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Microtubule-associated protein 1A (MAP-1A) [Cleaved into: MAP1A heavy chain; MAP1 light chain LC2]

 MAP1A_RAT               Reviewed;        2774 AA.
 P34926;
 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1994, sequence version 1.
 12-SEP-2018, entry version 136.
 RecName: Full=Microtubule-associated protein 1A;
          Short=MAP-1A;
 Contains:
   RecName: Full=MAP1A heavy chain;
 Contains:
   RecName: Full=MAP1 light chain LC2;
 Name=Map1a; Synonyms=Mtap1a;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Brain;
 PubMed=1379599;
 Langkopf A., Hammarback J.A., Mueller R., Vallee R.B., Garner C.C.;
 "Microtubule-associated proteins 1A and LC2. Two proteins encoded in
 one messenger RNA.";
 J. Biol. Chem. 267:16561-16566(1992).
 [2]
 INTERACTION WITH DLG1; DLG2 AND DLG4.
 PubMed=9786987;
 Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J.,
 Milroy T., Ralston H.J., Bredt D.S.;
 "Localization of postsynaptic density-93 to dendritic microtubules and
 interaction with microtubule-associated protein 1A.";
 J. Neurosci. 18:8805-8813(1998).
 [3]
 INTERACTION WITH CSNK1D, AND PHOSPHORYLATION BY CSNK1D.
 PubMed=15961172; DOI=10.1016/j.bbamcr.2005.05.004;
 Wolff S., Xiao Z., Wittau M., Suessner N., Stoeter M., Knippschild U.;
 "Interaction of casein kinase 1 delta (CK1 delta) with the light chain
 LC2 of microtubule associated protein 1A (MAP1A).";
 Biochim. Biophys. Acta 1745:196-206(2005).
 [4]
 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, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
 SCALE ANALYSIS].
 PubMed=22673903; DOI=10.1038/ncomms1871;
 Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
 Lundby C., Olsen J.V.;
 "Quantitative maps of protein phosphorylation sites across 14
 different rat organs and tissues.";
 Nat. Commun. 3:876-876(2012).
 -!- FUNCTION: Structural protein involved in the filamentous cross-
     bridging between microtubules and other skeletal elements.
 -!- SUBUNIT: 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. {ECO:0000250,
     ECO:0000269|PubMed:15961172, ECO:0000269|PubMed:9786987}.
 -!- INTERACTION:
     Q62696:Dlg1; NbExp=2; IntAct=EBI-631571, EBI-389325;
     Q63622:Dlg2; NbExp=4; IntAct=EBI-631571, EBI-396947;
     P31016:Dlg4; NbExp=16; IntAct=EBI-631571, EBI-375655;
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
 -!- TISSUE SPECIFICITY: Brain, heart and muscle.
 -!- DEVELOPMENTAL STAGE: Expressed late during neuronal development
     appearing when axons and dendrites begin to solidify and stabilize
     their morphology.
 -!- DOMAIN: The basic region containing the repeats may be responsible
     for the binding of MAP1A to microtubules.
 -!- PTM: Phosphorylated by CSNK1D. {ECO:0000269|PubMed:15961172}.
 -!- PTM: LC2 is generated from MAP1A by proteolytic processing. It is
     free to associate with both MAP1A and MAP1B.
 -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
 -----------------------------------------------------------------------
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 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; M83196; AAB48069.1; -; mRNA.
 PIR; A43359; A43359.
 RefSeq; NP_112257.1; NM_030995.1.
 UniGene; Rn.11402; -.
 ProteinModelPortal; P34926; -.
 BioGrid; 247217; 5.
 DIP; DIP-29265N; -.
 IntAct; P34926; 6.
 MINT; P34926; -.
 STRING; 10116.ENSRNOP00000019320; -.
 iPTMnet; P34926; -.
 PhosphoSitePlus; P34926; -.
 SwissPalm; P34926; -.
 PaxDb; P34926; -.
 PRIDE; P34926; -.
 GeneID; 25152; -.
 KEGG; rno:25152; -.
 UCSC; RGD:3042; rat.
 CTD; 4130; -.
 RGD; 3042; Map1a.
 eggNOG; KOG3592; Eukaryota.
 eggNOG; ENOG410XRYM; LUCA.
 HOGENOM; HOG000231839; -.
 HOVERGEN; HBG052408; -.
 InParanoid; P34926; -.
 KO; K10429; -.
 PhylomeDB; P34926; -.
 PRO; PR:P34926; -.
 Proteomes; UP000002494; Unplaced.
 GO; GO:0030424; C:axon; IDA:UniProtKB.
 GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
 GO; GO:0030425; C:dendrite; IDA:UniProtKB.
 GO; GO:0044307; C:dendritic branch; IDA:ARUK-UCL.
 GO; GO:0043198; C:dendritic shaft; IDA:ARUK-UCL.
 GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO; GO:0005875; C:microtubule associated complex; IDA:RGD.
 GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
 GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
 GO; GO:0150001; C:primary dendrite; IDA:ARUK-UCL.
 GO; GO:0003779; F:actin binding; IDA:RGD.
 GO; GO:0005518; F:collagen binding; IPI:RGD.
 GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL.
 GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
 GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:RGD.
 InterPro; IPR026074; MAP1.
 InterPro; IPR015656; MAP1A.
 InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
 PANTHER; PTHR13843; PTHR13843; 2.
 PANTHER; PTHR13843:SF6; PTHR13843:SF6; 2.
 SUPFAM; SSF56281; SSF56281; 1.
 1: Evidence at protein level;
 Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
 Phosphoprotein; Reference proteome; Repeat.
 CHAIN         1   2774       Microtubule-associated protein 1A.
                              /FTId=PRO_0000018602.
 CHAIN         1   2541       MAP1A heavy chain.
                              /FTId=PRO_0000418378.
 CHAIN      2542   2774       MAP1 light chain LC2.
                              /FTId=PRO_0000018603.
 REPEAT      336    338       1.
 REPEAT      415    417       2.
 REPEAT      420    422       3.
 REPEAT      424    426       4.
 REPEAT      427    429       5.
 REPEAT      431    433       6.
 REPEAT      436    438       7.
 REPEAT      440    442       8.
 REPEAT      444    446       9.
 REPEAT      449    451       10.
 REPEAT      539    541       11.
 REGION      336    541       11 X 3 AA repeats of K-K-[DE].
 COMPBIAS    309    496       Lys-rich (basic).
 MOD_RES     114    114       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     117    117       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES     118    118       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     121    121       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     155    155       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     177    177       Phosphotyrosine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     319    319       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     322    322       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     384    384       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     504    504       Phosphothreonine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES     526    526       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     527    527       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     604    604       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES     611    611       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     643    643       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     663    663       Phosphothreonine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     666    666       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     677    677       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     690    690       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     785    785       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES     872    872       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     875    875       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     876    876       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     889    889       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     892    892       Phosphothreonine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     894    894       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     898    898       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES     907    907       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     980    980       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     990    990       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES     998    998       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES    1007   1007       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1013   1013       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1022   1022       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1029   1029       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1037   1037       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1061   1061       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1132   1132       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1134   1134       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1148   1148       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1160   1160       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1178   1178       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1188   1188       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1191   1191       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1197   1197       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES    1206   1206       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1209   1209       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1252   1252       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1280   1280       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1301   1301       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1304   1304       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1307   1307       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES    1504   1504       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES    1568   1568       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1574   1574       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1594   1594       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1622   1622       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1643   1643       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1715   1715       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1742   1742       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1757   1757       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1763   1763       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1767   1767       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1772   1772       Phosphothreonine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1778   1778       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QYR6}.
 MOD_RES    1784   1784       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1897   1897       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    1923   1923       Phosphothreonine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    1988   1988       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2026   2026       Phosphothreonine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2043   2043       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2077   2077       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2204   2204       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2221   2221       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2225   2225       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2228   2228       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2229   2229       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2260   2260       Phosphoserine.
                              {ECO:0000244|PubMed:22673903}.
 MOD_RES    2424   2424       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    2620   2620       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 MOD_RES    2635   2635       Phosphoserine.
                              {ECO:0000250|UniProtKB:P78559}.
 SEQUENCE   2774 AA;  299531 MW;  3DEF74427BA9D7D7 CRC64;
 MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS ALFAVNGFNI
 LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING LLQRKVAELE EEQSQGSSSY
 SDWVKNLISP ELGVVFFNVP DKLRLPDASR KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV
 SNTIEPLTLF HKMGVGRLDM YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LANGKEAEIS
 VPYLTSITAL VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
 AGAVPANLKP SKIKHRADSK ESLKAAPKTA VSKLAKREEV LEEGAKEARS ELAKELAKTE
 KKAKEPSEKP PEKPSKSERV RGESSEALKA EKRRLIKDKA GKKHLKEKIS KLEEKKDKEK
 KEIKKERKEL KKEEGRKEEK KDAKKDEKRK DTKPEVKKLS KPDLKPFTPE VRKTLYKAKA
 PGRVKVDKGR AARGEKELSS EPRTPPAQKG AAPPAAVSGH RELALSSPED LTQDFEELKR
 EERGLLAEQR DTGLGEKPLP ADATEQGHPS AAIQVTQPSG PVLEGEHVER EKEVVPDSPG
 DKGSTNRGPD SGAEVEKEKE TWEERKQREA ELGPENTAAR EESEAEVKED VIEKAELEEM
 EETHPSDEEG EETKAESFYQ KHTQEALKAS PKSREALGGR DLGFQGKAPE KETASFLSSL
 ATPAGATEHV SYIQDETIPG YSETEQTISD EEIHDEPDER PAPPRFPTST YDLSGPEGPG
 PFEASQAADS AVPASSSKTY GAPETELTYP PNMVAAPLAE EEHVSSATSI TECDKLSSFA
 TSVAEDQSVA SLTAPQTEET GKSSLLLDTV TSIPSSRTEA TQGLDYVPSA GTISPTSSLE
 EDKGFKSPPC EDFSVTGESE KKGETVGRGL SGEKAVGKEE KYVVTSEKLS GQYAAVFGAP
 GHTLPPGEPA LGEVEERCLS PDDSTVKMAS PPPSGPPSAA HTPFHQSPVE DKSEPRDFQE
 DSWGETKHSP GVSKEDSEEQ TVKPGPEEGT SEEGKGPPTR SPQAQDMPVS IAGGQTGCTI
 QLLPEQDKAI VFETGEAGSN LGAGTLPGEV RTSTEEATEP QKDEVLRFTD QSLSPEDAES
 LSVLSVVSPD TTKQEATPRS PCSLKEQQPH KDLWPMVSPE DTQSLSFSEE SPSKETSLDI
 SSKQLSPESL GTLQFGELNL GKEERGPVMK AEDDSCHLAP VSIPEPHRAT VSPSTDETPA
 GTLPGGSFSH SALSVDRKHS PGEITGPGGH FMTSDSSLTK SPESLSSPAM EDLAVEWEGK
 APGKEKEPEL KSETRQQKGQ ILPEKVAVVE QDLIIHQKDG ALDEENKPGR QQDKTPEQKG
 RDLDEKDTAA ELDKGPEPKE KDLDREDQGQ RAGPPAEKDK ASEQRDTDLQ QTQATEPRDR
 AQERRDSEEK DKSLELRDRT PEEKDRILVQ EDRAPEHSIP EPTQTDRAPD RKGTDDKEQK
 EEASEEKEQV LEQKDWALGK EGETLDQEAR TAEQKDETLK EDKTQGQKSS FVEDKTTTSK
 ETVLDQKSAE KADSVEQQDG AALEKTRALG LEESPAEGSK AREQEKKYWK EQDVVQGWRE
 TSPTRGEPVG GQKEPVPAWE GKSPEQEVRY WRDRDITLQQ DAYWRELSCD RKVWFPHELD
 GQGARPRYCE ERESTFLDEG PDEQEITPLQ HTPRSPWTSD FKDFQEPLPQ KGLEVERWLA
 ESPVGLPPEE EDKLTRSPFE IISPPASPPE MTGQRVPSAP GQESPVPDTE STAPMRNEPT
 TPSWLAEIPP WVPKDRPLPP APLSPAPAPP TPAPEPHTPV PFSWGLAEYD SVVAAVQEGA
 AELEGGPYSP LGKDYRKAEG EREGEGGAGA PDSSSFSPKV PEAGESLATR DTEQTEPEQR
 EPTPYPDERS FQYADIYEQM MLTGLGPACP TREPPLGASG DWPPHLSTKE EAAGCNTSAE
 KETSSPASPQ NLQSDTPAFS YASLAGPAVP PRQEPDPGPN VEPSITPPAV PPRAPISLSK
 DLSPPLNGST VSCSPDRRTP SPKETGRGHW DDGTNDSDLE KGAREQPEKE TRSPSPHHPM
 PMGHSSLWPE TEAYSSLSSD SHLGSVRPSL DFPASAFGFS SLQPAPPQLP SPAEPRSAPC
 GSLAFSGDRA LALVPGTPTR TRHDEYLEVT KAPSLDSSLP QLPSPSSPGG PLLSNLPRPA
 SPALSEGSSS EATTPVISSV AERFPPGLEA AEQSAEGLGS GKESAAHSLW DLTPLSPAPS
 ASLDLAPAPA PAPAPAPGLP GDLGDGTLPC RPECTGELTK KPSPFLSPSG DHEANGPGET
 SLNPPGFVTA TAEKEEAEAP HAWERGSWPE GAERSSRPDT LLSSEQPLRP GKSSGGPPCS
 LSSEVEAGPQ GCATDPRPHC GELSPSFLNP PLPPSTDDSD LSTEEARLAG KGGRRRVGRP
 GATGGPCPMA DETPPTSASD SGSSQSDSDV PPETEECPSI TAEAALDSDE DGDFLPVDKA
 GGVSGTHHPR PGHDPPPTPL PDPRPSPPRP DVCMADPEGL SSESGRVERL REKGRPGRRA
 PGRAKPASPA RRLDIRGKRS PTPGKGPVDR TSRTVPRPRS TPSQVTSAEE KDGHSPMSKG
 LVNGLKAGST ALGSKGGSGP PVYVDLAYIP NHCSGKTADQ DFFRRVRASY YVVSGNDPAN
 GEPSRAVLDA LLEGKAQWGE NLQVTLIPTH DTEVTREWYQ QTHEQQQQLN VLVLASSSTV
 VMQDESFPAC KIEF

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26-400	HLA-F belongs to the HLA class I heavy chain paralogues. It is a non-classical heavy chain that forms a heterodimer with a beta-2 microglobulin light chain, with the heavy chain anchored in the membra	0.05 mg
EIAAB24954	Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Homo sapiens,Human,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3B,Mic
EIAAB24952	Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Bos taurus,Bovine,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3,MAP1L
EIAAB25247	Homo sapiens,Human,MAP1LC3B2,Microtubule-associated proteins 1A_1B light chain 3 beta 2,Microtubule-associated proteins 1A_1B light chain 3B-like
EIAAB12159	Axonemal beta dynein heavy chain 2,Ciliary dynein heavy chain 2,DNAH2,DNAHC2,DNHD3,Dynein heavy chain 2, axonemal,Dynein heavy chain domain-containing protein 3,Homo sapiens,Human,KIAA1503
EIAAB12165	Axonemal beta dynein heavy chain 7,Ciliary dynein heavy chain 7,DNAH7,Dynein heavy chain 7, axonemal,Dynein heavy chain-like protein 2,hDHC2,Homo sapiens,Human,KIAA0944
EIAAB12153	Axonemal beta dynein heavy chain 12,Axonemal dynein heavy chain 12-like protein,Axonemal dynein heavy chain 7-like protein,Ciliary dynein heavy chain 12,DHC3,DLP12,DNAH12,DNAH12L,DNAH7L,DNAHC3,DNHD2,D
EIAAB12157	Axonemal beta dynein heavy chain 17,Axonemal dynein heavy chain-like protein 1,Ciliary dynein heavy chain 17,Ciliary dynein heavy chain-like protein 1,DNAH17,DNAHL1,DNEL2,Dynein heavy chain 17, axonem
orb81209	Human Microtubule-Associated Protein Light Chain Alpha protein MAP1LC3A Recombinant Human produced in E.coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-120 a.a.) and	5
EIAAB12175	Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,DHC1B,DHC2,DNCH2,DYH1B,DYNC2H1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain 11,Dynein heavy chain isotype 1B,hDHC11,Homo sapi
EIAAB26010	17 kDa myosin light chain,Homo sapiens,Human,LC17,MLC-3,MYL6,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Smooth muscle and nonmuscle myosin light
EIAAB12173	Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,Dhc1b,Dlp4,Dnch2,Dnchc2,Dync2h1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain isotype 1B,Dynein-like protein 4,Rat,Rattus norv
EIAAB12152	Axonemal beta dynein heavy chain 12,Axonemal dynein heavy chain 12-like protein,Axonemal dynein heavy chain 7-like protein,Ciliary dynein heavy chain 12,Dnah12,Dnah12l,Dnah7l,Dnahc12,Dnahc7l,Dynein he
EIAAB12166	Axob,Axonemal beta dynein heavy chain 7,Axonemal dynein heavy chain b,Ciliary dynein heavy chain 7,Dlp7,Dnah7,Dynein heavy chain 7, axonemal,Dynein-like protein 7,Rat,Rattus norvegicus
EIAAB26011	17 kDa myosin light chain,LC17,MLC-3,Mouse,Mus musculus,Myl6,Myln,Myosin light chain 3,Myosin light chain A3,Myosin light chain alkali 3,Myosin light polypeptide 6,Smooth muscle and nonmuscle myosin l
EIAAB12174	Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,Dhc1b,Dnchc2,Dync2h1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain 11,Dynein heavy chain isotype 1B,Kiaa1997,mDHC11,Mouse,Mus
EIAAB12178	8 kDa dynein light chain,DLC8,Dncl1,Dnclc1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,Dynll1,PIN,Pin,Protein inhibitor of neuronal nitric oxide synthase,Rat,Rattus norvegicus
EIAAB12177	8 kDa dynein light chain,DLC1,DLC8,DNCL1,DNCLC1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,DYNLL1,Oryctolagus cuniculus,PIN,Protein inhibitor of neuronal nitric oxide synthase,Rab

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