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Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Rattus norvegicus (Rat)
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. Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation (By similarity). Interacts with TMEM185A (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD
  • microtubule binding Source: RGD
  • phospholipid binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • cellular response to growth factor stimulus Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • developmental maturation Source: RGD
  • induction of synaptic plasticity by chemical substance Source: RGD
  • microtubule bundle formation Source: RGD
  • negative regulation of microtubule depolymerization Source: RGD
  • nervous system development Source: RGD
  • neuron development Source: RGD
  • peripheral nervous system axon regeneration Source: RGD
  • positive regulation of axon extension Source: RGD
  • positive regulation of microtubule polymerization Source: RGD
  • positive regulation of neuron differentiation Source: RGD
  • response to axon injury Source: RGD
  • response to carbohydrate Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to inorganic substance Source: RGD
  • response to insecticide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to nutrient levels Source: RGD
  • response to vitamin A Source: RGD
  • response to wounding Source: RGD
  • synapse assembly Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Alternative name(s):
Neuraxin
Cleaved into the following 2 chains:
Gene namesi
Name:Map1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3043. Map1b.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • cytoskeleton Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: UniProtKB-SubCell
  • growth cone Source: RGD
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: RGD
  • neuronal cell body Source: RGD
  • perikaryon Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • varicosity Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3217383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000186082 – 2459Microtubule-associated protein 1BAdd BLAST2458
ChainiPRO_00004183812 – 2197MAP1B heavy chainAdd BLAST2196
ChainiPRO_00000186092198 – 2459MAP1 light chain LC1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei335PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei340PhosphoserineCombined sources1
Modified residuei342PhosphoserineCombined sources1
Modified residuei526PhosphothreonineCombined sources1
Modified residuei540PhosphoserineCombined sources1
Modified residuei543PhosphoserineBy similarity1
Modified residuei560PhosphoserineBy similarity1
Modified residuei613PhosphoserineBy similarity1
Modified residuei820PhosphoserineCombined sources1
Modified residuei823PhosphoserineCombined sources1
Modified residuei824PhosphoserineCombined sources1
Modified residuei880PhosphoserineBy similarity1
Modified residuei883PhosphoserineBy similarity1
Modified residuei891PhosphothreonineBy similarity1
Modified residuei900PhosphothreonineBy similarity1
Modified residuei928PhosphoserineCombined sources1
Modified residuei929PhosphoserineCombined sources1
Modified residuei940PhosphothreonineCombined sources1
Modified residuei955PhosphoserineCombined sources1
Modified residuei962PhosphoserineCombined sources1
Modified residuei984PhosphoserineCombined sources1
Modified residuei987PhosphoserineCombined sources1
Modified residuei1008PhosphoserineCombined sources1
Modified residuei1147PhosphoserineBy similarity1
Modified residuei1149PhosphoserineBy similarity1
Modified residuei1179PhosphoserineCombined sources1
Modified residuei1182PhosphoserineCombined sources1
Modified residuei1200PhosphoserineCombined sources1
Modified residuei1203PhosphoserineBy similarity1
Modified residuei1204PhosphoserineBy similarity1
Modified residuei1238PhosphoserineCombined sources1
Modified residuei1243PhosphoserineCombined sources1
Modified residuei1247PhosphoserineCombined sources1
Modified residuei1249PhosphoserineCombined sources1
Modified residuei1251PhosphoserineCombined sources1
Modified residuei1253PhosphoserineCombined sources1
Modified residuei1256PhosphoserineCombined sources1
Modified residuei1267PhosphoserineBy similarity1
Modified residuei1271PhosphoserineBy similarity1
Modified residuei1273PhosphothreonineCombined sources1
Modified residuei1290PhosphoserineBy similarity1
Modified residuei1304PhosphoserineBy similarity1
Modified residuei1314PhosphoserineCombined sources1
Modified residuei1316PhosphoserineBy similarity1
Modified residuei1318PhosphoserineBy similarity1
Modified residuei1320PhosphothreonineBy similarity1
Modified residuei1322PhosphoserineCombined sources1
Modified residuei1331PhosphoserineBy similarity1
Modified residuei1368PhosphoserineBy similarity1
Modified residuei1370PhosphoserineCombined sources1
Modified residuei1379PhosphoserineBy similarity1
Modified residuei1381PhosphoserineCombined sources1
Modified residuei1388PhosphoserineBy similarity1
Modified residuei1392PhosphoserineCombined sources1
Modified residuei1400PhosphoserineBy similarity1
Modified residuei1402PhosphotyrosineBy similarity1
Modified residuei1419PhosphoserineCombined sources1
Modified residuei1435PhosphoserineCombined sources1
Modified residuei1493PhosphoserineCombined sources1
Modified residuei1504PhosphoserineCombined sources1
Modified residuei1512PhosphoserineCombined sources1
Modified residuei1514PhosphoserineCombined sources1
Modified residuei1517PhosphothreonineCombined sources1
Modified residuei1519PhosphoserineCombined sources1
Modified residuei1609PhosphoserineBy similarity1
Modified residuei1611PhosphoserineCombined sources1
Modified residuei1616PhosphoserineCombined sources1
Modified residuei1644PhosphoserineCombined sources1
Modified residuei1654PhosphoserineCombined sources1
Modified residuei1657PhosphoserineCombined sources1
Modified residuei1681PhosphoserineBy similarity1
Modified residuei1763PhosphoserineCombined sources1
Modified residuei1770PhosphoserineCombined sources1
Modified residuei1773PhosphoserineBy similarity1
Modified residuei1776PhosphoserineCombined sources1
Modified residuei1779PhosphothreonineCombined sources1
Modified residuei1783PhosphoserineBy similarity1
Modified residuei1784PhosphoserineBy similarity1
Modified residuei1787PhosphotyrosineBy similarity1
Modified residuei1788PhosphoserineBy similarity1
Modified residuei1792PhosphoserineBy similarity1
Modified residuei1810PhosphoserineCombined sources1
Modified residuei1868PhosphoserineCombined sources1
Modified residuei1872PhosphoserineCombined sources1
Modified residuei1906PhosphoserineCombined sources1
Modified residuei1910PhosphoserineBy similarity1
Modified residuei1923PhosphothreonineCombined sources1
Modified residuei1930PhosphoserineBy similarity1
Modified residuei1940PhosphothreonineCombined sources1
Modified residuei2025PhosphoserineCombined sources1
Modified residuei2055Omega-N-methylarginineBy similarity1
Modified residuei2200PhosphoserineBy similarity1
Modified residuei2262PhosphoserineBy similarity1
Modified residuei2280PhosphoserineBy similarity1
Modified residuei2296PhosphothreonineBy similarity1
Modified residuei2405PhosphoserineBy similarity1
Modified residuei2455S-nitrosocysteineBy similarity1

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 (By similarity).By similarity
S-nitrosylation at Cys-2455 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, Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP15205.
PRIDEiP15205.

PTM databases

iPTMnetiP15205.
PhosphoSitePlusiP15205.

Expressioni

Tissue specificityi

Nervous system (spinal cord, brain stem, cerebellum and cerebrum). Not expressed in liver, spleen, kidney, heart or muscle.1 Publication

Developmental stagei

In cerebral cortex, spinal cord and sciatic nerve levels are high early in development but decrease during postnatal development and are low in adults. In dorsal root ganglia levels remain high throughout development.1 Publication

Inductioni

By nerve growth factor.1 Publication

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). Interacts (via N-terminus) with DAPK1. Interacts with TMEM185A. Interacts with MAP1LC3B. Interacts with KIRREL3 (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD
  • microtubule binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi248099. 5 interactors.
IntActiP15205. 2 interactors.
STRINGi10116.ENSRNOP00000023460.

Structurei

3D structure databases

ProteinModelPortaliP15205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1869 – 1885MAP1B 1Add BLAST17
Repeati1886 – 1902MAP1B 2Add BLAST17
Repeati1903 – 1919MAP1B 3Add BLAST17
Repeati1920 – 1936MAP1B 4Add BLAST17
Repeati1937 – 1953MAP1B 5Add BLAST17
Repeati1954 – 1970MAP1B 6Add BLAST17
Repeati1988 – 2004MAP1B 7Add BLAST17
Repeati2005 – 2021MAP1B 8Add BLAST17
Repeati2022 – 2038MAP1B 9Add BLAST17
Repeati2039 – 2055MAP1B 10Add BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2285 – 2459Mediates interaction with TMEM185ABy similarityAdd BLAST175

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi559 – 1035Glu-richAdd BLAST477
Compositional biasi588 – 786Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add BLAST199
Compositional biasi2224 – 2312Lys-richAdd BLAST89

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.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP15205.
KOiK10429.
PhylomeDBiP15205.

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.

P15205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIGNP AATTSPSLSH RFLDSKFYLL VVVGETVTEE
60 70 80 90 100
HLRRAIGNIE LGIRSWETNL 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 LEEESQGSTS NSDWMKNLIS
360 370 380 390 400
PDLGVVFLNV PENLKNPEPN IKMKRSTEEA CFTLQYLNKL SMKPEPLFRS
410 420 430 440 450
VGNAIEPVIL FQKMGVGKLK MYVLNPVKSS KEMQYFMQQW TGTNKDKAEL
460 470 480 490 500
ILPNGQEVDI PISYLASVSS LIVWHPANPA EKIIRVLFPG NSTQYNILEG
510 520 530 540 550
LEKLKHLDFL KQPLATQKDL TGQVSTPPVK QVKLKQRADS RESLKPATKP
560 570 580 590 600
LSSKSVRKES KEEAPEATKA SQVEKTPKVE SKEKVIVKKD KPGKVESKPS
610 620 630 640 650
VTEKEVPSKE EQSPVKAEVA EKAATESKPK VTKDKVVKKE IKTKPEEKKE
660 670 680 690 700
EKPKKEVAKK EDKTPLKKDE KPKKEEAKKE IKKEIKKEEK KELKKEVKKE
710 720 730 740 750
TPLKDAKKEV KKDEKKEVKK EEKEPKKEIK KISKDIKKST PLSDTKKPAA
760 770 780 790 800
LKPKVAKKEE PTKKEPIAAG KLKDKGKVKV IKKEGKTTEA AATAVGTAAV
810 820 830 840 850
AAAAGVAASG PAKELEAERS LMSSPEDLTK DFEELKAEEI DVAKDIKPQL
860 870 880 890 900
ELIEDEEKLK ETEPGEAYVI QKETEVSKGS AESPDEGITT TEGEGECEQT
910 920 930 940 950
PEELEPVEKQ GVDDIEKFED EGAGFEESSE AGDYEEKAET EEAEEPEEDG
960 970 980 990 1000
EDNVSGSASK HSPTEDEEIA KAEADVHIKE KRESVASGDD RAEEDMDEAL
1010 1020 1030 1040 1050
EKGEAEQSEE EGEEEEDKAE DAREEDHEPD KTEAEDYVMA VVDKAAEAGV
1060 1070 1080 1090 1100
TEDQYDFLGT PAKQPGVQSP SREPASSIHD ETLPGGSESE ATASDEENRE
1110 1120 1130 1140 1150
DQPEEFTATS GYTQSTIEIS SEPTPMDEMS TPRDVMTDET NNEETESPSQ
1160 1170 1180 1190 1200
EFVNITKYES SLYSQEYSKP VVASFNGLSD GSKTDATDGR DYNASASTIS
1210 1220 1230 1240 1250
PPSSMEEDKF SKSALRDAYR PEETDVKTGA ELDIKDVSDE RLSPAKSPSL
1260 1270 1280 1290 1300
SPSPPSPIEK TPLGERSVNF SLTPNEIKAS AEGEATAVVS PGVTQAVVEE
1310 1320 1330 1340 1350
HCASPEEKTL EVVSPSQSVT GSAGHTPYYQ SPTDEKSSHL PTEVTENAQA
1360 1370 1380 1390 1400
VPVSFEFTEA KDENERSSIS PMDEPVPDSE SPIEKVLSPL RSPPLIGSES
1410 1420 1430 1440 1450
AYEDFLSADD KALGRRSESP FEGKNGKQGF SDKESPVSDL TSDLYQDKQE
1460 1470 1480 1490 1500
EKRAGFIPIK EDFSPEKKAS DAEIMSSQSA LALDERKLGG DGSPTQVDVS
1510 1520 1530 1540 1550
QFGSFKEDTK MSISEGTVSD KSATPVDEGA EDTYSHMEGV ASVSTASVAT
1560 1570 1580 1590 1600
SSFPEPTTDD VSPSLHAEVG SPHSTEVDDS LSVSVVQTPT TFQETEMSPS
1610 1620 1630 1640 1650
KEECPRPMSI SPPDFSPKTA KSRTPVQDHR SEQSSMSIEF GQESPEHSLA
1660 1670 1680 1690 1700
MDFSRQSPDH PTVGAGMLHI TENGPTEVDY SPSDIQDSSL SHKIPPTEEP
1710 1720 1730 1740 1750
SYTQDNDLSE LISVSQVEAS PSTSSAHTPS QIASPLQEDT LSDVVPPRDM
1760 1770 1780 1790 1800
SLYASLASEK VQSLEGEKLS PKSDISPLTP RESSPTYSPG FSDSTSGAKE
1810 1820 1830 1840 1850
STAAYQTSSS PPIDAAAAEP YGFRSSMLFD TMQHHLALSR DLTTSSVEKD
1860 1870 1880 1890 1900
NGGKTPGDFN YAYQKPESTT ESPDEEDYDY ESHEKTIQAH DVGGYYYEKT
1910 1920 1930 1940 1950
ERTIKSPCDS GYSYETIEKT TKTPEDGGYS CEITEKTTRT PEEGGYSYEI
1960 1970 1980 1990 2000
SEKTTRTPEV SGYTYEKTER SRRLLDDISN GYDDTEDGGH TLGDCSYSYE
2010 2020 2030 2040 2050
TTEKITSFPE SESYSYETTT KTTRSPDTSA YCYETMEKIT KTPQASTYSY
2060 2070 2080 2090 2100
ETSDRCYTPE RKSPSEARQD VDLCLVSSCE FKHPKTELSP SFINPNPLEW
2110 2120 2130 2140 2150
FAGEEPTEES ERPLTQSGGA PPPSGGKQQG RQCDETPPTS VSESAPSQTD
2160 2170 2180 2190 2200
SDVPPETEEC PSITADANLD SEDESETIPT DKTVTYKHMD PPPAPMQDRS
2210 2220 2230 2240 2250
PSPRHPDVSM VDPEALAIEQ NLGKALKKDL KEKAKTKKPG TKTKSSSPVK
2260 2270 2280 2290 2300
KGDGKSKPSA ASPKPGALKE SSDKVSRVAS PKKKESVEKA MKTTTTPEVK
2310 2320 2330 2340 2350
ATRGEEKDKE TKNAANASAS KSVKTATAGP GTTKTAKSST VPPGLPVYLD
2360 2370 2380 2390 2400
LCYIPNHSNS KNVDVEFFKR VRSSYYVVSG NDPAAEEPSR AVLDALLEGK
2410 2420 2430 2440 2450
AQWGSNMQVT LIPTHDSEVM REWYQETHEK QQDLNIMVLA SSSTVVMQDE

SFPACKIEL
Length:2,459
Mass (Da):269,500
Last modified:September 26, 2001 - v2
Checksum:i2E3F6872DEDB8BA2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti127M → V in AAB17068 (PubMed:8666295).Curated1
Sequence conflicti140T → S (PubMed:8666295).Curated1
Sequence conflicti2112R → K in CAA34620 (PubMed:2555150).Curated1
Sequence conflicti2169L → I in CAA34620 (PubMed:2555150).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52950 mRNA. Translation: AAB17068.1.
X60370 mRNA. Translation: CAC16162.1.
X16623 mRNA. Translation: CAA34620.1. Sequence problems.
PIRiA56577.
RefSeqiNP_062090.1. NM_019217.1.
UniGeneiRn.220177.
Rn.98152.

Genome annotation databases

GeneIDi29456.
KEGGirno:29456.
UCSCiRGD:3043. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52950 mRNA. Translation: AAB17068.1.
X60370 mRNA. Translation: CAC16162.1.
X16623 mRNA. Translation: CAA34620.1. Sequence problems.
PIRiA56577.
RefSeqiNP_062090.1. NM_019217.1.
UniGeneiRn.220177.
Rn.98152.

3D structure databases

ProteinModelPortaliP15205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248099. 5 interactors.
IntActiP15205. 2 interactors.
STRINGi10116.ENSRNOP00000023460.

Chemistry databases

ChEMBLiCHEMBL3217383.

PTM databases

iPTMnetiP15205.
PhosphoSitePlusiP15205.

Proteomic databases

PaxDbiP15205.
PRIDEiP15205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29456.
KEGGirno:29456.
UCSCiRGD:3043. rat.

Organism-specific databases

CTDi4131.
RGDi3043. Map1b.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP15205.
KOiK10429.
PhylomeDBiP15205.

Miscellaneous databases

PROiP15205.

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_RAT
AccessioniPrimary (citable) accession number: P15205
Secondary accession number(s): Q62958, Q9ER21, Q9QW92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 26, 2001
Last modified: November 2, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

A C-terminal fragment of this protein (residues 1597 to 2459) was originally described as neuraxin in PubMed:2555150.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.