wanglab/gogpt-training-data huggingface dataset:
Protein: Homeodomain-like superfamily protein (Q9SIZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- F18C1.6 protein
- Zinc knuckle
- Sequence-specific DNA binding transcription factor
- Eukaryotic translation initiation factor 5B
- Trihelix transcription factor ASR3
- Alpha/beta-Hydrolases superfamily protein
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- At2g32500
- Enoyl-CoA hydratase 2, peroxisomal
Sequence:
MRSSSQNSENSKTCLSNNIKATTKNEEDKDEEDDEEGEEDEEERSGDQSPSSNSYEEESGSHHHDQNKKNGGSVRPYNRSKTPRLRWTPELHICFLQAVERLGGPDRATPKLVLQLMNVKGLSIAHVKSHLQMYRSKKTDEPNEGDQGFSFEHGAGYTYNLSQLPMLQSFDQRPSSSLGYGGGSWTDHRRQIYRSPWRGLTTRENTRTRQTMFSSQPGERYHGVSNSILNDKNKTISFRINSHEGVHDNNGVAGAVPRIHRSFLEGMKTFNKSWGQSLSSNLKSSTATIPQDHIATTLNSYQWENAGVAEGSENVLKRKRLLFSDDCNKSDQDLDLSLSLKVPRTHDNLGECLLEDEVKEHDDHQDIKSLSLSLSSSGSSKLDRTIRKEDQTDHKKRKISVLASPLDLTL
Protein: Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR) (Q99N13)
Organism: Mus musculus (Mouse)
Function: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription, inhibits skeletal myogenesis and may be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:11390982, ECO:0000269|PubMed:15546868, ECO:0000269|PubMed:15711539}.
Interaction partners:
- Histone deacetylase 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Polyamine deacetylase HDAC10
- Protein deacetylase HDAC6
- Histone deacetylase 2
- Histone acetyltransferase KAT5
- Myocyte-specific enhancer factor 2B
- Myocyte-specific enhancer factor 2D
- Histone deacetylase 8
- Histone H2A.Z
Sequence:
MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSSIAASSSHVHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQVIGKDLAPGFVIKVII
Protein: DNA mismatch repair protein MutS (P23909)
Organism: Escherichia coli (strain K12)
Function: This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Interaction partners:
- DNA mismatch repair protein MutL
- Beta sliding clamp
- DNA polymerase I
- Flap endonuclease Xni
- Transcription-repair-coupling factor
- UvrABC system protein C
- DNA mismatch repair protein MutH
- Excinuclease cho
- UPF0758 protein YfjY
- UPF0758 protein YeeS
Sequence:
MSAIENFDAHTPMMQQYLRLKAQHPEILLFYRMGDFYELFYDDAKRASQLLDISLTKRGASAGEPIPMAGIPYHAVENYLAKLVNQGESVAICEQIGDPATSKGPVERKVVRIVTPGTISDEALLQERQDNLLAAIWQDSKGFGYATLDISSGRFRLSEPADRETMAAELQRTNPAELLYAEDFAEMSLIEGRRGLRRRPLWEFEIDTARQQLNLQFGTRDLVGFGVENAPRGLCAAGCLLQYAKDTQRTTLPHIRSITMEREQDSIIMDAATRRNLEITQNLAGGAENTLASVLDCTVTPMGSRMLKRWLHMPVRDTRVLLERQQTIGALQDFTAGLQPVLRQVGDLERILARLALRTARPRDLARMRHAFQQLPELRAQLETVDSAPVQALREKMGEFAELRDLLERAIIDTPPVLVRDGGVIASGYNEELDEWRALADGATDYLERLEVRERERTGLDTLKVGFNAVHGYYIQISRGQSHLAPINYMRRQTLKNAERYIIPELKEYEDKVLTSKGKALALEKQLYEELFDLLLPHLEALQQSASALAELDVLVNLAERAYTLNYTCPTFIDKPGIRITEGRHPVVEQVLNEPFIANPLNLSPQRRMLIITGPNMGGKSTYMRQTALIALMAYIGSYVPAQKVEIGPIDRIFTRVGAADDLASGRSTFMVEMTETANILHNATEYSLVLMDEIGRGTSTYDGLSLAWACAENLANKIKALTLFATHYFELTQLPEKMEGVANVHLDALEHGDTIAFMHSVQDGAASKSYGLAVAALAGVPKEVIKRARQKLRELESISPNAAATQVDGTQMSLLSVPEETSPAVEALENLDPDSLTPRQALEWIYRLKSLV
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Allergen Glb33) (Glyoxalase I) (Glx I) (Glyoxylase I 11) (OsGLYI-11) (OsGLYI11) (Ketone-aldehyde mutase) (Methylglyoxalase) (PP33) (S-D-lactoylglutathione methylglyoxal lyase) (allergen Ory s Glyoxalase I) (Q948T6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (By similarity). Involved in the detoxifiation of methylglyoxal. Can functionally complement growth defect of a yeast mutant lacking GLY I. Involved in abiotic stress response. Over-expression of GLYI-11 in tobacco increases tolerance to osmotic, oxidative and salt stresses.
Interaction partners:
- OSJNBb0004A17.4 protein
- hydroxyacylglutathione hydrolase
- hydroxyacylglutathione hydrolase
- tryptophan synthase
- Tryptophan synthase
- Threonine dehydratase
- Os11g0591550 protein
- Amine oxidase
- Amine oxidase
- Amine oxidase
Sequence:
MASGSEAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDVYKLAEKIKSSCCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ
Protein: Zinc finger HIT domain-containing protein 3 (HNF-4a coactivator) (Thyroid hormone receptor interactor 3) (Thyroid receptor-interacting protein 3) (TR-interacting protein 3) (TRIP-3) (Q15649)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28335020}. Nucleus {ECO:0000269|PubMed:28335020}.
Interaction partners:
- FMR1-interacting protein NUFIP1
- Box C/D snoRNA protein 1
- Nucleolar protein 58
- PIH1 domain-containing protein 1
- NHP2-like protein 1
- RuvB-like 1
- Nucleolar protein 56
Sequence:
MASLKCSTVVCVICLEKPKYRCPACRVPYCSVVCFRKHKEQCNPETRPVEKKIRSALPTKTVKPVENKDDDDSIADFLNSDEEEDRVSLQNLKNLGESATLRSLLLNPHLRQLMVNLDQGEDKAKLMRAYMQEPLFVEFADCCLGIVEPSQNEES
Protein: Dilute domain-containing protein SPAC25B8.08 (Q9UTB0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable allantoicase
Sequence:
MDQWSDNKDAIGMLSESLKEKVVTNEIAPALKEVKNHKYNFETEILNTGNVWNNDSKNGESGSAFGLDKIFQSSDSGNIAEGLELDLGNIMLETHNLESPAWKHADYDGVAASVNDNNNDWKFFVFDEREIDSMLQLFVRDFRADKPALRLAPSKLFYLASRFAFFYMPKEKELGTVLLNAFLCEVNQVTQQHPNDMVLCVQWLANVSLLLFYLKKDNKLDDLTVDIQNRCSELMNSLYITICQDAMRRMNENLEEGMVKYTGIQGLEDILRSRSWNLLRRRPTNDASTSPRSTPSASPRSITKIIASTLHLLEVFYIHPLIRAQCIEQLFSWLGARLFNIVISNKKYLSRAAAMETRFNISSLEEWSQTNSPKLQKPFDYPDEDLKVDLISKLLSLVQLLQWLQCLYRLSEDEDPRALQETLESLDALNPRQIYTAAKLYRPDITETKVSKTFLKKLDAFHEEKLREKINSSDKGDVSYEFELLKDETVFSPLKLPTKAQLINAYSYIVSGNGFNEDRKIVFQPHVSNILIDKLEENGLSMERAELPTSVFEDELQRREWRPDQEVEELLST
Protein: T-complex protein 1 subunit gamma (TCP-1-gamma) (CCT-gamma) (O74341)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- Probable T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta
- Phosducin-like protein C2A9.09
- 10 kDa heat shock protein, mitochondrial
- Elongation factor 1-gamma
Sequence:
MQSPVFVMNTNGNRQVGHKAQMSNIQAAKAVADVIRTCLGPRAMLKMLLDPVGSVLLTNDGHAILREIEVAHPAAKSMIELARTQDEEVGDGTTSVIILAGEILAAASPLLDRKIHPVVMIRSFKQALEDALSIIDEITLPVNVDDNAEMFRLIRTCIGTKLVARWSDLMCHLALRAVRTVASTSNGRMEIDIKRYARVEKVPGGEIESSCVLDGVMLNKDVTHPKMRRRIENPRIVLLDCPLEYRKGESQTNIEISKDTDWNRILEIEEEQVKRMCDYIIAVKPDLVITEKGVSDLAQHYLLKANITALRRTRKSDNNRIARACGANIVNRLEDLREKDVGTGCGLFYIDKLGDEYYTFLTGCKNPKACTILLRGPSKDIINEVERNLQDAMAVARNVFFHPKLSPGGGATEMAVSVRLAEKARSIEGVAQWPYRAVADAIEIIPRTLVQNCGANPIKALTELRAKHAEGQHSFGIDGETGRVVDMHEYGVWEPEAVKLQSIKTAIESACLLLRVDDIVSGVRKHSE
Protein: GTPase HRas (EC 3.6.5.2) (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed] (P01112)
Organism: Homo sapiens (Human)
Function: Involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20171}; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
Interaction partners:
- Ral guanine nucleotide dissociation stimulator
- Son of sevenless homolog 1
- RAF proto-oncogene serine/threonine-protein kinase
- Ras association domain-containing protein 5
- Serine/threonine-protein kinase B-raf
- Ras GTPase-activating protein 1
- Afadin
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Ras-specific guanine nucleotide-releasing factor 1
Sequence:
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS
Protein: Parvin alpha (E9PS97)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGCGALCPQVSELQEEGMNAINLPLSPIPFELDPEDTMLEENEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRH
Protein: Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) (UDP-MurNAc-pentapeptide phosphotransferase) (O66465)
Organism: Aquifex aeolicus (strain VF5)
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038}.
Interaction partners:
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Undecaprenyl-diphosphatase
- UDP-N-acetylmuramate--L-alanine ligase
- Penicillin binding protein 2
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Uncharacterized protein aq_054
- 4-hydroxybenzoate polyprenyltransferase
Sequence:
MLYQLALLLKDYWFAFNVLKYITFRSFTAVLIAFFLTLVLSPSFINRLRKIQRLFGGYVREYTPESHEVKKYTPTMGGIVILIVVTLSTLLLMRWDIKYTWVVLLSFLSFGTIGFWDDYVKLKNKKGISIKTKFLLQVLSASLISVLIYYWADIDTILYFPFFKELYVDLGVLYLPFAVFVIVGSANAVNLTDGLDGLAIGPAMTTATALGVVAYAVGHSKIAQYLNIPYVPYAGELTVFCFALVGAGLGFLWFNSFPAQMFMGDVGSLSIGASLATVALLTKSEFIFAVAAGVFVFETISVILQIIYFRWTGGKRLFKRAPFHHHLELNGLPEPKIVVRMWIISILLAIIAISMLKLR
Protein: SsrA-binding protein (Small protein B) (P0A832)
Organism: Escherichia coli (strain K12)
Function: Required for rescue of stalled ribosomes mediated by trans-translation. Binds to tmRNA RNA (also known as SsrA or 10Sa RNA, 363 nucleotides in this organism), required for stable binding of tmRNA to ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB (Probable). tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. Able to recruit charged tmRNA to ribosomes. Does not play a role in transcription, processing or Ala-aminoacylation of tmRNA. Other studies have shown it stimulates aminoacylation of tmRNA. May protect tmRNA from degradation. Binds to tmRNA that cannot be aminoacylated (tmRNA G3A), does not bind to tmRNA mutations near the tRNA-like termini (tmRNA G19C, A334U); other tmRNA mutations that block trans-translation still bind SmpB. With tmRNA may play a role in bacterial persistence. During trans-translation Ala-aminoacylated transfer-messenger RNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023, ECO:0000269|PubMed:11917023, ECO:0000269|PubMed:15069072}. Note=The tmRNA-SmpB complex associates with stalled ribosomes (PubMed:10393194, PubMed:11917023, PubMed:15699355, PubMed:20940705, PubMed:22622583). SmpB associates with ribosomes even in the absence of tmRNA (PubMed:15069072). {ECO:0000255|HAMAP-Rule:MF_00023, ECO:0000269|PubMed:10393194, ECO:0000269|PubMed:11917023, ECO:0000269|PubMed:15069072, ECO:0000269|PubMed:15699355, ECO:0000269|PubMed:20940705, ECO:0000269|PubMed:22622583}.
Interaction partners:
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL27
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL3
Sequence:
MTKKKAHKPGSATIALNKRARHEYFIEEEFEAGLALQGWEVKSLRAGKANISDSYVLLRDGEAFLFGANITPMAVASTHVVCDPTRTRKLLLNQRELDSLYGRVNREGYTVVALSLYWKNAWCKVKIGVAKGKKQHDKRSDIKEREWQVDKARIMKNAHR
Protein: adenylate cyclase (EC 4.6.1.1) (M9PEP2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- G protein alpha s subunit subunit alpha)
- Guanine nucleotide-binding protein G
- Bis
- RAC serine/threonine-protein kinase
- Inosine triphosphate pyrophosphatase
- IP06402p
- LD28489p
- GH08173p
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
Sequence:
MSESRRQSVSSRAMPPGVLVNDSRANSTDDIQIALAPHIQTYLSQTGRRHSCCSVMLPVAFERAAAKSWLDPKFDSPVLEEQYQASVFPHVRMRYRFTLSYILLCSLMWCLYFVVDGGSEDFWRPISSSFSMLSLVTIMALCFTHWDLYREHRTVTSAVTALLLCGASLAFLTYTGRAFSPLGHFAICLEIVLLIYTALPMPLWLGASTAISYSIAFEMVSHMVIGCSAIHGGPMHGGGGAAGGSGMEANGDPSNRILILRIMAHLSVHLVGVHVLIMNLVRMRGTFMKVGQNLLVRRQLEMEKQLKEKMIHSVMPPKVADMLLNEGGPSGLDAGGLPPESHYMRPRASNDVKSLFRPFHMHSMENVSILFADIVGFTRMSSTKTAEQLVEILNDLFERFDDLCSLSGCEKISTLGDCYYCVSGCPEPRADHAICCVEMGLGMIDAMRCFDAQRHEGVKMRVGVHTGTVLCGIVGTRRVKFDVWSNDVSLANKMESSGKPEQVHISQETSSFLGDAYYLEEGEEVFGHRTYFVVGRRRDFTRTNSLSPSMPANATGSSLLLPGAHGASLSQSATNVSAVQPNVPPASPVGQLSSSLNPSPVLSMRPRLTSLSMKMRKKSQSRDRDVERGIIHPAAAGIPPVIVVRERPKIIITTKSLPGSLDSDEQPPVSPPLLPPANPPAAETRSKIKLKVWKIPRFLKRFEDLTNRSSCGGSSSAGHLDKEREREREKEKEELHQHNQLNPEETLAFMDNQMQNGNGCGYQQLPVLVESNHRTQTLDIPAARPVLHHAATSTALASSVLRSPEAGVSGGGGCCSPGQYSMYDDIIDVRSYISQSRSDISPFGRSGSYRSQCGRQSTGGVNGAGPAGVGAEGRAGTSQTAPPVEQSPLPRPRASTLATGRPTPNSLEPGPSSTSPCCLPAPGNSVGGGGIFPPTHSRQSSICPSATSRKDSGIKSNSRRSSIQQQIYALNQTAISQHRVSGYFTSSTSSISNLGEVQGLGLPLAVQPPPPLLMPACSSQMADPLAACLQQLRKQSDLQLIRCVRDNARSQRSYLVKPPLRKFSLYFKSRQLERDFRSKAHRFGAENETEGPPTLATPRYNTYIDIFVGIAVYLCISVSLFLMTQNTVSPSFRLWVTLFSCFTGIQVFALFLFTRQMCRRQSGSNVSNRFRSKSTTSEDLERDERGAAPGGRPHFESCADRIFEAISSWYPWHICLAVLMAMPVLLIIANFLLLDLEQLEAFEYHYGFLIFVCIVHFCNFTQLNCWVRNVLAFLAALCFIGIAVSQLMVYSHNRSDQQQDQEASNFIQEIKWFQDYHVEIYLDLLLILVLVWFLNREFEIGYRLTFYGNAVANQDKVRVQNMKNQADMLLHNIIPKHVAEHLKNTAKYSENHHNIAIIFASIVNFNEMYDESYLGGKEFLRVLNELIGDFDELLSRPEFRAVEKIKTIGSTFMAASGLDPSHRGTGDEHIHTLMEFSIAMQEVVDAFNKDLLEFNLILRIGMNIGDVTAGVIGTSKLYYDIWGDAVNVASRMDSTGLPNRIQVGKDCLPFLTNRYEFEPRGSVYVKGKDHMEVFLYTTRRDNPLDDDEADKVEQLGTKKMEHEGRDEDVVQGEQQAEDKDEEEEEEEEDDDLHSSETTTLFKSQESLQANGGSHLAPNAAATSHTHTITLTNNNNHNSSNINNNIATSNTTTTANNNSMPVET
Protein: Immunoglobulin superfamily member 6 (IgSF6) (Protein DORA) (O95976)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein-L-histidine N-pros-methyltransferase
- Myeloid cell nuclear differentiation antigen
Sequence:
MGTASRSNIARHLQTNLILFCVGAVGACTLSVTQPWYLEVDYTHEAVTIKCTFSATGCPSEQPTCLWFRYGAHQPENLCLDGCKSEADKFTVREALKENQVSLTVNRVTSNDSAIYICGIAFPSVPEARAKQTGGGTTLVVREIKLLSKELRSFLTALVSLLSVYVTGVCVAFILLSKSKSNPLRNKEIKEDSQKKKSARRIFQEIAQELYHKRHVETNQQSEKDNNTYENRRVLSNYERP
Protein: Leu/Ile/Val-binding protein BraC3 (Q1MDE9)
Organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium leguminosarum bv. viciae)
Function: Part of the ABC transporter complex BraDEFGC/C3 involved in transport of branched-chain amino acids Leu, Ile and Val (LIV). Essential for the development of bacteroids, the differentiated legume-symbiotic forms of this bacterium, and for the effective N(2) fixation by them.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTLKTLTATLVASLAFAPLAHADITIGLIAPLTGPVAAYGDQVKNGAQTAVDEINKKGGILGEKVVLELADDAGEPKQGVSAANKVVGDGIRFVVGPVTSGVAIPVSDVLAENGVLMVTPTATAPDLTKRGLTNVLRTCGRDDQQAEVAAKYVLKNFKDKRVAIVNDKGAYGKGLADAFKATLNAGGITEVVNDAITPGDKDFSALTTRIKSEKVDVVYFGGYHPEGGLLARQLHDLAANATIIGGDGLSNTEFWAIGTDAAGGTIFTNASDATKSPDSKAAADALAAKNIPAEAFTLNAYAAVEVLKAGIEKAGSAEDAEAVATALKDGKEIPTAIGKVTYGETGDLTSQSFSLYKWEAGKIVAAE
Protein: Dopamine receptor 3 (Dopamine D2-like receptor dop-3) (Q6RYS9)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor which binds to the neurotransmitter dopamine with high affinity leading to the activation of an associated G-protein and downstream signaling pathways. Couples to G-proteins to inhibit adenylate cyclase (AC) activity and cAMP production. Antagonizes the D1-like dopamine receptor dop-1 to negatively regulate the rate of locomotion. In GABAergic, RIC, and SIA neurons, antagonizes the function of dop-1 to play a role in behavioral plasticity and regulate the decision-making process when conflicting alternatives are present. Antagonizes octopamine signaling in response to food by promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons. This is most likely in association with the G(o)-alpha G-protein subunit goa-1. Promotes male mating behavior by antagonizing acetylcholine signaling to control the protrusion of copulatory spicules from the tail of males during hermaphrodite vulval location.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dopamine receptor 4
- Dopamine receptor 2
- Sodium-dependent dopamine transporter
- G-protein coupled receptors family 1 profile domain-containing protein
- Metallo-beta-lactamase domain-containing protein 1
- Regulator of G-protein signaling egl-10
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 7
Sequence:
MLAGQHHVTDIESPLMVVLWRVAAGVFLPLVPTMAVFGNVLVIMSVFRERSLQTVTNMLIVSLAVSDFMVAIGVMSFGVYYEWNDFKWGLGSFFCHVYQALDVACSTASILNLLAISLDRYIAIGHPISYAQYGARGGRAMISITIVWGVSVAVALPLLLGVNPMEENDLQECELANPYFNMISSIFSFFIPCIAMIILYTIIFRRLRQRERARSLRQAQRSENDKISSALLGGAQIARQMGKHFKNRTDQILLEISFQTSSFPTMSESSEDASTISPMINSFNNFLPKKTPYPSTSIPAIPECGSMPNLTIIERPEAEKEKEISIMDLRDTVEMLDDKYSSAILTSFQTSRSFGEELEEILPFIDGSNSVKHSREQLHTTRSNTSTTRLLDVKPELRSISVPSIQDEKKLSQKSNDLPFSHQNGTHKQKLLPNPGILMKSKSTTLLKTNGYMDTDSLNRNSHKKSLADLLANDEFSFSDSMRVYKNRLFKSLSRATSGWNKPRPSRHMVKKATKQMRREHKATVTLAVVLAVFLFCWLPFFVLHLSNSICLIIDENSACVGFLPLYLATWLGYLNSSLNPLIYTVFDQRFRNAFRNILSCGIFKKR
Protein: Exocyst complex component Sec8 (A0A8C0N5P9)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Interaction partners:
Sequence:
MAAEAAGGKYRGTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMVSKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIDELHRHLYIKSTSRVVQRNKEKGRVSSLIKDASPVPLIDVTNLPTPRKFLDTSQYSTPGSSSAREINLQDIKEDLELDPEENSTLFMGILIKGLAKLKKIPETVKAIKERLEQELQQIVKRSTTQVADSGYQRGESLTVENQPRLLLELLELLFDKFNAVATAHSVVLGYLQDTVVAPLTQQEDVKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGRDFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLRDFLTVYIKNIFLNQVLAEINKEIEGVTKTSDPLKILANADTMKVMGVQRPLLQSTIIVEKTVQDLMNLMHDLSAYSDQFLNMVCVKLQEYKDTCTTACRGIVQSEEKLVISASWAKDDDISRLLKSLPNWINMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLAGRTKSAFSNLSTSQMLSPAQESHMNMDLPPVSEQIMQTLSELAKSFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAIEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNMRLQRLKEIICEQAAIKQATKDKKITTV
Protein: Defective proboscis extension response 6, isoform E (M9PF70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPIAHPLPLCVAWLLLLVVIVMSDMTNGGVQGPIEGYNSLDDLLTTTPTPGQAALLLPTAPTAAYTHPKWMEPYFDPSTPRNVTALMGKSAYLSCRVRNLANKTVSWIRHRDIHILTVGSYTYTSDQRFQATHHQDTEDWTLQIKWAQKRDAGMYECQISTQPVRSYFVRLNVVVPTATILGGPDLHVDKGSTINLTCTVKFSPEPPAYIFWYHHEEVINYDSSRGGVSVITEKGDVTTSFLLIQNADLADSGKYSCAPSNADVASVRVHVLNGHISTQLQRN
Protein: Putative ammonium transporter 2 (Q20605)
Organism: Caenorhabditis elegans
Function: Involved in the uptake of ammonia (Probable). Implicated in aging.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- DNA N6-methyl methyltransferase
Sequence:
MNTLQNLTLKMDRQPTIRMKPDKQLDCSLSQDDGVWMMASSFIIFTMTAGFGLLESGRVSSKDEVNCMVKNVFDVIFGGLAYWMFGYGLTFGDSKHQLGRYVGFGDFFFDPERVSDDDSTDEKGISYSLFIFQMSFATTTSTIVSAGMSERIHLKSHCFISFFITLVHSVAGHWVWDQEGVFRMMGVVDSAGCSAVHLVGGVSGLVATLYLKPRRNRFAKNGIRTVSDPTKAILGFLMIWWGWLAFNTSSNYAVTHGQWTEGMRSAVGTILASAGGGVVTVIITRLSTKKIQMDMLIDGMLASLVASTGGCLYFTPWQATLVGAIGSSLALAAYPVTEWLKIDDPVGVFPVHVVGSIWGMIAPAIFVYRRPMNFGPPECDFQTSDEINGLLYGGGFYLLFLQSFVILVIGTYSAICAFIILFLIHHSPVGLRVDKYTEELGADLIEHGLAGFNVMTYTIEKKLDTKTLSAVLMIIVRWRAKAKLGAQRRKKIHDSGSVAPQQAESVEMNVIHRRH
Protein: Oligopeptide transporter 3 (AtOPT3) (O23482)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the translocation of tetra- and pentapeptides across the cellular membrane in an energy-dependent manner. Acts also as a metal transporter that could be a component of the copper transport machinery. Essential for early embryo development.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Metal-nicotianamine transporter YSL3
- Metal-nicotianamine transporter YSL1
- Metal transporter Nramp4
- Ferric reduction oxidase 3, mitochondrial
- Fe
- Ferric reduction oxidase 2
- Metal-nicotianamine transporter YSL2
- Uncharacterized protein
- Transcription factor bHLH47
- Transcription factor bHLH101
Sequence:
MDAEKATDKTNVHLSSDHERCPVEEVALVVPETDDPSLPVMTFRAWFLGLTSCVLLIFLNTFFTYRTQPLTISAILMQIAVLPIGKFMARTLPTTSHNLLGWSFSLNPGPFNIKEHVIITIFANCGVAYGGGDAYSIGAITVMKAYYKQSLSFICGLFIVLTTQILGYGWAGILRRYLVDPVDMWWPSNLAQVSLFRALHEKENKSKGLTRMKFFLVALGASFIYYALPGYLFPILTFFSWVCWAWPNSITAQQVGSGYHGLGVGAFTLDWAGISAYHGSPLVAPWSSILNVGVGFIMFIYIIVPVCYWKFNTFDARKFPIFSNQLFTTSGQKYDTTKILTPQFDLDIGAYNNYGKLYLSPLFALSIGSGFARFTATLTHVALFNGRDIWKQTWSAVNTTKLDIHGKLMQSYKKVPEWWFYILLAGSVAMSLLMSFVWKESVQLPWWGMLFAFALAFIVTLPIGVIQATTNQQPGYDIIGQFIIGYILPGKPIANLIFKIYGRISTVHALSFLADLKLGHYMKIPPRCMYTAQLVGTVVAGVVNLGVAWWMLESIQDICDIEGDHPNSPWTCPKYRVTFDASVIWGLIGPRRLFGPGGMYRNLVWLFLIGAVLPVPVWALSKIFPNKKWIPLINIPVISYGFAGMPPATPTNIASWLVTGTIFNYFVFNYHKRWWQKYNYVLSAALDAGTAFMGVLLFFALQNAGHDLKWWGTEVDHCPLASCPTAPGIKAKGCPVF