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Protein

Microtubule-associated protein 1A

Gene

Map1a

Organism
Rattus norvegicus (Rat)
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

  • actin binding Source: RGD
  • collagen binding Source: RGD

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:Mtap1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3042. Map1a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27742774Microtubule-associated protein 1APRO_0000018602Add
BLAST
Chaini1 – 25412541MAP1A heavy chainPRO_0000418378Add
BLAST
Chaini2542 – 2774233MAP1 light chain LC2PRO_0000018603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphoserineCombined sources
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei121 – 1211PhosphoserineBy similarity
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei177 – 1771PhosphotyrosineBy similarity
Modified residuei319 – 3191PhosphoserineCombined sources
Modified residuei322 – 3221PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei504 – 5041PhosphothreonineBy similarity
Modified residuei526 – 5261PhosphoserineCombined sources
Modified residuei527 – 5271PhosphoserineCombined sources
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei611 – 6111PhosphoserineCombined sources
Modified residuei643 – 6431PhosphoserineCombined sources
Modified residuei663 – 6631PhosphothreonineCombined sources
Modified residuei666 – 6661PhosphoserineCombined sources
Modified residuei677 – 6771PhosphoserineBy similarity
Modified residuei690 – 6901PhosphoserineCombined sources
Modified residuei785 – 7851PhosphoserineBy similarity
Modified residuei872 – 8721PhosphoserineBy similarity
Modified residuei875 – 8751PhosphoserineBy similarity
Modified residuei876 – 8761PhosphoserineBy similarity
Modified residuei889 – 8891PhosphoserineCombined sources
Modified residuei892 – 8921PhosphothreonineCombined sources
Modified residuei894 – 8941PhosphoserineCombined sources
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei907 – 9071PhosphoserineCombined sources
Modified residuei980 – 9801PhosphoserineCombined sources
Modified residuei990 – 9901PhosphoserineCombined sources
Modified residuei998 – 9981PhosphoserineBy similarity
Modified residuei1007 – 10071PhosphoserineCombined sources
Modified residuei1013 – 10131PhosphoserineCombined sources
Modified residuei1022 – 10221PhosphoserineCombined sources
Modified residuei1029 – 10291PhosphoserineCombined sources
Modified residuei1037 – 10371PhosphoserineCombined sources
Modified residuei1061 – 10611PhosphoserineBy similarity
Modified residuei1132 – 11321PhosphoserineCombined sources
Modified residuei1134 – 11341PhosphoserineCombined sources
Modified residuei1148 – 11481PhosphoserineBy similarity
Modified residuei1160 – 11601PhosphoserineBy similarity
Modified residuei1178 – 11781PhosphoserineCombined sources
Modified residuei1188 – 11881PhosphoserineCombined sources
Modified residuei1191 – 11911PhosphoserineCombined sources
Modified residuei1197 – 11971PhosphoserineBy similarity
Modified residuei1206 – 12061PhosphoserineCombined sources
Modified residuei1209 – 12091PhosphoserineCombined sources
Modified residuei1252 – 12521PhosphoserineCombined sources
Modified residuei1280 – 12801PhosphoserineCombined sources
Modified residuei1301 – 13011PhosphoserineCombined sources
Modified residuei1304 – 13041PhosphoserineCombined sources
Modified residuei1307 – 13071PhosphoserineBy similarity
Modified residuei1504 – 15041PhosphoserineBy similarity
Modified residuei1568 – 15681PhosphoserineBy similarity
Modified residuei1574 – 15741PhosphoserineCombined sources
Modified residuei1594 – 15941PhosphoserineCombined sources
Modified residuei1622 – 16221PhosphoserineCombined sources
Modified residuei1643 – 16431PhosphoserineCombined sources
Modified residuei1715 – 17151PhosphoserineBy similarity
Modified residuei1742 – 17421PhosphoserineCombined sources
Modified residuei1757 – 17571PhosphoserineCombined sources
Modified residuei1763 – 17631PhosphoserineCombined sources
Modified residuei1767 – 17671PhosphoserineCombined sources
Modified residuei1772 – 17721PhosphothreonineCombined sources
Modified residuei1778 – 17781PhosphoserineBy similarity
Modified residuei1784 – 17841PhosphoserineCombined sources
Modified residuei1897 – 18971PhosphoserineCombined sources
Modified residuei1923 – 19231PhosphothreonineBy similarity
Modified residuei1988 – 19881PhosphoserineCombined sources
Modified residuei2026 – 20261PhosphothreonineCombined sources
Modified residuei2043 – 20431PhosphoserineCombined sources
Modified residuei2077 – 20771PhosphoserineCombined sources
Modified residuei2204 – 22041PhosphoserineCombined sources
Modified residuei2221 – 22211PhosphoserineCombined sources
Modified residuei2225 – 22251PhosphoserineCombined sources
Modified residuei2228 – 22281PhosphoserineCombined sources
Modified residuei2229 – 22291PhosphoserineCombined sources
Modified residuei2260 – 22601PhosphoserineCombined sources
Modified residuei2424 – 24241PhosphoserineBy similarity
Modified residuei2620 – 26201PhosphoserineBy similarity
Modified residuei2635 – 26351PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CSNK1D.1 Publication
LC2 is generated from MAP1A by proteolytic processing. It is free to associate with both MAP1A and MAP1B.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP34926.
PRIDEiP34926.

PTM databases

iPTMnetiP34926.
PhosphoSiteiP34926.

Expressioni

Tissue specificityi

Brain, heart and muscle.

Developmental stagei

Expressed late during neuronal development appearing when axons and dendrites begin to solidify and stabilize their morphology.

Interactioni

Subunit structurei

Interacts with TIAM2 (By similarity). 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 similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg1Q626962EBI-631571,EBI-389325
Dlg2Q636224EBI-631571,EBI-396947
Dlg4P3101612EBI-631571,EBI-375655

GO - Molecular functioni

  • actin binding Source: RGD
  • collagen binding Source: RGD

Protein-protein interaction databases

BioGridi247217. 4 interactions.
DIPiDIP-29265N.
IntActiP34926. 6 interactions.
MINTiMINT-199032.
STRINGi10116.ENSRNOP00000019320.

Structurei

3D structure databases

ProteinModelPortaliP34926.
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 repeats of K-K-[DE]Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi309 – 496188Lys-rich (basic)Add
BLAST

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.
HOGENOMiHOG000231839.
HOVERGENiHBG052408.
InParanoidiP34926.
KOiK10429.
PhylomeDBiP34926.

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.

Sequencei

Sequence statusi: Complete.

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

P34926-1 [UniParc]FASTAAdd to basket

« 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 VSKLAKREEV LEEGAKEARS
360 370 380 390 400
ELAKELAKTE KKAKEPSEKP PEKPSKSERV RGESSEALKA EKRRLIKDKA
410 420 430 440 450
GKKHLKEKIS KLEEKKDKEK KEIKKERKEL KKEEGRKEEK KDAKKDEKRK
460 470 480 490 500
DTKPEVKKLS KPDLKPFTPE VRKTLYKAKA PGRVKVDKGR AARGEKELSS
510 520 530 540 550
EPRTPPAQKG AAPPAAVSGH RELALSSPED LTQDFEELKR EERGLLAEQR
560 570 580 590 600
DTGLGEKPLP ADATEQGHPS AAIQVTQPSG PVLEGEHVER EKEVVPDSPG
610 620 630 640 650
DKGSTNRGPD SGAEVEKEKE TWEERKQREA ELGPENTAAR EESEAEVKED
660 670 680 690 700
VIEKAELEEM EETHPSDEEG EETKAESFYQ KHTQEALKAS PKSREALGGR
710 720 730 740 750
DLGFQGKAPE KETASFLSSL ATPAGATEHV SYIQDETIPG YSETEQTISD
760 770 780 790 800
EEIHDEPDER PAPPRFPTST YDLSGPEGPG PFEASQAADS AVPASSSKTY
810 820 830 840 850
GAPETELTYP PNMVAAPLAE EEHVSSATSI TECDKLSSFA TSVAEDQSVA
860 870 880 890 900
SLTAPQTEET GKSSLLLDTV TSIPSSRTEA TQGLDYVPSA GTISPTSSLE
910 920 930 940 950
EDKGFKSPPC EDFSVTGESE KKGETVGRGL SGEKAVGKEE KYVVTSEKLS
960 970 980 990 1000
GQYAAVFGAP GHTLPPGEPA LGEVEERCLS PDDSTVKMAS PPPSGPPSAA
1010 1020 1030 1040 1050
HTPFHQSPVE DKSEPRDFQE DSWGETKHSP GVSKEDSEEQ TVKPGPEEGT
1060 1070 1080 1090 1100
SEEGKGPPTR SPQAQDMPVS IAGGQTGCTI QLLPEQDKAI VFETGEAGSN
1110 1120 1130 1140 1150
LGAGTLPGEV RTSTEEATEP QKDEVLRFTD QSLSPEDAES LSVLSVVSPD
1160 1170 1180 1190 1200
TTKQEATPRS PCSLKEQQPH KDLWPMVSPE DTQSLSFSEE SPSKETSLDI
1210 1220 1230 1240 1250
SSKQLSPESL GTLQFGELNL GKEERGPVMK AEDDSCHLAP VSIPEPHRAT
1260 1270 1280 1290 1300
VSPSTDETPA GTLPGGSFSH SALSVDRKHS PGEITGPGGH FMTSDSSLTK
1310 1320 1330 1340 1350
SPESLSSPAM EDLAVEWEGK APGKEKEPEL KSETRQQKGQ ILPEKVAVVE
1360 1370 1380 1390 1400
QDLIIHQKDG ALDEENKPGR QQDKTPEQKG RDLDEKDTAA ELDKGPEPKE
1410 1420 1430 1440 1450
KDLDREDQGQ RAGPPAEKDK ASEQRDTDLQ QTQATEPRDR AQERRDSEEK
1460 1470 1480 1490 1500
DKSLELRDRT PEEKDRILVQ EDRAPEHSIP EPTQTDRAPD RKGTDDKEQK
1510 1520 1530 1540 1550
EEASEEKEQV LEQKDWALGK EGETLDQEAR TAEQKDETLK EDKTQGQKSS
1560 1570 1580 1590 1600
FVEDKTTTSK ETVLDQKSAE KADSVEQQDG AALEKTRALG LEESPAEGSK
1610 1620 1630 1640 1650
AREQEKKYWK EQDVVQGWRE TSPTRGEPVG GQKEPVPAWE GKSPEQEVRY
1660 1670 1680 1690 1700
WRDRDITLQQ DAYWRELSCD RKVWFPHELD GQGARPRYCE ERESTFLDEG
1710 1720 1730 1740 1750
PDEQEITPLQ HTPRSPWTSD FKDFQEPLPQ KGLEVERWLA ESPVGLPPEE
1760 1770 1780 1790 1800
EDKLTRSPFE IISPPASPPE MTGQRVPSAP GQESPVPDTE STAPMRNEPT
1810 1820 1830 1840 1850
TPSWLAEIPP WVPKDRPLPP APLSPAPAPP TPAPEPHTPV PFSWGLAEYD
1860 1870 1880 1890 1900
SVVAAVQEGA AELEGGPYSP LGKDYRKAEG EREGEGGAGA PDSSSFSPKV
1910 1920 1930 1940 1950
PEAGESLATR DTEQTEPEQR EPTPYPDERS FQYADIYEQM MLTGLGPACP
1960 1970 1980 1990 2000
TREPPLGASG DWPPHLSTKE EAAGCNTSAE KETSSPASPQ NLQSDTPAFS
2010 2020 2030 2040 2050
YASLAGPAVP PRQEPDPGPN VEPSITPPAV PPRAPISLSK DLSPPLNGST
2060 2070 2080 2090 2100
VSCSPDRRTP SPKETGRGHW DDGTNDSDLE KGAREQPEKE TRSPSPHHPM
2110 2120 2130 2140 2150
PMGHSSLWPE TEAYSSLSSD SHLGSVRPSL DFPASAFGFS SLQPAPPQLP
2160 2170 2180 2190 2200
SPAEPRSAPC GSLAFSGDRA LALVPGTPTR TRHDEYLEVT KAPSLDSSLP
2210 2220 2230 2240 2250
QLPSPSSPGG PLLSNLPRPA SPALSEGSSS EATTPVISSV AERFPPGLEA
2260 2270 2280 2290 2300
AEQSAEGLGS GKESAAHSLW DLTPLSPAPS ASLDLAPAPA PAPAPAPGLP
2310 2320 2330 2340 2350
GDLGDGTLPC RPECTGELTK KPSPFLSPSG DHEANGPGET SLNPPGFVTA
2360 2370 2380 2390 2400
TAEKEEAEAP HAWERGSWPE GAERSSRPDT LLSSEQPLRP GKSSGGPPCS
2410 2420 2430 2440 2450
LSSEVEAGPQ GCATDPRPHC GELSPSFLNP PLPPSTDDSD LSTEEARLAG
2460 2470 2480 2490 2500
KGGRRRVGRP GATGGPCPMA DETPPTSASD SGSSQSDSDV PPETEECPSI
2510 2520 2530 2540 2550
TAEAALDSDE DGDFLPVDKA GGVSGTHHPR PGHDPPPTPL PDPRPSPPRP
2560 2570 2580 2590 2600
DVCMADPEGL SSESGRVERL REKGRPGRRA PGRAKPASPA RRLDIRGKRS
2610 2620 2630 2640 2650
PTPGKGPVDR TSRTVPRPRS TPSQVTSAEE KDGHSPMSKG LVNGLKAGST
2660 2670 2680 2690 2700
ALGSKGGSGP PVYVDLAYIP NHCSGKTADQ DFFRRVRASY YVVSGNDPAN
2710 2720 2730 2740 2750
GEPSRAVLDA LLEGKAQWGE NLQVTLIPTH DTEVTREWYQ QTHEQQQQLN
2760 2770
VLVLASSSTV VMQDESFPAC KIEF
Length:2,774
Mass (Da):299,531
Last modified:February 1, 1994 - v1
Checksum:i3DEF74427BA9D7D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83196 mRNA. Translation: AAB48069.1.
PIRiA43359.
RefSeqiNP_112257.1. NM_030995.1.
UniGeneiRn.11402.

Genome annotation databases

GeneIDi25152.
KEGGirno:25152.
UCSCiRGD:3042. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83196 mRNA. Translation: AAB48069.1.
PIRiA43359.
RefSeqiNP_112257.1. NM_030995.1.
UniGeneiRn.11402.

3D structure databases

ProteinModelPortaliP34926.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247217. 4 interactions.
DIPiDIP-29265N.
IntActiP34926. 6 interactions.
MINTiMINT-199032.
STRINGi10116.ENSRNOP00000019320.

PTM databases

iPTMnetiP34926.
PhosphoSiteiP34926.

Proteomic databases

PaxDbiP34926.
PRIDEiP34926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25152.
KEGGirno:25152.
UCSCiRGD:3042. rat.

Organism-specific databases

CTDi4130.
RGDi3042. Map1a.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000231839.
HOVERGENiHBG052408.
InParanoidiP34926.
KOiK10429.
PhylomeDBiP34926.

Miscellaneous databases

PROiP34926.

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. "Microtubule-associated proteins 1A and LC2. Two proteins encoded in one messenger RNA."
    Langkopf A., Hammarback J.A., Mueller R., Vallee R.B., Garner C.C.
    J. Biol. Chem. 267:16561-16566(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A."
    Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T., Ralston H.J., Bredt D.S.
    J. Neurosci. 18:8805-8813(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4.
  3. "Interaction of casein kinase 1 delta (CK1 delta) with the light chain LC2 of microtubule associated protein 1A (MAP1A)."
    Wolff S., Xiao Z., Wittau M., Suessner N., Stoeter M., Knippschild U.
    Biochim. Biophys. Acta 1745:196-206(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK1D, PHOSPHORYLATION BY CSNK1D.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-319; SER-322; SER-384; SER-526; SER-527; SER-611; SER-643; THR-663; SER-666; SER-690; SER-889; THR-892; SER-894; SER-907; SER-980; SER-990; SER-1007; SER-1013; SER-1022; SER-1029; SER-1037; SER-1132; SER-1134; SER-1178; SER-1188; SER-1191; SER-1206; SER-1209; SER-1252; SER-1280; SER-1301; SER-1304; SER-1574; SER-1594; SER-1622; SER-1643; SER-1742; SER-1757; SER-1763; SER-1767; THR-1772; SER-1784; SER-1897; SER-1988; THR-2026; SER-2043; SER-2077; SER-2204; SER-2221; SER-2225; SER-2228; SER-2229 AND SER-2260, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1A_RAT
AccessioniPrimary (citable) accession number: P34926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 123 of the entry and version 1 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. 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.