wanglab/gogpt-training-data huggingface dataset:
Protein: 1-deoxy-D-xylulose-5-phosphate synthase (EC 2.2.1.7) (1-deoxyxylulose-5-phosphate synthase) (DXP synthase) (DXPS) (P9WNS3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Interaction partners:
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- Thiazole synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- 1-deoxy-D-xylulose-5-phosphate synthase
Sequence:
MLQQIRGPADLQHLSQAQLRELAAEIREFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPIIFDTGHQAYVHKMLTGRSQDFATLRKKGGLSGYPSRAESEHDWVESSHASAALSYADGLAKAFELTGHRNRHVVAVVGDGALTGGMCWEALNNIAASRRPVIIVVNDNGRSYAPTIGGVADHLATLRLQPAYEQALETGRDLVRAVPLVGGLWFRFLHSVKAGIKDSLSPQLLFTDLGLKYVGPVDGHDERAVEVALRSARRFGAPVIVHVVTRKGMGYPPAEADQAEQMHSTVPIDPATGQATKVAGPGWTATFSDALIGYAQKRRDIVAITAAMPGPTGLTAFGQRFPDRLFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQIMMDVALHKLPVTMVLDRAGITGSDGASHNGMWDLSMLGIVPGIRVAAPRDATRLREELGEALDVDDGPTALRFPKGDVGEDISALERRGGVDVLAAPADGLNHDVLLVAIGAFAPMALAVAKRLHNQGIGVTVIDPRWVLPVSDGVRELAVQHKLLVTLEDNGVNGGAGSAVSAALRRAEIDVPCRDVGLPQEFYEHASRSEVLADLGLTDQDVARRITGWVAALGTGVCASDAIPEHLD
Protein: Testis-expressed protein 264 (Putative secreted protein Zsig11) (Q9Y6I9)
Organism: Homo sapiens (Human)
Function: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}; Single-pass type III membrane protein {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}. Cytoplasm, cytosol {ECO:0000269|PubMed:32152270}. Nucleus {ECO:0000269|PubMed:32152270}. Chromosome {ECO:0000269|PubMed:32152270}. Note=Is trafficked from tubular ER to growing autophagosomes via its cytosolic LIR motif (PubMed:31006537). Also found in the cytosol, nucleus and chromatin (PubMed:32152270). In response to formation of covalent DNA-protein cross-links (DPCs), localizes to the nuclear periphery, and associates with DNA replication forks (PubMed:32152270). {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:32152270}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Cell cycle progression protein 1
- Translocation protein SEC62
- Atlastin-3
- Reticulophagy regulator 1
- Reticulon-3
- Gamma-aminobutyric acid receptor-associated protein-like 2
Sequence:
MSDLLLLGLIGGLTLLLLLTLLAFAGYSGLLAGVEVSAGSPPIRNVTVAYKFHMGLYGETGRLFTESCSISPKLRSIAVYYDNPHMVPPDKCRCAVGSILSEGEESPSPELIDLYQKFGFKVFSFPAPSHVVTATFPYTTILSIWLATRRVHPALDTYIKERKLCAYPRLEIYQEDQIHFMCPLARQGDFYVPEMKETEWKWRGLVEAIDTQVDGTGADTMSDTSSVSLEVSPGSRETSAATLSPGASSRGWDDGDTRSEHSYSESGASGSSFEELDLEGEGPLGESRLDPGTEPLGTTKWLWEPTAPEKGKE
Protein: Calmodulin-like protein 10 (22 kDa calmodulin-like calcium-binding protein) (CABP-22) (P30187)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Plasma membrane-associated cation-binding protein 1
- Mitogen-activated protein kinase 8
- Kinesin-like protein KIN-14E
- Calmodulin-binding transcription activator 3
- Two pore calcium channel protein 1
- CDPK-related kinase 1
- Calreticulin-3
- Calreticulin-1
- Calreticulin-2
- Heat shock 70 kDa protein 4
Sequence:
MANKFTRQQISEFREQFSVYDKNGDGHITTEEFGAVMRSLGLNLTQAELQEEINDSDLDGDGTINFTEFLCAMAKDTYSEKDLKKDFRLFDIDKNGFISAAEMRYVRTILRWKQTDEEIDEIIKAADVDGDGQINYREFARLMMAKNQGHDTKYDTTGGTLERDLAAGVAKNIIAAPMTDFIKNLFEALFS
Protein: Cyclin-T2 (CycT2) (Q7TQK0)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin T) complex, also called positive transcription elongation factor B (P-TEFB), which is proposed to facilitate the transition from abortive to production elongation by phosphorylating the CTD (carboxy-terminal domain) of the large subunit of RNA polymerase II (RNAP II). The activity of this complex is regulated by binding with 7SK snRNA (By similarity). Plays a role during muscle differentiation; P-TEFB complex interacts with MYOD1; this tripartite complex promotes the transcriptional activity of MYOD1 through its CDK9-mediated phosphorylation and binds the chromatin of promoters and enhancers of muscle-specific genes; this event correlates with hyperphosphorylation of the CTD domain of RNA pol II. In addition, enhances MYOD1-dependent transcription through interaction with PKN1 (By similarity). Involved in early embryo development.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23060074}. Nucleus {ECO:0000269|PubMed:23060074}. Note=Nucleus in differentiating cells. {ECO:0000269|PubMed:23060074}.
Interaction partners:
- Cyclin-dependent kinase 9
- AF4/FMR2 family member 4
- AF4/FMR2 family member 1
- Bromodomain-containing protein 4
- Cyclin-dependent kinase 13
- RNA polymerase II elongation factor ELL2
- Cyclin-T1
- Cyclin-dependent kinase 12
- RNA polymerase II elongation factor ELL
- RNA polymerase II elongation factor ELL3
Sequence:
MASGRGASSRWFFTREQLENTPSRRCGVEADEELSHRQQAANLIQDMGQRLNVSQLTINTAIVYMHRFYMHHSFTKFNRNIISPTALFLAAKVEEQARKLEHVIKVAHACLHPLEPLLDTKCDAYLQQTQELVLLETIMLQTLGFEITIEHPHTDVVKCTQLVRASKDLAQTSYFMATNSLHLTTFCLQYKPTVIACVCIHLACKWSNWEIPVSTDGKHWWEYVDPTVTLELLDELTHEFLQILEKTPSRLKRIRNWRAMAKKPKVDGQVSETPLLGSSLVQNSILVDSVTGVPANPSFQKPSTSTFPAPIPLNSGSTSVQDSRASDNLSVLAAGMPSTSYSLSSHQEWPQHPDSARTDPVYTQKQEATLSGSQYISFQQGPSMALHSGLHHRPDKVADHSSAKQEYTHKAGSSKHHGPIPATPGMLPQKMSLDKYREKRKLETLDVDTRDHYLAAHAEQQHKHGPAQAVTGTSVTSPIKMKLPLTNSDRPEKHVAEKKERSGSLKLRIPIPPPDKGPSKEELKMKIKVASSERHSSSDEGSGKSKHSSPHISRDHKEKHKEHPANRHHSSHKYLHMHSGGSKHTADGMPPTVLRSPVGLGPEGVSSASSARKKLHSSEASHNHHSKMSKSSKSAGSSSSSSSVKQYLSSHSSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVEPHGPEANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM
Protein: HTH cro/C1-type domain-containing protein (Q9I063)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Uncharacterized protein
- PA2779 family protein
- Peptidase M48, Ste24p
Sequence:
MLGTRLKAARIRAGYSQKQLGMLVGMDEFSASARMNQYERERHSPNMRTSEQLAMVLQVPMAYLYCPEDELAELILKVSSLTPEFKKELTRFIEQLLAAQGSTSRQPVRTRSEL
Protein: Immune-related lectin-like receptor 3 splice variant b (Immune-related, lectin-like receptor 3 isoform b) (Q24K31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGSVYENSVFAFSTGNSDENDSQYKGHFSNYRESKREVNTAKWTKVLLIVFAVSLVFALGGLCAVRIQYVSVSAQLSAQETNGTMLMKELTANYSRVKEQLSISEETVRRLSRFNQSSGCAICAIHWTHSGEKCYYFSTVKMNWTQSRDHCVTKGGHLVIITSQAEQEFLTSNVKETHWIGLNDLDTEGRWLWVDNQPLSQTEEFWMKRENGVSEPDNWTKQHVDGEDCASLGHPDGETDFWTDAYCFEEKRFVCEAAAAV
Protein: Uncharacterized protein (Q389E6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKYLENTTTIVKPNGKKNGLTKSSSECINYSLCEGADCNARADLQEGGASCPCSPPLAAERMGCEQQKYAASSLGDGQHRGKRGRGGEVSNGNCENVLPEASPCVSAEVSASSIVHSAVAVGASPVTLESRKETERRGKRISWHDDENGGVESDSLSSSSLRSGAKRRIDNMFIYPREQLSLPKVITENTPYCERQNDDGTSYISYKLQGPSRRFTMWRQRPVSGDCEGRKESKFEDQPCGNRPHKRINSLFSSIYESYDPKSDEQTVQLRIATFDEESEVNGALCAGNLQMPFACVSRITNDPVPIPLAPSTEPKNAQVNGQHS
Protein: Ribosomal protein L5a (EC 3.6.5.3) (Q7ZUI0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein eL42
Sequence:
MGFVKVVKNKSYFRRYQVKFRRRREGKTDYFARKRLVIQDKNKYNTPKYRMIIRFSNRDIVCQIAYAKIEGDAIVCAAYSHELPKYGIACGLTNYAAAYCTGLLCARRLLNKFGLDKVYEGQVEVTGDEFNVESIDGQPGAFSCYLDAGLTRTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHILGLNVSEYMSLLMEEDEELYKKQFSRFIKNGVTPESIEEMYKKAHASIRENPVHERKPKREVKKKRWNRAKLTLAQRKDRVAQKKASFLRAQEAAADD
Protein: Seminal vesicle secretory protein 3A (Seminal vesicle secretory protein III) (SVS III) (F2Z472)
Organism: Mus musculus (Mouse)
Function: Component of the copulatory plug.
Subcellular location: Secreted {ECO:0000269|PubMed:11723121}.
Interaction partners:
- Seminal vesicle secretory protein 6
- Seminal vesicle secretory protein 5
- Ubiquitin-like protein FUBI
- Seminal vesicle secretory protein 4
- H/ACA ribonucleoprotein complex subunit 3
- H/ACA ribonucleoprotein complex subunit DKC1
- H/ACA ribonucleoprotein complex subunit 1
- Prostate and testis expressed protein 4
- Amine oxidase
- Semenogelin 1
Sequence:
MKSIFFSLSLLLLLEKKAAGIELYAGGTKGHFLVKTSPLMFIGKNQFLYGHKEEQEEAPEESIFVQTKHHEYGQDADADMGGALSSQELTSLKEDIVCEEEDELAQQKSQLPSQSQIKSQTQVKSYAAQLKSQPGQLKTIGQVKSQTMLKSHGAPLKSFKARLNLREDIPQQVKGRGYGLAEDLAQVRQQPAKVHRLKGKHRQSRKTAAFYPQFRRRSRPYPRYFVQFQEQLQGSVHHTKSFYPGPGMCYCPRGGVILYQDAFTD
Protein: Fumarate reductase (CoM/CoB) subunit B (EC 1.3.4.1) (Thiol:fumarate reductase subunit B) (D9PUX5)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the reduction of fumarate with reduced coenzyme M (CoM-S-H) and coenzyme B (CoB-S-H). In vitro, is able to reduces fumarate with reduced benzyl viologen, oxidize CoM-S-H and CoB-S-H to CoM-S-S-CoB with methylene blue, and reduce CoM-S-S-CoB with reduced benzyl viologen. The enzyme has specificity for the two thiol compounds as the CoB--CoM heterodisulfide reductase. The enzyme is very sensitive to oxygen.
Subcellular location: Cytoplasm {ECO:0000303|PubMed:2499256}.
Interaction partners:
- Fumarate reductase
- Conserved iron-sulfur cluster binding protein
- Succinate--CoA ligase subunit alpha
- Predicted rRNA methylase
- Fumarase related protein
- Predicted fumarate hydratase
- Succinate--CoA ligase subunit beta
- Predicted fumarate hydratase
- Fumarate hydratase
- H
Sequence:
MINVKVLRFEPGVDEKPHLESYDIPSKEKMKVLDALQLINKMYNANIAFRSSCRAGQCGSCAVKMNGEVVLACRAEVEDGAVIEPVDLPVIKDLMVDRSEIEDKVRAMGLYLQSEARGIQRIKPEDYQDTKKLRGCIECFSCISSCPVIKESTEYAGPYFMRYISKFAFDPRDEAERAAGGVEEGLYCCTTCGKCAEVCPKELNVPGDAIEKLRAMACREGAGPLDAHRKIKKLISETGRSVDHIGKGFIESVGQNPGSRIGFFTGCLVDYRMPDVGMALLRVLREHGFEVDVPDGQVCCGSPMIRTGQLDIVEDLVERNRRALEGYDTIITVCAGCGATLKKDYPRYGVELNVLDISEFLADRIDDIKMKPVNMRVTYHDPCHLLRGQGVKLEPRKILNSIPGLEFVEMEKQGQCCGSGGGVKSGKPEIAESLGKKKAEMIRKLNVDAVITICPFCQLHIKDSLEKEGLGDVKVMNILELLDMAYSDD
Protein: Heat-inducible transcription repressor HrcA (P9WMK3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Interaction partners:
- Chaperone protein DnaJ 2
- Protein GrpE
- Chaperone protein DnaK
- Co-chaperonin GroES
- Probable heat shock protein transcriptional repressor HspR
- Chaperonin GroEL 1
- Chaperonin GroEL 2
- Chaperone protein DnaJ 1
- Ribosomal RNA small subunit methyltransferase E
- Hypothetical alanine and valine rich protein
Sequence:
MGSADERRFEVLRAIVADFVATQEPIGSKSLVERHNLGVSSATVRNDMAVLEAEGYITQPHTSSGRVPTEKGYREFVDRLEDVKPLSSAERRAIQSFLESGVDLDDVLRRAVRLLAQLTRQVAVVQYPTLSTSTVRHLEVIALTPARLLMVVITDSGRVDQRIVELGDVIDDHQLAQLREILGQALEGKKLSAASVAVADLASQLGGAGGLGDAVGRAATVLLESLVEHTEERLLLGGTANLTRNAADFGGSLRSILEALEEQVVVLRLLAAQQEAGKVTVRIGHETASEQMVGTSMVSTAYGTAHTVYGGMGVVGPTRMDYPGTIASVAAVALYIGDVLGAR
Protein: Leukocyte cell-derived chemotaxin 1 (Chondromodulin) [Cleaved into: Chondrosurfactant protein (CH-SP); Chondromodulin-1 (Chondromodulin-I) (ChM-I)] (O75829)
Organism: Homo sapiens (Human)
Function: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization.
Subcellular location: [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage.; SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Leukocyte cell-derived chemotaxin-2
Sequence:
MTENSDKVPIALVGPDDVEFCSPPAYATLTVKPSSPARLLKVGAVVLISGAVLLLFGAIGAFYFWKGSDSHIYNVHYTMSINGKLQDGSMEIDAGNNLETFKMGSGAEEAIAVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGAVTKQSISSKLEGKIMPVKYEENSLIWVAVDQPVKDNSFLSSKVLELCGDLPIFWLKPTYPKEIQRERREVVRKIVPTTTKRPHSGPRSNPGAGRLNNETRPSVQEDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVIMPCSWWVARILGMV
Protein: UPF0187 domain membrane protein (AFU_orthologue AFUA_5G06660) (Q5BB29)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDGGTAHSAPPADAGHAAAHTDGPAPVQAETRHANNAQGQHSGPPSEKSSSPGRMTPRPTFLENLADSRDSQFMLNRRDSDDLDRYFHGPRDLDKHSKWPIMMRMHGSIMPKMILPITFVAGWSTCITLISRFVYRLSVDNILLTVLGFVVGLSLSFRSSTAYERWADGRKYWSLLVQTSRNLSRTIWINTLEREGELGKEDLLRKLTAINLILAFAVALKHKLRFEPDVGYEDLAGLVGYLDTFAKEAHDRQVIQPRKRTIWKVTGEYLGVSFAESNPRKLIKRSKKPLGHLPLEILNHLSAYIDSVIRNETLNISLHQSQAIACLAQLNEVVTGTERVLDTPLPVAYSIAIAQIAWIYVLVLPFQLYDSLGWVTIPGSIVAAYIILGLATIGSEIENPFGHDVNDLPLDTYCRQIALELDIVTAVPPPSVDEFTSREDNYVLYPLSTSGQPEWKERSVEDIRAALRAKVVANTSPTASKTSTVLEEVNTKLNKQSSV
Protein: Glucosyltransferase 3 (EC 2.4.1.-) (A0A0M3KKZ0)
Organism: Streptococcus agalactiae serotype III (strain COH1)
Function: Required for polymorphic O-glycosylation of the serine-rich repeat protein Srr2. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Srr2; does not use other sugar nucleotides as substrates. Complements deletion of the gtf3 gene from S.parasanguinis strain FW213.
Interaction partners:
Sequence:
MRTYITNLNGHSITSTAQIAQNMVTDIAVSLGFRELGIHSYPIDTDSPEEMSKRLDGICSGLRKNDIVIFQTPTWNTTTFDEKLFHKLKIFGVKIVIFIHDVVPLMFDGNFYLMDRTIAYYNEADVLIAPSQAMVDKLQSYGLTVKKILVQGMWDHPTNITLQAVNHKKLVHFPGNPERFNFIKNWRIPTELHVYTDHNMQLPTTVVKEPYQSDEQLIMKMSEGGYGLVWMDDRDKQYQSLYCPYKLGAYIAAGIPVIIQKGIANQDIIEKNNLGFIIEKIDDISNIVESTTEEEYMEIVSDVRRFNPLVRQGYFTRKLLTDAVFSALNSM
Protein: PABIR family member 1 (Q6P4D5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAQEKMKLGFKSLPSSTTADGNILRRVNSAPLINGLGFNSQVLQADMLRIRTNRTTFRNRRSLLLPPPPFHGSISRLHQIKQEEAMDLINRETMSEWKLQSEIQISHSWEEGLKLVKWHFNINQKRFSKAQPTCFLLILPNCQKIMCIYFQLLLMETTAMLDLLVIRQLKSALSQTLLCHLLILVLICSSRQTFN
Protein: Ammonium transporter Rh type C-like 2 (Rhesus blood group family type C glycoprotein-like 2) (Rh family type C glycoprotein-like 2) (Rh type C glycoprotein-like 2) (drRhcg1) (Q8JI14)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions as an ammonia transporter. May play a role in the elimination of ammonia in the gill (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sodium/hydrogen exchanger
- Carbonic anhydrase
- Sodium/hydrogen exchanger
- Urea transporter
- Anion exchange protein
- Facilitated urea transporter
- ATP-sensitive inward rectifier potassium channel 1a.1 isoform X2
- Carbonic anhydrase
- Apolipoprotein D
- Carbonic anhydrase II
Sequence:
MGNCFGSRGICDRPKNTNIRLSLPAVCFVWQVSMIILFGVFVRYNEEADTNWVYTKKEKNITSDIENDFYFRYPSFQDVHVMIFVGFGFLMTFLKRYSFGAVGFNFLIAAFGLQWALLMQGWFSPLGDDGKIKIGIENLINADFCVASCLIAYGAVLGKVSPVQLLVMTLFGITLYAVEEFIILRVLNAKDAGGSMVIHTFGAYYGLSISRVLYRPNLNKSKHMNGSVYHSDVFAMIGTLFLWMFWPSFNSAICNHGDGQHRAAINTYLALASTVLTTVAISSMFEKTGKLDMVHIQNSTLAGGVAVGTAAEFMLMPYGSLIVGFFCGIISTLGYIYLTPFLEERLKIQDTCGIHNLHAMPGVIGGIVGAISAAAASKEVYGDLGLKNIFSIEGSNVTRLPTVQGGYQAAALCVALCFGIGGGTFVGLVLKLPIWGDPADEHCFNDEMYWEVPEDEESIIPPVLSYNNHMIPNNKHEEMRETNFAEQS
Protein: 5-formyltetrahydrofolate cyclo-ligase, mitochondrial (5-FCL) (EC 6.3.3.2) (Q8L539)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to tetrahydrofolate metabolism and photorespiration through the regulation of serine hydroxymethyltransferase. Prefers the pentalutamyl to the monoglutamyl form of 5-formyltetrahydrofolate.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:12207015}.
Interaction partners:
- 5-formyltetrahydrofolate cyclo-ligase-like protein COG0212
- Formate--tetrahydrofolate ligase
- GTP cyclohydrolase 1
- 10-formyltetrahydrofolate synthetase
- 10-formyltetrahydrofolate synthetase
- Bifunctional protein FolD 2
- Bifunctional protein FolD 1
- Phosphoribosylglycinamide formyltransferase, chloroplastic
- Bifunctional protein FolD 4, chloroplastic
- Bifunctional protein FolD 3, chloroplastic
Sequence:
MIGARVFCITTTALRRSPIFFFPKIPTRPVFRLSPATRPIVAMSTTSKNQEELDSIFKQKRVVRSTVRKSLKAMDPSLRTQQDEAIQKTVLEAPWFKSCKGLCAYISCKSLNEVDTSKILSEILQHPDSNTQKKLYVPWVEDKNSNMRMLHISHMEDLVANSMNILEPAPVDAQGNDREDVLQADEPIDLFILPGLAFDRCGRRLGRGGGYYDTFLKRYQDRAKEKGWRYPLMVALSYSPQILEDGSIPVTPNDVLIDALVTPSGVVPITPRATESM
Protein: Inositol phosphorylceramide synthase catalytic subunit aur1 (IPC synthase catalytic subunit aur1) (EC 2.-.-.-) (Aureobasidin A resistance protein homolog) (Phosphatidylinositol:ceramide phosphoinositol transferase) (Q10142)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inositol phosphorylceramide synthase regulatory subunit kei1
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Large ribosomal subunit protein uL11m
- Alpha-galactosidase mel1
- L-2-aminoadipate reductase
Sequence:
MSALSTLKKRLAACNRASQYKLETSLNPMPTFRLLRNTKWSWTHLQYVFLAGNLIFACIVIESPGFWGKFGIACLLAIALTVPLTRQIFFPAIVIITWAILFYSCRFIPERWRPPIWVRVLPTLENILYGSNLSSLLSKTTHSILDILAWVPYGVMHYSAPFIISFILFIFAPPGTLPVWARTFGYMNLFGVLIQMAFPCSPPWYENMYGLEPATYAVRGSPGGLARIDALFGTSIYTDGFSNSPVVFGAFPSLHAGWAMLEALFLSHVFPRYRFCFYGYVLWLCWCTMYLTHHYFVDLVGGMCLAIICFVFAQKLRLPQLQTGKILRWEYEFVIHGHGLSEKTSNSLARTGSPYLLGRDSFTQNPNAVAFMSGLNNMELANTDHEWSVGSSSPEPLPSPAADLIDRPASTTSSIFDASHLP
Protein: oleoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.14) (Q8MR70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LSVELDLGKEENVYLAGHTIDGRVLFPATGYMTLAWMSLAQQQGLDYLRTPVLFEDVVFHRATILSVGTVVKLTLNFFPGSSSFEICEGTSLVTSGKIRLVSNVQQEQLQLSSLPGIAGSNKLSTKDIYKELRLRGYDYTGVFQGILESDISAVTGQLQWADNWISFMDTMLQFRILSNDIRELYVPTGIERALIDPLKHLELAKKHQQKLTVNWHRNISVVKCGGVEIHKMKTAQTQRRSGGQSPPSLERYRFWPHSQHLGQREEQEKSRSTALAVAIQLIIENSGGAVKLKGVELAGSRSTLDALSAVQLLELIEREPILVGDMAVVTSSSNESELGEQLKEHGIRVIVKDIKAGAVEQQCHFVYSVNMLAQNSVKDLQHCLDSLKSDSGFLLLEEAASRYNIIGKEKLNKLKLVSVLEQFFGTDRVLVLVRKLSKVQSSQALTLHLTNKQFKWVNELKNSIAKAQAEEKNLYLVAQGEPNSGALGLMNCLKREAGGHFLRLYLILDEGVPQFSLDDPFYAAQLAKDLVVNVYRNGSWGSYRHLKMESRPPMLPVEQAYVNTLVKGDLSSLRWIESPRSSPIQSQLEPCTVYYAPLNFRDVMLASGKLGVDALPGDLAYQDCVLGLEFAGRDSCGRRVMAMVTAKSLATNCLANRNLLWEVPSKWTMEQASTVPCVYATVYYALVVRGQMKEGERILIHAGSGGVGQAAISVALAHGLTVFTTVGSKEKREFLLKRFPKLKAKNIGNSRDTSFEQLIMSETHGNGVELVLNSLSEEKLQASIRCLALNGRFLEIGKFDLSNNTPLGMSVFLKNTSFHGILLDSVMEGEEEMQLMVAKLVAEGIKSGAVQPLPTTVFAEQEIEKAFRFMASGKHIGKVVIKVRLEEEQQAALPRLRQIQAIPRSYMHPEKSYILVGGLGGFGLELANWLVSRGARFLVLSSRSGVKSGYQALMIRRWHDRGVQVQIDTNDVTTAVGCQRLLEVSNKLALVGGIFNLAAVLRDGLIEDQSPKNFEKVSAPKLLATIHLDKISREICPALEYFVCFSSLSCGRGNMGQTNYGLANSTMERICEQRQEYGYPGTAIQWGAIGDTGLIIEHMGNNETVVGGTLPQRMISCLETLDLFLQQPHPVMASMVVAEKRKTEQANRLSLIATIANIMGLRDVKSVSDKTTLFDLGMDSLMSTEIKQTLERHFDLVLSAQEIRQLTFSALRQIDAQEPPSASVSSPSASSTLSRIKEEACVEVQPQSDETRKVFAKEVLPQEVMVRLRSKAPVASEDPAVFFLAPIEGFTIAVEALAASLTCPAYGLQCTEQVPLDSIEACAAYYLRQIQKLQPLGPYHIVGYSYGCLLAHAIAVALEQRRFGVKVIMLDGAPTMASGYVQEAKKQTDDLNRQQSMTLAYFGALLADVDYNQLLQLLDGVQTWPSKLDKLADTLAGYTQQTREVIKKAACMFKQKLLLSESYKGAKQLHSDVVLIKSAEHNAIMAQDYGLKEICSAQIDMHVVEGTHRTFLKEPHTLQIIERVLRKRP
Protein: B3 domain-containing protein At5g06250 (Q9FNI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- Polyketide cyclase/dehydrase/lipid transport superfamily protein
- Protein CUP-SHAPED COTYLEDON 3
- Cytochrome P450 78A5
Sequence:
MSVNHYSTDHHHTLLWQQQQHRHTTDTSETTTTATWLHDDLKESLFEKSLTPSDVGKLNRLVIPKQHAEKYFPLNAVLVSSAAADTSSSEKGMLLSFEDESGKSWRFRYSYWNSSQSYVLTKGWSRFVKDKQLDPGDVVFFQRHRSDSRRLFIGWRRRGQGSSSSVAATNSAVNTSSMGALSYHQIHATSNYSNPPSHSEYSHYGAAVATAAETHSTPSSSVVGSSRTVRLFGVNLECQMDENDGDDSVAVATTVESPDGYYGQNMYYYYSHPHNMVILTLL
Protein: Gibberellin 2-beta-dioxygenase 1 (EC 1.14.11.13) (Gibberellin 2-beta-hydroxylase 1) (Gibberellin 2-oxidase 1) (GA 2-oxidase 1) (OsGA2ox1) (Q5W726)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development. Controls the level of bioactive GAs in the shoot apical meristem, which regulates the vegetative to reproductive phase transition. In vitro, converts GA1, GA4, GA9, GA20, and GA44 to the corresponding 2-beta-hydroxylated products GA8, GA34, GA51, GA29, and GA98, respectively.
Interaction partners:
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 3
- Gibberellin 3-beta-dioxygenase 2
- Os05g0257800 protein
- Gibberellin 3-beta-dioxygenase 1
- Os04g0517600 protein
Sequence:
MVVPSATTPARQETVVAAAPPAAAASGVVGGGGGVTIATVDMSAERGAVARQVATACAAHGFFRCVGHGVPAAAPVAARLDAATAAFFAMAPAEKQRAGPASPLGYGCRSIGFNGDVGELEYLLLHANPAAVAHRARTIDAMDPSRFSAIVNEYIEAMKKLACEILDLLGEGLGLKDPRYFSKLTTNADSDCLLRINHYPPSCNIHKLDHDDQCNIKSLVSTKASNGGNLMAGGRIGFGEHSDPQILSLLRANDVEGLQVFVPDHEGKEMWVQVPSDPSAIFVNVGDVLQALTNGRLISIRHRVIATACRPRLSTIYFASPPLHARISALPETITASSPRRYRSFTWAEYKTTMYSLRLSHSRLELFKIDDDDSDNASEGKA