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Protein

Microtubule-associated protein 1A

Gene

Map1a

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

Functioni

Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements.

GO - Molecular functioni

  • microtubule binding Source: MGI

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1A
Short name:
MAP-1A
Cleaved into the following 2 chains:
Gene namesi
Name:Map1a
Synonyms:Mtap1, Mtap1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1306776. Map1a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • microtubule Source: UniProtKB-KW
  • neuronal postsynaptic density Source: MGI
  • photoreceptor outer segment Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27762776Microtubule-associated protein 1APRO_0000072753Add
BLAST
Chaini1 – 25422542MAP1A heavy chainPRO_0000418377Add
BLAST
Chaini2543 – 2776234MAP1 light chain LC2PRO_0000269727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei117 – 1171PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei155 – 1551PhosphoserineCombined sources
Modified residuei177 – 1771PhosphotyrosineCombined sources
Modified residuei319 – 3191PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei504 – 5041PhosphothreonineBy similarity
Modified residuei526 – 5261PhosphoserineCombined sources
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei611 – 6111PhosphoserineBy similarity
Modified residuei633 – 6331PhosphothreonineCombined sources
Modified residuei644 – 6441PhosphoserineCombined sources
Modified residuei667 – 6671PhosphoserineCombined sources
Modified residuei678 – 6781PhosphoserineCombined sources
Modified residuei786 – 7861PhosphoserineBy similarity
Modified residuei873 – 8731PhosphoserineCombined sources
Modified residuei876 – 8761PhosphoserineCombined sources
Modified residuei877 – 8771PhosphoserineCombined sources
Modified residuei890 – 8901PhosphoserineCombined sources
Modified residuei893 – 8931PhosphothreonineCombined sources
Modified residuei895 – 8951PhosphoserineCombined sources
Modified residuei899 – 8991PhosphoserineCombined sources
Modified residuei908 – 9081PhosphoserineCombined sources
Modified residuei981 – 9811PhosphoserineCombined sources
Modified residuei991 – 9911PhosphoserineCombined sources
Modified residuei999 – 9991PhosphoserineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1014 – 10141PhosphoserineBy similarity
Modified residuei1023 – 10231PhosphoserineCombined sources
Modified residuei1062 – 10621PhosphoserineCombined sources
Modified residuei1068 – 10681PhosphothreonineCombined sources
Modified residuei1131 – 11311PhosphoserineCombined sources
Modified residuei1133 – 11331PhosphoserineCombined sources
Modified residuei1147 – 11471PhosphoserineCombined sources
Modified residuei1159 – 11591PhosphoserineBy similarity
Modified residuei1177 – 11771PhosphoserineCombined sources
Modified residuei1187 – 11871PhosphoserineBy similarity
Modified residuei1190 – 11901PhosphoserineBy similarity
Modified residuei1196 – 11961PhosphoserineCombined sources
Modified residuei1205 – 12051PhosphoserineCombined sources
Modified residuei1208 – 12081PhosphoserineBy similarity
Modified residuei1251 – 12511PhosphoserineBy similarity
Modified residuei1289 – 12891PhosphoserineCombined sources
Modified residuei1310 – 13101PhosphoserineCombined sources
Modified residuei1313 – 13131PhosphoserineCombined sources
Modified residuei1316 – 13161PhosphoserineCombined sources
Modified residuei1516 – 15161PhosphoserineCombined sources
Modified residuei1580 – 15801PhosphoserineBy similarity
Modified residuei1606 – 16061PhosphoserineCombined sources
Modified residuei1634 – 16341PhosphoserineBy similarity
Modified residuei1648 – 16481PhosphoserineBy similarity
Modified residuei1720 – 17201PhosphoserineBy similarity
Modified residuei1747 – 17471PhosphoserineCombined sources
Modified residuei1762 – 17621PhosphoserineCombined sources
Modified residuei1768 – 17681PhosphoserineCombined sources
Modified residuei1772 – 17721PhosphoserineCombined sources
Modified residuei1777 – 17771PhosphothreonineCombined sources
Modified residuei1783 – 17831PhosphoserineCombined sources
Modified residuei1789 – 17891PhosphoserineCombined sources
Modified residuei1902 – 19021PhosphoserineBy similarity
Modified residuei1928 – 19281PhosphothreonineBy similarity
Modified residuei1993 – 19931PhosphoserineBy similarity
Modified residuei2031 – 20311PhosphothreonineBy similarity
Modified residuei2048 – 20481PhosphoserineBy similarity
Modified residuei2082 – 20821PhosphoserineCombined sources
Modified residuei2209 – 22091PhosphoserineBy similarity
Modified residuei2226 – 22261PhosphoserineBy similarity
Modified residuei2230 – 22301PhosphoserineBy similarity
Modified residuei2233 – 22331PhosphoserineBy similarity
Modified residuei2234 – 22341PhosphoserineBy similarity
Modified residuei2425 – 24251PhosphoserineBy similarity
Modified residuei2623 – 26231PhosphoserineBy similarity
Modified residuei2637 – 26371PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CSNK1D.By similarity
LC2 is generated from MAP1A by proteolytic processing. It is free to associate with both MAP1A and MAP1B (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QYR6.
PaxDbiQ9QYR6.
PRIDEiQ9QYR6.

PTM databases

iPTMnetiQ9QYR6.
PhosphoSiteiQ9QYR6.
SwissPalmiQ9QYR6.

Expressioni

Tissue specificityi

Both isoforms highly expressed in brain, and to a lesser extent in embryo. Isoform 1 is also expressed at a low level in other tissues including heart and muscle.1 Publication

Gene expression databases

BgeeiQ9QYR6.
CleanExiMM_MTAP1A.
ExpressionAtlasiQ9QYR6. baseline and differential.
GenevisibleiQ9QYR6. MM.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. Interacts with guanylate kinase-like domain of DLG1, DLG2 and DLG4. Binds to CSNK1D (By similarity). Interacts with TIAM2.By similarity1 Publication

GO - Molecular functioni

  • microtubule binding Source: MGI

Protein-protein interaction databases

BioGridi201583. 5 interactions.
IntActiQ9QYR6. 5 interactions.
MINTiMINT-1203191.
STRINGi10090.ENSMUSP00000092223.

Structurei

3D structure databases

ProteinModelPortaliQ9QYR6.
SMRiQ9QYR6. Positions 51-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati336 – 33831
Repeati415 – 41732
Repeati420 – 42233
Repeati424 – 42634
Repeati427 – 42935
Repeati431 – 43336
Repeati436 – 43837
Repeati440 – 44238
Repeati444 – 44639
Repeati449 – 451310
Repeati539 – 541311

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni336 – 54120611 X 3 AA approximate repeats of K-K-[DE]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi338 – 677340Glu-richAdd
BLAST
Compositional biasi1748 – 2303556Pro-richAdd
BLAST
Compositional biasi2530 – 255122Pro-richAdd
BLAST
Compositional biasi2747 – 27504Poly-Gln

Domaini

The basic region containing the repeats may be responsible for the binding of MAP1A to microtubules.

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOVERGENiHBG052408.
InParanoidiQ9QYR6.
KOiK10429.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR015656. MAP1A.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF6. PTHR13843:SF6. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QYR6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS
60 70 80 90 100
ALFAVNGFNI LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING
110 120 130 140 150
LLQRKVAELE EEQSQGSSSY SDWVKNLISP ELGVVFFNVP DKLRLPDASR
160 170 180 190 200
KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV SNTIEPLTLF HKMGVGRLDM
210 220 230 240 250
YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LANGKEAEIS VPYLTSITAL
260 270 280 290 300
VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
310 320 330 340 350
AGAVPANLKP SKIKHRADSK ESLKAAPKTA MSKLAKREEV LEEGAKEARS
360 370 380 390 400
ELAKELAKSE KKAKEPSEKP PEKPSKPERV RTESSEALKA EKRKLIKDKV
410 420 430 440 450
GKKHLKEKIS KLEEKRDKEK KEIKKERKEL KKEEGRKEEK KDAKKDEKRK
460 470 480 490 500
DTKPELKKFS KPDLKPFTPE VRKTLYKAKA PGRLKVDKGR AARGEKELSS
510 520 530 540 550
EPRTPPAQKG AAPPPAASGH RELALSSPED LTQDFEELKR EERGLLAEPR
560 570 580 590 600
DTELGEKPLP ADASEQGRPS TAIQVTQPPA SVLEQEQVER EKEVVPDFPE
610 620 630 640 650
DKGSKNRAPD SGAEVEREKE TWEERKPREA ELTPENIAAA REESEPEVKE
660 670 680 690 700
DVIEKAELEE MEEVHPSDEE EEETKAESFY QKHMQEALKV IPKGREALGG
710 720 730 740 750
RELGFQGKAP EKETASFLSS LATPAGAAEH VSYIQDETIP GYSETEQTIS
760 770 780 790 800
DEEIHDEPDE RPAPPRFPTS TYDLSGPEGP GPFEASQSAE SAVPASSSKT
810 820 830 840 850
YGAPETELTY PPNMVAAPLA EEEHVSSATS ITECDKLSSF ATSVAEDQSV
860 870 880 890 900
ASLTAPQTEE TGKSSLLLDT VTSIPSSRTE ATQGLDYVPS AGTISPTSSL
910 920 930 940 950
EEDKGFKSPP CEDFSVTGES EKKGESVGRG LTGEKAVGKE EKNVTTSEKL
960 970 980 990 1000
SSQYAAVFGA PGHALHPGEP ALGEVEERCL SPDDSTVKMA SPPPSGPPSA
1010 1020 1030 1040 1050
AHTPFHQSPV EEKSEPQDFQ EDSWGDTKHA PGVSKEDAEE QTVKPGPEEA
1060 1070 1080 1090 1100
MSEEGKVPLS RSPQAQDTLG SLAGGQTGCT IQLLPEQDKA VVFETGEAGA
1110 1120 1130 1140 1150
ASGAGSLPGE VRTQEPAEPQ KDELLGFTDQ SFSPEDAESL SVLSVVSPDT
1160 1170 1180 1190 1200
AKQEATPRSP CTPKEQQLHK DLWPMVSPED TQSLSFSEES PSKETSLDIS
1210 1220 1230 1240 1250
SKQLSPESLG TLQFGELSLG KEEKGPLVKA EDNSCHLAPV SIPEPHTATV
1260 1270 1280 1290 1300
SPPTDEAAGE AGLTDESPAG NLPGSSFSHS ALSGDRKHSP GEITGPGGHF
1310 1320 1330 1340 1350
MTSDSSLTKS PESLSSPAME DLAMEWGGKA PGSEDRATEQ KEKELERKSE
1360 1370 1380 1390 1400
TLQQKDQILS EKAALVQRDS VMHQKDEALD EENKPGGQQD KTSEQKGRDL
1410 1420 1430 1440 1450
DKKDTAVELG KGPEPKGKDL YLEDQGLAEK DKALEQRGAA LQQTQAPEPR
1460 1470 1480 1490 1500
ARAQEHRDLE QKDEHLELRD KTPEEKDKVL VLEDRAPEHI IPQPTQTDRA
1510 1520 1530 1540 1550
PEHRSKVDKE QKDEASEEKE QVLEQKDWAR EKEGAALDQD NRAAGQKDGT
1560 1570 1580 1590 1600
LKEDKTQGQK SSFLEDKSTT PKEMTLDQKS PEKAKGVEQQ DGAVPEKTRA
1610 1620 1630 1640 1650
LGLEESPEEE GKAREQEEKY WKEQDVVQGW RETSPTRGEP VPAWEGKSPE
1660 1670 1680 1690 1700
QEVRYWRDRD ITLQQDAYWK ELSCERKVWF PHELDGQGAR PRYSEEREST
1710 1720 1730 1740 1750
FLDEGPNEQE ITPLQHTPRS PWASDFKDFQ EPLPQKGLEV ERWLAESPVG
1760 1770 1780 1790 1800
LPPEEEDKLT RSPFEIISPP ASPPEMTGQR VPSAPGQESP VPDTKSTPPT
1810 1820 1830 1840 1850
RNEPTTPSWL AEIPPWVPKD RPLPPAPLSP APAPPTPAPD PHAPAPFSWG
1860 1870 1880 1890 1900
IAEYDSVVAA VQEGAAELEG GPYSPLGKDY RKAEGEREGE GGAGAPDSSS
1910 1920 1930 1940 1950
FSSKVPEVTE SHTTRDAEQT EPEQREPTPY PDERSFQYAD IYEQMMLTGL
1960 1970 1980 1990 2000
GPACPTREPP LGASGDWPPH LSTKEEAAGR NKSAEKELSS AVSPPNLHSD
2010 2020 2030 2040 2050
TPTFSYASLA GPTIPPRQEP EPGPNVEPSF TPPAVPPRAP ISLSQDPSPP
2060 2070 2080 2090 2100
LNGSTTSCGP DRRTPSPKEA GRSHWDDGTN DSDLEKGARE QPEKETQSPS
2110 2120 2130 2140 2150
PHHPMPVGHP SLWPETEAHS SLSSDSHLGP VRPSLDFPAS AFGFSSLQPA
2160 2170 2180 2190 2200
PPQLPSPAEP RSAPCGSLAF SGDRALALVP GTPTRTRHDE YLEVTKAPSL
2210 2220 2230 2240 2250
DSSLPQLPSP SSPGAPLLSN LPRPASPALS EGSSSEATTP VISSVAERFP
2260 2270 2280 2290 2300
PGLEVAEQSS GELGPGNEPA AHSLWDLTPL SPAPLASRDL APAPAPAPAP
2310 2320 2330 2340 2350
SLPGNLGDGT LSCRPECSGE LTKKPSPFLS HSGDHEANGP GETSLNPPGF
2360 2370 2380 2390 2400
ATATAEKEEA EALHAWERGS WPEGAERSSR PDTLLSSEQR PGKSSGGPPC
2410 2420 2430 2440 2450
SLSSEVEAGP QGCATDPRPH CGELSPSFLN PPLPPSTDDS DLSTEEARLA
2460 2470 2480 2490 2500
GKGGRRRAGR PGATGGPCPM ADETPPTSAS DSGSSQSDSD VPPETEECPS
2510 2520 2530 2540 2550
ITAEAALDSD EDGDFLPVDK AGGVSGTHHP RPGHDPPPAP LPDPRPPPPR
2560 2570 2580 2590 2600
PDVCMADPEG LSSESGRVER LREKVQGRPG RKAPGRAKPA SPARRLDIRG
2610 2620 2630 2640 2650
KRSPTPGKGP VDRTSRALPR PRSTPSQVTS EEKDGHSPMS KGLVNGLKAG
2660 2670 2680 2690 2700
STALGSKGSS GPPVYVDLAY IPNHCSGKTA DQDFFRRVRA SYYVVSGNDP
2710 2720 2730 2740 2750
ANGEPSRAVL DALLEGKAQW GENLQVTLIP THDTEVTREW YQQTHEQQQQ
2760 2770
LNVLVLASSS TVVMQDESFP ACKIEF
Length:2,776
Mass (Da):300,140
Last modified:January 9, 2007 - v2
Checksum:i62A8CC584CCAB21A
GO
Isoform 2 (identifier: Q9QYR6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → METTPELGLQ...LNPEPVLPTM

Show »
Length:3,000
Mass (Da):324,586
Checksum:i58EB524496EB49C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti349 – 3491R → C in BAE27940 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → METTPELGLQSLGAPPAQNP AEPLCEAGAAVAAARWDLRK YSLLIVIGDIGTESQLRAVR AHLEQGILSWNIDLSSFDLN QQLRLFITRHLAHFSSEVKG QRTLCHQSETLETIILVNPT ADSISSEVHHLLSSPSAHKL LILSGQTLEPEGDLILQSGT YSYQNFAQVLHKPEIAQLLS NRDPGIQAFLTVSCLGEGDW SHLGLSSSQETLHLRLNPEP VLPTM in isoform 2. 1 PublicationVSP_003201

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147474 mRNA. Translation: BAE27940.1.
AK160546 mRNA. Translation: BAE35863.1.
AK163468 mRNA. Translation: BAE37354.1.
AL845466 Genomic DNA. Translation: CAM24218.1.
AF182211, AF182208, AF182209 Genomic DNA. Translation: AAF06164.1.
AF182211 Genomic DNA. Translation: AAF06163.1.
AF182213 mRNA. Translation: AAD55790.1.
AF182212 mRNA. Translation: AAD55789.1.
CCDSiCCDS50685.1. [Q9QYR6-1]
RefSeqiNP_001166977.1. NM_001173506.1. [Q9QYR6-1]
NP_115769.1. NM_032393.2.
UniGeneiMm.36501.

Genome annotation databases

EnsembliENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254. [Q9QYR6-1]
GeneIDi17754.
KEGGimmu:17754.
UCSCiuc008lyj.2. mouse. [Q9QYR6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147474 mRNA. Translation: BAE27940.1.
AK160546 mRNA. Translation: BAE35863.1.
AK163468 mRNA. Translation: BAE37354.1.
AL845466 Genomic DNA. Translation: CAM24218.1.
AF182211, AF182208, AF182209 Genomic DNA. Translation: AAF06164.1.
AF182211 Genomic DNA. Translation: AAF06163.1.
AF182213 mRNA. Translation: AAD55790.1.
AF182212 mRNA. Translation: AAD55789.1.
CCDSiCCDS50685.1. [Q9QYR6-1]
RefSeqiNP_001166977.1. NM_001173506.1. [Q9QYR6-1]
NP_115769.1. NM_032393.2.
UniGeneiMm.36501.

3D structure databases

ProteinModelPortaliQ9QYR6.
SMRiQ9QYR6. Positions 51-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201583. 5 interactions.
IntActiQ9QYR6. 5 interactions.
MINTiMINT-1203191.
STRINGi10090.ENSMUSP00000092223.

PTM databases

iPTMnetiQ9QYR6.
PhosphoSiteiQ9QYR6.
SwissPalmiQ9QYR6.

Proteomic databases

MaxQBiQ9QYR6.
PaxDbiQ9QYR6.
PRIDEiQ9QYR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254. [Q9QYR6-1]
GeneIDi17754.
KEGGimmu:17754.
UCSCiuc008lyj.2. mouse. [Q9QYR6-1]

Organism-specific databases

CTDi4130.
MGIiMGI:1306776. Map1a.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOVERGENiHBG052408.
InParanoidiQ9QYR6.
KOiK10429.

Miscellaneous databases

PROiQ9QYR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYR6.
CleanExiMM_MTAP1A.
ExpressionAtlasiQ9QYR6. baseline and differential.
GenevisibleiQ9QYR6. MM.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR015656. MAP1A.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF6. PTHR13843:SF6. 1 hit.
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Characterization of two promoters that regulate alternative transcripts in the microtubule-associated protein (MAP) 1A gene."
    Nakayama A., Odajima T., Murakami H., Mori N., Takahashi M.
    Biochim. Biophys. Acta 1518:260-266(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-224 (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633; SER-644; SER-667; SER-981; SER-1768 AND SER-1772, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: INTERACTION WITH TIAM2.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-117; SER-118; SER-121; SER-155; SER-384; SER-526; SER-527; THR-633; SER-667; SER-678; SER-873; SER-876; SER-877; SER-890; THR-893; SER-895; SER-899; SER-908; SER-981; SER-991; SER-999; SER-1008; SER-1023; SER-1062; THR-1068; SER-1131; SER-1133; SER-1147; SER-1177; SER-1196; SER-1205; SER-1289; SER-1310; SER-1313; SER-1316; SER-1516; SER-1606; SER-1747; SER-1762; SER-1768; SER-1772; THR-1777; SER-1783; SER-1789 AND SER-2082, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiMAP1A_MOUSE
AccessioniPrimary (citable) accession number: Q9QYR6
Secondary accession number(s): A2ARN9
, Q3TQM8, Q3TUV8, Q3UHB7, Q9QZH9, Q9QZI0, Q9QZI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 129 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.