wanglab/gogpt-training-data huggingface dataset:
Protein: cDNA, FLJ96613, highly similar to Homo sapiens vacuolar protein sorting 33A (yeast) (VPS33A), mRNA (B2RDH6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004492}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004492}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004492}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}.
Interaction partners:
Sequence:
MAAHLSYGRVNLNVLREAVRRELREFLDKCAGSKAIVWDEYLTGPFGLIAQYSLLKEHEVEKMFTLKGNRLPAADVKNIIFFVRPRLELMDIIAENVLSEDRRGPTRDFHILFVPRRSLLCEQRLKDLGVLGSFIHREEYSLDLIPFDGDLLSMESEGAFKECYLEGDQTSLYHAAKGLMTLQALYGTIPQIFGKGECARQVANMMIRMKREFTGSQNSIFPVFDNLLLLDRNVDLLTPLATQLTYEGLIDEIYGIQNSYVKLPPEKFAPKKQGDGGKDLPTEAKKLQLNSAEELYAEIRDKNFNAVGSVLSKKAKIISAAFEERHNAKTVGEIKQFVSQLPHMQAARGSLANRTSIAELIKDVTTSEDFFDKLTVEQEFMSGIDTDKVNNYIEDCIAQKHSLIKVLRLVCLQSVCNSGLKQKVLDYYKREILQTYGYEHILTLHNLEKAGLLKPQTGGRNNYPTIRKTLRLWMDDVNEQNPTDISYVYSGYAPLSVRLAQLLSRPGWRSIEEVLRILPGPHFEERQPLPTGLQKKRQPGENRVTLIFFLGGVTFAEIAALRFLSQLEDGGTEYVIATTKLMNGTSWIEALMEKPF
Protein: Derlin-1 (Degradation in endoplasmic reticulum protein 1) (Der1-like protein 1) (Q99J56)
Organism: Mus musculus (Mouse)
Function: Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. Forms homotetramers which encircle a large channel traversing the endoplasmic reticulum (ER) membrane. This allows the retrotranslocation of misfolded proteins from the ER into the cytosol where they are ubiquitinated and degraded by the proteasome. The channel has a lateral gate within the membrane which provides direct access to membrane proteins with no need to reenter the ER lumen first. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BUN8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BUN8}.
Interaction partners:
- E3 ubiquitin-protein ligase synoviolin
- Protein sel-1 homolog 1
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- E3 ubiquitin-protein ligase AMFR
- Protein OS-9
- Derlin-3
- Derlin-2
- Endoplasmic reticulum chaperone BiP
- Endoplasmic reticulum lectin 1
Sequence:
MSDIGDWFRSIPAITRYWFAATVAVPLIGKLGIISPAYFFLWPEAFLYRFQIWRPFTATFYFPVGPGTGFLYLVNLYFLYQYSTRLEAGAFDGRPADYLFMLLFNWICIVITGLAMDMQLLMIPLIMSVLYVWAQLNRDLIVSFWFGTRFKACYLPWVILGFNYIIGGSVINELIGNLVGHLYFFLMFRYPMDLGGRNFLSTPQFLYRWLPSRRGGVSGFGVPPASMRRAADQNGGGGRHNWGQGFRLGDQ
Protein: AP-1 complex subunit beta-1 (Beta-1-adaptin) (Clathrin assembly protein complex 1 beta-1 large chain) (Clathrin assembly protein large beta-1 chain) (P36000)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin.
Subcellular location: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Interaction partners:
- Adaptin medium chain homolog APM2
- AP-1 complex subunit sigma-1
- AP-1 complex subunit gamma-1
- AP-1 complex subunit mu-1-I
- Clathrin heavy chain
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- AP-2 complex subunit alpha
- Clathrin light chain
- Epsin-5
Sequence:
MPPLDKRIKKFLKDSIRIAPKISGKGELSELRTGLVSQYPQTRKDAIKKTIQQMTLGKDVSSLFPDVLKNIATIDVEQKKLVYLYVMNYAETHPELCILAVNTFITDAQDPNPLIRCMAIRTMSMIRVDKILEYIETPLRRTLHDDNAYVRKTAVICVAKLFQLNKDLCVELGVVEDLVNALDDSNPLVIANATAALIEIHNMDMDAVDLSSLIQSHVSQFLLALNECTEWARIIILGTLSEYSAKDSLEAQDIIDRVTAHLQHVNPAVVLATIKVIVRNLPQIEYSSNSLIMKRLSSAFVSLMSTPPEMQYVALKNIRIILEKYPELLTKELRIFYVKFNDPLYVKLEKIDILVRLVDPSNLKQCTLLLTELKEYAMEYEPEFVSRAIQALSQLGIKYAQESFVSKVLDILLELLERQDTIKDDCCISLCDLLRHCPGNDKMAKQVCAVFNTWSNPEVLLQSDIAKCNYVWLLGQHPNNFSDLESKINIFIENFVQEEALTQMSLLMTIVRLHATLTGSMLQSVLELATQQTHELDVRDMAMMYWRCLSMPNNESLVNDLCQNKLPMISNTLEKFSPEVLEKLLMELGTISSIYFKPDSNRRKGKKYVQNIVKGKHIEELESMAKNEISSKANDDVLLDFDERDDVTNTNAGMLNTLTTLGDLDDLFDFGPSEDATQINTNDTKAVQGLKELKLGGDSNGISSGGKNNPDVSGGNIVSQDLLDLF
Protein: Histidine protein kinase NIK1 (EC 2.7.13.3) (Q5A599)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Histidine kinase involved in a two-component signaling pathway that regulates cell wall mannan biosynthesis. Required for hyphal formation and virulence. Plays a role in fungicides sensitivity, probably through the positive regulation of the HOG1-signaling pathway. Presumed to mediate phosphotransfer to the HOG1 MAP kinase pathway during oxidative and perhaps osmotic stress.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphorelay intermediate protein YPD1
- MAP kinase kinase kinase
- Mitogen-activated protein kinase HOG1
Sequence:
MNPTKKPRLSPMQPSVFEILNDPELYSQHCHSLRETLLDHFNHQATLIDTYEHELEKSKNANKAFQQALSEIGTVVISVAMGDLSKKVEIHTVENDPEILKVKITINTMMDQLQTFANEVTKVATEVANGELGGQAKNDGSVGIWRSLTDNVNIMALNLTNQVREIADVTRAVAKGDLSRKINVHAQGEILQLQRTINTMVDQLRTFAFEVSKVARDVGVLGILGGQALIENVEGIWEELTDNVNAMALNLTTQVRNIANVTTAVAKGDLSKKVTADCKGEILDLKLTINQMVDRLQNFALAVTTLSREVGTLGILGGQANVQDVEGAWKQVTENVNLMATNLTNQVRSIATVTTAVAHGDLSQKIDVHAQGEILQLKNTINKMVDSLQLFASEVSKVAQDVGINGKLGIQAQVSDVDGLWKEITSNVNTMASNLTSQVRAFAQITAAATDGDFTRFITVEASGEMDALKTKINQMVFNLRESLQRNTAAREAAELANSAKSEFLANMSHEIRTPLNGIIGMTQLSLDTELTQYQREMLSIVHNLANSLLTIIDDILDISKIEANRMTVEQIDFSLRGTVFGALKTLAVKAIEKNLDLTYQCDSSFPDNLIGDSFRLRQVILNLAGNAIKFTKEGKVSVSVKKSDKMVLDSKLLLEVCVSDTGIGIEKDKLGLIFDTFCQADGSTTRKFGGTGLGLSISKQLIHLMGGEIWVTSEYGSGSNFYFTVCVSPSNIRYTRQTEQLLPFSSHYVLFVSTEHTQEELDVLRDGIIELGLIPIIVRNIEDATLTEPVKYDIIMIDSIEIAKKLRLLSEVKYIPLVLVHHSIPQLNMRVCIDLGISSYANTPCSITDLASAIIPALESRSISQNSDESVRYKILLAEDNLVNQKLAVRILEKQGHSVEVVENGLEAYEAIKRNKYDVVLMDVQMPVMGGFEATEKIRQWEKKSNPIDSLTFRTPIIALTAHAMLGDREKSLAKGMDDYVSKPLKPKLLMQTINKCIHNINQLKELSRNSRGSDFAKKMTRNTPGSTTRQGSDEGSVEDMIGDTPRQGSVEGGGTSSRPVQRRSATEGSITTISEQIDR
Protein: LD14555p (Q95RS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSHVGPASARVLNPFMCVCVASSSVCACVGAKWNQTSQRVEQCCQRSLITALKKKSPFFAPPPPLCQRKLKIQIVLQKFWLPWKFKSLCVHLFSPKTLKQ
Protein: DMGDH protein (Dimethylglycine dehydrogenase) (Q8TCC6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
YLIEPEKIQEMFPLLNMNKVLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMRANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYLRQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLKKADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEPPFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLESKCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKFNIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSELHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTKSLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRLEKAFRAWGLEMNCDTNPLEAGLEYFVKLNKDQNSCFAHFKEENGWVSRWAIRPY
Protein: Flagellar assembly factor FliW (Q72EP7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185}.
Interaction partners:
- Translational regulator CsrA
- Flagellar hook-associated protein FlgL, putative
- Flagellin
- Flagellin
- Flagellar hook-associated protein 1
- Flagellar protein FliS
- Flagellar hook-basal body complex protein FliE
- Flagellin FlaG, putative
- Flagellar motor switch protein FliM
- Flagellar basal body rod protein FlgB
Sequence:
MARQNEIEIQTRIGRQRITLDKIIHFPRGLAGFEGRHDFTLLQLREGAPFLVLQSLDDPGLGLLVADPYSFLTDYQIRVGDPEQRLLKLENIRQVAVLVTVSIPAGQPEKTALNLTGPILINHRARIGLQVPQTDASLPPQFYLHMDDANGSTTVRRKASPPAAGEDKGDVQE
Protein: Cleavage stimulation factor subunit 2 (A0A8I5ZY65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGLPVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGESISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLISGNPQPVHVAGPGSGPNVSMNQQNPQAPQAQSLSGMHVNGAPPMMQASMPGGVPAPVQMAAAVAGPGPGSLAPAGVMQAQVGMQGAGPVPMERGQGDAPNDPRGGTLMTVTGEVEPRAYLGPPPPPHQGPPMHHVPGHEGRGPPPHDMRGGPLAEPRPLMAEPRGPMLDQRGPPLDARGGRDPRGLDARGMEARAMEARGLEARAMEARAMEARAMEARAMEARAMEARAMEARGMDTRGPVPGPRGPIPSGIQGPNPMNMGAVVPQGSRQVPVMQGAGMQGASMQGGSQPGGFSPGQSQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP
Protein: Phosphoribosyl pyrophosphate synthase-associated protein 2 (Q6ZTP6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHGDGDMGPCRLHKAKWKSRFFTVNVGRPFFFPGCLTYYCRSAHIHSFPSVLWQDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRRIEESAIDEVVVTNTIPHEVQKLQCPKIKTVDISMILSEAIRRIHNGESMSYLFRNIGLDD
Protein: Serotransferrin (B8JL43)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR002549}.
Interaction partners:
- Transferrin receptor protein 1
- Transferrin receptor 1b.
- Transferrin receptor 2.
- Apolipoprotein A-Ia
- Apolipoprotein A-II
Sequence:
MKVLLISLLGCLVVALPSASAQKKVKWCVTTQNEQSKCRHLATKAADIECHLQPTVIDCMRSIAAGGTDIVTVDGANVFTGGLNNYLLRPIIAEKKKECCYAVAAVKAGSGFNINELKGKSSCHSCYQRSGGWNTPIGKLIATNKITWEGPNEMPVERAVSEFFSSSCVPGVSKPKYPNLCKACQGDCSCSHNEKYFGDDGAFQCLKNDNGQVAFVCHHAIPESERQNYELLCMDGSRKSVEDYKTCNFAREPARTVIARTDTDLQYVYDVLKQIPASDLFSSQAFGGKDLIFSDSATELMLLPKRTDSLLYLKEEYYEAMQAFKDGNPSAPTSQTKLAMCTIGHAEKNKCDSLDHVKKSCILEASVDDCIEKIKRKEADFLAVDGGQVYIAGKCGLVPVMAEQSNSQSCSSGSGGTASYYAVAVVRKGSGLTWNNLEGKKSCHTGLGRSAGWKIPESAICGEKDKCTLDKFFSEGCAPGADPTSNMCKLCKGSGKPVGDESKCKPSAEEQYYGYDGAFRCLAEKAGDVAFIKHTVVGDYTDGKGKDWAKDLKSEDFELICPNTPDTTMKYTDFEKCNLAQVPVHAVITREDARSAVVSFLSDIQSKNNDLFTSKDGKNLLFTDGTKCLQEIKGSVDDFLTKKYIDMIERTYKTSQNVPDLVKACTFGNCISS
Protein: Pteridine reductase (O76290)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVCQADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFAQRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKDKWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
Protein: Uncharacterized protein (Q38EU7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSTLPSARSEIAQARKEFWIAPRGHLAINRLKPTEVPQSLSVIVATSVDEVQPVAFTRPVASLVPNDTKSTRIHGIGARGGSGRHGAIPPLFKAQIYVWKDTTIREIFEEVLRSTPAAALVLLPPSSRKSGEITSHTNDDVSPDVSAEDRTHKCDSYKLNGRDGTEDRRYGDEANGEHPAKRVCTEAQRGNMEMGTHKGGTASFSAGQHSESGRRPAAPAAKVCVFHVYANVDRRVQVQSMTVLRTDKPSFHTGDFLTMKELRTTRGAERGWRSGDLLVFAPSVQHYCPP
Protein: Box C/D snoRNA protein 1 (Serologically defined breast cancer antigen NY-BR-75) (Zinc finger HIT domain-containing protein 6) (Q9NWK9)
Organism: Homo sapiens (Human)
Function: Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Interaction partners:
- FMR1-interacting protein NUFIP1
- Nucleolar protein 58
- Zinc finger HIT domain-containing protein 3
- PIH1 domain-containing protein 1
- Nucleolar protein 56
- RuvB-like 1
- RuvB-like 2
- Transcription initiation factor TFIID subunit 9
Sequence:
MEFAAENEGKSGGGLHSVAEGVRLSPEPGREGVRDLAGAEEFGGGEEGTGLTGIKEIGDGEEGSGQRPEEIPMDLTVVKQEIIDWPGTEGRLAGQWVEQEVEDRPEVKDENAGVLEVKQETDSSLVVKEAKVGEPEVKEEKVKEEVMDWSEVKEEKDNLEIKQEEKFVGQCIKEELMHGECVKEEKDFLKKEIVDDTKVKEEPPINHPVGCKRKLAMSRCETCGTEEAKYRCPRCMRYSCSLPCVKKHKAELTCNGVRDKTAYISIQQFTEMNLLSDYRFLEDVARTADHISRDAFLKRPISNKYMYFMKNRARRQGINLKLLPNGFTKRKENSTFFDKKKQQFCWHVKLQFPQSQAEYIEKRVPDDKTINEILKPYIDPEKSDPVIRQRLKAYIRSQTGVQILMKIEYMQQNLVRYYELDPYKSLLDNLRNKVIIEYPTLHVVLKGSNNDMKVLHQVKSESTKNVGNEN
Protein: Uncharacterized protein (Q388A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVVIHSGLVTPVLEIMSLVKPLPFDVDVLLDEHPDMTVYHRPPLQSRGSGSKYICNHHPVELLSYEVYLCDTEDEPVVDFEVNNRIVVRYQLNPYCAAQLSHLRGFEPLVYPYESRYLRPAYVEVAHGSGGCCFNGSGSSYGINVCVAPTDIFAGFPRSNNGDDAVIYSTVPHIRKLLQRPFSPFMECGPLIADDVFFHWDTLGLLSLTDTCDLGMFTIEGVCGVSSHIM
Protein: Cytochrome P450 71D180 (Carvacrol synthase) (EC 1.14.14.-) (Carveol synthase) (EC 1.14.14.51, EC 1.14.14.53) (Gamma-terpinene hydroxylase) (Limonene hydroxylase) (P0DO39)
Organism: Origanum vulgare (Wild marjoram)
Function: Involved in the biosynthesis of phenolic monoterpenes natural products thymol and carvacrol which have a broad range of biological activities acting as antimicrobial compounds, insecticides, antioxidants and pharmaceutical agents. Catalyzes the C2-hydroxylation of gamma-terpinene to produce carvacrol (Ref.1). Mediates also the C6-hydroxylation of (4S)-limonene and (4R)-limonene to form carveol (Ref.1).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCVNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIVDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRTLVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS
Protein: 14-3-3 protein beta/alpha (Protein 1054) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed] (P31946)
Organism: Homo sapiens (Human)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.; SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11260479}. Note=(Microbial infection) Upon infection with Chlamydia trachomatis, this protein is associated with the pathogen-containing vacuole membrane where it colocalizes with IncG. {ECO:0000269|PubMed:11260479}.
Interaction partners:
- RAF proto-oncogene serine/threonine-protein kinase
- M-phase inducer phosphatase 2
- M-phase inducer phosphatase 3
- Serine/threonine-protein kinase B-raf
- 14-3-3 protein zeta/delta
- Serine/threonine-protein kinase A-Raf
- Transcriptional coactivator YAP1
- Bcl2-associated agonist of cell death
- 14-3-3 protein epsilon
- 14-3-3 protein theta
Sequence:
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Protein: Aconitate hydratase 3, mitochondrial (Aconitase 3) (mACO1) (EC 4.2.1.3) (Citrate hydro-lyase 3) (Q9SIB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. Contributes to oxidative stress tolerance. Modulates cytosolic citrate metabolism during lipid mobilization. Required during seedling growth.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:25061985}. Cytoplasm {ECO:0000269|PubMed:25061985, ECO:0000269|PubMed:25307043}. Note=Cytosolic localization in 3-day-old seedlings, but mitochondrial in 10-day-old plantlets. {ECO:0000269|PubMed:25061985}.
Interaction partners:
- Isocitrate dehydrogenase, chloroplastic/mitochondrial
- Cytosolic isocitrate dehydrogenase
- Peroxisomal isocitrate dehydrogenase
- Citrate synthase 1, peroxisomal
- Citrate synthase 2, peroxisomal
- Citrate synthase 5, mitochondrial
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Isocitrate lyase
- Isocitrate dehydrogenase catalytic subunit 6, mitochondrial
Sequence:
MYLTASSSASSSIIRAASSRSSSLFSFRSVLSPSVSSTSPSSLLARRSFGTISPAFRRWSHSFHSKPSPFRFTSQIRAVSPVLDRLQRTFSSMASEHPFKGIFTTLPKPGGGEFGKFYSLPALNDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKTSPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLRKHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMIEAYLRANNMFVDYNEPQQDRVYSSYLELNLDDVEPCISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQEKVVNFSFDGQPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKTSLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGAAITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNIDFETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKGNPMWNKLSVPENTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLLNFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIMARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTIILAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIHLPTDISEIRPGQDVTVTTDNGKSFTCTVRFDTEVELAYFNHGGILPYVIRNLSKQ
Protein: Serine/threonine-protein kinase StkP (Ser/Thr-protein kinase StkP) (EC 2.7.11.1) (Eukaryotic-type Ser/Thr protein kinase) (ESTPK) (Q8KY50)
Organism: Streptococcus pneumoniae
Function: Protein kinase involved in signal transduction pathways that regulate various cellular processes. Likely senses intracellular peptidoglycan subunits present in the cell division septa of actively growing cells; thus, intracellular unlinked peptidoglycan may serve as the signal molecules that trigger StkP phosphorylation activity on a set of substrates. Plays a crucial role in the regulation of cell shape and cell division of S.pneumoniae through control of at least DivIVA activity. Is involved in competence triggering, via the transduction of signals culminating directly or indirectly in ComD activation. Is important for the resistance of S.pneumoniae to various environmental stress conditions. Appears to be a global regulator that positively controls the transcription of a set of genes encoding functions involved in cell wall metabolism, pyrimidine biosynthesis, DNA repair, iron uptake, and oxidative stress response, and that seems to down-regulate genes employed in competence. Since StkP is unlikely to directly regulate transcription, the input signal must be transmitted through an effector molecule. Identified target substrates that are specifically phosphorylated by StkP in vivo, mainly on threonine residues, are DivIVA, GlmM, PpaC, MapZ, KhpB (also called EloR/Jag) and StkP itself. Autophosphorylated StkP is a substrate for the cotranscribed protein phosphatase PhpP; PhpP and StkP appear to constitute a functional signaling couple in vivo.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15720398, ECO:0000269|PubMed:17307148, ECO:0000269|PubMed:19502404, ECO:0000269|PubMed:22431591}; Single-pass membrane protein {ECO:0000269|PubMed:15720398, ECO:0000269|PubMed:17307148, ECO:0000269|PubMed:19502404, ECO:0000269|PubMed:22431591}. Note=The C-terminal PASTA domain is located in the periplasmic space, beneath the peptidoglycan cell wall, and the kinase domain is located in the cytoplasm. However, another study in the virulent strain TIGR4 (PubMed:20223804) showed that the C-terminal PASTA domain is exposed extracellularly. Localizes to the midcell division sites.
Interaction partners:
Sequence:
MIQIGKIFAGRYRIVKQIGRGGMADVYLAKDLILDGEEVAVKVLRTNYQTDPIAVARFQREARAMADLDHPHIVRITDIGEEDGQQYLAMEYVAGLDLKRYIKEHYPLSNEEAVRIMRQILLAMRLAHTRGIVHRDLKPQNILLTPDGTAKVTDFGIAVAFAETSLTQTNSMLGSVHYLSPEQARGSKATVQSDIYAMGIIFYEMLTGHIPYDGDSAVTIALQHFQNPLPSVIAENSSVPQALENVIIKATAKKLTNRYRSVSEMYVDLSSSLSYNRRNESKLIFDETSKADTKTLPKVSQSTLTSIPKVQAQTEHKSIKNPSQAVTEETYQPQAPKKHRFKMRYLILLASLVLVAASLIWILSRSPATIAIPDVAGQTVAEAKATLKKANFEIGEEKTEASEKVEEGRIIRTDPGAGTGRKEGTKINLVVSSGKQSFQISNYVGRKSSDVIAELKEKKVPDNLIKIEEEESNESEAGTVLKQSLPEGTTYDLSKATQIVLTVAKKATTIQLGNYIGRNSTEVISELKQKKVPENLIKIEEEESSESEPGTIMKQSPGAGTTYDVSKPTQIVLTVAKKVTSVAMPSYIGSSLEFTKNNLIQIVGIKEANIEVVEVTTAPAGSVEGMVVEQSPRAGEKVDLNKTRVKISIYKPKTTSATP
Protein: Bile salt hydrolase (I3QNT7)
Organism: Bifidobacterium pseudolongum
Interaction partners:
Sequence:
VDGEDNMFFGRNLDWSFSYGEKVLYTPKDYNYQPVFNGEDRNHAVLGIGIVVDDTPLYFDCANDAGLAVAGLNFPGYAEYASDSVNLTVNVAAYEFPLWVARNFTSVDDVAEALKNVTIVAKPINDQYPVAMLHWIISDATRTIVVEYTASGMHVYDDDI
Protein: Zinc finger protein CONSTANS-LIKE 1 (O50055)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor that may be involved in the light input to the circadian clock but does not affect flowering time.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein LHY
- Protein CCA1
- Protein GIGANTEA
- AGAMOUS-like 83
- At1g32630
- Adagio protein 3
- Cold-regulated protein 27
- Protein EARLY FLOWERING 3
- Inactive protein FRIGIDA
- Cyclic dof factor 1
Sequence:
MLKVESNWAQACDTCRSAACTVYCRADSAYLCSSCDAQVHAANRLASRHERVRVCQSCERAPAAFFCKADAASLCTTCDSEIHSANPLARRHQRVPILPISEYSYSSTATNHSCETTVTDPENRLVLGQEEEDEDEAEAASWLLPNSGKNSGNNNGFSIGDEFLNLVDYSSSDKQFTDQSNQYQLDCNVPQRSYGEDGVVPLQIEVSKGMYQEQQNFQLSINCGSWGALRSSNGSLSHMVNVSSMDLGVVPESTTSDATVSNPRSPKAVTDQPPYPPAQMLSPRDREARVLRYREKKKMRKFEKTIRYASRKAYAEKRPRIKGRFAKKKDVDEEANQAFSTMITFDTGYGIVPSF
Protein: ATP synthase, putative (EC 3.6.3.14) (Q383Y7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar proton pump subunit B
- Uncharacterized protein
- V-type proton ATPase subunit
- V-type proton ATPase subunit F
- V-type ATPase, C subunit, putative
- 
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- H
- Vacuolar ATP synthase subunit D, putative
Sequence:
MSEARQIQSMIDFIEREAQEKADELNSAAQEEYDVEKMRLVEAEKVKVRANNEQKLKQVDVGRRVARANFSKAQRLRIMEAQSNIVEQLKENIKTKLMAFVKNTDSYKKLLVSILHEALSAVRTDAIVYTCKNDEPIVTGMLSELEQWYLKTVGTRVSIRMGKEYLNAEEALGGVVVKSHDGHIVCNWTLSSRMRNCVNDQLPTIRYYLFNPESSI
Protein: Protein CADMIUM TOLERANCE 3 (Cd tolerant 3) (OsCDT3) (Q5VRD7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Confers resistance to heavy metal ions (e.g. aluminium) by chelating them at the plasma membrane of root cells, thus stopping their entry and reducing their accumulation. Binds to and confers tolerance to aluminium (Al).
Subcellular location: Cell membrane {ECO:0000269|PubMed:23888867}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MYNPPAAQEMSYSDHVKKRHEDKGCLYACLFTLCCCFCCYETCECCLECLCCC