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Q24451

- MAN2_DROME

UniProt

Q24451 - MAN2_DROME

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Protein

Alpha-mannosidase 2

Gene

alpha-Man-II

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway By similarity.By similarity

Catalytic activityi

Hydrolysis of the terminal (1->3)- and (1->6)-linked alpha-D-mannose residues in the mannosyl-oligosaccharide Man5(GlcNAc)3.1 Publication

Cofactori

Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531ZincBy similarity
Metal bindingi155 – 1551ZincBy similarity
Active sitei267 – 2671NucleophileBy similarity
Metal bindingi267 – 2671ZincBy similarity
Metal bindingi534 – 5341ZincBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. mannosidase activity Source: FlyBase
  3. mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity Source: UniProtKB-EC
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. encapsulation of foreign target Source: FlyBase
  2. mannose metabolic process Source: InterPro
  3. protein deglycosylation Source: FlyBase
  4. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.2.1.114. 1994.
SABIO-RKQ24451.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase 2 (EC:3.2.1.114)
Alternative name(s):
Golgi alpha-mannosidase II
Short name:
AMan II
Short name:
Man II
Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase
Gene namesi
Name:alpha-Man-II
Synonyms:GmII
ORF Names:CG18802
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0011740. alpha-Man-II.

Subcellular locationi

Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: FlyBase
  2. Golgi stack Source: FlyBase
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11081108Alpha-mannosidase 2PRO_0000206906Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ24451.

Expressioni

Inductioni

Inhibited by swainsonine and by copper sulfate.1 Publication

Gene expression databases

BgeeiQ24451.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

BioGridi66291. 2 interactions.
DIPiDIP-22953N.
MINTiMINT-874970.

Structurei

Secondary structure

1
1108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi97 – 993
Beta strandi105 – 1073
Helixi108 – 1147
Beta strandi123 – 1253
Helixi135 – 1373
Beta strandi144 – 15310
Beta strandi156 – 1605
Helixi162 – 1687
Helixi170 – 18314
Beta strandi189 – 1913
Helixi194 – 20310
Helixi206 – 21712
Beta strandi220 – 2256
Beta strandi233 – 2353
Helixi238 – 25619
Beta strandi262 – 2654
Beta strandi268 – 2714
Helixi274 – 2807
Turni281 – 2833
Beta strandi286 – 2894
Helixi294 – 3029
Beta strandi306 – 3105
Beta strandi322 – 3265
Helixi334 – 3363
Beta strandi338 – 3403
Helixi342 – 3454
Helixi346 – 3483
Helixi350 – 3523
Turni371 – 3733
Helixi374 – 38916
Beta strandi392 – 40413
Helixi410 – 42920
Helixi431 – 4333
Beta strandi435 – 4395
Helixi442 – 45413
Beta strandi462 – 4654
Beta strandi471 – 4733
Helixi480 – 4823
Helixi486 – 50722
Helixi513 – 5153
Helixi517 – 53115
Turni534 – 5385
Helixi543 – 57129
Turni575 – 5773
Beta strandi586 – 5905
Beta strandi592 – 5954
Turni597 – 5993
Turni610 – 6123
Beta strandi613 – 62210
Beta strandi624 – 6263
Beta strandi628 – 63710
Beta strandi641 – 6455
Beta strandi653 – 66412
Turni665 – 6684
Beta strandi669 – 68719
Beta strandi691 – 6999
Beta strandi707 – 7093
Beta strandi711 – 7155
Beta strandi732 – 7343
Beta strandi739 – 7424
Beta strandi748 – 7514
Beta strandi757 – 7615
Beta strandi763 – 7664
Beta strandi769 – 77810
Beta strandi782 – 7843
Beta strandi794 – 7974
Beta strandi808 – 8125
Beta strandi817 – 8237
Beta strandi826 – 83611
Beta strandi838 – 8436
Beta strandi851 – 8599
Beta strandi866 – 8716
Turni872 – 8743
Beta strandi875 – 8806
Helixi887 – 8904
Beta strandi892 – 90110
Beta strandi903 – 91311
Beta strandi915 – 9184
Beta strandi924 – 93310
Beta strandi938 – 9403
Beta strandi951 – 96111
Beta strandi973 – 9753
Helixi979 – 98911
Beta strandi993 – 9975
Beta strandi1007 – 10093
Beta strandi1020 – 10278
Beta strandi1034 – 104411
Helixi1062 – 10643
Beta strandi1065 – 107511
Beta strandi1081 – 10855
Helixi1087 – 10893
Beta strandi1099 – 11079

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HTYX-ray1.40A94-1108[»]
1HWWX-ray1.87A94-1108[»]
1HXKX-ray1.50A94-1108[»]
1PS3X-ray1.80A64-1108[»]
1QWNX-ray1.20A76-1108[»]
1QWUX-ray2.03A76-1108[»]
1QX1X-ray1.30A76-1108[»]
1R33X-ray1.80A76-1108[»]
1R34X-ray1.95A76-1108[»]
1TQSX-ray1.30A76-1108[»]
1TQTX-ray1.90A76-1108[»]
1TQUX-ray2.03A76-1108[»]
1TQVX-ray2.03A76-1108[»]
1TQWX-ray1.20A76-1108[»]
2ALWX-ray1.86A76-1108[»]
2F18X-ray1.30A76-1108[»]
2F1AX-ray1.45A76-1108[»]
2F1BX-ray1.45A76-1108[»]
2F7OX-ray1.43A76-1108[»]
2F7PX-ray1.28A76-1108[»]
2F7QX-ray1.85A76-1108[»]
2F7RX-ray1.35A76-1108[»]
2FYVX-ray1.90A76-1108[»]
2OW6X-ray1.19A76-1108[»]
2OW7X-ray1.77A76-1108[»]
3BLBX-ray1.30A76-1108[»]
3BUBX-ray1.38A76-1108[»]
3BUDX-ray1.85A76-1108[»]
3BUIX-ray1.25A76-1108[»]
3BUPX-ray2.03A76-1108[»]
3BUQX-ray2.01A76-1108[»]
3BVTX-ray1.30A76-1108[»]
3BVUX-ray1.12A76-1108[»]
3BVVX-ray1.30A76-1108[»]
3BVWX-ray1.20A76-1108[»]
3BVXX-ray1.10A76-1108[»]
3CV5X-ray1.60A76-1108[»]
3CZNX-ray1.40A76-1108[»]
3CZSX-ray1.30A76-1108[»]
3D4YX-ray1.52A76-1108[»]
3D4ZX-ray1.39A76-1108[»]
3D50X-ray1.79A76-1108[»]
3D51X-ray1.43A76-1108[»]
3D52X-ray1.60A76-1108[»]
3DDFX-ray1.20A76-1108[»]
3DDGX-ray1.74A76-1108[»]
3DX0X-ray1.70A76-1108[»]
3DX1X-ray1.21A76-1108[»]
3DX2X-ray1.40A76-1108[»]
3DX3X-ray1.42A76-1108[»]
3DX4X-ray1.38A76-1108[»]
3EJPX-ray1.32A76-1108[»]
3EJQX-ray1.45A76-1108[»]
3EJRX-ray1.27A76-1108[»]
3EJSX-ray1.35A76-1108[»]
3EJTX-ray1.35A76-1108[»]
3EJUX-ray1.32A76-1108[»]
ProteinModelPortaliQ24451.
SMRiQ24451. Positions 93-1108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ24451.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Topological domaini31 – 11081078LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00510000046304.
InParanoidiQ24451.
KOiK01231.
OMAiNTEIVMR.
OrthoDBiEOG7JQBMJ.
PhylomeDBiQ24451.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Q24451-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRIRRRFAL VICSGCLLVF LSLYIILNFA APAATQIKPN YENIENKLHE
60 70 80 90 100
LENGLQEHGE EMRNLRARLA ETSNRDDPIR PPLKVARSPR PGQCQDVVQD
110 120 130 140 150
VPNVDVQMLE LYDRMSFKDI DGGVWKQGWN IKYDPLKYNA HHKLKVFVVP
160 170 180 190 200
HSHNDPGWIQ TFEEYYQHDT KHILSNALRH LHDNPEMKFI WAEISYFARF
210 220 230 240 250
YHDLGENKKL QMKSIVKNGQ LEFVTGGWVM PDEANSHWRN VLLQLTEGQT
260 270 280 290 300
WLKQFMNVTP TASWAIDPFG HSPTMPYILQ KSGFKNMLIQ RTHYSVKKEL
310 320 330 340 350
AQQRQLEFLW RQIWDNKGDT ALFTHMMPFY SYDIPHTCGP DPKVCCQFDF
360 370 380 390 400
KRMGSFGLSC PWKVPPRTIS DQNVAARSDL LVDQWKKKAE LYRTNVLLIP
410 420 430 440 450
LGDDFRFKQN TEWDVQRVNY ERLFEHINSQ AHFNVQAQFG TLQEYFDAVH
460 470 480 490 500
QAERAGQAEF PTLSGDFFTY ADRSDNYWSG YYTSRPYHKR MDRVLMHYVR
510 520 530 540 550
AAEMLSAWHS WDGMARIEER LEQARRELSL FQHHDGITGT AKTHVVVDYE
560 570 580 590 600
QRMQEALKAC QMVMQQSVYR LLTKPSIYSP DFSFSYFTLD DSRWPGSGVE
610 620 630 640 650
DSRTTIILGE DILPSKHVVM HNTLPHWREQ LVDFYVSSPF VSVTDLANNP
660 670 680 690 700
VEAQVSPVWS WHHDTLTKTI HPQGSTTKYR IIFKARVPPM GLATYVLTIS
710 720 730 740 750
DSKPEHTSYA SNLLLRKNPT SLPLGQYPED VKFGDPREIS LRVGNGPTLA
760 770 780 790 800
FSEQGLLKSI QLTQDSPHVP VHFKFLKYGV RSHGDRSGAY LFLPNGPASP
810 820 830 840 850
VELGQPVVLV TKGKLESSVS VGLPSVVHQT IMRGGAPEIR NLVDIGSLDN
860 870 880 890 900
TEIVMRLETH IDSGDIFYTD LNGLQFIKRR RLDKLPLQAN YYPIPSGMFI
910 920 930 940 950
EDANTRLTLL TGQPLGGSSL ASGELEIMQD RRLASDDERG LGQGVLDNKP
960 970 980 990 1000
VLHIYRLVLE KVNNCVRPSE LHPAGYLTSA AHKASQSLLD PLDKFIFAEN
1010 1020 1030 1040 1050
EWIGAQGQFG GDHPSAREDL DVSVMRRLTK SSAKTQRVGY VLHRTNLMQC
1060 1070 1080 1090 1100
GTPEEHTQKL DVCHLLPNVA RCERTTLTFL QNLEHLDGMV APEVCPMETA

AYVSSHSS
Length:1,108
Mass (Da):126,721
Last modified:June 16, 2003 - v2
Checksum:i55E370EC8CAC6D4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711E → K in CAA54732. (PubMed:7890162)Curated
Sequence conflicti305 – 3062QL → HV in CAA10755. (PubMed:10504337)Curated
Sequence conflicti397 – 3971L → V in CAA10755. (PubMed:10504337)Curated
Sequence conflicti970 – 9701E → K in CAA54732. (PubMed:7890162)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77652 mRNA. Translation: CAA54732.1.
AJ132715 Genomic DNA. Translation: CAA10755.1.
AE014297 Genomic DNA. Translation: AAF54375.1.
AY119464 mRNA. Translation: AAM50118.1.
PIRiJC4037.
RefSeqiNP_524291.2. NM_079567.3.
UniGeneiDm.2459.

Genome annotation databases

EnsemblMetazoaiFBtr0082031; FBpp0081509; FBgn0011740.
GeneIDi41126.
KEGGidme:Dmel_CG18802.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X77652 mRNA. Translation: CAA54732.1 .
AJ132715 Genomic DNA. Translation: CAA10755.1 .
AE014297 Genomic DNA. Translation: AAF54375.1 .
AY119464 mRNA. Translation: AAM50118.1 .
PIRi JC4037.
RefSeqi NP_524291.2. NM_079567.3.
UniGenei Dm.2459.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HTY X-ray 1.40 A 94-1108 [» ]
1HWW X-ray 1.87 A 94-1108 [» ]
1HXK X-ray 1.50 A 94-1108 [» ]
1PS3 X-ray 1.80 A 64-1108 [» ]
1QWN X-ray 1.20 A 76-1108 [» ]
1QWU X-ray 2.03 A 76-1108 [» ]
1QX1 X-ray 1.30 A 76-1108 [» ]
1R33 X-ray 1.80 A 76-1108 [» ]
1R34 X-ray 1.95 A 76-1108 [» ]
1TQS X-ray 1.30 A 76-1108 [» ]
1TQT X-ray 1.90 A 76-1108 [» ]
1TQU X-ray 2.03 A 76-1108 [» ]
1TQV X-ray 2.03 A 76-1108 [» ]
1TQW X-ray 1.20 A 76-1108 [» ]
2ALW X-ray 1.86 A 76-1108 [» ]
2F18 X-ray 1.30 A 76-1108 [» ]
2F1A X-ray 1.45 A 76-1108 [» ]
2F1B X-ray 1.45 A 76-1108 [» ]
2F7O X-ray 1.43 A 76-1108 [» ]
2F7P X-ray 1.28 A 76-1108 [» ]
2F7Q X-ray 1.85 A 76-1108 [» ]
2F7R X-ray 1.35 A 76-1108 [» ]
2FYV X-ray 1.90 A 76-1108 [» ]
2OW6 X-ray 1.19 A 76-1108 [» ]
2OW7 X-ray 1.77 A 76-1108 [» ]
3BLB X-ray 1.30 A 76-1108 [» ]
3BUB X-ray 1.38 A 76-1108 [» ]
3BUD X-ray 1.85 A 76-1108 [» ]
3BUI X-ray 1.25 A 76-1108 [» ]
3BUP X-ray 2.03 A 76-1108 [» ]
3BUQ X-ray 2.01 A 76-1108 [» ]
3BVT X-ray 1.30 A 76-1108 [» ]
3BVU X-ray 1.12 A 76-1108 [» ]
3BVV X-ray 1.30 A 76-1108 [» ]
3BVW X-ray 1.20 A 76-1108 [» ]
3BVX X-ray 1.10 A 76-1108 [» ]
3CV5 X-ray 1.60 A 76-1108 [» ]
3CZN X-ray 1.40 A 76-1108 [» ]
3CZS X-ray 1.30 A 76-1108 [» ]
3D4Y X-ray 1.52 A 76-1108 [» ]
3D4Z X-ray 1.39 A 76-1108 [» ]
3D50 X-ray 1.79 A 76-1108 [» ]
3D51 X-ray 1.43 A 76-1108 [» ]
3D52 X-ray 1.60 A 76-1108 [» ]
3DDF X-ray 1.20 A 76-1108 [» ]
3DDG X-ray 1.74 A 76-1108 [» ]
3DX0 X-ray 1.70 A 76-1108 [» ]
3DX1 X-ray 1.21 A 76-1108 [» ]
3DX2 X-ray 1.40 A 76-1108 [» ]
3DX3 X-ray 1.42 A 76-1108 [» ]
3DX4 X-ray 1.38 A 76-1108 [» ]
3EJP X-ray 1.32 A 76-1108 [» ]
3EJQ X-ray 1.45 A 76-1108 [» ]
3EJR X-ray 1.27 A 76-1108 [» ]
3EJS X-ray 1.35 A 76-1108 [» ]
3EJT X-ray 1.35 A 76-1108 [» ]
3EJU X-ray 1.32 A 76-1108 [» ]
ProteinModelPortali Q24451.
SMRi Q24451. Positions 93-1108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66291. 2 interactions.
DIPi DIP-22953N.
MINTi MINT-874970.

Chemistry

BindingDBi Q24451.

Protein family/group databases

CAZyi GH38. Glycoside Hydrolase Family 38.

Proteomic databases

PaxDbi Q24451.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082031 ; FBpp0081509 ; FBgn0011740 .
GeneIDi 41126.
KEGGi dme:Dmel_CG18802.

Organism-specific databases

CTDi 41126.
FlyBasei FBgn0011740. alpha-Man-II.

Phylogenomic databases

eggNOGi COG0383.
GeneTreei ENSGT00510000046304.
InParanoidi Q24451.
KOi K01231.
OMAi NTEIVMR.
OrthoDBi EOG7JQBMJ.
PhylomeDBi Q24451.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 3.2.1.114. 1994.
SABIO-RK Q24451.

Miscellaneous databases

ChiTaRSi alpha-Man-II. drosophila.
EvolutionaryTracei Q24451.
GenomeRNAii 41126.
NextBioi 822320.
PROi Q24451.

Gene expression databases

Bgeei Q24451.

Family and domain databases

Gene3Di 1.20.1270.50. 1 hit.
2.60.40.1180. 1 hit.
3.20.110.10. 1 hit.
InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013780. Glyco_hydro_13_b.
IPR027291. Glyco_hydro_38/57_N.
IPR011682. Glyco_hydro_38_C.
IPR015341. Glyco_hydro_38_cen.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view ]
Pfami PF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view ]
SMARTi SM00872. Alpha-mann_mid. 1 hit.
[Graphical view ]
SUPFAMi SSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of GmII, a Drosophila melanogaster homologue of the cDNA encoding murine Golgi alpha-mannosidase II."
    Foster J.M., Yudkin B., Lockyer A.E., Roberts D.B.
    Gene 154:183-186(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The Drosophila GMII gene encodes a Golgi alpha-mannosidase II."
    Rabouille C., Kuntz D.A., Lockyer A.E., Watson R., Signorelli T., Rose D.R., van den Heuvel M., Roberts D.B.
    J. Cell Sci. 112:3319-3330(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiMAN2_DROME
AccessioniPrimary (citable) accession number: Q24451
Secondary accession number(s): Q9TYG5, Q9VHD8, Q9VHD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 16, 2003
Last modified: October 29, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3