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Protein

Fatty acid synthase

Gene

Fasn

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

Functioni

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein.

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+.
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
Active sitei2301For thioesterase activityPROSITE-ProRule annotation1
Active sitei2474For thioesterase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1664 – 1681NADP (ER)By similarityAdd BLAST18
Nucleotide bindingi1879 – 1894NADP (KR)By similarityAdd BLAST16

GO - Molecular functioni

GO - Biological processi

  • acetyl-CoA metabolic process Source: Ensembl
  • cellular response to interleukin-4 Source: MGI
  • fatty acid biosynthetic process Source: MGI
  • mammary gland development Source: CACAO

Keywordsi

Molecular functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD, NADP, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-163765 ChREBP activates metabolic gene expression
R-MMU-199220 Vitamin B5 (pantothenate) metabolism
R-MMU-75105 Fatty acyl-CoA biosynthesis

Protein family/group databases

ESTHERimouse-FASN Thioesterase

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase (EC:2.3.1.85)
Including the following 7 domains:
[Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.39)
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39)
Oleoyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
Gene namesi
Name:Fasn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95485 Fasn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1795189

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001802771 – 2504Fatty acid synthaseAdd BLAST2504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei59N6-acetyllysineCombined sources1
Modified residuei63PhosphoserineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei528N6-acetyllysineBy similarity1
Modified residuei673N6-acetyllysineBy similarity1
Modified residuei725PhosphoserineCombined sources1
Modified residuei790N6-acetyllysineCombined sources1
Modified residuei993N6-acetyllysineCombined sources1
Modified residuei1071N6-acetyllysineCombined sources1
Modified residuei1276N6-acetyllysineCombined sources1
Modified residuei1577PhosphoserineCombined sources1
Modified residuei1587PhosphoserineCombined sources1
Modified residuei1697N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei1697N6-acetyllysine; alternateBy similarity1
Modified residuei1764N6-acetyllysineBy similarity1
Modified residuei1840N6-acetyllysineCombined sources1
Modified residuei1988N6-acetyllysineBy similarity1
Modified residuei2150O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
Modified residuei2150Phosphoserine; alternateBy similarity1
Modified residuei2190PhosphoserineCombined sources1
Modified residuei2229PhosphoserineBy similarity1
Modified residuei2384N6-acetyllysineCombined sources1
Cross-linki2442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19096
MaxQBiP19096
PaxDbiP19096
PeptideAtlasiP19096
PRIDEiP19096

PTM databases

iPTMnetiP19096
PhosphoSitePlusiP19096
SwissPalmiP19096

Expressioni

Inductioni

Up-regulated by endocannabinoid anandamide/AEA.1 Publication

Gene expression databases

BgeeiENSMUSG00000025153
CleanExiMM_FASN
ExpressionAtlasiP19096 baseline and differential
GenevisibleiP19096 MM

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion (By similarity). Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199596, 6 interactors
IntActiP19096, 9 interactors
MINTiP19096
STRINGi10090.ENSMUSP00000052872

Chemistry databases

BindingDBiP19096

Structurei

Secondary structure

12504
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Beta strandi16 – 18Combined sources3
Helixi19 – 27Combined sources9
Beta strandi36 – 40Combined sources5
Helixi44 – 46Combined sources3
Helixi62 – 65Combined sources4
Helixi69 – 73Combined sources5
Helixi77 – 92Combined sources16
Helixi97 – 100Combined sources4
Beta strandi106 – 111Combined sources6
Helixi115 – 120Combined sources6
Turni124 – 126Combined sources3
Helixi130 – 135Combined sources6
Helixi139 – 148Combined sources10
Beta strandi154 – 158Combined sources5
Helixi160 – 162Combined sources3
Helixi163 – 176Combined sources14
Beta strandi181 – 189Combined sources9
Helixi194 – 202Combined sources9
Beta strandi227 – 235Combined sources9
Helixi236 – 238Combined sources3
Beta strandi243 – 253Combined sources11
Helixi266 – 276Combined sources11
Helixi278 – 280Combined sources3
Helixi284 – 286Combined sources3
Beta strandi287 – 291Combined sources5
Helixi300 – 311Combined sources12
Helixi313 – 315Combined sources3
Beta strandi320 – 323Combined sources4
Helixi326 – 329Combined sources4
Helixi333 – 335Combined sources3
Helixi336 – 349Combined sources14
Helixi367 – 370Combined sources4
Beta strandi373 – 376Combined sources4
Beta strandi387 – 393Combined sources7
Beta strandi397 – 406Combined sources10
Helixi416 – 418Combined sources3
Beta strandi422 – 430Combined sources9
Helixi431 – 443Combined sources13
Turni444 – 446Combined sources3
Helixi448 – 456Combined sources9
Turni462 – 464Combined sources3
Beta strandi467 – 477Combined sources11
Beta strandi480 – 484Combined sources5
Beta strandi492 – 496Combined sources5
Turni504 – 507Combined sources4
Helixi509 – 512Combined sources4
Helixi514 – 527Combined sources14
Turni528 – 531Combined sources4
Helixi534 – 539Combined sources6
Helixi545 – 547Combined sources3
Helixi549 – 569Combined sources21
Beta strandi575 – 579Combined sources5
Helixi583 – 590Combined sources8
Helixi596 – 611Combined sources16
Turni612 – 614Combined sources3
Beta strandi618 – 625Combined sources8
Helixi627 – 633Combined sources7
Beta strandi639 – 643Combined sources5
Beta strandi645 – 654Combined sources10
Helixi655 – 658Combined sources4
Helixi660 – 666Combined sources7
Turni667 – 669Combined sources3
Beta strandi672 – 675Combined sources4
Helixi685 – 687Combined sources3
Turni688 – 690Combined sources3
Helixi691 – 701Combined sources11
Beta strandi702 – 704Combined sources3
Beta strandi715 – 717Combined sources3
Helixi719 – 721Combined sources3
Beta strandi722 – 724Combined sources3
Helixi725 – 728Combined sources4
Helixi732 – 740Combined sources9
Helixi745 – 749Combined sources5
Beta strandi757 – 764Combined sources8
Helixi768 – 774Combined sources7
Beta strandi779 – 782Combined sources4
Helixi792 – 804Combined sources13
Turni805 – 807Combined sources3
Helixi812 – 815Combined sources4
Helixi831 – 833Combined sources3
Helixi847 – 849Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MY0X-ray2.94A/B/C/D2-852[»]
5MY2X-ray2.70A/B/C/D2-852[»]
ProteinModelPortaliP19096
SMRiP19096
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2112 – 2192CarrierPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 414Beta-ketoacyl synthaseAdd BLAST414
Regioni429 – 817Acyl and malonyl transferasesAdd BLAST389
Regioni1628 – 1856Enoyl reductaseAdd BLAST229
Regioni1857 – 2111Beta-ketoacyl reductaseAdd BLAST255
Regioni2201 – 2504ThioesteraseAdd BLAST304

Phylogenomic databases

eggNOGiKOG1202 Eukaryota
COG3321 LUCA
GeneTreeiENSGT00530000063309
HOGENOMiHOG000019642
HOVERGENiHBG005640
InParanoidiP19096
KOiK00665
OMAiDVNKPKY
OrthoDBiEOG091G003K
PhylomeDBiP19096
TreeFamiTF300549

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
1.10.1470.20, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 2 hits
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR001227 Ac_transferase_dom_sf
IPR036736 ACP-like_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR013149 ADH_C
IPR023102 Fatty_acid_synthase_dom_2
IPR011032 GroES-like_sf
IPR032821 KAsynt_C_assoc
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR016036 Malonyl_transacylase_ACP-bd
IPR013217 Methyltransf_12
IPR036291 NAD(P)-bd_dom_sf
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
IPR020843 PKS_ER
IPR013968 PKS_KR
IPR020806 PKS_PP-bd
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
IPR029063 SAM-dependent_MTases
IPR001031 Thioesterase
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF00107 ADH_zinc_N, 1 hit
PF16197 KAsynt_C_assoc, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PF08659 KR, 1 hit
PF08242 Methyltransf_12, 1 hit
PF00550 PP-binding, 1 hit
PF14765 PS-DH, 1 hit
PF00975 Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827 PKS_AT, 1 hit
SM00826 PKS_DH, 1 hit
SM00829 PKS_ER, 1 hit
SM00825 PKS_KS, 1 hit
SM00823 PKS_PP, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 2 hits
SSF52151 SSF52151, 2 hits
SSF53335 SSF53335, 1 hit
SSF53474 SSF53474, 1 hit
SSF53901 SSF53901, 2 hits
SSF55048 SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 1 hit

Sequencei

Sequence statusi: Complete.

P19096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR
60 70 80 90 100
SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL
110 120 130 140 150
RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF
160 170 180 190 200
KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAALVGGINL LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR RVYATILNAG
260 270 280 290 300
TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG
310 320 330 340 350
DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH
360 370 380 390 400
GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV
410 420 430 440 450
HVILQPNTRQ APAPTAHAAL PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF
460 470 480 490 500
VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ EVQQVSTNKR PLWFICSGMG
510 520 530 540 550
TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS TDERTFDDIV
560 570 580 590 600
HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV
610 620 630 640 650
LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT
660 670 680 690 700
ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK
710 720 730 740 750
VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW
760 770 780 790 800
HIPEHAVVLE IAPHALLQAV LKRGVKSSCT IIPLMKRDHK DNLEFFLTNL
810 820 830 840 850
GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPVAEDF
860 870 880 890 900
PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA
910 920 930 940 950
RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG
960 970 980 990 1000
NLIVSGKVYL WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY
1010 1020 1030 1040 1050
DYGPQFQGIC EATLEGEQGK LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP
1060 1070 1080 1090 1100
TRVTAIYIDP ATHRQKVYRL KEDTQVADVT TSRCLGITVS GGIHISRLQT
1110 1120 1130 1140 1150
TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ LCKGLARALQ
1160 1170 1180 1190 1200
TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE
1210 1220 1230 1240 1250
RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR
1260 1270 1280 1290 1300
IPALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS
1310 1320 1330 1340 1350
SLGALDLLVC NCALATLGDP ALALDNMVAA LKEGGFLLVH TVLKGHALGE
1360 1370 1380 1390 1400
TLACLPSEVQ PAPSLLSQEE WESLFSRKAL HLVGLKRSFY GTALFLCRRA
1410 1420 1430 1440 1450
IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD CPTSGVVGLV
1460 1470 1480 1490 1500
NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR
1510 1520 1530 1540 1550
DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS
1560 1570 1580 1590 1600
SSGAQLCTVY YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD
1610 1620 1630 1640 1650
RCGRRVMGLV PAEGLATSVL LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY
1660 1670 1680 1690 1700
SLVVRGRIQR GETVLIHSGS GGVGQAAISI ALSLGCRVFT TVGSAEKRAY
1710 1720 1730 1740 1750
LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS LAEEKLQASV
1760 1770 1780 1790 1800
RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW
1810 1820 1830 1840 1850
REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR
1860 1870 1880 1890 1900
EEEPEAVLPG AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR
1910 1920 1930 1940 1950
GAQRLVLTSR SGIRTGYQAK HIREWRRQGI QVLVSTSNVS SLEGARALIA
1960 1970 1980 1990 2000
EATKLGPVGG VFNLAMVLRD AMLENQTPEL FQDVNKPKYN GTLNLDRATR
2010 2020 2030 2040 2050
EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ RRHDGLPGLA
2060 2070 2080 2090 2100
VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS
2110 2120 2130 2140 2150
SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS
2160 2170 2180 2190 2200
LMGVEVRQIL EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR
2210 2220 2230 2240 2250
SDTSLKQNQL NLSTLLVNPE GPTLTQLNSV QSSERPLFLV HPIEGSTTVF
2260 2270 2280 2290 2300
HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA YYIDCIKQVQ PEGPYRIAGY
2310 2320 2330 2340 2350
SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY TQSYRAKMTP
2360 2370 2380 2390 2400
GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS
2410 2420 2430 2440 2450
HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED
2460 2470 2480 2490 2500
LGADYNLSQV CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS

VREG
Length:2,504
Mass (Da):272,428
Last modified:October 11, 2004 - v2
Checksum:i2B48068B9D370C6F
GO

Sequence cautioni

The sequence CAA31525 differs from that shown. Reason: Frameshift at positions 1842, 1855, 1863, 1964 and 1967.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1992T → N in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2028G → C in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2045G → V in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2117T → N in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2175Q → R in CAA31525 (PubMed:2920037).Curated1
Sequence conflicti2295Y → H in CAA31525 (PubMed:2920037).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF127033 mRNA Translation: AAG02285.1
AL663090 Genomic DNA No translation available.
BC046513 mRNA Translation: AAH46513.1
BC059850 mRNA Translation: AAH59850.1
AK080374 mRNA Translation: BAC37895.1
X13135 mRNA Translation: CAA31525.1 Frameshift.
CCDSiCCDS25759.1
PIRiA32262
RefSeqiNP_032014.3, NM_007988.3
UniGeneiMm.236443

Genome annotation databases

EnsembliENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153
GeneIDi14104
KEGGimmu:14104
UCSCiuc007mut.1 mouse

Similar proteinsi

Entry informationi

Entry nameiFAS_MOUSE
AccessioniPrimary (citable) accession number: P19096
Secondary accession number(s): B1ATU8
, Q6PB72, Q8C4Z0, Q9EQR0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 11, 2004
Last modified: May 23, 2018
This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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