wanglab/gogpt-training-data huggingface dataset:
Protein: Protamine-2 (Sperm histone P2) (Sperm protamine P2) [Cleaved into: PP2-A; PP2-C; PP2-D; PP2-B (Protamine mP2)] (P07978)
Organism: Mus musculus (Mouse)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus. Chromosome {ECO:0000269|PubMed:28366643}.
Interaction partners:
- Nuclear transition protein 2
- Adenylate cyclase type 5
- Spermatid nuclear transition protein 1
- Calmodulin-like protein 4
- Calmodulin 5
- Calmodulin-4
- Calmodulin-like protein 3
- Calmodulin-1
- A-kinase anchor protein 5
- A-kinase anchor protein 1, mitochondrial
Sequence:
MVRYRMRSPSEGPHQGPGQDHEREEQGQGQGLSPERVEDYGRTHRGHHHHRHRRCSRKRLHRIHKRRRSCRRRRRHSCRHRRRHRRGCRRSRRRRRCRCRKCRRHHH
Protein: Receptor-like serine/threonine-protein kinase SD1-8 (EC 2.7.11.1) (Arabidopsis thaliana receptor kinase 3) (S-domain-1 (SD1) receptor kinase 8) (SD1-8) (O81905)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of cellular expansion and differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14506206}; Single-pass type I membrane protein {ECO:0000269|PubMed:14506206}.
Interaction partners:
- U-box domain-containing protein 8
- Signal transducer, putative
- AT4g21620/F17L22_80
- AT3g15480/MJK13_14
- Lysine-specific demethylase JMJ28
- Protein LURE 1.1
- Subtilisin-like protease SBT3.1
- Pentatricopeptide repeat-containing protein At4g21170
Sequence:
MRGLPNFYHSYTFFFFFLLILFPAYSISANTLSASESLTISSNNTIVSPGNVFELGFFKPGLDSRWYLGIWYKAISKRTYVWVANRDTPLSSSIGTLKISDSNLVVLDQSDTPVWSTNLTGGDVRSPLVAELLDNGNFVLRDSKNSAPDGVLWQSFDFPTDTLLPEMKLGWDAKTGFNRFIRSWKSPDDPSSGDFSFKLETEGFPEIFLWNRESRMYRSGPWNGIRFSGVPEMQPFEYMVFNFTTSKEEVTYSFRITKSDVYSRLSISSSGLLQRFTWIETAQNWNQFWYAPKDQCDEYKECGVYGYCDSNTSPVCNCIKGFKPRNPQVWGLRDGSDGCVRKTLLSCGGGDGFVRLKKMKLPDTTTASVDRGIGVKECEQKCLRDCNCTAFANTDIRGSGSGCVTWTGELFDIRNYAKGGQDLYVRLAATDLEDKRNRSAKIIGSSIGVSVLLLLSFIIFFLWKRKQKRSILIETPIVDHQLRSRDLLMNEVVISSRRHISRENNTDDLELPLMEFEEVAMATNNFSNANKLGQGGFGIVYKGKLLDGQEMAVKRLSKTSVQGTDEFKNEVKLIARLQHINLVRLLACCVDAGEKMLIYEYLENLSLDSHLFDKSRNSKLNWQMRFDIINGIARGLLYLHQDSRFRIIHRDLKASNILLDKYMTPKISDFGMARIFGRDETEANTRKVVGTYGYMSPEYAMDGIFSMKSDVFSFGVLLLEIISSKRNKGFYNSDRDLNLLGCVWRNWKEGKGLEIIDPIITDSSSTFRQHEILRCIQIGLLCVQERAEDRPTMSLVILMLGSESTTIPQPKAPGYCLERSLLDTDSSSSKQRDDESWTVNQITVSVLDAR
Protein: Biogenesis of lysosome-related organelles complex 1 subunit BLS1 (BLOC-1 subunit BLS1) (BLOS1-homolog) (Q06071)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex involved in endosomal cargo sorting.
Subcellular location: Endosome {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit KXD1
- Biogenesis of lysosome-related organelles complex 1 subunit SNN1
- Biogenesis of lysosome-related organelles complex 1 subunit VAB2
- Biogenesis of lysosome-related organelles complex 1 subunit BLI1
- Biogenesis of lysosome-related organelles complex 1 subunit CNL1
Sequence:
MFLTFSMCVNWIIVKMPNRSEELDRLLDKIINSPHRTEASKTLQEIENNQSYILNVQLKKLLRLHDDSFKNKCVSPINYMLEKYTPYMGHTEALQKEAELVDRDLRILEMTYQLIEKNRNSK
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102) (O55029)
Organism: Mus musculus (Mouse)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit epsilon
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- ADP-ribosylation factor GTPase-activating protein 2
- Bifunctional glutamate/proline--tRNA ligase
- Coatomer subunit zeta-2
Sequence:
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKGFQPSRPTAQQEPDGKPASSPVIMASQTTHKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD
Protein: Polyhomeotic distal, isoform A (Q9W523)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Polycomb group protein Pc
- Polycomb group protein Psc
- Polycomb protein PHO
- Polyhomeotic-proximal chromatin protein
- Polycomb group protein Asx
- Polycomb protein esc
- Polycomb protein esc
- Polycomb protein Su
- Pipsqueak, isoform M
Sequence:
MPHGFGAAPSVSVSGDTESESATTIRTPPPSPEATTSVKVNSTTRVDPQRPLRCLETLAQKAGISFDEDFAKSPSQSPSSKAARGSVGTPSIRRRHPLLPLSSRSPSAPDSKTTGRKLEKSQSPAQQVAAATNVPLQISPEQLQQLYANNPYAIQVKQEFPTHTTSGSGTELKHATNIMEVQQQLQLQQQLSEANGGGAASAGAGGAASPANSQQSQQQQHSTAISTMSPMQLAAATGGVGGDWTQGRTVQLMQPSTSFLYPQMIVSGNLLHPGGLGQQPIQVITAGKPFQGNGPQMLTTTTQNAKQMIGGQAGFAGGNYATCIPSNHNQSPQTVLISPVNVISHSPQQQQNLLQSMAAAAQQQQLTQQQQQQLNQQQQQLNQQQQQQQLTAALAKVGVDAQGKLAQKVVQKVTTTSSTVQAATGPGSTGSTQTQQVQQVQQQQQQTTQTTQQCVQVSQSTLPVGVGGQSVQTAQLLNAGQAQQMQIPWFWQNAAGLQPFGSNQIILRNQPDGTQGMFIQQQPATQTLQTQQNQIIQCNVTQTPTKARTQLDALAPKQQQQQQQVGTTNQTQQQQLAVATAQLQQQQQQLTAAALQRPGAPVMPHNGTQVRPASSVSTQTAQNQSLLKAKMRNKQQPVRPALATLKTEIGQVAGQNKVVGHLTTVQQQQQATNLQQVVNAAGNKMVVMSTTGTPITLQNGQTLHAATAAGVDKQQQQLQLFQKQHILQQQMLQQQIAAIQMQQQQAAVQAQQQQQQQVSQQQQVNAQQQQAVAQQQQAVAQAQQQQREQQQQVAQAQAQHQQALANATQQILQVAPNQFITSHQQQQQQQLHNQLIQQQLQQQAQAQVQAQVQAQAQQQQQQREQQQNIIQQIVVQQSTGATSQQQQQQPQQQSGQLQLSSVPFSVSPSMTAEDIAGITSSALQEALSVSGAIFQTTKPITCSSSTLPTSSVVTITSQSSTPLVTSSTVASMQQAQTQGTQIHQHQQLISATIAGGSQQQQQQQQLGLPSLTPTTPSPTTNPILAMTSMMNATVGHLSTAPPVSVSSTAVTPSSGQLVTLSSASSGGGAGFPATPTKETPSKGPTATLVPIDSPKTPVSGKDTCTTPKSSTPATVSASVEASSSTGEALSNGDASDRSSTPSKGATTPTSKQSNAAVQPPSSTIPNSVSGKEEPKLTTCGSLTSATSTSTTTTITNGIGVARTTASTAVSTASTTTTSSGTFTTSCTSTTTTTTSSISNGSKDLPKAMIKPNVLTHVIDGFIIQEANEPFPVTRQRYADKDVSDEPPKKKATMQEDIKLSGIASAPGSDMVACEQCGKMEHKAKLKRKRYCSPGCSRQAKNGIGGVGSGETNGLGTGGIVGVDAMALVDRLDEAMAEEKMQTESYQTVSDALPIQAATPEVPPISMPVLAAMSTSSPLSLPLTLPLPIAIAPTVSLPVVSAGVVAPVLAIPSSNINGSDRPPISSWSVEEVSNFIRELPGCQDYVDDFIQQEIDGQALLLLKENHLVNAMGMKLGPALKIVAKVESIKEVPPGDVKD
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (E1JH26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- P-type Cu
- Extracellular superoxide dismutase
- Copper transport protein ATOX1
- superoxide dismutase
- Superoxide dismutase
- Gemini, isoform C
- Copper transport protein
- Protein Malvolio
- Copper transport protein
- Cytochrome c oxidase assembly protein COX11
Sequence:
MSSIKIEFAVQMRRGDESYAGALRSALDGVGQVEIDTQEGRVIIQTQRPWSEIQDKIEATGVRAVLSGFGGQSAVALINTTGSVVDKTPIQGVVRFTTITADKKPGVVVDGVVDGLSPGLHGLHIHESGDTSAGCSSVGEHYNPRQSPHGSPAAGAEERHAGDLGNIRADENGRATFRFVDPVLEVWDIIGRAVVLTANADDLGRGGNDQSLIDGNSGERIACGIIARSAGILENFKRICACDGVTLWDERNKPLAGKERSQKL
Protein: Ribonuclease P protein subunit RPR2 (EC 3.1.26.5) (RNA-processing protein RPR2) (RNase P 16.4 kDa subunit) (P40571)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease P/MRP protein subunit RPP1
- RNases MRP/P 32.9 kDa subunit
- Ribonucleases P/MRP protein subunit POP6
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease MRP protein subunit RMP1
- Ribonucleases P/MRP protein subunit POP7
- Ribonucleases P/MRP protein subunit POP3
- Ribonuclease P protein component, mitochondrial
Sequence:
MGKKAHGGKMKPEIDENGTLLVPPPRTIANQDHFHRLNYLYQISAYQTRARQKARTDAHTPLARNYIKSMDLISKKTKTSLLPTIKRTICKKCHRLLWTPKKLEITSDGALSVMCGCGTVKRFNIGADPNYRTYSEREGNLLNS
Protein: Osteocrin (Musclin) [Cleaved into: Processed Osteocrin] (P61366)
Organism: Homo sapiens (Human)
Function: Hormone that acts as a regulator of dendritic growth in the developing cerebral cortex in response to sensory experience. Induced in the brain following membrane depolarization and inhibits dendritic branching in neurons of the developing cortex. Probably acts by binding to natriuretic peptide receptor NPR3/NPR-C, thereby preventing binding between NPR3/NPR-C and natriuretic peptides, leading to increase cGMP production (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:14523025}.
Interaction partners:
- Atrial natriuretic peptide receptor 3
- C-type natriuretic peptide
Sequence:
MLDWRLASAHFILAVTLTLWSSGKVLSVDVTTTEAFDSGVIDVQSTPTVREEKSATDLTAKLLLLDELVSLENDVIETKKKRSFSGFGSPLDRLSAGSVDHKGKQRKVVDHPKRRFGIPMDRIGRNRLSNSRG
Protein: RILP-like protein 2 (Rab-interacting lysosomal-like protein 2) (Q99LE1)
Organism: Mus musculus (Mouse)
Function: Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (By similarity). Plays a role in cellular protein transport, including protein transport away from primary cilia. May function via activation of RAC1 and PAK1 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23264467}. Cell projection, cilium {ECO:0000269|PubMed:23264467}.
Interaction partners:
- Ras-related protein Rab-8A
- Ras-related protein Rab-10
- Unconventional myosin-Va
- Melanophilin
- Ras-related protein Rab-8B
- Ras-related protein Rab-7L1
- Protein phosphatase 1H
- Ras-related protein Rab-36
Sequence:
MEDHPVREEEDGEEDEGALAKSPLQLTTDDVYDISYVVGRELMALGSDPRVTRLQFKIVRVMEMLETLVNEGSLAVEELRMERDNLKQEVEGLRKAGVSGAQVNLGPDKMVVDLTDPNRPRFTLQELREVLQERNKLKSQLLLVQEELQCYRSGLLPPRETPGGRREKDAVVAMGNGEKEERTIMKKLFSFRSGKHT
Protein: Chitin synthase 2 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 2) (P14180)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Required for septum formation (Probable).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytokinesis protein 2
- Cytokinesis protein 3
- Chitin synthase 3
- Ingression protein 1
- UDP-N-acetylglucosamine pyrophosphorylase
- Ras GTPase-activating-like protein IQG1
- Chitin synthase export chaperone
- Chitin synthase 1
- Myosin-1
- Chitin synthase regulator SKT5
Sequence:
MTRNPFMVEPSNGSPNRRGASNLSKFYANANSNSRWANPSEESLEDSYDQSNVFQGLPASPSRAALRYSPDRRHRTQFYRDSAHNSPVAPNRYAANLQESPKRAGEAVIHLSEGSNLYPRDNADLPVDPYHLSPQQQPSNNLFGSGRLYSQSSKYTMSTTSTTAPSLAEADDEKEKYLTSTTSYDDQSTIFSADTFNETKFELNHPTRQQYVRRANSESKRRMVSDLPPPSKKKALLKLDNPIPKGLLDTLPRRNSPEFTEMRYTACTVEPDDFLREGYTLRFAEMNRECQIAICITMYNEDKYSLARTIHSIMKNVAHLCKREKSHVWGPNGWKKVSVILISDGRAKVNQGSLDYLAALGVYQEDMAKASVNGDPVKAHIFELTTQVSINADLDYVSKDIVPVQLVFCLKEENKKKINSHRWLFNAFCPVLQPTVVTLVDVGTRLNNTAIYRLWKVFDMDSNVAGAAGQIKTMKGKWGLKLFNPLVASQNFEYKISNILDKPLESVFGYISVLPGALSAYRYRALKNHEDGTGPLRSYFLGETQEGRDHDVFTANMYLAEDRILCWELVAKRDAKWVLKYVKEATGETDVPEDVSEFISQRRRWLNGAMFAAIYAQLHFYQIWKTKHSVVRKFFLHVEFLYQFIQMLFSWFSIANFVLTFYYLAGSMNLVIKHGEALFIFFKYLIFCDLASLFIISMGNRPQGAKHLFITSMVILSICATYSLICGFVFAFKSLASGTESHKIFVDIVISLLSTYGLYFFSSLMYLDPWHMFTSSIQYFLTLPAFTCTLQIFAFCNTHDVSWGTKGSTQESKQLSKAIVVQGPDGKQIVETDWPQEVDKKFLEIKSRLKEPEFEESSGNEKQSKNDYYRDIRTRIVMIWMLSNLILIMSIIQVFTPQDTDNGYLIFILWSVAALAAFRVVGSMAFLFMKYLRIIVSYRNKVEGSGSWEVSKLDLPNVFHKKG
Protein: KIAA0040 (A0A384DVV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHYVHVHRVTTQPRNKPQTKCPSGGQSQGPRGQFLDTVLAAMCPIAMLLTADPGMPPTCLWHTPHAKHKEHLSIHLNMVPKCVHMHVTHTHTNSGSRYVGKYILLIKWSLAMYFVQGSTLSTVTKMSHGKALPDSDTYIQFPNQQGPHTPSIP
Protein: Flagellar assembly factor FliW (P96503)
Organism: Bacillus subtilis (strain 168)
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 (hag), which is implicated in polymerization, and participates in the assembly of the flagellum. An antagonist to translational regulator CsrA, it binds CsrA at an allosteric site and non-competitively inhibits CsrA binding to hag RNA. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA and inhibits CsrA binding to mRNA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates. Binds to CsrA and displaces it from hag mRNA. Binds to hag mRNA itself, but only at much higher concentrations than those required to displace CsrA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185, ECO:0000305}.
Interaction partners:
- Translational regulator CsrA
- Flagellar hook-associated protein 3
- Flagellin
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 2
- Uncharacterized protein YviE
- Flagellar motor switch protein FliM
- Uncharacterized protein YvyC
- Negative regulator of flagellin synthesis
Sequence:
MIIHTKYHGQMNIKEEQIILFESGIPGFLEEKQFVILPLSEDSPFVALQSVTSENLAFIVVSPFIFFKNYEFDLDESTAELLDIDNIQDVEVMTILTMAEPFEKSTANLLAPIIVNRKNMMAKQVVLHDSSYTTKHPIGGESC
Protein: Ankyrin repeat and sterile alpha motif domain-containing protein 1B (Amyloid-beta protein intracellular domain-associated protein 1) (AIDA-1) (E2A-PBX1-associated protein) (EB-1) (Q8BIZ1)
Organism: Mus musculus (Mouse)
Function: Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.
Subcellular location: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 4]: Postsynaptic density. Cell projection, dendritic spine. Nucleus.
Interaction partners:
- Ras/Rap GTPase-activating protein SynGAP
- Disks large homolog 4
Sequence:
MGKDQELLEAARTGNVALVEKLLSGRKGGILGGGSGPLPLSNLLSIWRGPNVNCTDSSGYTALHHAALNGHKDIVLKLLQYEASTNVADNKGYFPIHLAAWKGDVEIVKILIHHGPSHSRVNEQNNENETALHCAAQYGHSEVVAVLLEELTDPTIRNSKLETPLDLAALYGRLRVVKMIISAHPNLMSCNTRKHTPLHLAARNGHKAVVQVLLEAGMDVSCQTEKGSALHEAALFGKVDVVRVLLETGIDANIKDSLGRTVLDILKEHPSQKSLQIATLLQDYLEGAGRSAAVLEEHAQEDTAQETHLSSPAESPQKTKSETVTGELSKLLDEIKLCQEKDYSFEDLCHTISDHYLDNLSKISEEELGKNGSQSVRTSSTINLSPGEVEDEEEDPNSCGPTGLWEALTPCNGCRNLGFPMLAQESYPKKRNFPMEMEPSASLDTFPSENENFLCELVDTAVTKKPCSLEIARAPSPRTDNASEVAITAPGTSHHRNSSTGPTPDCSPPSPDTALKNIVKVIRPQPKQRTSIVSSLDFQRMNHNQEYFEISTSTGCTSFTSSPAASPPTSSVETTEVKNEGAEHADDLSQQEDDEPPKEYDAGQFAGLLHGSSPACESPENPFHLYGKRNTCEDGPDEASLANSPLPFKQTPIENNPEPSVKKVKPKVVSRTIFHKRNHQLENHTIVGTRMSRSGSRNGDQWGVNPGGFVERACTLGRIRSLPKALIDMHLSKNVSKSDSDLIAYPSKDKARVNWSKSSTAERSSKDNSERTPSFTSEWEEIDKIMNSIDVGINSELEGMNGETTRPRCPVQTVGQWLESIGLPQYENHLMANGFDSVQFMGSNVMEDQDLLEIGILNSGHRQRILQAIQLLPKMRPIGHDGYHPTSVAEWLDSIELGDYTKAFLINGYTSMDLLKKIWELELINVLKISLIGHRKRILASLGDRLHDDPPQKPPRSITLREPSGNHTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRRNENYFDDIPRSKLERQMAQTGDWGEPSITLRPPNEATASTPVQYWQHHPEKLIFQSCDYKAFYLGSMLIKELRGTESTQDACAKMRANCRKSTEQMKKVPTIILSVSYKGVKFIDAANKNIIAEHEIRNISCAAQDPEDLSTFAYITKDLKSNHHYCHVFTAFDVNLAYEIILTLGQAFEVAYQLALQARKGGHSSTLPESFENKPSKPIPKPRVSIRKSVQIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Protein: Beta-1,4-galactosyltransferase 4 (Beta-1,4-GalTase 4) (Beta4Gal-T4) (b4Gal-T4) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Lactotriaosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.275) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 4) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 4) (O60513)
Organism: Homo sapiens (Human)
Function: Galactose (Gal) transferase involved in the synthesis of terminal N-acetyllactosamine (LacNac) unit present on glycan chains of glycoproteins and glycosphingolipids. Catalyzes the transfer of Gal residue via a beta1->4 linkage from UDP-Gal to the non-reducing terminal N-acetyl glucosamine 6-O-sulfate (6-O-sulfoGlcNAc) in the linearly growing chain of both N- and O-linked keratan sulfate proteoglycans. Cooperates with B3GNT7 N-acetyl glucosamine transferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Transfers Gal residue via a beta1->4 linkage to terminal 6-O-sulfoGlcNAc within the LacNac unit of core 2 O-glycans forming 6-sulfo-sialyl-Lewis X (sLex). May contribute to the generation of sLex epitope on mucin-type glycoproteins that serve as ligands for SELL/L-selectin, a major regulator of leukocyte migration. In the biosynthesis pathway of neolacto-series glycosphingolipids, transfers Gal residue via a beta1->4 linkage to terminal GlcNAc of a lactotriaosylceramide (Lc3Cer) acceptor to form a neolactotetraosylceramide.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:32827291}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:32827291}.
Interaction partners:
- Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
- Beta-1,3-galactosyltransferase 5
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- Beta-1,3-galactosyltransferase 1
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Lactosylceramide 4-alpha-galactosyltransferase
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Beta-1,3-galactosyltransferase 2
Sequence:
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKGKTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKALQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLEALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSREQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAERMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA
Protein: STAS domain-containing protein (Q5B9Q0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sulfate transporter family protein
Sequence:
MPGDIPTKVGHGLAKVLRLKLPEKPQPDAVTRGESTFSVGTFDTYSYVEPEPTAAEWFAEITPSWKEIGLYFYRLFPFLSWITRYNTTWLIGDLVAGITVGAVVVPQGMAYAQLAQLPVEYGLYSSFMGVLIYWFFATSKDITIGPVAVMSTLVGNIVTEAAETLPDVEPHVIASCLAVICGGIVTFMGLARLGFIVDFIPLPAITAFMTGSAINICSGQVSTMLGETDKVNTRGATYNTIIQTLRALPSSTLDAAMGVTACAMLYIIRFACNTAAKKQPHRAKMWFFISTLRTVFVILFYTMISAATNLHRRDNPAFKVLGTVPRGFKHAAVPTVNAEIIKTFASELPAAVIVLLIEHIAISKSFGRVNNYTIDPSQELVAIGVTNLLGPFLGGYPATGSFSRTAIKSKAGVRTPLAGVITAVVVLLAIYALPALFWYIPKASLAGVIIHAVGDLITPPNVVYQFYRVSPLDCVIFFVGVIVTVFTSIEIGVYCTVCISVAVLLFRVAKARGEFLGRVTIHSVVGDHVLEESKPGLGDADRTRSIFLPLNHADGSNPEIEIEQPYPGIFIYRFSEGFNYPNANHYTDYLVETIFQKTRRTNPFTYSNPGDRPWNNPGPRKGKQEEDRSHLPTLRAVILDFSSVNNVDVTSVQNLIDVRNQLDIYASPHTVQWHFAHVKNRWTKRALAAAGFGYPTPQSEDGFHRWKPIFSVTEIEGQSSAAAHAEIVANENTRQASSHGHDLESGIKNPSHTAERETHGIEESSNSSIGEDDKLQRDLKDSKAYQNRRKMAVVQGVNLPFFHIDITSALESALANSQEEPADVSSD
Protein: Caffeyl-CoA reductase-Etf complex subunit CarE (EC 1.3.1.108) (Electron transfer flavoprotein large subunit) (ETFLS) (Electron transfer flavoprotein subunit alpha) (Alpha-ETF) (H6LGM8)
Organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
Function: Caffeyl-CoA reductase-Etf complex catalyzes the reduction of caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. The electron transfer flavoprotein (Etf) mediates the electron transfer between the different donors and acceptors. The iron-sulfur cluster may be involved in electron transport, possibly in the intramolecular electron transfer from the Etf protein subunit to the caffeyl-CoA reductase subunit inside the complex. The complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23479729}.
Interaction partners:
- Caffeyl-CoA reductase-Etf complex subunit CarC
- Caffeyl-CoA reductase-Etf complex subunit CarD
- Lactate dehydrogenase
- Acyl-CoA synthetase
- Pyruvate:ferredoxin oxidoreductase
- Iron hydrogenase HydB
- NADH:quinone oxidoreductase subunit G
- NADH:quinone oxidoreductase subunit F
- NmrA-like domain-containing protein
- NADH-quinone oxidoreductase subunit F
Sequence:
MAIKVIEEKCIGCSKCQKSCPFDAITIENKIAVIGDACTNCGTCIDVCPTEAILQEGTEKIVRDLSMYKGVWVFAEQREGKIMPVVFELLGEGKKLANEIGTELCAILCGSNVAELTDELFAYGADKVYLADAPELEKYTTDGYSKIINEAIGLYKPEIVLYGATHIGRDLAPCLAVKVNTGLTADCTKLEIDPDDKKIRQTRPAFGGNLMATIVCPGSRPQMSTVRPGVMDKAAYDPSQKGEVIKLDATFNEGDIRTKVLEIVKTTTDNISISDADFIVSGGMGLGKPEGFELLKQLADKLGGTVATSRACVDAGWADHAQQVGQTGTTVKPQIYFACGISGAIQHIAGMQDSDIIIAINKNENAPIFEVADYGIVGDLYKVIPAIIEELDKIGK