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Q9FHN6

- SKS2_ARATH

UniProt

Q9FHN6 - SKS2_ARATH

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Protein

Monocopper oxidase-like protein SKS2

Gene

SKS2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Cofactori

Cu cationCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi455 – 4551Copper 2; type 2By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-2300-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Monocopper oxidase-like protein SKS2
Gene namesi
Name:SKS2
Ordered Locus Names:At5g51480
ORF Names:K17N15.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G51480.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: TAIR
  2. anchored component of plasma membrane Source: TAIR
  3. plasma membrane Source: TAIR
  4. plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 564541Monocopper oxidase-like protein SKS2PRO_0000251281Add
BLAST
Propeptidei565 – 59228Removed in mature formSequence AnalysisPRO_0000251282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Lipidationi564 – 5641GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9FHN6.
PRIDEiQ9FHN6.

Expressioni

Gene expression databases

GenevestigatoriQ9FHN6.

Interactioni

Protein-protein interaction databases

IntActiQ9FHN6. 1 interaction.
STRINGi3702.AT5G51480.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9FHN6.
SMRiQ9FHN6. Positions 30-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000241637.
InParanoidiQ9FHN6.
OMAiNGSTEMD.
PhylomeDBiQ9FHN6.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FHN6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAATDFFFAF VFSFALIFGF SFAGDPYVSY DFTLSYITAS PLGVPQQVIA
60 70 80 90 100
VNGKFPGPVI NATTNYNVHV NVLNHLDEPL LLTWPGVQMR RNSWQDGVLG
110 120 130 140 150
TNCPIPPNWN FTYDFQLKDQ IGSYFYSPSL NFQRASGGFG ALIINNRDLV
160 170 180 190 200
PIPFTEPDGE IIFIIGDWYT QNHTALRRIL DSGKELGMPD GVLINGKGPF
210 220 230 240 250
KYNSSVPDGI EHETVNVDPG KTYRIRVHNV GISTSLNFRI QNHKLLLIET
260 270 280 290 300
EGRYTSQMNF TDFDVHVGQS YSFLVTMDQN ATSDYYIVAS ARFVNETVWQ
310 320 330 340 350
RVTGVGILHY SNSKGPASGP LPVSATDVNH PWSAMNQPRA IKQNTSASGA
360 370 380 390 400
RPNPQGSFHY GQINITRTYI LRSLPPTKIN GKLRATLNGI SFVNPSTPMR
410 420 430 440 450
LADDHKVKGD YMLDFPDRPL DEKLPRLSSS IINATYKGFI QVIFQNNDTK
460 470 480 490 500
IQSFHIDGYA FYVVAMDFGI WSEDRNSSYN NWDAVARSTV EVYPGAWTAV
510 520 530 540 550
LISLDNVGVW NIRVENLDRW YLGQETYMRI INPEENGSTE MDPPENVMYC
560 570 580 590
GALQAMQKEQ HHSSATKSMT NGQLILIFSM MMVLLSSFSS FC
Length:592
Mass (Da):66,407
Last modified:March 1, 2001 - v1
Checksum:i7F833E2E7CEEF602
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018109 Genomic DNA. Translation: BAB08664.1.
CP002688 Genomic DNA. Translation: AED96089.1.
BT004990 mRNA. Translation: AAO50523.1.
BT004129 mRNA. Translation: AAO42151.1.
RefSeqiNP_199961.1. NM_124527.4.
UniGeneiAt.29677.

Genome annotation databases

EnsemblPlantsiAT5G51480.1; AT5G51480.1; AT5G51480.
GeneIDi835222.
KEGGiath:AT5G51480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018109 Genomic DNA. Translation: BAB08664.1 .
CP002688 Genomic DNA. Translation: AED96089.1 .
BT004990 mRNA. Translation: AAO50523.1 .
BT004129 mRNA. Translation: AAO42151.1 .
RefSeqi NP_199961.1. NM_124527.4.
UniGenei At.29677.

3D structure databases

ProteinModelPortali Q9FHN6.
SMRi Q9FHN6. Positions 30-510.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9FHN6. 1 interaction.
STRINGi 3702.AT5G51480.1-P.

Proteomic databases

PaxDbi Q9FHN6.
PRIDEi Q9FHN6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G51480.1 ; AT5G51480.1 ; AT5G51480 .
GeneIDi 835222.
KEGGi ath:AT5G51480.

Organism-specific databases

TAIRi AT5G51480.

Phylogenomic databases

eggNOGi COG2132.
HOGENOMi HOG000241637.
InParanoidi Q9FHN6.
OMAi NGSTEMD.
PhylomeDBi Q9FHN6.

Enzyme and pathway databases

BioCyci ARA:GQT-2300-MONOMER.

Gene expression databases

Genevestigatori Q9FHN6.

Family and domain databases

Gene3Di 2.60.40.420. 3 hits.
InterProi IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
    Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
    Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
  5. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
    Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
    J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSKS2_ARATH
AccessioniPrimary (citable) accession number: Q9FHN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3