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Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  • cytoskeletal regulatory protein binding Source: MGI

GO - Biological processi

  • axon extension Source: MGI
  • axonogenesis Source: MGI
  • cellular process Source: MGI
  • dendrite development Source: MGI
  • establishment of monopolar cell polarity Source: MGI
  • microtubule-based process Source: MGI
  • microtubule bundle formation Source: MGI
  • mitochondrion transport along microtubule Source: MGI
  • negative regulation of intracellular transport Source: MGI
  • positive regulation of axon extension Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Alternative name(s):
MAP1(X)
MAP1.2
Cleaved into the following 2 chains:
Gene namesi
Name:Map1b
Synonyms:Mtap1b, Mtap5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1306778. Map1b.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • dendritic spine Source: UniProtKB-SubCell
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: MGI
  • photoreceptor outer segment Source: MGI
  • plasma membrane Source: MGI
  • postsynaptic density Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000186062 – 2464Microtubule-associated protein 1BAdd BLAST2463
ChainiPRO_00004183802 – 2202MAP1B heavy chainAdd BLAST2201
ChainiPRO_00000186072203 – 2464MAP1 light chain LC1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei336PhosphoserineCombined sources1
Modified residuei339PhosphoserineCombined sources1
Modified residuei341PhosphoserineBy similarity1
Modified residuei343PhosphoserineCombined sources1
Modified residuei527PhosphothreonineBy similarity1
Modified residuei541PhosphoserineCombined sources1
Modified residuei544PhosphoserineCombined sources1
Modified residuei561PhosphoserineCombined sources1
Modified residuei614PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Modified residuei828PhosphoserineCombined sources1
Modified residuei829PhosphoserineCombined sources1
Modified residuei885PhosphoserineCombined sources1
Modified residuei888PhosphoserineCombined sources1
Modified residuei896PhosphothreonineCombined sources1
Modified residuei905PhosphothreonineCombined sources1
Modified residuei933PhosphoserineBy similarity1
Modified residuei934PhosphoserineBy similarity1
Modified residuei945PhosphothreonineCombined sources1
Modified residuei960PhosphoserineBy similarity1
Modified residuei967PhosphoserineCombined sources1
Modified residuei974PhosphoserineCombined sources1
Modified residuei989PhosphoserineCombined sources1
Modified residuei992PhosphoserineCombined sources1
Modified residuei1013PhosphoserineCombined sources1
Modified residuei1141PhosphoserineCombined sources1
Modified residuei1151PhosphoserineCombined sources1
Modified residuei1153PhosphoserineCombined sources1
Modified residuei1183PhosphoserineBy similarity1
Modified residuei1186PhosphoserineBy similarity1
Modified residuei1204PhosphoserineCombined sources1
Modified residuei1207PhosphoserineCombined sources1
Modified residuei1208PhosphoserineCombined sources1
Modified residuei1225PhosphoserineCombined sources1
Modified residuei1242PhosphoserineCombined sources1
Modified residuei1247PhosphoserineCombined sources1
Modified residuei1251PhosphoserineCombined sources1
Modified residuei1253PhosphoserineCombined sources1
Modified residuei1255PhosphoserineCombined sources1
Modified residuei1257PhosphoserineCombined sources1
Modified residuei1260PhosphoserineCombined sources1
Modified residuei1271PhosphoserineBy similarity1
Modified residuei1275PhosphoserineBy similarity1
Modified residuei1277PhosphothreonineBy similarity1
Modified residuei1293PhosphoserineBy similarity1
Modified residuei1307PhosphoserineCombined sources1
Modified residuei1317PhosphoserineCombined sources1
Modified residuei1319PhosphoserineCombined sources1
Modified residuei1321PhosphoserineCombined sources1
Modified residuei1323PhosphothreonineCombined sources1
Modified residuei1325PhosphoserineCombined sources1
Modified residuei1334PhosphoserineCombined sources1
Modified residuei1371PhosphoserineCombined sources1
Modified residuei1373PhosphoserineCombined sources1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1384PhosphoserineCombined sources1
Modified residuei1391PhosphoserineCombined sources1
Modified residuei1395PhosphoserineCombined sources1
Modified residuei1403PhosphoserineCombined sources1
Modified residuei1405PhosphotyrosineCombined sources1
Modified residuei1422PhosphoserineBy similarity1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1497PhosphoserineCombined sources1
Modified residuei1508PhosphoserineCombined sources1
Modified residuei1516PhosphoserineBy similarity1
Modified residuei1518PhosphoserineBy similarity1
Modified residuei1521PhosphothreonineBy similarity1
Modified residuei1523PhosphoserineCombined sources1
Modified residuei1614PhosphoserineBy similarity1
Modified residuei1616PhosphoserineCombined sources1
Modified residuei1621PhosphoserineCombined sources1
Modified residuei1649PhosphoserineBy similarity1
Modified residuei1659PhosphoserineBy similarity1
Modified residuei1662PhosphoserineCombined sources1
Modified residuei1686PhosphoserineCombined sources1
Modified residuei1768PhosphoserineCombined sources1
Modified residuei1775PhosphoserineCombined sources1
Modified residuei1778PhosphoserineCombined sources1
Modified residuei1781PhosphoserineCombined sources1
Modified residuei1784PhosphothreonineCombined sources1
Modified residuei1788PhosphoserineCombined sources1
Modified residuei1789PhosphoserineCombined sources1
Modified residuei1792PhosphotyrosineCombined sources1
Modified residuei1793PhosphoserineCombined sources1
Modified residuei1797PhosphoserineCombined sources1
Modified residuei1815PhosphoserineBy similarity1
Modified residuei1877PhosphoserineCombined sources1
Modified residuei1911PhosphoserineCombined sources1
Modified residuei1915PhosphoserineBy similarity1
Modified residuei1928PhosphothreonineCombined sources1
Modified residuei1945PhosphothreonineCombined sources1
Modified residuei2030PhosphoserineCombined sources1
Modified residuei2060Omega-N-methylarginineCombined sources1
Modified residuei2205PhosphoserineBy similarity1
Modified residuei2267PhosphoserineBy similarity1
Modified residuei2285PhosphoserineBy similarity1
Modified residuei2301PhosphothreonineBy similarity1
Modified residuei2410PhosphoserineCombined sources1
Modified residuei2460S-nitrosocysteine1 Publication1

Post-translational modificationi

LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B.
S-nitrosylation at Cys-2460 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.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP14873.
PaxDbiP14873.
PeptideAtlasiP14873.
PRIDEiP14873.

PTM databases

iPTMnetiP14873.
PhosphoSitePlusiP14873.
SwissPalmiP14873.

Expressioni

Gene expression databases

BgeeiENSMUSG00000052727.
CleanExiMM_MTAP1B.
GenevisibleiP14873. MM.

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 (PubMed:12807913, PubMed:17320046). Interacts with the tubulin tyrosine TTL (PubMed:18075266). Interacts (via C-terminus) with GAN (via Kelch domains) (PubMed:12147674). Interacts (via N-terminus) with DAPK1 (By similarity). Interacts with TMEM185A (By similarity). Interacts with MAP1LC3B (By similarity). Interacts with KIRREL3 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Scn8aQ9WTU37EBI-764653,EBI-6396042

GO - Molecular functioni

  • cytoskeletal regulatory protein binding Source: MGI

Protein-protein interaction databases

BioGridi201584. 13 interactors.
IntActiP14873. 7 interactors.
MINTiMINT-4101165.
STRINGi10090.ENSMUSP00000068374.

Structurei

3D structure databases

ProteinModelPortaliP14873.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1874 – 1890MAP1B 1Add BLAST17
Repeati1891 – 1907MAP1B 2Add BLAST17
Repeati1908 – 1924MAP1B 3Add BLAST17
Repeati1925 – 1941MAP1B 4Add BLAST17
Repeati1942 – 1958MAP1B 5Add BLAST17
Repeati1959 – 1975MAP1B 6Add BLAST17
Repeati1993 – 2009MAP1B 7Add BLAST17
Repeati2010 – 2026MAP1B 8Add BLAST17
Repeati2027 – 2043MAP1B 9Add BLAST17
Repeati2044 – 2060MAP1B 10Add BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2290 – 2464Mediates interaction with TMEM185ABy similarityAdd BLAST175

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi589 – 787Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add BLAST199

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.1 Publication

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP14873.
KOiK10429.
OMAiGYSYETI.
OrthoDBiEOG091G12OH.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 6 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE
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 LEEERSQGST SNSDWMKNLI
360 370 380 390 400
SPDLGVVFLN VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR
410 420 430 440 450
SVGNTIEPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE
460 470 480 490 500
LILPNGQEVD IPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE
510 520 530 540 550
GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD SRESLKPATK
560 570 580 590 600
PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP
610 620 630 640 650
SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK
660 670 680 690 700
EEKPKKEVVK KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK
710 720 730 740 750
ETPLKDAKKE VKKEEKKEVK KEEKEPKKEI KKISKDIKKS TPLSDTKKPS
760 770 780 790 800
ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK VIKKEGKTTE AAATAVGTAA
810 820 830 840 850
TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL KAEEIDVAKD
860 870 880 890 900
IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG
910 920 930 940 950
ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE
960 970 980 990 1000
PEEDGEDNAS GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED
1010 1020 1030 1040 1050
MDDVLEKGEA EQSEEEGEEE DKAEDAREEG YEPDKTEAED YVMAVADKAA
1060 1070 1080 1090 1100
EAGVTEEQYG YLGTSAKQPG IQSPSREPAS SIHDETLPGG SESEATASDE
1110 1120 1130 1140 1150
ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM SDETNNEETE
1160 1170 1180 1190 1200
SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA
1210 1220 1230 1240 1250
STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK
1260 1270 1280 1290 1300
SPSLSPSPPS PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV
1310 1320 1330 1340 1350
VEEHCASPEE KTLEVVSPSQ SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK
1360 1370 1380 1390 1400
PQAVPVSFEF SEAKDENERA SLSPMDEPVP DSESPVEKVL SPLRSPPLLG
1410 1420 1430 1440 1450
SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV SDLTSTGLYQ
1460 1470 1480 1490 1500
DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ
1510 1520 1530 1540 1550
IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST
1560 1570 1580 1590 1600
ASVATSSFPE PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET
1610 1620 1630 1640 1650
EMSPSKEECP RPMSISPPDF SPKTAKSRTP VQDHRSEQSS MSIEFGQESP
1660 1670 1680 1690 1700
EHSLAMDFSR QSPDHPTLGA SVLHITENGP TEVDYSPSDI QDSSLSHKIP
1710 1720 1730 1740 1750
PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP LQEDTLSDVV
1760 1770 1780 1790 1800
PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST
1810 1820 1830 1840 1850
SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS
1860 1870 1880 1890 1900
SVEKDSGGKT PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY
1910 1920 1930 1940 1950
YYEKTERTIK SPCDSGYSYE TIEKTIKTPE DGGYTCEITE KTTRTPEEGG
1960 1970 1980 1990 2000
YSYEISEKTT RTPEVSGYTY EKTERSRRLL DDISNGYDDT EDGGHTLGDC
2010 2020 2030 2040 2050
SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET MEKITKTPQA
2060 2070 2080 2090 2100
STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP
2110 2120 2130 2140 2150
NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA
2160 2170 2180 2190 2200
PSQTDSDVPP ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP
2210 2220 2230 2240 2250
MQDRSPSPRH PDVSMVDPDA LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS
2260 2270 2280 2290 2300
SSPVKKGDGK SKPLAASPKP GALKESSDKV SRVASPKKKE SVEKATKTTT
2310 2320 2330 2340 2350
TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT AKSSTVPPGL
2360 2370 2380 2390 2400
PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA
2410 2420 2430 2440 2450
LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV
2460
VMQDESFPAC KIEL
Length:2,464
Mass (Da):270,255
Last modified:July 27, 2011 - v2
Checksum:i2835101531B0694A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti743L → Q in CAA35761 (PubMed:2480963).Curated1
Sequence conflicti1348 – 1351TEKP → SENA in CAA35761 (PubMed:2480963).Curated4
Sequence conflicti1654L → F in CAA35761 (PubMed:2480963).Curated1
Sequence conflicti1688S → C in CAA35761 (PubMed:2480963).Curated1
Sequence conflicti1898 – 1899GG → VR in CAA35761 (PubMed:2480963).Curated2
Sequence conflicti1926I → T in CAA35761 (PubMed:2480963).Curated1
Sequence conflicti2231L → V in CAA35761 (PubMed:2480963).Curated1
Sequence conflicti2333A → T in CAA35761 (PubMed:2480963).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51396 mRNA. Translation: CAA35761.1.
AC170188 Genomic DNA. No translation available.
CCDSiCCDS26723.1.
PIRiS07549. QRMSP1.
RefSeqiNP_032660.2. NM_008634.2.
UniGeneiMm.4173.
Mm.474609.
Mm.474896.

Genome annotation databases

EnsembliENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
GeneIDi17755.
KEGGimmu:17755.
UCSCiuc007rpr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51396 mRNA. Translation: CAA35761.1.
AC170188 Genomic DNA. No translation available.
CCDSiCCDS26723.1.
PIRiS07549. QRMSP1.
RefSeqiNP_032660.2. NM_008634.2.
UniGeneiMm.4173.
Mm.474609.
Mm.474896.

3D structure databases

ProteinModelPortaliP14873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201584. 13 interactors.
IntActiP14873. 7 interactors.
MINTiMINT-4101165.
STRINGi10090.ENSMUSP00000068374.

PTM databases

iPTMnetiP14873.
PhosphoSitePlusiP14873.
SwissPalmiP14873.

Proteomic databases

MaxQBiP14873.
PaxDbiP14873.
PeptideAtlasiP14873.
PRIDEiP14873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
GeneIDi17755.
KEGGimmu:17755.
UCSCiuc007rpr.2. mouse.

Organism-specific databases

CTDi4131.
MGIiMGI:1306778. Map1b.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP14873.
KOiK10429.
OMAiGYSYETI.
OrthoDBiEOG091G12OH.
TreeFamiTF350229.

Miscellaneous databases

PROiP14873.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000052727.
CleanExiMM_MTAP1B.
GenevisibleiP14873. MM.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 6 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 8 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAP1B_MOUSE
AccessioniPrimary (citable) accession number: P14873
Secondary accession number(s): E9QM11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.