wanglab/gogpt-training-data huggingface dataset:
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (Alpha 2,3-ST 1) (Beta-galactoside alpha-2,3-sialyltransferase 1) (EC 2.4.3.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Monosialoganglioside sialyltransferase) (EC 2.4.3.2) (SIATFL) (ST3Gal I) (ST3GalI) (ST3GalA.1) (ST3O) (Sialyltransferase 4A) (SIAT4-A) (Q11201)
Organism: Homo sapiens (Human)
Function: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage. Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (By similarity). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:9182658}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:9182658}; Single-pass type II membrane protein {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans cisternae of Golgi (PubMed:9182658). Secreted into the body fluid. {ECO:0000269|PubMed:9182658}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- C1GALT1-specific chaperone 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4
- Galactoside alpha-
- Beta-1,3-galactosyltransferase 4
- Beta-1,3-galactosyltransferase 5
- Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase
- Galactoside alpha-
Sequence:
MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCTCTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKELFRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEADVGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVKQDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHYWENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
Protein: Ragulator complex protein LAMTOR2 homolog (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2) (Q9V8I2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids.
Interaction partners:
- Ragulator complex protein LAMTOR3 homolog
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR4 homolog
- GH04846p
- GH16429p
- Raptor, isoform B
- Serine/threonine-protein kinase mTor
- GATOR complex protein NPRL2
- FI18258p1
Sequence:
MLKPKALTQVLSQANTGGVENTLLLSQEGALLAYSGYGDKDARITAAIASNIWAAYEKHGRNAFREGRLTFVLIDCENGHVAITQVASVLLCLYAKQTVGLGLLKQKAMSLASYLERPLKQISAS
Protein: Probable methylmalonyl-CoA mutase large subunit (MCM) (EC 5.4.99.2) (P9WJK5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Interaction partners:
- Probable methylmalonyl-CoA mutase small subunit
- Probable GTPase Rv1496
- Conserved protein
- 2-oxoglutarate oxidoreductase subunit KorA
- Succinate--CoA ligase subunit alpha
- Succinate--CoA ligase subunit beta
- Malate dehydrogenase
- Pyruvate carboxylase
- Conserved protein
- Methionine synthase
Sequence:
MTTKTPVIGSFAGVPLHSERAAQSPTEAAVHTHVAAAAAAHGYTPEQLVWHTPEGIDVTPVYIAADRAAAEAEGYPLHSFPGEPPFVRGPYPTMYVNQPWTIRQYAGFSTAADSNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVQGDVGMAGVAIDSILDMRQLFDGIDLSTVSVSMTMNGAVLPILALYVVAAEEQGVAPEQLAGTIQNDILKEFMVRNTYIYPPKPSMRIISDIFAYTSAKMPKFNSISISGYHIQEAGATADLELAYTLADGVDYIRAGLNAGLDIDSFAPRLSFFWGIGMNFFMEVAKLRAGRLLWSELVAQFAPKSAKSLSLRTHSQTSGWSLTAQDVFNNVARTCIEAMAATQGHTQSLHTNALDEALALPTDFSARIARNTQLVLQQESGTTRPIDPWGGSYYVEWLTHRLARRARAHIAEVAEHGGMAQAISDGIPKLRIEEAAARTQARIDSGQQPVVGVNKYQVPEDHEIEVLKVENSRVRAEQLAKLQRLRAGRDEPAVRAALAELTRAAAEQGRAGADGLGNNLLALAIDAARAQATVGEISEALEKVYGRHRAEIRTISGVYRDEVGKAPNIAAATELVEKFAEADGRRPRILIAKMGQDGHDRGQKVIATAFADIGFDVDVGSLFSTPEEVARQAADNDVHVIGVSSLAAGHLTLVPALRDALAQVGRPDIMIVVGGVIPPGDFDELYAAGATAIFPPGTVIADAAIDLLHRLAERLGYTLD
Protein: Chloride intracellular channel protein 1 (Glutaredoxin-like oxidoreductase CLIC1) (EC 1.8.-.-) (Glutathione-dependent dehydroascorbate reductase CLIC1) (EC 1.8.5.1) (Nuclear chloride ion channel 27) (NCC27) (Q9Z1Q5)
Organism: Mus musculus (Mouse)
Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00299}. Nucleus membrane {ECO:0000250|UniProtKB:O00299}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00299}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Cell membrane {ECO:0000250|UniProtKB:O00299}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00299}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6MG61}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). Might not be present in the nucleus of cardiac cells (By similarity). {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q6MG61}.
Interaction partners:
Sequence:
MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAMLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta) (P9WN39)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Also able to use GTP. D-glutamate is a poor substrate, and DL-glutamate shows about 50% of the standard specific activity. Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion. Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (Probable).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9278431}.
Interaction partners:
- Glutamate synthase large chain
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
- NAD-specific glutamate dehydrogenase
- assimilatory sulfite reductase
- Nitrogen regulatory protein P-II
- Glutamate synthase small chain
- Glutamate decarboxylase
- Glutamine--fructose-6-phosphate aminotransferase
- Nitrite reductase small subunit
- Probable glycine dehydrogenase
Sequence:
MTEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEPVNIRPHPYEFALYYDV
Protein: DNAation factor-related protein 1, isoform A (RE40745p) (Q6NR36)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METAANSGDSKKPFKVKDVTRNIKKAVCASSLEEIRSKVAEKFEKCDHLPTIHLDSDGTEIDDEEYFRTLDENTELVAVFPGEHWIDPTHYVTITTPHGNEAGTGNGELNGGGEGDTTDANNSESARIRQLVGQLQNNLCNVSVMNDADLDSLSNMDPNSLVDITGKEFMEQLKDAGRPLCAKRNAEDRLNLLKLLKAGAIFCSERYPEDAEAIDREIGRQLNEAESGQMSTTTTSNTRTIEVVQCDNQNTTITITVGEATTTCATASGAMGSSAAEAAANEANANPNRNPNANGDI
Protein: Putative F-box protein At4g17200 (Q9M0M7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTMSDLSPDLVGEILTRVPMTSLISVRCTCKMWNALSKEGIFFKAARKQFMGFTMMDSRVCSMKFDLQGIRNNEHDFVDPCIKQIAKLDQIEVSKVLQCDGLLLCVGKDNSRLLVWNPYLGQTRFIKPRKRFNKLEWYALGYDNNHNYKILMNYDTGHLFGYEIYDFSSDSWRVLDVSPDCHIPFHQQSVSLNGNTYFLAQEKIIVEGEEEEVVDEIEKFLLCFDFTTERFGPRLPLPFHSDVLETVAISCVRDDQLAVLYQRFETWEIWVTTKIDPTAVSWSMFLSVDMEPPTGCQFDDEAGSFFIDEENKVAVFFNSDLFNPRVENRNRRYPTAYIIGQDGYFKSATLREAPDLVKPDPYVYCCPLVWSSYAPSLVQL
Protein: Krt5 protein (Q6P3K5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSGGMGGGMGGGIRKNFSSMSTSAVPMGSRSSVSFRRSGGGGGGGGFGAGSGGSFSYSMGGGGGGGGSGFGGGFGSGGGFGSGGGFGGGAGFGGGSAYGGGAGFGGGFGPGGVVPITAVTVNQNLLAPLNLEIDPNIQVVRTQEKEQIKTLNNRFASFIDKVRFLEQQNKVLETKWSLLQEQTTTRSNIDAMFEAYIANLRRQLDGLGNEKMKLEGELKNMQNLVEDFKNKYEDEINKRAAVENEFVLLKKDVDAAYMNKVELEAKVDSLQDEINFLRAIFEEELRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAESWYKQKFEEMQSSAGKYGDDLRNTKAEIADLNRMISRLQNEIEAVKGQRANLEAQIAEAEERGELAVKDAKLRIKDLEDALQRAKQDMARQVREYQELMNVKLALDIEIATYRKLLEGEESRIASGGNTATIHIQESSSSSGGGGGGFGYGGGSGYGGGSGFGGGSGYGGGSGFGGGSGFGYGGGSGMSIGGGSGMSMSGGGGGQISMSRSSIVSSQKRRF
Protein: Transcription factor Sox-9 (Xt-sox9) (Q6F2E7)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1. Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis. Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes. Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells. Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). Unlikely to play a role in sex determination but may function during testicular and ovarian differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:18816826}. Cytoplasm {ECO:0000269|PubMed:18816826}. Note=Restricted to the nucleus of Sertoli-like cells in the testis, but localizes to the cytoplasm of previtellogenic oocytes in the ovary before being translocated into the nucleus of vitellogenic oocytes. {ECO:0000269|PubMed:18816826}.
Interaction partners:
Sequence:
MNLLDPFMKMTEEQDKCMSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGDPELKKETEDEKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNEGEKRPFVEEAERLRIQHKKDHPDYKYQPRRRKSVKNGQSEQEDGAEQTHISPNAIFKALQADSPHSASSMSEVHSPGEHSGQSQGPPTPPTTPKTDVQPGKPDLKREGRPLQESGRQPPHIDFRDVDIGELSSEVISTIETFDVNEFDQYLPPNGHPGVGSTQAPYTGSYGINSTPSATPGAGPAWMSKQQQQQQQQPQPPQHSLSTINSEQSQSQQRTHIKTEQLSPSHYSDQQQQHSPQQLNYSSFNLQHYSSSYPTITRAQYDYTEHQGSNSYYSHASGQNSGLYSNFSYMNPSQRPMYTPIADTTGVPSIPQTHSPQHWEQPVYTQLTRP
Protein: Syntrophin-like 1, isoform C (M9PGE3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MVESSSLGRTPPAAQQPIPQQHSPSPSGLRCGNMETRVRGAWYRVLVTLETDFLAVSLDESCEAAQPSNDGQSTTLNGTLGSNHSGGGGGGAGGGGTGGGGQNGTLPNSASLQGMNIQDTELDGSASNDNGDRDPCLNNNNNAGDGGGMDMCDVPDHVANQKRHVRIIKSDNNGLGISIKGGRENRMPILISKIFRGMAADQAKGLYVGDAILTVNGEELRDATHDEAVRALKRSGRVVDLEVKFLREVTPYFRKASIISEVGWELQRAFLCPLGPGVPTSPPAPKTTPRADTRYIPLQLTHLARNLKYIDPENRCFELHSPDGVHSCILRAADSAEALVWFNALHSAMGTSTQRALAEANRALTNLIGELKHIGWLSKRMSGGGSSGSAGGGAASGGSGTSNSVVAGELPSGRSSSESSDESDKWLPIFVAVTEREFRIYESAPWSVEAWSRPLEIYALATTRLAGAGNNSSLNGQQTTVFCVRCGTARGVLVYWLRSETHRDMAAWARSLVQGSHQAVNYQREFSFRCLFQGRQCQLVVHINRGFFLYDCGGFAPTTPTVATAKTQLWQFAFDKLKGSADDGARMLYLDFGEDGEIELDMECCPKPVVFVVHNCLSAKVHNIA
Protein: Phosphatidylethanolamine-binding protein 1 (PEBP-1) (HCNPpp) (Neuropolypeptide h3) (Prostatic-binding protein) (Raf kinase inhibitor protein) (RKIP) [Cleaved into: Hippocampal cholinergic neurostimulating peptide (HCNP)] (P30086)
Organism: Homo sapiens (Human)
Function: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Polyunsaturated fatty acid lipoxygenase ALOX15
- RAF proto-oncogene serine/threonine-protein kinase
- Beta-adrenergic receptor kinase 1
- Serine/threonine-protein kinase B-raf
- Mitochondrial ribosomal protein L40
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS9
Sequence:
MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDSGKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRYVWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKLYEQLSGK
Protein: Large ribosomal subunit protein uL24 (50S ribosomal protein L24) (P60624)
Organism: Escherichia coli (strain K12)
Function: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro.
Interaction partners:
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS17
Sequence:
MAAKIRRDDEVIVLTGKDKGKRGKVKNVLSSGKVIVEGINLVKKHQKPVPALNQPGGIVEKEAAIQVSNVAIFNAATGKADRVGFRFEDGKKVRFFKSNSETIK
Protein: Iron-sulfur assembly protein 2 (Q57W48)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Iron-sulfur cluster assembly protein, putative
Sequence:
MLRTSLFLRCVPPLSAVYGKSFSVTPRVWRRISEKNAEEGYGNDLRYLRLMIESGGCHGYAYKFLFEENSELVADEDVVVAESDVVQLPQPKSQELRTVAEGEGEGDVGESKAKGPPPRLVVDKHSVAKLLSAVVDFHSELKGSAFVVIGNELVDKSCACAMSFSMKKQQQKV
Protein: G patch domain-containing protein 1 homolog (Q9VUA0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- MIP04834p
- WD repeat domain-containing protein 83
- Serine/arginine repetitive matrix protein 1
- RNA helicase
- RING-type E3 ubiquitin transferase
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase
- Serrate RNA effector molecule homolog
- Pleiotropic regulator 1
Sequence:
MDEEEHLHRFGTPLPALQKDVVPAKKPVAIEDQIVKDENGKRRFHGAFTGGFSAGFWNTVGSLEGWTPQTFKSSRGERASSKAQLKPEDFMDQEDLGEFGIAPQGIRTRDEFANEDEQKQRSDQRRRKLMQPELGVGAIPGLPVLEQLLRPVRDKVAVRILKSMGWKPGQGVGPRQTRKEKRQATARNSKEQYLMEHYGAEGLPSNKENKGEEDSNNEDEDDEDITFAPDDYEPIFYTPKENRFGMSYSGLNRDPILSKSSSSSAKPMQHINLFGEMEAQANKKQLSIRGQAFGVGAFEEEDEDIYARDDMTRYDFSLADKKPKQKKQQHVQQRHVIDGFSEDNSPAVLQRPYAIDLPRDFQPRNWLQRRSRFAPMDKERAQKLETASEYKRSGLGRHDLNPDQRAQILGEQQQEEKTAEEQPKRNPFKDHSKSLMERINARTEGFTKGGVITENGEEQQTELAKEVKEANAAIQERAALKTKDLPSAMNSSSAFKPFIADEAKQLRYEKFVSSKLTDDKEITEFLARMQPVTLSLWDREMEKKEFIQAAKIYRPLVGLMNDRFVSEANVQAEKVEQQEKPPEERKIVMERTKTMWKPTALLCKRYNIAEPFGGAMLEPEKELKAKAKISVFDYLETSVNTKANFETPSIFPKHIEKSIPEKVETPPSPPPAPQPEAEIQDKPNTKEEPSKHTFVPKTPLEQAVDESRNKPISEKVDLFKSIFEDSDEEETELSEQDKLAILQESFGLPVTSTTSAAAQNVLRNTSPPRGIFASLFSPKIKDAAKEPAPTKFGPIEGSKLKIAYKPRKERLRNDRELAMAEVAPEDIYGPKLPTAPPQKPAAPEIQAEANIDDRLQQLWQQHAPKKRKAEKWVEKKCISGSEDSDASSSNESSSSDSSDDNDKRSKLSKPKKSHKGSSSKKSKKSKLKSKKKSKKSEESKHKAKKKKKKSKH
Protein: Signal transducer and activator of transcription C (Dd-STATc) (STAT5 homolog C) (Q54BD4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Transcription factor that regulates gene expression during development. May play a role in regulating gene expression in response to osmotic stress.
Subcellular location: Cytoplasm. Nucleus. Note=Tyrosine phosphorylation is not required for translocation to the nucleus. DIF inhibits export from the nucleus. Predominantly nuclear in pstO cells at the rear of the prestalk region in the slug. Subject to crm1-dependent nuclear export.
Interaction partners:
- Tyrosine-protein phosphatase 3
- Dual specificity protein kinase pyk3
- Dual specificity protein kinase splB
- Probable serine/threonine-protein kinase DDB_G0291664
- Basic-leucine zipper transcription factor B
- Protein rtoA
Sequence:
MSNNNPKKRPLDAISNTFEVKQEEPEFSSDGFNTTNDDLMSLMTFLDNGTGQQNQQNQQNQQPQPQPQPQPQLPQPQSQQPIYNSNTTTVTVKTEGIATSPLSNASSPISTNNNINNNTNNNNNNNNNNNNNNNNNNNNNNNINTATPPAIGVQQNSNIPYSYPIYTDVTGQQTQHQQNIGQNSVNIDPYFQTIDGAQIQQQQLLQQQLQPIQQVNNPQIDQAQIQQQQAQQIQQQQAQIQAQQAQIQQQQLEQQHLQQQQFQFQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHHQQQQQQQQHQQQQQHQQQQQHQQHQQQQHQQHQQIHQNHQNQLNHQNQLNNQNQLNNQNQLNNQNQLNHQNQLNQPTQPQMQQIELPILHQLPVEPQHLHPIPTHINNNGNNNNNNNNNGSNSSNSSNGIGSPDDIIEPNILSSIQHCNNNNLPLPDHLLINTPYGNVLQPHQQIINECLKLHLAQKEQLDKMKIVQKQVLAHPQKETFQMLDNEQNTLKKQIDAEITSLQQIDQTFVLSPPEIRNVIFLLHELTIQSIQLELYHEELQLLVRPQNPPPTIAALVVIEQPFPMVITKCKPLEDDPVVVQLLCGTRTELQMIGKVRATMIVENQQGSKTSSSPKTIETEVVSMDETNRLAKYHLKFLNGTRKNPVTLKFGMQVQVVGGTAVNIESPPTSPFIVITNECQYEESDGTLLKKDSFGNNNEIPWASYANKLQRHFLRATRQDFMKPTRYLSRHELMYIHHQFFGSKPMIPQSSFDSFWIWFGKGLQKLRYQRHVCSMWQSGLIYGFISRQSVEEALRNEEQGTFLIRFSERHAGHFAVGYKVDDPDPEKRIRHYLVKADDTAGAKKTLPDFLSECPQFTKILQLTIDVSTGEPRLRNFPKDVVLEPYYSKRETLPATNGYDSLPTIL
Protein: Pyruvate carboxylase 2 (EC 6.4.1.1) (Pyruvic carboxylase 2) (PCB 2) (P32327)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Subcellular location: Cytoplasm.
Interaction partners:
- Pyruvate carboxylase 1
- Pyruvate kinase 1
- Phosphoenolpyruvate carboxykinase
- NAD-dependent malic enzyme, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Malate dehydrogenase, peroxisomal
- Malate dehydrogenase, mitochondrial
- Citrate synthase 3, mitochondrial
- Citrate synthase, peroxisomal
- Citrate synthase, mitochondrial
Sequence:
MSSSKKLAGLRDNFSLLGEKNKILVANRGEIPIRIFRSAHELSMRTIAIYSHEDRLSMHRLKADEAYVIGEEGQYTPVGAYLAMDEIIEIAKKHKVDFIHPGYGFLSENSEFADKVVKAGITWIGPPAEVIDSVGDKVSARHLAARANVPTVPGTPGPIETVQEALDFVNEYGYPVIIKAAFGGGGRGMRVVREGDDVADAFQRATSEARTAFGNGTCFVERFLDKPKHIEVQLLADNHGNVVHLFERDCSVQRRHQKVVEVAPAKTLPREVRDAILTDAVKLAKVCGYRNAGTAEFLVDNQNRHYFIEINPRIQVEHTITEEITGIDIVSAQIQIAAGATLTQLGLLQDKITTRGFSIQCRITTEDPSKNFQPDTGRLEVYRSAGGNGVRLDGGNAYAGATISPHYDSMLVKCSCSGSTYEIVRRKMIRALIEFRIRGVKTNIPFLLTLLTNPVFIEGTYWTTFIDDTPQLFQMVSSQNRAQKLLHYLADLAVNGSSIKGQIGLPKLKSNPSVPHLHDAQGNVINVTKSAPPSGWRQVLLEKGPSEFAKQVRQFNGTLLMDTTWRDAHQSLLATRVRTHDLATIAPTTAHALAGAFALECWGGATFDVAMRFLHEDPWERLRKLRSLVPNIPFQMLLRGANGVAYSSLPDNAIDHFVKQAKDNGVDIFRVFDALNDLEQLKVGVNAVKKAGGVVEATVCYSGDMLQPGKKYNLDYYLEVVEKIVQMGTHILGIKDMAGTMKPAAAKLLIGSLRTRYPDLPIHVHSHDSAGTAVASMTACALAGADVVDVAINSMSGLTSQPSINALLASLEGNIDTGINVEHVRELDAYWAEMRLLYSCFEADLKGPDPEVYQHEIPGGQLTNLLFQAQQLGLGEQWAETKRAYREANYLLGDIVKVTPTSKVVGDLAQFMVSNKLTSDDIRRLANSLDFPDSVMDFFEGLIGQPYGGFPEPLRSDVLRNKRRKLTCRPGLELEPFDLEKIREDLQNRFGDIDECDVASYNMYPRVYEDFQKIRETYGDLSVLPTKNFLAPAEPDEEIEVTIEQGKTLIIKLQAVGDLNKKTGQREVYFELNGELRKIRVADKSQNIQSVAKPKADVHDTHQIGAPMAGVIIEVKVHKGSLVKKGESIAVLSAMKMEMVVSSPADGQVKDVFIKDGESVDASDLLVVLEEETLPPSQKK
Protein: ER degradation-enhancing alpha-mannosidase-like protein 3 (EC 3.2.1.113) (Alpha-1,2-mannosidase EDEM3) (Q9BZQ6)
Organism: Homo sapiens (Human)
Function: Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. May also participate in mannose trimming from all glycoproteins and not just misfolded ones targeted to ERAD. May have alpha 1,2-mannosidase activity (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- ER degradation-enhancing alpha-mannosidase-like protein 2
- Protein sel-1 homolog 1
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Protein OS-9
- Alpha-mannosidase 2
- Endoplasmic reticulum lectin 1
- Calreticulin
- Alpha-1-antitrypsin
- Endoplasmin
- DnaJ homolog subfamily C member 10
Sequence:
MSEAGGRGCGSPVPQRARWRLVAATAAFCLVSATSVWTAGAEPMSREEKQKLGNQVLEMFDHAYGNYMEHAYPADELMPLTCRGRVRGQEPSRGDVDDALGKFSLTLIDSLDTLVVLNKTKEFEDAVRKVLRDVNLDNDVVVSVFETNIRVLGGLLGGHSLAIMLKEKGEYMQWYNDELLQMAKQLGYKLLPAFNTTSGLPYPRINLKFGIRKPEARTGTETDTCTACAGTLILEFAALSRFTGATIFEEYARKALDFLWEKRQRSSNLVGVTINIHTGDWVRKDSGVGAGIDSYYEYLLKAYVLLGDDSFLERFNTHYDAIMRYISQPPLLLDVHIHKPMLNARTWMDALLAFFPGLQVLKGDIRPAIETHEMLYQVIKKHNFLPEAFTTDFRVHWAQHPLRPEFAESTYFLYKATGDPYYLEVGKTLIENLNKYARVPCGFAAMKDVRTGSHEDRMDSFFLAEMFKYLYLLFADKEDIIFDIEDYIFTTEAHLLPLWLSTTNQSISKKNTTSEYTELDDSNFDWTCPNTQILFPNDPLYAQSIREPLKNVVDKSCPRGIIRVEESFRSGAKPPLRARDFMATNPEHLEILKKMGVSLIHLKDGRVQLVQHAIQAASSIDAEDGLRFMQEMIELSSQQQKEQQLPPRAVQIVSHPFFGRVVLTAGPAQFGLDLSKHKETRGFVASSKPSNGCSELTNPEAVMGKIALIQRGQCMFAEKARNIQNAGAIGGIVIDDNEGSSSDTAPLFQMAGDGKDTDDIKIPMLFLFSKEGSIILDAIREYEEVEVLLSDKAKDRDPEMENEEQPSSENDSQNQSGEQISSSSQEVDLVDQESSEENSLNSHPESLSLADMDNAASISPSEQTSNPTENHETTNLNGECTDLDNQLQEQSETEEDSNPNVSWGKKVQPIDSILADWNEDIEAFEMMEKDEL
Protein: Serine/threonine-protein kinase (EC 2.7.11.1) (Q08BC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLLSKFNTFAHISTVDMPAKIQLQVKEKEPFDKVYQVGTVLGSGGFGTVYAGLRIADGAPVAIKHVAKDRVTEWGELPNGARVPMEIVLLKKVGTGFRGVIKMLDWYERPDSFIIVMERPEVVKDLFDFITEKGALPEELARNFFRQVLEAVRHCHNSGVVHRDIKDENILIDLRTGDLKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIKFHRYHGRSATVWSLGILLYDMVCGDIPFEQDEEIVRGQVLFRRRISTECQQLIKWCLALRPADRPSFEDIINHDWMQSTAPPTDSTEIRLHSISHEHQPAAFPAVTVCK