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Protein

Receptor protein kinase TMK1

Gene

TMK1

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

Functioni

Transmembrane kinase receptor (PubMed:1332795). Phosphorylates only serine and threonine residues (PubMed:8224199). Involved in auxin signal transduction and cell expansion and proliferation regulation (PubMed:23613767). Forms with ABP1 a cell surface auxin perception complex that activates ROP signaling pathways (PubMed:24578577). Required for auxin promotion of pavement cell interdigitation (PubMed:24578577). Auxin promotes the formation of the ABP1-TMK1 protein complex (PubMed:24578577).1 Publication3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei616 – 6161ATPPROSITE-ProRule annotation
Active sitei717 – 7171Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi594 – 6029ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • transmembrane receptor protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • signal transduction Source: TAIR
  • transmembrane receptor protein serine/threonine kinase signaling pathway Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G66150-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor protein kinase TMK11 Publication (EC:2.7.11.11 Publication)
Alternative name(s):
BARK1-like kinase 11 Publication
Transmembrane kinase 11 Publication
Gene namesi
Name:TMK11 Publication
Synonyms:BLK11 Publication
Ordered Locus Names:At1g66150Imported
ORF Names:F15E12.4Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G66150.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 482459ExtracellularSequence analysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence analysisAdd
BLAST
Topological domaini504 – 942439CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular region Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype (PubMed:23613767). Tmk1 and tmk2 double mutants, tmk1 and tmk3 double mutants and tmk1, tmk2 and tmk3 triple mutants have no visible phenotypes (PubMed:23613767). Tmk1 and tmk4 double mutants, tmk1, tmk2 and tmk4 triple mutants and tmk1, tmk3 and tmk4 triple mutants have a severe reduction in organ size, a substantial delay in growth and development, and a decrease in fertility (PubMed:23613767). Tmk1, tmk2, tmk3 and tmk4 quadruple mutants are embryo lethal (PubMed:23613767, PubMed:24578577).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 942919Receptor protein kinase TMK1PRO_0000024388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 601 Publication
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)1 Publication
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)1 Publication
Disulfide bondi314 ↔ 3211 Publication
Disulfide bondi351 ↔ 3591 Publication
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Autophosphorylated on serine and threonine residues.1 Publication
Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP43298.
PRIDEiP43298.

PTM databases

iPTMnetiP43298.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, siliques and flowers.2 Publications

Gene expression databases

GenevisibleiP43298. AT.

Interactioni

Subunit structurei

Interacts (via extracellular domain) with ABP1.1 Publication

Protein-protein interaction databases

BioGridi28151. 3 interactions.
DIPiDIP-46512N.
IntActiP43298. 2 interactions.
MINTiMINT-8063714.
STRINGi3702.AT1G66150.1.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HQ1X-ray1.55A1-469[»]
ProteinModelPortaliP43298.
SMRiP43298. Positions 24-447, 575-873.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati63 – 8725LRR 1CuratedAdd
BLAST
Repeati88 – 11023LRR 2CuratedAdd
BLAST
Repeati111 – 13323LRR 3CuratedAdd
BLAST
Repeati135 – 15925LRR 4CuratedAdd
BLAST
Repeati161 – 18222LRR 5CuratedAdd
BLAST
Repeati185 – 20925LRR 6CuratedAdd
BLAST
Repeati211 – 23121LRR 7CuratedAdd
BLAST
Repeati232 – 25322LRR 8CuratedAdd
BLAST
Repeati254 – 27825LRR 9CuratedAdd
BLAST
Repeati280 – 30021LRR 10CuratedAdd
BLAST
Repeati361 – 38424LRR 11CuratedAdd
BLAST
Repeati385 – 40824LRR 12CuratedAdd
BLAST
Repeati409 – 43628LRR 13CuratedAdd
BLAST
Domaini588 – 869282Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi448 – 46417Ser-richPROSITE-ProRule annotationAdd
BLAST

Domaini

The leucine-rich repeat (LRR) domain is disrupted by a non-LRR region, resulting in the formation of two LRR solenoid structures shaped like the Arabic number "7". This is strikingly different from the horseshoe structures of the canonical LRR proteins.1 Publication

Sequence similaritiesi

Contains 13 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IIW7. Eukaryota.
ENOG41102Z7. LUCA.
HOGENOMiHOG000240631.
InParanoidiP43298.
KOiK00924.
OMAiCKWTHIV.
PhylomeDBiP43298.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
3.80.10.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 5 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 7 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRRTFLLF SFTFLLLLSL SKADSDGDLS AMLSLKKSLN PPSSFGWSDP
60 70 80 90 100
DPCKWTHIVC TGTKRVTRIQ IGHSGLQGTL SPDLRNLSEL ERLELQWNNI
110 120 130 140 150
SGPVPSLSGL ASLQVLMLSN NNFDSIPSDV FQGLTSLQSV EIDNNPFKSW
160 170 180 190 200
EIPESLRNAS ALQNFSANSA NVSGSLPGFL GPDEFPGLSI LHLAFNNLEG
210 220 230 240 250
ELPMSLAGSQ VQSLWLNGQK LTGDITVLQN MTGLKEVWLH SNKFSGPLPD
260 270 280 290 300
FSGLKELESL SLRDNSFTGP VPASLLSLES LKVVNLTNNH LQGPVPVFKS
310 320 330 340 350
SVSVDLDKDS NSFCLSSPGE CDPRVKSLLL IASSFDYPPR LAESWKGNDP
360 370 380 390 400
CTNWIGIACS NGNITVISLE KMELTGTISP EFGAIKSLQR IILGINNLTG
410 420 430 440 450
MIPQELTTLP NLKTLDVSSN KLFGKVPGFR SNVVVNTNGN PDIGKDKSSL
460 470 480 490 500
SSPGSSSPSG GSGSGINGDK DRRGMKSSTF IGIIVGSVLG GLLSIFLIGL
510 520 530 540 550
LVFCWYKKRQ KRFSGSESSN AVVVHPRHSG SDNESVKITV AGSSVSVGGI
560 570 580 590 600
SDTYTLPGTS EVGDNIQMVE AGNMLISIQV LRSVTNNFSS DNILGSGGFG
610 620 630 640 650
VVYKGELHDG TKIAVKRMEN GVIAGKGFAE FKSEIAVLTK VRHRHLVTLL
660 670 680 690 700
GYCLDGNEKL LVYEYMPQGT LSRHLFEWSE EGLKPLLWKQ RLTLALDVAR
710 720 730 740 750
GVEYLHGLAH QSFIHRDLKP SNILLGDDMR AKVADFGLVR LAPEGKGSIE
760 770 780 790 800
TRIAGTFGYL APEYAVTGRV TTKVDVYSFG VILMELITGR KSLDESQPEE
810 820 830 840 850
SIHLVSWFKR MYINKEASFK KAIDTTIDLD EETLASVHTV AELAGHCCAR
860 870 880 890 900
EPYQRPDMGH AVNILSSLVE LWKPSDQNPE DIYGIDLDMS LPQALKKWQA
910 920 930 940
YEGRSDLESS TSSLLPSLDN TQMSIPTRPY GFAESFTSVD GR
Length:942
Mass (Da):102,388
Last modified:November 1, 1995 - v1
Checksum:i93E300B52FF549DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti849 – 8491A → S in BAF00566 (PubMed:11130712).Curated
Sequence conflicti849 – 8491A → S in AAP04161 (PubMed:14593172).Curated
Sequence conflicti905 – 9051S → G in ACN59264 (PubMed:20064227).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00670 Genomic DNA. Translation: AAA32876.1.
FJ708669 mRNA. Translation: ACN59264.1.
AC026480 Genomic DNA. Translation: AAG51302.1.
CP002684 Genomic DNA. Translation: AEE34468.1.
BT006178 mRNA. Translation: AAP04161.1.
AK228659 mRNA. Translation: BAF00566.1.
PIRiJQ1674.
RefSeqiNP_176789.1. NM_105286.3.
UniGeneiAt.28076.

Genome annotation databases

EnsemblPlantsiAT1G66150.1; AT1G66150.1; AT1G66150.
GeneIDi842930.
GrameneiAT1G66150.1; AT1G66150.1; AT1G66150.
KEGGiath:AT1G66150.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00670 Genomic DNA. Translation: AAA32876.1.
FJ708669 mRNA. Translation: ACN59264.1.
AC026480 Genomic DNA. Translation: AAG51302.1.
CP002684 Genomic DNA. Translation: AEE34468.1.
BT006178 mRNA. Translation: AAP04161.1.
AK228659 mRNA. Translation: BAF00566.1.
PIRiJQ1674.
RefSeqiNP_176789.1. NM_105286.3.
UniGeneiAt.28076.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HQ1X-ray1.55A1-469[»]
ProteinModelPortaliP43298.
SMRiP43298. Positions 24-447, 575-873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi28151. 3 interactions.
DIPiDIP-46512N.
IntActiP43298. 2 interactions.
MINTiMINT-8063714.
STRINGi3702.AT1G66150.1.

PTM databases

iPTMnetiP43298.

Proteomic databases

PaxDbiP43298.
PRIDEiP43298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G66150.1; AT1G66150.1; AT1G66150.
GeneIDi842930.
GrameneiAT1G66150.1; AT1G66150.1; AT1G66150.
KEGGiath:AT1G66150.

Organism-specific databases

TAIRiAT1G66150.

Phylogenomic databases

eggNOGiENOG410IIW7. Eukaryota.
ENOG41102Z7. LUCA.
HOGENOMiHOG000240631.
InParanoidiP43298.
KOiK00924.
OMAiCKWTHIV.
PhylomeDBiP43298.

Enzyme and pathway databases

BioCyciARA:AT1G66150-MONOMER.

Miscellaneous databases

PROiP43298.

Gene expression databases

GenevisibleiP43298. AT.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
3.80.10.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 5 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 7 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase."
    Chang C., Schaller G.E., Patterson S.E., Kwok S.F., Meyerowitz E.M., Bleecker A.B.
    Plant Cell 4:1263-1271(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
    Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
    BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "Receptor-like kinase activity in membranes of Arabidopsis thaliana."
    Schaller G.E., Bleecker A.B.
    FEBS Lett. 333:306-310(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION.
  8. "Using mutant alleles to determine the structure and function of leucine-rich repeat receptor-like kinases."
    Dievart A., Clark S.E.
    Curr. Opin. Plant Biol. 6:507-516(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  9. "The TMK subfamily of receptor-like kinases in Arabidopsis display an essential role in growth and a reduced sensitivity to auxin."
    Dai N., Wang W., Patterson S.E., Bleecker A.B.
    PLoS ONE 8:E60990-E60990(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE FAMILY, NOMENCLATURE.
  10. "Identification of Arabidopsis BAK1-associating receptor-like kinase 1 (BARK1) and characterization of its gene expression and brassinosteroid-regulated root phenotypes."
    Kim M.H., Kim Y., Kim J.W., Lee H.S., Lee W.S., Kim S.K., Wang Z.Y., Kim S.H.
    Plant Cell Physiol. 54:1620-1634(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  11. Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH ABP1.
  12. "Crystal structure of an LRR protein with two solenoids."
    Liu P., Hu Z., Zhou B., Liu S., Chai J.
    Cell Res. 23:303-305(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-469, GLYCOSYLATION AT ASN-158 AND ASN-285, DISULFIDE BOND, DOMAIN.

Entry informationi

Entry nameiTMK1_ARATH
AccessioniPrimary (citable) accession number: P43298
Secondary accession number(s): C0LGH9, Q84R13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 139 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.