Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000186021 – 2774Microtubule-associated protein 1AAdd BLAST2774
ChainiPRO_00004183781 – 2541MAP1A heavy chainAdd BLAST2541
ChainiPRO_00000186032542 – 2774MAP1 light chain LC2Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114PhosphoserineCombined sources1
Modified residuei117PhosphoserineBy similarity1
Modified residuei118PhosphoserineBy similarity1
Modified residuei121PhosphoserineBy similarity1
Modified residuei155PhosphoserineBy similarity1
Modified residuei177PhosphotyrosineBy similarity1
Modified residuei319PhosphoserineCombined sources1
Modified residuei322PhosphoserineCombined sources1
Modified residuei384PhosphoserineCombined sources1
Modified residuei504PhosphothreonineBy similarity1
Modified residuei526PhosphoserineCombined sources1
Modified residuei527PhosphoserineCombined sources1
Modified residuei604PhosphoserineBy similarity1
Modified residuei611PhosphoserineCombined sources1
Modified residuei643PhosphoserineCombined sources1
Modified residuei663PhosphothreonineCombined sources1
Modified residuei666PhosphoserineCombined sources1
Modified residuei677PhosphoserineBy similarity1
Modified residuei690PhosphoserineCombined sources1
Modified residuei785PhosphoserineBy similarity1
Modified residuei872PhosphoserineBy similarity1
Modified residuei875PhosphoserineBy similarity1
Modified residuei876PhosphoserineBy similarity1
Modified residuei889PhosphoserineCombined sources1
Modified residuei892PhosphothreonineCombined sources1
Modified residuei894PhosphoserineCombined sources1
Modified residuei898PhosphoserineBy similarity1
Modified residuei907PhosphoserineCombined sources1
Modified residuei980PhosphoserineCombined sources1
Modified residuei990PhosphoserineCombined sources1
Modified residuei998PhosphoserineBy similarity1
Modified residuei1007PhosphoserineCombined sources1
Modified residuei1013PhosphoserineCombined sources1
Modified residuei1022PhosphoserineCombined sources1
Modified residuei1029PhosphoserineCombined sources1
Modified residuei1037PhosphoserineCombined sources1
Modified residuei1061PhosphoserineBy similarity1
Modified residuei1132PhosphoserineCombined sources1
Modified residuei1134PhosphoserineCombined sources1
Modified residuei1148PhosphoserineBy similarity1
Modified residuei1160PhosphoserineBy similarity1
Modified residuei1178PhosphoserineCombined sources1
Modified residuei1188PhosphoserineCombined sources1
Modified residuei1191PhosphoserineCombined sources1
Modified residuei1197PhosphoserineBy similarity1
Modified residuei1206PhosphoserineCombined sources1
Modified residuei1209PhosphoserineCombined sources1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1280PhosphoserineCombined sources1
Modified residuei1301PhosphoserineCombined sources1
Modified residuei1304PhosphoserineCombined sources1
Modified residuei1307PhosphoserineBy similarity1
Modified residuei1504PhosphoserineBy similarity1
Modified residuei1568PhosphoserineBy similarity1
Modified residuei1574PhosphoserineCombined sources1
Modified residuei1594PhosphoserineCombined sources1
Modified residuei1622PhosphoserineCombined sources1
Modified residuei1643PhosphoserineCombined sources1
Modified residuei1715PhosphoserineBy similarity1
Modified residuei1742PhosphoserineCombined sources1
Modified residuei1757PhosphoserineCombined sources1
Modified residuei1763PhosphoserineCombined sources1
Modified residuei1767PhosphoserineCombined sources1
Modified residuei1772PhosphothreonineCombined sources1
Modified residuei1778PhosphoserineBy similarity1
Modified residuei1784PhosphoserineCombined sources1
Modified residuei1897PhosphoserineCombined sources1
Modified residuei1923PhosphothreonineBy similarity1
Modified residuei1988PhosphoserineCombined sources1
Modified residuei2026PhosphothreonineCombined sources1
Modified residuei2043PhosphoserineCombined sources1
Modified residuei2077PhosphoserineCombined sources1
Modified residuei2204PhosphoserineCombined sources1
Modified residuei2221PhosphoserineCombined sources1
Modified residuei2225PhosphoserineCombined sources1
Modified residuei2228PhosphoserineCombined sources1
Modified residuei2229PhosphoserineCombined sources1
Modified residuei2260PhosphoserineCombined sources1
Modified residuei2424PhosphoserineBy similarity1
Modified residuei2620PhosphoserineBy similarity1
Modified residuei2635PhosphoserineBy similarity1

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.
PhosphoSitePlusiP34926.

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 interactors.
DIPiDIP-29265N.
IntActiP34926. 6 interactors.
MINTiMINT-199032.
STRINGi10116.ENSRNOP00000019320.

Structurei

3D structure databases

ProteinModelPortaliP34926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati336 – 33813
Repeati415 – 41723
Repeati420 – 42233
Repeati424 – 42643
Repeati427 – 42953
Repeati431 – 43363
Repeati436 – 43873
Repeati440 – 44283
Repeati444 – 44693
Repeati449 – 451103
Repeati539 – 541113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni336 – 54111 X 3 AA repeats of K-K-[DE]Add BLAST206

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi309 – 496Lys-rich (basic)Add BLAST188

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 interactors.
DIPiDIP-29265N.
IntActiP34926. 6 interactors.
MINTiMINT-199032.
STRINGi10116.ENSRNOP00000019320.

PTM databases

iPTMnetiP34926.
PhosphoSitePlusiP34926.

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...

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: November 2, 2016
This is version 124 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.