
InParanoidⁱ	P46821
KEGG Orthology (KO) More...KOⁱ	K10429
OMAⁱ	KPQGRQC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G12OH
PhylomeDBⁱ	P46821
TreeFamⁱ	TF350229

Family and domain databases

InterProⁱ	View protein in InterPro IPR026074 MAP1 IPR027321 MAP1B IPR000102 MAP1B_neuraxin
PANTHERⁱ	PTHR13843 PTHR13843, 1 hit PTHR13843:SF5 PTHR13843:SF5, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00414 MAP1B_neuraxin, 5 hits
PROSITEⁱ	View protein in PROSITE PS00230 MAP1B_NEURAXIN, 6 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show all Align All

P46821-1 [UniParc]FASTA Add to basket

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        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

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

D6RA40	D6RA40_HUMAN	Microtubule-associated protein 1B Microtubule-associated protein 1B	MAP1B	569	Annotation score:
D6RA32	D6RA32_HUMAN	Microtubule-associated protein 1B Microtubule-associated protein 1B	MAP1B	670	Annotation score:
D6RCL2	D6RCL2_HUMAN	Microtubule-associated protein 1B Microtubule-associated protein 1B	MAP1B	103	Annotation score:
D6RGJ3	D6RGJ3_HUMAN	Microtubule-associated protein 1B Microtubule-associated protein 1B	MAP1B	122	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_036016	326	R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs766004582Ensembl.	1
Natural variantⁱVAR_036017	574	V → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs369022142Ensembl.	1
Natural variantⁱVAR_024530	594	I → V3 PublicationsCorresponds to variant dbSNP:rs1866374Ensembl.	1
Natural variantⁱVAR_030347	869	E → G. Corresponds to variant dbSNP:rs16876070Ensembl.	1
Natural variantⁱVAR_034105	1296	P → L. Corresponds to variant dbSNP:rs34093016Ensembl.	1
Natural variantⁱVAR_056123	1917	S → 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4012.1
NCBI Reference Sequences More...RefSeqⁱ	NP_005900.2, NM_005909.4
UniGeneⁱ	Hs.335079

Genome annotation databases

Ensemblⁱ	ENST00000296755; ENSP00000296755; ENSG00000131711
GeneIDⁱ	4131
KEGGⁱ	hsa:4131
UCSC genome browser More...UCSCⁱ	uc003kbw.5 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P46821	Microtubule-associated protein 1B (Fragment)		HUMAN		569	UniRef100_P46821
UPI000387C973		HUMAN		2342

Protein	Similar proteins		Species	Score	Length	Source
P46821	Microtubule-associated protein 1B		RAT		2461	UniRef90_P15205
Microtubule-associated protein 1B		MOUSE		2464
Uncharacterized protein		CERAT		2584
Microtubule-associated protein (Fragment)		BOVIN		120
Microtubule-associated protein 1B (Fragment)		MUSPF		116
+103

Protein	Similar proteins		Species	Score	Length	Source
P46821	Microtubule-associated protein 1B		RAT		2461	UniRef50_P15205
Microtubule-associated protein 1B		MOUSE		2464
Uncharacterized protein		CERAT		2584
Microtubule-associated protein (Fragment)		BOVIN		120
Microtubule-associated protein 1B (Fragment)		MUSPF		116
+374

Cross-referencesⁱ

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
CCDSⁱ	CCDS4012.1
RefSeqⁱ	NP_005900.2, NM_005909.4
UniGeneⁱ	Hs.335079

3D structure databases

ProteinModelPortalⁱ	P46821
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110304, 67 interactors
DIPⁱ	DIP-33474N
IntActⁱ	P46821, 38 interactors
MINTⁱ	P46821
STRINGⁱ	9606.ENSP00000296755

Chemistry databases

ChEMBLⁱ	CHEMBL3217382

ChEMBLⁱ

CHEMBL3217382

PTM databases

CarbonylDBⁱ	P46821
iPTMnetⁱ	P46821
PhosphoSitePlusⁱ	P46821

Polymorphism and mutation databases

BioMutaⁱ	MAP1B
DMDMⁱ	317373388

Proteomic databases

EPDⁱ	P46821
MaxQBⁱ	P46821
PaxDbⁱ	P46821
PeptideAtlasⁱ	P46821
PRIDEⁱ	P46821
ProteomicsDBⁱ	55766

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4131
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000296755; ENSP00000296755; ENSG00000131711
GeneIDⁱ	4131
KEGGⁱ	hsa:4131
UCSCⁱ	uc003kbw.5 human

Organism-specific databases

CTDⁱ	4131
DisGeNETⁱ	4131
EuPathDBⁱ	HostDB:ENSG00000131711.14
GeneCardsⁱ	MAP1B
HGNCⁱ	HGNC:6836 MAP1B
HPAⁱ	CAB009792 HPA022275
MIMⁱ	157129 gene
neXtProtⁱ	NX_P46821
OpenTargetsⁱ	ENSG00000131711
PharmGKBⁱ	PA30581
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3592 Eukaryota ENOG410XRYM LUCA
GeneTreeⁱ	ENSGT00550000074593
HOGENOMⁱ	HOG000063256
HOVERGENⁱ	HBG052409
InParanoidⁱ	P46821
KOⁱ	K10429
OMAⁱ	KPQGRQC
OrthoDBⁱ	EOG091G12OH
PhylomeDBⁱ	P46821
TreeFamⁱ	TF350229

Enzyme and pathway databases

SIGNORⁱ	P46821

SIGNORⁱ

P46821

Miscellaneous databases

ChiTaRSⁱ	MAP1B human
GeneWikiⁱ	MAP1B
GenomeRNAiⁱ	4131
Protein Ontology More...PROⁱ	PR:P46821
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000131711 Expressed in 243 organ(s), highest expression level in entorhinal cortex
CleanExⁱ	HS_MAP1B
ExpressionAtlasⁱ	P46821 baseline and differential
Genevisibleⁱ	P46821 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR026074 MAP1 IPR027321 MAP1B IPR000102 MAP1B_neuraxin
PANTHERⁱ	PTHR13843 PTHR13843, 1 hit PTHR13843:SF5 PTHR13843:SF5, 1 hit
Pfamⁱ	View protein in Pfam PF00414 MAP1B_neuraxin, 5 hits
PROSITEⁱ	View protein in PROSITE PS00230 MAP1B_NEURAXIN, 6 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MAP1B_HUMAN
Accessionⁱ	P46821Primary (citable) accession number: P46821 Secondary accession number(s): A2BDK5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
	Last sequence update:	January 11, 2011
	Last modified:	November 7, 2018
	This is version 170 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

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

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UniProtKB - P46821 (MAP1B_HUMAN)

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Microtubule-associated protein 1B

MAP1B

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ