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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.
13-FEB-2019, entry version 139.
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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EMBL; M83196; AAB48069.1; -; mRNA.
PIR; A43359; A43359.
RefSeq; NP_112257.1; NM_030995.1.
UniGene; Rn.11402; -.
ProteinModelPortal; P34926; -.
BioGrid; 247217; 6.
DIP; DIP-29265N; -.
IntAct; P34926; 6.
MINT; P34926; -.
STRING; 10116.ENSRNOP00000019320; -.
iPTMnet; P34926; -.
PhosphoSitePlus; P34926; -.
SwissPalm; P34926; -.
jPOST; 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; -.
OrthoDB; 86642at2759; -.
PhylomeDB; P34926; -.
PRO; PR:P34926; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0042995; C:cell projection; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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:0045202; C:synapse; IBA:GO_Central.
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:0015631; F:tubulin binding; IBA:GO_Central.
GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
GO; GO:0016358; P:dendrite development; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:RGD.
GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
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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BE
BG
Pathways :
WP1502: Mitochondrial biogenesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1339: Electron Transport Chain
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation
WP1647: Fatty acid biosynthesis
WP1708: Terpenoid backbone biosynthesis
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP295: Electron Transport Chain
WP542: Electron Transport Chain
WP59: Electron Transport Chain
WP772: Electron Transport Chain
WP884: Electron Transport Chain
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
Related Genes :
Bibliography :
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