wanglab/gogpt-training-data huggingface dataset:
Protein: Receptor-type guanylate cyclase gcy-6 (EC 4.6.1.2) (N1NVB7)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward the salt ion Mg(2+) and to a lesser extent toward Cl(1-) in ASE left (ASEL) sensory neuron.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIGVYLRSVIFPLLFVIQTICQPPGNVFHLGFLHCDVLENNVEGSTTYINYRTSASAASIAIDKIKREGLLLGYDFKFTILYDQCDENIAAGNAIKLFAEHNVDVLFGPTTNNAAMPVFILATYYNIPLITWGITSSATLDDESRFPTAGMLSIGSRSLAVTFREVMKEYGWDQFVFAYSLEMNDEKCETLRDDFQNMVAYYGDIVLSYAVQIMDHSEEGLLAILKDVSTRGRIIVPCFHEGNSRGLHRRWMLVAARNGFVNDEYVYIFPSLRSRGYAVPQADGTFRYPWTEATGPQPGDQEALLGFQKSIFIVDMQGQGNVGSNYTQFEHEIIQRMKEPPYNCTDACASPEYQTAATYAGQLHDSVYIYGVVMDQIMKTVPNQYKNGTAFPRKMAGVFNGVGGTVAIDEGGGLQPTLFVLTLDSNNNSSLIMTVDVDQQEAVVTKHYTNEATALWSHRKGIRPPDQPICGYTGSLCPANVFFQYIGWFIAAIIIIFFTIMGAILAFIYLCHAKQQEVERQNALWQIPFKSMMTVTKKGKGEHSMRSISSVPSTISSTRSSTLSEVGETRNYLFFQIQNDVEMERVAAKKHSIRMVFDNKTCATMRQMRLIDHANLNKFIGMSLDAPQLYSVWRFCSRGSLADVIRKASMQMDGFFIYSLMKDIINGLTWIHESSHEFHGMLTSKNCLLNDRWQLKITDFGLRIFRTHDQYNKSDRLWTSPELLRTDDILGSREGDIYSFGIISAELITRSSVFDLENRKEDAEEIIYMLKKGGLQSPRPSLEHDESIEINPALLHLVRDCWTERPSERPDIKQVASQLRSMNTNRNDNLMDHVFNVLESYASTLEDEVAERMKELVEEKKKSDVLLYRMLPRQVADKLKLGQTVEPETFDIVTLFFSDVVSFTTLAGKCTPLQVVNLLNGLYTIFDGIIEQHDVYKVETIGDGYFVASGVPRRNGNEHTRNIASMSINFVKSLADFSIPHLPGEKIKIRVGFHCGSVVAGVVGLTMPRYCLFGDAVNTASRMESNSKPGQIHLSEEANQMLMRLGGFTTEPRGEVIIKGKGVMATYWLLKMDESAAPKILKKKQD
Protein: AKT-interacting protein (Ft1) (Fused toes protein homolog) (Q9H8T0)
Organism: Homo sapiens (Human)
Function: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14749367}. Cell membrane {ECO:0000269|PubMed:14749367}; Peripheral membrane protein {ECO:0000269|PubMed:14749367}.
Interaction partners:
- FHF complex subunit HOOK-interacting protein 1B
- Protein Hook homolog 2
- Protein Hook homolog 1
- Protein Hook homolog 3
- FHF complex subunit HOOK-interacting protein 1A
- Telomeric repeat-binding factor 1
- Tumor necrosis factor ligand superfamily member 13B
- RAC-alpha serine/threonine-protein kinase
Sequence:
MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT
Protein: Beta,beta-carotene 15,15'-dioxygenase (EC 1.13.11.63) (Beta-carotene dioxygenase 1) (Beta-carotene oxygenase 1) (Q9HAY6)
Organism: Homo sapiens (Human)
Function: Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9I993}.
Interaction partners:
- Intestine-specific homeobox
- Retinol dehydrogenase 10
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Retinol dehydrogenase 12
- Aldehyde dehydrogenase 1A1
- Retinol dehydrogenase 11
- Retinol dehydrogenase 8
- Short-chain dehydrogenase/reductase 3
- Dehydrogenase/reductase SDR family member 9
Sequence:
MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT
Protein: Boron transporter 1 (Q8VYR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Efflux-type boron (B) transporter for xylem loading, responsive of boron translocation from roots to shoots under boron limitation. Boron is essential for maintaining the integrity of plants cell walls.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12447444, ECO:0000269|PubMed:27449211}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:12447444, ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:27449211}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:12447444, ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:27449211}; Multi-pass membrane protein {ECO:0000255}. Note=Transferred from the plasma membrane via the endosomes to the vacuole under high-concentration of boron in a DRP1A-dependent manner (PubMed:16103374, PubMed:20194745, PubMed:27449211). Localized to the polar inner/stele-side domain of the plasma membrane under low-boron conditions, this polar localization is established after cell division (PubMed:27449211). Co-localizes with DRP1A in the cell plate and the plasma membrane (PubMed:27449211). Under boron excess, BOR1 is transferred from the plasma membrane via the endosomes to the vacuole for degradation in a DRP1A-dependent manner (PubMed:16103374, PubMed:20194745, PubMed:27449211). {ECO:0000269|PubMed:16103374, ECO:0000269|PubMed:20194745, ECO:0000269|PubMed:27449211}.
Interaction partners:
- Probable aquaporin NIP5-1
- peptidylprolyl isomerase
- Aquaporin NIP6-1
- Receptor-like cytosolic serine/threonine-protein kinase RBK2
Sequence:
MEETFVPFEGIKNDLKGRLMCYKQDWTGGFKAGFRILAPTTYIFFASAIPVISFGEQLERSTDGVLTAVQTLASTAICGMIHSIIGGQPLLILGVAEPTVIMYTFMFNFAKARPELGRDLFLAWSGWVCVWTALMLFVLAICGACSIINRFTRVAGELFGLLIAMLFMQQAIKGLVDEFRIPERENQKLKEFLPSWRFANGMFALVLSFGLLLTGLRSRKARSWRYGTGWLRSLIADYGVPLMVLVWTGVSYIPAGDVPKGIPRRLFSPNPWSPGAYGNWTVVKEMLDVPIVYIIGAFIPASMIAVLYYFDHSVASQLAQQKEFNLRKPSSYHYDLLLLGFLTLMCGLLGVPPSNGVIPQSPMHTKSLATLKYQLLRNRLVATARRSIKTNASLGQLYDNMQEAYHHMQTPLVYQQPQGLKELKESTIQATTFTGNLNAPVDETLFDIEKEIDDLLPVEVKEQRVSNLLQSTMVGGCVAAMPILKMIPTSVLWGYFAFMAIESLPGNQFWERILLLFTAPSRRFKVLEDYHATFVETVPFKTIAMFTLFQTTYLLICFGLTWIPIAGVMFPLMIMFLIPVRQYLLPRFFKGAHLQDLDAAEYEEAPALPFNLAAETEIGSTTSYPGDLEILDEVMTRSRGEFRHTSSPKVTSSSSTPVNNRSLSQVFSPRVSGIRLGQMSPRVVGNSPKPASCGRSPLNQSSSN
Protein: 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase BtrO (EC 1.14.14.13) (Butirosin biosynthesis protein V) (Q4H4E3)
Organism: Niallia circulans (Bacillus circulans)
Function: NAD(P)H:FMN oxidoreductase component of a two-component system involved in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Together with BtrO, mediates hydroxylation of gamma-L-Glu-GABA-S-BtrI.
Interaction partners:
Sequence:
MDNKERNTLYQVVYAISGVTGEDGDELVETFKQGPMEVDKRDFFEIVQRVESLFDCTLDMNLEGPYLIHADEIVTKITKLNV
Protein: Uncharacterized protein YjiK (P39382)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lipopolysaccharide core heptose
- Lipopolysaccharide glucosyltransferase WaaG
- Phosphoethanolamine transferase EptC
Sequence:
MTKSISLSKRISIIVILFAIVAVCTFFVQSCARKSNHAASFQNYHATIDGKEIAGITNNISSLTWSAQSNTLFSTINKPAAIVEMTTNGDFIRTIPLDFVKDLETIEYIGDNQFVISDERDYAIYVISLTPNSEVKILKKIKIPLQDSPTNCGFEGLAYSRQDHTFWFFKEKNPIEVYKVNGLLSSNELHISKDEALQRQFTLDDVSGAEFNQQKNTLLVLSHESRALQEVTLVGEVIGEMSLTKGSRGLSHNIKQAEGVAMDASGNIYIVSEPNRFYRFTPQSSH
Protein: Protein kinase, putative (C4MBQ2)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Interaction partners:
- SH3 domain-containing protein
- DH domain-containing protein
Sequence:
MSTPYSSIRNIIKEGCVVKQGHIIWNWYNRWLVLTKEQLYYYDESKQKLRGTVPLDFASVKSCEIEDHPFSFEVYCPTQNKTYFFEALSEEERTSWIKKISEVVDISEPTDYHHLTHVAYEEGGFVGIPYEWENVFLACGITREEIKSNKEDAIKVLEFTQIFQDDETEETQKQPLPENDVPVVLKELITSGDPTVLYKDYVPIGEGMSGVVFHCYETSTNKEVAMKKILIKNDSVNIQEIKIMQTLNQRNIVGYLGCYELDNYLYIAMEYMDRNNLTAMLDFFPEFSLSERHIAYVVHESNTALKYLHSLHRIHRDIKSDNILLNHRGEIKLADFGISVQLTKRKSKRNTVVGTPYWMAPEVIKGKDYGTNIDIWSLGIMCREMMEGVPPYIDDPPLRALFKISTKGIPPVQYGDYTPTILDFVDKCLTFDPTKRPDCEELDKDPFMSLACSREEFAEFIQKIVQQAEK
Protein: Leukocyte surface antigen CD53 (Cell surface glycoprotein CD53) (Leukocyte antigen MRC OX-44) (CD antigen CD53) (P24485)
Organism: Rattus norvegicus (Rat)
Function: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250}. Cell junction {ECO:0000250}. Membrane; Multi-pass membrane protein. Note=Concentrates in localized microdomains along the plasma membrane at the contact sites between cells of fused myotubes. {ECO:0000250}.
Interaction partners:
- Lysosomal protein transmembrane 5
- CD48 antigen
- Receptor-type tyrosine-protein phosphatase C
- CD82 antigen
- Integrin beta
- T-cell surface antigen CD2
Sequence:
MGMSSLKLLKYVLFFFNFLFWVCGCCILGFGIHLLVQNTYGILFRNLPFLTLGNVLVIVGSIIMVVAFLGCMGSIKENKCLLMSFFVLLLLILLAEVTLAILLFVYEKKINTLVAEGLNDSIQHYHSDNSTRMAWDFIQSQLQCCGVNGSSDWISGPPSSCPSGADVQGCYKKGQAWFHSNFLYIGIVTICVCVIQVLGMSFALTLNCQIDKTSQALGL
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (E2K) (Q9VGQ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable 2-oxoadipate dehydrogenase complex component E1 homolog
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyl dehydrogenase
- 2-oxoglutarate dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
Sequence:
MTGIISIVTRRLPQTLGMRALRSNEVKRCIRQYSRLVACAAQQQQLLRQDGSNRCQEATRLLTWQGIHTTSSLWSEQTVNVPPFADSIAEGDIKFTCKVGDSFAADEAVMEIETDKTTVAVPAPFSGTLTDILVKDGDTVKPGQALFKIKPGAAPAKAAAPAAAPAPAAPKAAPAPAAAPKPAPPPPAAGAPKPPPPPPPKAAPRPPPPAPVAALKPAVAQVKVPPADGSRQILGTRSEQRVKMNRMRLKIAARLKDAQNTCAMLTTFNEVDMSYAMDFRKQNLDAFTKKYGIKFGFMSIFAKASAYALQDQPVVNAVIDGTDIVYRDYVDISVAVATPRGLVVPVIRNVEGMNYADIEIALAGLADKARRDAITVEDMDGGTFTISNGGVFGSLMGTPIINPPQSAILGMHGIFERPIAVKGEVKIRPMMYIALTYDHRIIDGREAVLFLRKIKAAVENPAIIVAGL
Protein: U-box domain-containing protein 12 (EC 2.3.2.27) (Plant U-box protein 12) (OsPUB12) (RING-type E3 ubiquitin transferase PUB12) (Q5VRH9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses E3 ubiquitin-protein ligase in vitro.
Interaction partners:
Sequence:
MPKRVADEIAALPEPRGPLRRPCADLSRRVRLLAPLLDHLPASSSSSSSTPLADALGAARDLLRKTRDGSKIDQAMRGDAFLDEFAGVNRQIHLALDALPYNTFHMPQEVQEQVALVHSQFQRASTRTDPPDTQLSMDLAWALTDNPSDPALLTRISHKLQLHTMADMKNESIALHNMVISTAGEPDGCVDQMSSLLKKLKDCVVTEDHANDALTTRSASIKHRSPIIPDEFRCPISLELMQDPVIVSSGQTYERSCIQKWLDSGHKTCPKTQQPLSHTSLTPNFVLKSLISQWCEANGIELPKNKQNSRDKKAAKSSDYDHAGLVSLMNRLRSGNQDEQRAAAGEIRLLAKRNVNNRICIAEAGAIPLLVNLLSSSDPRTQEHAVTALLNLSIHENNKASIVDSHAIPKIVEVLKTGSMETRENAAATLFSLSVVDENKVTIGAAGAIPPLINLLCDGSPRGKKDAATAIFNLCIYQGNKVRAVKAGIVIHLMNFLVDPTGGMIDEALSLLSILAGNPEGKIVIARSEPIPPLVEVIKTGSPRNRENAAAILWLLCSADTEQTLAAKAAGVEDALKELSETGTDRAKRKASSILELMHQANEDSLKGNGH
Protein: DNA mismatch repair protein MLH (Q8IIJ0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA mismatch repair protein PMS1, putative
- DNA mismatch repair protein MSH2, putative
- DNA mismatch repair protein MSH2, putative
- Exonuclease 1
- DNA mismatch repair protein
- 3'-5' exonuclease
- FANCJ-like helicase, putative
- DNA mismatch repair protein, putative
- DNA 3'-5' helicase
- DNA 3'-5' helicase
Sequence:
MINEDINICGNINMKDNDRDNDNNDKYNDKYNNNNNDNILMNDSNGDRRIIKLAEEDINRIAAGEVIIRPCNALKELVENSLDANSSSISIHLNKGGLKSLQIIDDGDGIHKEDLRIVCERFTTSKISNHKDIRNIKTFGFRGEALASISHVSYLTITSKKRNSPFCYTCNYKDGKPTQDEPTVCSGKNGTIIRFDDLFYNMPARLKTMNPNDEYNKCLEVLQKYAIHYPNVSFTCKKWLSNTVDLNTQKVGKGIGGYAGIYIIKKKRKERFDENNTTDGNLPCDNNMTCNNLPHDNNITCNNLPHDNNITCNNIPHDNNITCNNLPHDNNITCNNLQHDNNITCNNLPHDNNITCNNLPCDNNHTDKEATDNPDASSCMYNELEKKILEEEKYLDENYEKHLNNVRCVIQKVYGRNISKELSTIFLKEKSIPTFFKCYGLISNPTYNGKKGCYIFFINDRLVESNIIKKSCENQYSNFLAKGNYPWIYLSLRLKYDIVDINVHPTKKEVHFLYQEEISMLIGKKIQEFLKSFHNMRTFNITGEKLLQTKLDINSSMLEIKKEDKELSKLRQGLLHDNNNVIKRQIDTKRVRTDFKQITLTNYFVKKENMIDDHLDNNKSVDMLYNGDHNGDAKQIDLYEHNDEYNKTYDQTNIRANLHMNYNNNNNKIEEKEYEILKLKGPNSVLYNTQIDKHISNKIYDRKYPCEADEISSIKKLKMICEEKEKKELTECLKNSIYVGPVDNMHSLIQYKEKLLLIKMPLIIKEVTYQSILNRLGKIPPFEFDPPIPLYDLLLVAVNNSYSGFYENPNYANKNIEKVCNELEQIFYTYNEMYSDYFSIIIEDGCIVTFPACCGEYFPGQEFLPFLFLRLATQIDYSKEINCINGICYLLANFYSKITLLNDKEWTYQDDLLMIQEKEKEIQMLLNKSNKHINNSNHHNQHYDETNLDYILGDESVVDINKHLSVSRNINLVFEKYFFPMIQLNNIMKIPTTFSNNGYIIELTSLNQLYKIFERC
Protein: Metabotropic glutamate receptor-like protein J (Q75JT4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act during the development and be a negative regulator.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17501984}. Membrane {ECO:0000269|PubMed:17501984}; Multi-pass membrane protein {ECO:0000269|PubMed:17501984}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17501984}. Golgi apparatus membrane {ECO:0000269|PubMed:17501984}. Nucleus envelope {ECO:0000269|PubMed:17501984}. Note=May also localize to internal membranes.
Interaction partners:
Sequence:
MKILLYIAIILSFFSLITISSECKIAVLLSGSPNDLGYNYLMNEARVKAESELKLDFSIYYENLEESMEEAEKAFQDALHKGANLIVVGSFVHVGLGLKYAALTKDQDIYWIIRGNKRPNPDLPHVVILNFNSFELHYLLGYFSGLMTKTGIVGFVAPGPDVNTISTDNSFYLGAKYARPNITFLNVYVQSWYNPNVSYSAAKMLIKNGADLIGMSQDDMSCQKAMMDSGLIGIGATGYPTHLLFGGNVGVSYITNWTNLYVKYAQHVLNDDWPDYSSYFTNLSREDSIFIDDYSYKVPIDIQNLVNDEIQRLKNTSYIPYRSDPYLAQLGIPFDSKGLLVEDQFRANKKLLKGDSISKVIDFGQYSIPIEFIDYPNSLKYGVTIVSGVCIFICLVCMTLVVVFKKARVIKSSSPAFLLLILLGCCIIFAACILFAQSPTNQTCSARIWLLSLGYTLFLGNLLVKNWRIWLLFDNPKLKKRAITNWKLYPWVFAILAIDVMILAIWQGLGNINAESRIGYDSLTQYQYKNVCSSDDQGSIALYLLLVFHGLVLLVACFISFKIKVVDIEEFNESKPITTSVYIITFCLFIVIPLMVSPQSLTSQTTIICVCAIVTTLISMLLLFGSKFYKMATQGLAINETFATSTKSSSKSSKSSYGKDNPNPNAINFGEDDTSDETSEEKHKSPKQKSVNFSNKSNSHLAVFTSDEETSKTSKLSIDFENSSKDISIDQLQQQKQQPINTNGDLENKSNDKIDDDNDNSSVLSKRISNQQNGETEIDSNNV
Protein: S-ribosylhomocysteine lyase (EC 4.4.1.21) (AI-2 synthesis protein) (Autoinducer-2 production protein LuxS) (P45578)
Organism: Escherichia coli (strain K12)
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Interaction partners:
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine gamma-synthase
- Methionine synthase
- Cystathionine beta-lyase MetC
- Autoinducer-2 kinase
- Transcriptional regulator LsrR
- Cysteine synthase A
- Homocysteine S-methyltransferase
- Autoinducer 2-binding protein LsrB
Sequence:
MPLLDSFTVDHTRMEAPAVRVAKTMNTPHGDAITVFDLRFCVPNKEVMPERGIHTLEHLFAGFMRNHLNGNGVEIIDISPMGCRTGFYMSLIGTPDEQRVADAWKAAMEDVLKVQDQNQIPELNVYQCGTYQMHSLQEAQDIARSILERDVRINSNEELALPKEKLQELHI
Protein: Metal transporter cnnm-5 (CNNM family homolog 5) (G5ED05)
Organism: Caenorhabditis elegans
Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-3 and cnnm-4 to regulate Mg(2+) homeostasis.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Membrane Bound O-Acyl transferase, MBOAT
- non-specific serine/threonine protein kinase
- Probable GMP synthase
Sequence:
MSLFLFAIFQLALGSPGAPNGPNVPLQLTGVRRGLDHVQKLPSEAFSFKLFGKNLAEDGYYFTTATRCEDSHLSTVSTVRATVKESYCSYAILSVPEGLPFNVSTSVYHLCHKNATIYTQKFLVVHEKKAAAAKYMGDEIVFCFFCILMSAYASGMTLGYMKFSMIDLNTMLKIAEGDAAKKRVRRIMHFRRRSTQLVVTFSLFSSVFTVLFTTTCEKMLHGVSNEDVLKMAVPALICLIFAEMIPQAVCNSKFGFNLAASLWFVTVIIFFVTLPIAYPASLVLGRFLKRDVREVMTPEEKTCLLRSMAQNEREKTILENATTFTLKKVGQLMVPIEEVFMLSRSQKLNRSTVLTLVEKGYTRIPVYDNKNRSVIVGMLNMKNFNLLMVKTNLIDEPTVKEALHALELLKDRTVKFAVKYVNIEMNAHLLLNRMKTGDFHFACVVEYSAYDSKVVGIITIEDILEKLIGKIDEINELRVRSSIDDRGDNAVIGWCREAGSDKKYPLPFSQQLRILQHLLSECQVLKSLDIGIMKAKQILSLDRIRVGKKNDKLELHDLLLVIFEGTVLVTNEVETFERVIDVPSQRSSSTVNSQQHRQQTTDNSRSTPVPVLIIGKPLLNRLMKSLGSPFSEPLGPKDNVSELVVVSEEASYFKLRLEDLMNSINGCRKVDRNGHTTTGESLLQTLNSRASTSTSTTPACRTPLSVDARSQDETTPFMEKQE
Protein: Kinesin-like protein 1 (Q92376)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Uncharacterized WD repeat-containing protein C32H8.09
- Meiotically up-regulated gene 172 protein
- Kinesin-like protein cut7
- Spindle pole body component alp4
- Dynein heavy chain, cytoplasmic
- Anaphase spindle elongation protein 1
- Microtubule integrity protein mal3
- Phosphoprotein p93
- ADP-ribosylation factor 1
- Tubulin alpha-2 chain
Sequence:
MVIENTKDISINTGYKRQEDALNTDSEDLIYRPKKIIKTNQEDAVHDLKYENFVSKNHVLQSDINGKKRDSNRDKAAVVTAPIASTHESNYEESVSKFKESWLPQLKDLIESHKTICESTLAYESDQAMASSNTLKRIKDLKSKPKNIIQLERLHMLSNGEHRLLSKDETDDIESAYLNLRSHLQVQEQVYAEKDHEYSLQLQSYREAAEKAKQDILETKENLSSELSISNIQLKEAKERLEAANASYQKLRREHKELALYHEKKTHSLVCNLNGERKSFGDFVENEVKSYKHEYANICESLRRALVLIQGSCTEKILRFKEKILDLLEMKQQEENDRISHIEYENDLTVKKLKRRISELEMAVKEYESEKSYSEKEYEEKISSLRIELEDKLAEIDMLRNKLLKEEHKHHSTSEKLEELSKYVASIQDKERNNGQNALELQARIQQLERRNEDMYNKLLAEEIIRRKLHNDIQELKGNIRVFCRVRPLLPSEESEYCIADVLQFPDKDALEPQKLILKGPNVESSLGHTYDRNYEFSFDRVFAPESDNSSVFEEISQLIQSAIDGYNVSIFAYGQTGSGKTYTMSSQDGMIAMSIKHIFNYLSTLREKGWVYKLRGQFLEIYNETIYDLLNKAEMLKNPKHDIHHDEKERRTTVDNVSIIDFNEEDTVYKMLNRAGENRFIAATKANERSSRSHTVFMLYIDGENSRTKQICKGTLNLVDLAGSERLSYSQAVGDRLRETQAINKSLSCLGDVIHALGNASNSTTKEKSHIPYRNSKLTYLLKYSLGKGAKTLMFVNVSPLKSQFMDTLNSLRFATKVNDTKVGSIKHYKR
Protein: Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (K7EMU7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGAQGMGLTRLGDPYHPEG
Protein: Transcription repressor OFP7 (Ovate family protein 7) (AtOFP7) (Q9ZU65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription repressor OFP18
- Transcription repressor OFP15
- Transcription repressor OFP16
- Transcription repressor OFP17
- At2g18890
- Splicing factor 3B subunit 4
- BEL1-like homeodomain protein 1
Sequence:
MTKRFKLKISRILSFKSCRLKDPSSLPFNPVSSSLRRTSPLVNSSADVTTVPQRRRSSFRLHVLTVFGCGRSSTPLDVDLRNSPVLSPPQTPTFQWESEGKWHVIAQVTEEEYETPRRKIYNGGSEKDNRRRLKKKEKSNSRRRGSISSAEEETDRESLLPSSTNLSPEYSSSELPRVTRRPRQLLKKAVIEEESESSSPPPSPARLSSFVQRLMPCTMAAAVMVEGVAVVKKSEDPYEDFKGSMMEMIVEKKMFEVAELEQLLSCFLSLNAKRHHRAIVRAFSEIWVALFSGGSGGGRRSSSFSSVRLSDYDEC
Protein: Zinc finger protein C19B12.07c (Q9P374)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSSDDAIIIRCPFDCEFAGDSISFISHLTTIHNSSVQTLAKNAYLCASEIANELNQNPNLKDQEILLLQIAQENSLKRVLRQQQKERREGKIKSLQCLFCNNEGLLNRQEWFEHSFHVHGLNIGLADNIVYINRLLEKIKNELESFRCLCCHVPCKNKKLLREHMNNKRHFRLDPKSSEYDEFYIINYASVTKSITISHSQFAINEDINETDDTISDINDEDAEPLSVECIFCTNFYEPVFCFEHCKIVHDWDIKKIQKDYSLDVYGAIRVINYSRKTKKKSIPAETDSFWKEPGWLIPVVPDDALIICLSEVIEDPRL
Protein: Inhibin beta A chain (Activin beta-A chain) (P07995)
Organism: Bos taurus (Bovine)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P08476}.
Interaction partners:
- Follistatin
- Activin receptor type-2A
- receptor protein serine/threonine kinase
- Activin receptor type-2B
- Activin receptor type-1C
- Inhibin beta B chain
- Inhibin alpha chain
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta
- Nodal growth differentiation factor
Sequence:
MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALATLPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEIWLFLKVPKANRTRSKVTIRLFQQQKHLQGSLDAGEEAEEVGLKGEKSEMLISEKVVDARKSTWHIFPVSSCIQRLLDQGKSSLDIRIACEQCQETGASLVLLGKKKKKEEEGEGKKRDGEGGAGGDEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
Protein: Endoplasmic reticulum protein SC65 (Leprecan-like protein 4) (Prolyl 3-hydroxylase family member 4) (Synaptonemal complex protein SC65) (Q64375)
Organism: Rattus norvegicus (Rat)
Function: Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92791}.
Interaction partners:
Sequence:
MARAAWGLLWLLLGSAGAQYEKYSFRGFPPEDLMPLATAYGHALEQYEGESWRESARYLEAALRLHRLLRDSEAFCHANCSGPATSQPRPAPGPDGDNEGDGEDWARELRLFGHVLERAACLRRCKRTLPAFQVPYPSRQLLRDFQNRLPYQYLHYAHFKANRLEKAVAAAYTFLQRNPKHELTAKYLNYYRGMLDIGDESLTDLEAQPYEAVFLQAVKLYNSGDFRSSTEHMERALADYMTVFARCLAGCEGAHEQVDFKDFYPAIADLFAESLQCKVDCEANLTPNVGGFFVDKFVATMYHYLQFAYYKLNDVHQAARSAASYMLFDPKDSVMQQNLVYYRFHRARWGLEEEDFQPREEAVLYHNQTSELRELLDFTHMYLQSDDEMELEETESLPEPEKPLSDAEFEGEGDYEEGLYADWWQEPDAKGDEDEAEPEPELA
Protein: Junction adhesion molecule like (E9PJJ4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MFCPLKLILLPVLLDYSLGLNDLNVSPPELTVHVGDSALMGCVFQSTEDKCIFKIDWTLSPGEHAKDEYVLYYYSNLSVPIGRFQNRVHLMGDILCNDGSLLLQDVQEADQGTYICEIRLKGESQVFKKAVVLHVLPEEPKELMVHVGGLIQMGC