wanglab/gogpt-training-data huggingface dataset:
Protein: Pyruvate dehydrogenase E1 component (PDH E1 component) (EC 1.2.4.1) (P0AFG8)
Organism: Escherichia coli (strain K12)
Function: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase
- D-lactate dehydrogenase
- Phosphoenolpyruvate synthase
- Pyruvate kinase I
- Pyruvate dehydrogenase
- NADP-dependent malic enzyme
- Formate acetyltransferase 1
- Pyruvate kinase II
- Quinone-dependent D-lactate dehydrogenase
Sequence:
MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA
Protein: AP-2 complex subunit mu (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat-associated protein AP50) (Mu2-adaptin) (Plasma membrane adaptor AP-2 50 kDa protein) (Probable clathrin coat assembly protein AP50) (Q09718)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component 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. AP50 is a subunit of the plasma membrane adaptor (Potential).
Subcellular location: Cell membrane {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. {ECO:0000250}.
Interaction partners:
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha
- AP-2 complex subunit beta
- AP-1 complex subunit beta-1
- Probable clathrin heavy chain
- AP-1 complex subunit gamma-1
- AP-3 complex subunit delta
- Uncharacterized calcium-binding protein C800.10c
- AP-1 complex subunit sigma-1
- Putative ATP-dependent RNA helicase ucp12
Sequence:
MISGLFIFNLKGDTLICKTFRHDLKKSVTEIFRVAILTNTDYRHPIVSIGSSTYIYTKHEDLYVVAITKGNPNVMIVLEFLESLIQDLTHYFGKLNENTVKDNVSFIFELLDEMIDYGIIQTTEPDALARSVSITAVKKKGNALSLKRSHSSQLAHTTSSEIPGSVPWRRAGIKYRKNSIYIDIVERMNLLISSTGNVLRSDVSGVVKMRAMLSGMPECQFGLNDKLDFKLKQSESKSKSNNSRNPSSVNGGFVILEDCQFHQCVRLPEFENEHRITFIPPDGEVELMSYRSHENINIPFRIVPIVEQLSKQKIIYRISIRADYPHKLSSSLNFRIPVPTNVVKANPRVNRGKAGYEPSENIINWKIPRFLGETELIFYAEVELSNTTNQQIWAKPPISLDFNILMFTSSGLHVQYLRVSEPSNSKYKSIKWVRYSTRAGTCEIRI
Protein: Protein kinase C and casein kinase substrate in neurons 2 protein (Synaptic dynamin-associated protein II) (Syndapin-2) (Syndapin-II) (SdpII) (Q9QY17)
Organism: Rattus norvegicus (Rat)
Function: Regulates the morphogenesis and endocytosis of caveolae. Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10704453}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9WVE8}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10704453}; Peripheral membrane protein {ECO:0000269|PubMed:10704453}; Cytoplasmic side {ECO:0000269|PubMed:10704453}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q9WVE8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVE8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVE8}. Early endosome {ECO:0000250|UniProtKB:Q9WVE8}. Recycling endosome membrane {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22718246}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9WVE8}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9WVE8}. Cell projection {ECO:0000250|UniProtKB:Q9UNF0}. Membrane, caveola {ECO:0000269|PubMed:22718246}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9WVE8}. Note=Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1. {ECO:0000250|UniProtKB:Q9WVE8}.
Interaction partners:
- Protein kinase C and casein kinase substrate in neurons 3
- EH domain-containing protein 1
- Protein kinase C and casein kinase substrate in neurons protein 1
- EH domain-containing protein 2
- EH domain-containing protein 3
- Actin nucleation-promoting factor WASL
- Caveolae-associated protein 1
- Protein cordon-bleu
- Dynamin-2
- Caveolin-1
Sequence:
MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCGDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAVMSEAERVSELHLEVKASLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVDAAKKAHHTACKEEKLAVSREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKDKYEKALKELDQTTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKGIYRELEQSIKAADAVEDLRWFRANHGPGMAMNWPQFEDEEWSADLNRTLSRREKKKAADGVTLTGINQTGDQSGQNKPSSNLSVPSNPAQSTQLQSSYNPFEDEDDTGSSVSEKEDIKAKNVSSYEKTQNYPADWSDDESNNPFSSTDANGDSNPFDEDTTSGTEVRVRALYDYEGQEHDELSFKAGDELTKIEDEDEQGWCKGRLDSGQVGLYPANYVEAIQ
Protein: Ephrin-B3 (EPH-related receptor transmembrane ligand ELK-L3) (EPH-related receptor tyrosine kinase ligand 8) (LERK-8) (Q15768)
Organism: Homo sapiens (Human)
Function: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Ephrin type-B receptor 3
- Ephrin type-A receptor 4
- Ephrin type-B receptor 6
- Ephrin type-B receptor 2
- Ephrin type-B receptor 1
- Ephrin type-B receptor 4
- Ephrin type-A receptor 1
- Regulator of G-protein signaling 3
- Cytoplasmic protein NCK2
- Ephrin type-A receptor 2
Sequence:
MGPPHSGPGGVRVGALLLLGVLGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPNYEFYKLYLVGGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSLEPGKENLPGDPTSNATSRGAEGPLPPPSMPAVAGAAGGLALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGAADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
Protein: Sodium/sulphate symporter, putative (Q383G2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKFGKRLIEEEVEQWKDFYVNYKRLKKFIHSSPLTGVEFSEELFRIIGEELERAGGLFKELLEELHRCHDELLEQDPQLPAVPSKLPWMFNRKRVHREKLNSPREGLSIAFESSTENSMMNEIVVEQREGFVSKFKKCFLKLIGDSQKQEIEEDTPRARFLEWHSSAHMLQHFAELNLEAIRKSAKKLRKYRRNEGDFTISIEAEISRSQIGRSLPRLHVFMTDVDADYERKFGEALVQFKNITINQTYHAKWRFVFLSAALFWILMFFPILESHPSAHNCVALFGVIISLWITEAIPFFCTAMLIPIIAVPLGIITDPATHRVASTTVASRIILSRMMDHVQILVLGGLTIGKALGRTHLEVYAAGALYRLTAHRPSMYLLGVMLCSSVLCAFVSNIAAPLLVLGVIRPTLWEFPEDTEAPHAILLGLAFACDIGGMLSPIASPQNAVALSVLSFHDVSFLSWVTVALPLVLVGVVASWAIILLVWKPFKNVSSIPLQVVNTEGNKEVRLADQVVVVMVSLITVVLWVLPPNLLFGDTGVVALIPIVVFFGIGILAKEDFNTLSWHLMFLLAGGNMLGLCARDSKMLDIIADSLHDTLVSQPPYTTLVSLILVVGVVTTFVSHTVAAMILLPMILKIGLVLPKEEGVFAVSPFTLVFLSALMCSGAMAFPISSFPNVNSLLAEDSRGRPYLKAKDFLFCGTIITFLLFICFVTWMVPFTYVVFEGKP
Protein: Small ubiquitin-related modifier 1 (SUMO-1) (Q5I0H3)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000250|UniProtKB:P63166}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (By similarity). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000250|UniProtKB:P63166}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- SUMO-activating enzyme subunit 2
- SUMO-conjugating enzyme UBC9
- Ran GTPase-activating protein 1
- Death domain-associated protein 6
- E3 SUMO-protein ligase PIAS4
- SUMO-activating enzyme subunit 1
- Cellular tumor antigen p53
- Protein inhibitor of activated STAT, 1
- E3 SUMO-protein ligase PIAS2
Sequence:
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
Protein: Ribosomal RNA large subunit methyltransferase H (EC 2.1.1.177) (23S rRNA (pseudouridine1915-N3)-methyltransferase) (23S rRNA m3Psi1915 methyltransferase) (rRNA (pseudouridine-N3-)-methyltransferase RlmH) (P0A8I8)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00658, ECO:0000305}.
Interaction partners:
- Ribosomal silencing factor RsfS
- Peptidoglycan D,D-transpeptidase MrdA
- tRNA
- tRNA
- tRNA
- Ribosomal RNA small subunit methyltransferase E
- Nicotinate-nucleotide adenylyltransferase
- Endolytic peptidoglycan transglycosylase RlpA
- 23S rRNA
- Ribosomal large subunit pseudouridine synthase D synthase)
Sequence:
MKLQLVAVGTKMPDWVQTGFTEYLRRFPKDMPFELIEIPAGKRGKNADIKRILDKEGEQMLAAAGKNRIVTLDIPGKPWDTPQLAAELERWKLDGRDVSLLIGGPEGLSPACKAAAEQSWSLSALTLPHPLVRVLVAESLYRAWSITTNHPYHRE
Protein: AT3g18370/MYF24_8 (C2 domain-containing protein) (Q93ZM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Calcium-dependent lipid-binding
- Thioredoxin-like fold domain-containing protein MRL7, chloroplastic
- Pentatricopeptide repeat-containing protein At1g15510, chloroplastic
- Synaptotagmin-1
- Bidirectional sugar transporter SWEET4
- Homeobox protein knotted-1-like 3
Sequence:
MGRRIKRKGLINTEAAREFINHLVAERHSLLLLVPLVLAFWAIERWVFAFSNWVPLVVAVWASLQYGSYQRALLAEDLTKKWRQTVFNASTITPLEHCQWLNKLLSEIWLNYMNKKLSLRFSSMVEKRLRQRRSRLIENIQLLEFSLGSCPPLLGLHGTCWSKSGEQKIMRLDFNWDTTDLSILLQAKLSMPFNRTARIVVNSLCIKGDILIRPILEGRALLYSFVSNPEVRIGVAFGGGGGQSLPATELPGVSSWLVKILTETLNKKMVEPRRGCFSLPATDLHKTAIGGIIYVTVVSGNNLNRRILRGSPSKSSEIGEGSSGNSSSKPVQTFVEVELEQLSRRTEMKSGPNPAYQSTFNMILHDNTGTLKFNLYENNPGSVRYDSLASCEVKMKYVGDDSTMFWAVGSDNGVIAKHAEFCGQEIEMVVPFEGVSSGELTVRLLLKEWHFSDGSHSLNSVNSSSLHSLDSSSALLSKTGRKIIVTVLAGKNLVSKDKSGKCDASVKLQYGKIIQKTKIVNAAECVWNQKFEFEELAGEEYLKVKCYREEMLGTDNIGTATLSLQGINNSEMHIWVPLEDVNSGEIELLIEALDPEYSEADSSKGLIELVLVEARDLVAADIRGTSDPYVRVQYGEKKQRTKVIYKTLQPKWNQTMEFPDDGSSLELHVKDYNTLLPTSSIGNCVVEYQGLKPNETADKWIILQGVKHGEVHVRVTRKVTEIQRRASAGPGTPFNKALLLSNQMKQVMIKFQNLIDDGDLEGLAEALEELESLEDEQEQYLLQLQTEQSLLINKIKDLGKEILNSSPAQAPSRDS
Protein: Hydroxyproline O-arabinosyltransferase 3 (EC 2.4.2.58) (Q9FY51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase involved in the O-arabinosylation of several proteins including extensins and small signaling peptides. Catalyzes the transfer of the initial L-arabinose to the hydroxyl group of Hyp residues. Contributes redundantly with HPAT1 and HPAT2 to arabinosylation of EXT3, but main contributor to arabinosylation of CLE peptides.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:24036508}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Arabinosyltransferase RRA3
- Arabinosyltransferase RRA1
- Arabinosyltransferase XEG113
- Arabinosyltransferase RRA2
- Hydroxyproline O-arabinosyltransferase 2
- Hydroxyproline O-arabinosyltransferase 1
- Prolyl 4-hydroxylase 5
- Prolyl 4-hydroxylase 2
- Extensin-3
- Ras-related protein RABE1c
Sequence:
MGKASGLLLFLLGFGFFVVTYNLLTLIVHNRSGVSNSDGSPLLDPVVQMPLNIRKAKSSPAPFHVALTATDAPYNKWQCRIMYYWYKQKKALPGSDMGGFTRILHSGNSDNLMDEIPTFVVDPLPPGLDRGYVVLNRPWAFVQWLERATIKEDYVLMAEPDHVFVNPLPNLAVGGFPAAFPFFYITPEKYENIVRKYYPAEMGPVTNIDPIGNSPVIISKESLEKIAPTWMNVSLTMKNDPETDKAFGWVLEMYGYAIASAIHGVRHILRKDFMLQPPWDLSTKGKFIIHYTYGCDYNMKGELTYGKIGEWRFDKRSHLRGPPPRNMSLPPPGVPESVVTLVKMVNEATATIPNWDTL
Protein: Basic endochitinase C (EC 3.2.1.14) (Rye seed chitinase-c) (RSC-c) (Q9FRV0)
Organism: Secale cereale (Rye)
Function: Defense against chitin-containing fungal pathogens. Binds the hyphal tips of fungi and degrades nascent chitin.
Interaction partners:
Sequence:
MRSLAVVVAVVATVAMAIGTAHGSVSSIISHAQFDRMLLHRNDGACQAKGFYTYDAFVAAANAFPGFGATGSTDARKRDVAAFLAQTSHETTGGWATAPDGAFAWGYCFKQERGAAADYCTPSAQWPCAPGKRYYGRGPIQLSHNYNYGPAGRAIGVDLLRNPDLVATDPTVSFKTALWFWMTAQAPKPSSHAVITGKWSPSGADRAAGRAPGFGVITNIINGGLECGHGQDSRVADRIGFYKRYCDILGVGYGDNLDCYNQRPFA
Protein: Barttin (E7F4W6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Chloride channel protein.
- Solute carrier family 12 member 1.
- ATP-sensitive inward rectifier potassium channel 1a.1 isoform X2
- Potassium inwardly rectifying channel subfamily J member 16.
Sequence:
MAENKPYRYGLIVLGMAFVALGMFMISVEEPHVFVTFCAMGVIMMGIGTVWTVCQCYPRVTVILQEKEELCGAEKQDLIEGRSDEKSSAKPVKAPLAGFCDDDEAEISADPKLHTESKRSEHVIVLQTCRSSPSVLTCSSSPQTDRKSSRPDPNREMYYGRVKDSCNVTSELESE
Protein: Cytochrome c oxidase subunit 7C, isoform A (Cytochrome c oxidase subunit 7C, isoform B) (Cytochrome c oxidase subunit 7C, isoform C) (Cytochrome c oxidase subunit 7C, isoform D) (LD14731p) (Q7JW00)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cyclope, isoform A
- Cytochrome c oxidase subunit 4
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 5B, isoform A
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 4
Sequence:
MLGRSSVIARNFSQSMVRFSGHGGVPGENLPFGLTNKYRITALFTIGCVLGFGSPFLIVRHQLLKK
Protein: Transcriptional regulatory protein TcrA (O07776)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the three-protein two-component system HK1/HK2/TcrA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase component HK2
- Sensor histidine kinase component HK1
- Sensor-type histidine kinase PrrB
- Possible exported protein
- Sensor histidine kinase TrcS
- Sensor-like histidine kinase SenX3
- Probable sensor histidine kinase TcrY
- HTH-type transcriptional regulator Cmr
- histidine kinase
- Signal transduction histidine-protein kinase/phosphatase MprB
Sequence:
MADETTMRAGRGPGRACGRVSGVRILVVEDEPKMTALLARALTEEGHTVDTVADGRHAVAAVDGGDYDAVVLDVMLPGIDGFEVCARLRRQRVWTPVLMLTARGAVTDRIAGLDGGADDYLTKPFNLDELFARLRALSRRGPIPRPPTLEAGDLRLDPSEHRVWRADTEIRLSHKEFTLLEALIRRPGIVHTRAQLLERCWDAAYEARSNIVDVYIRYLRDKIDRPFGVTSLETIRGAGYRLRKDGGRHALPR
Protein: Thymidylate synthase (TS) (TSase) (EC 2.1.1.45) (P04818)
Organism: Homo sapiens (Human)
Function: Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:21876188}. Cytoplasm {ECO:0000269|PubMed:21876188}. Mitochondrion {ECO:0000269|PubMed:21876188}. Mitochondrion matrix {ECO:0000269|PubMed:21876188}. Mitochondrion inner membrane {ECO:0000269|PubMed:21876188}.
Interaction partners:
- Dihydrofolate reductase 2, mitochondrial
- Dihydrofolate reductase
- Deoxycytidylate deaminase
- Serine hydroxymethyltransferase, cytosolic
- Thymidylate kinase
- Serine hydroxymethyltransferase, mitochondrial
- Thymidine kinase 2, mitochondrial
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Folylpolyglutamate synthase, mitochondrial
Sequence:
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV
Protein: Probable cold shock protein A (P9WP75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized protein
- Small ribosomal subunit protein uS12
- Elongation factor Tu
- ATP-dependent RNA helicase DeaD
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein bL36
- ESAT-6-like protein EsxO
- ESAT-6-like protein EsxW
- Large ribosomal subunit protein bL31
- ESAT-6-like protein EsxJ
Sequence:
MPQGTVKWFNAEKGFGFIAPEDGSADVFVHYTEIQGTGFRTLEENQKVEFEIGHSPKGPQATGVRSL
Protein: Pheromone-regulated membrane protein 9 (DUP240 protein PRM9) (P39551)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in endoplasmic reticulum exit trafficking of proteins.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12101299}; Multi-pass membrane protein {ECO:0000269|PubMed:12101299}.
Interaction partners:
- Putative uncharacterized membrane protein YAR047C
- Uncharacterized protein YAR061W
- Putative uncharacterized protein YGL052W
Sequence:
MSPQYHFYFVSFRNLVLNEKCLRSKKQVMKSFNWYKTDRYFDPHNILQHHSRAIEKTRYKLGMQTSSESTDAKSDFLDEPSAYLIEKNVALPKDIFGSYLSYWIYEVTRHKAAVILLVLIVTSILLLVFFYNTEFCVAFEILLFSFCFPGTCMVVIAFSEPIGDREFKVKLLMEIITRKPAVKGKEWRTITYKMNQYLFDHGLWDTPYYFYRDEDCHRYFLSLIKGRTFKKQKESSASNVKDAQSNDETAGTPNEAAESSSFSAGPNFIKLLTKAAEIEQQFQKEYWRQEYPGVDEFF
Protein: Cotton fiber protein (A4GVG5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEVKQKWQIRLGMLTPRWMKLVQMLRYQKLQRLAKKKRLLVLKKPRLQWRFKRNLQKLVAQMGLKLQKKGKPLLKRCHKLRQRRMVHVRNNQKTQKL
Protein: R-spondin-2 (Roof plate-specific spondin-2) (hRspo2) (Q6UXX9)
Organism: Homo sapiens (Human)
Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. During embryonic development, plays a crucial role in limb specification, amplifying the Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3, hence governing the number of limbs an embryo should form.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8BFU0}.
Interaction partners:
- E3 ubiquitin-protein ligase ZNRF3
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Leucine-rich repeat-containing G-protein coupled receptor 4
- E3 ubiquitin-protein ligase RNF43
- Leucine-rich repeat-containing G-protein coupled receptor 6
- Keratin, type II cytoskeletal 71
- Receptor-type tyrosine-protein phosphatase kappa
- Fibroblast growth factor 5
Sequence:
MQFRLFSFALIILNCMDYSHCQGNRWRRSKRASYVSNPICKGCLSCSKDNGCSRCQQKLFFFLRREGMRQYGECLHSCPSGYYGHRAPDMNRCARCRIENCDSCFSKDFCTKCKVGFYLHRGRCFDECPDGFAPLEETMECVEGCEVGHWSEWGTCSRNNRTCGFKWGLETRTRQIVKKPVKDTILCPTIAESRRCKMTMRHCPGGKRTPKAKEKRNKKKKRKLIERAQEQHSVFLATDRANQ
Protein: 1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC 1.1.1.267) (A0A1U9X9N3)
Organism: Thymus vulgaris (Thyme)
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). Required for chloroplast development.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250|UniProtKB:Q9XFS9}.
Interaction partners:
Sequence:
PLAKKHNVKILPADSEHSAIFQCIQGLPEGALRRIILTASGGAFRDLPVEKLKEVKVADALKHPNWNMGKKITVDSATLFNKGLEVIEAHYLFGAEYDDIEIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTLSWPERVYCSEITWPRLDLCNVDLTFKKPDHVKYPSMDLAYAAGRAGGTMTGVLSAANEKAVEMFIDEKISYLD
Protein: aminodeoxychorismate synthase (EC 2.6.1.85) (Para-aminobenzoate synthase) (p-aminobenzoic acid synthase) (Q4WDI0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- tryptophan synthase
- Tryptophan synthase
- Anthranilate phosphoribosyltransferase, putative
- Aminodeoxychorismate lyase
- Chorismate synthase
- Chorismate mutase
- MSF1 domain protein
- anthranilate synthase
- Folic acid synthesis protein FOL1
Sequence:
MAPFIGDDERASGSGQPSDSSVDAPARRNVLYIDAYDSFSYNVVAMLEEVLDVRVSVMTIDSDWPDGNMVEYLQHFEAVVLGPGPGDPNVAKDVGIMRDVWTLSGADMLPVFGICLGFQSLCLHQGIPIGRLPYPLHGQVHRIKTVNRDIFENVQDVEVTLYHSLYARLDSPEQSTRGVDSGNPQADRFASKDLDLLAWFLLEDGETQIPMAVRHQKRPIWGVQFHPESCKSDREACVKLLRRWWDMALNYNKKTGRGGYGILLNSNHCASGSITLPDAASTMLDWSTSTSSCSSYRTFTARNLDAEVVCENLNAPNSPTVLFQSNGRYSIISVPSPNSWRLEYYCETQSLLLEKLQDRRGTEIGPTRQSVAESIVERSLTVSQFWDVLRFVTDTKKVDSGSLTVPFWGGFLGYFSYEMGLACLARPKTAAGIHTTCENENAGEDPADASLLWTERSIVVDHKTGQITVQSTRVDDDLPRGWLHQAVQFLQDLAITRSQCKVYTSDTTAEFLDSILKRSVIKFPTQENYQRQIRACQAELEAGESYELCLTGETLITLPSPVSQSGRASFPWELYKRLRKYNPAAFSGFARLGHVKIASSSPECFLNWDRDSTLEMKPMKGTVRKTEDMTMEKAREILGSTKEMAENLMIADLIRHDLYGICGSGGVHVEKLLEVEDHGRVYQMITHVKAKVDRSRPGFAARDMPQLPSSNMSGYGLTALQRCLPPGSMTGAPKERSCMHLSSIEDRKRGIYSGVMGFLDLGGGGSFSVLIRTAFTCSNEQDDEQLWRIGAGGAVTTLSTPEGEWDEMLTKLRTVCGIFAPLNP
Protein: Putative uncharacterized protein BUD30 (Q12064)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MSTSLLFSLSPSSSSSMRLRASNSFPILNFFLDLDATPSLSSSSASFSELSAPLSIVSRPFCTRDDPLPSDLMNPLLKSPFSLTKFPAANGPLEITCVLFKYLAIRLCWPPAPVTLLFLLLKCFLSLPLLDSSSSFTLDAAASLSSLDFLATAFGLNFNEGLADPPPLEEESFNDGKRPFPLLLLILNECYPA