wanglab/gogpt-training-data huggingface dataset:
Protein: Pyridoxal reductase (PL reductase) (PL-red) (EC 1.1.1.65) (O14295)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase C6F6.11c
- Putative pyridoxal kinase C18.10
Sequence:
MPIVSGFKVGPIGFGLMGLTWKPKQTPDEEAFEVMNYALSQGSNYWDAGEFYGVDPPTSNLDLLARYFEKYPENANKVFLSVKGGLDFKTLVPDGNPDFVSKSVENVIAHLRGTKKLDLFQCARVDPNVPIETTMKTLKGFVDSGKISCVGLSEVSAETIKRAHAVVPIAAVEVEYSLFSRDIETNGIMDICRKLSIPIIAYSPFCRGLLTGRIKTVEDLKEFAKSFPFLEYLDRFSPDVFAKNLPFLQAVEQLAKKFGMTMPEFSLLFIMASGNGLVIPIPGSTSVSRTKSNLNALNKSLSPEQFKEAKEVLSKYPIYGLRYNEQLAGTLSV
Protein: HAUS augmin-like complex subunit 5 (O94927)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 7
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 4
- HAUS augmin-like complex subunit 3
- Protein NEDD1
- Tubulin gamma-1 chain
- Nuclear mitotic apparatus protein 1
Sequence:
MELAQEARELGCWAVEEMGVPVAARAPESTLRRLCLGQGADIWAYILQHVHSQRTVKKIRGNLLWYGHQDSPQVRRKLELEAAVTRLRAEIQELDQSLELMERDTEAQDTAMEQARQHTQDTQRRALLLRAQAGAMRRQQHTLRDPMQRLQNQLRRLQDMERKAKVDVTFGSLTSAALGLEPVVLRDVRTACTLRAQFLQNLLLPQAKRGSLPTPHDDHFGTSYQQWLSSVETLLTNHPPGHVLAALEHLAAEREAEIRSLCSGDGLGDTEISRPQAPDQSDSSQTLPSMVHLIQEGWRTVGVLVSQRSTLLKERQVLTQRLQGLVEEVERRVLGSSERQVLILGLRRCCLWTELKALHDQSQELQDAAGHRQLLLRELQAKQQRILHWRQLVEETQEQVRLLIKGNSASKTRLCRSPGEVLALVQRKVVPTFEAVAPQSRELLRCLEEEVRHLPHILLGTLLRHRPGELKPLPTVLPSIHQLHPASPRGSSFIALSHKLGLPPGKASELLLPAAASLRQDLLLLQDQRSLWCWDLLHMKTSLPPGLPTQELLQIQASQEKQQKENLGQALKRLEKLLKQALERIPELQGIVGDWWEQPGQAALSEELCQGLSLPQWRLRWVQAQGALQKLCS
Protein: Major urinary protein 18 (A0A8I5YBU2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLLLLLLCLGLTLVCGHAEEASSTTGNRDVDKLNGDWFSIVVASDKREKIEENGSMRVFVQHIRVLENSLAFKFRIKENGVCTEFSLVAYKTPKDGEYFVEYDGGNTFTILKTDYDRYVMFHLVNFKNGETFQLMELYGRTKDLSSDIKEKFAKLCVAHGITRDNIIDLTKTVDLVPEHVLFLTLQIVVSRPEVEERPEPPVLSGDFSPGLQHHNFLSMEHPEKFCDLISILFHR
Protein: R2-like ligand binding oxidase (EC 1.-.-.-) (MtR2lox) (Ribonucleotide reductase R2 subunit homolog) (Ribonucleotide reductase small subunit homolog) (P9WH69)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probable oxidase that might be involved in lipid metabolism. Is not essential for the survival of M.tuberculosis in stress conditions.
Interaction partners:
- Ribonucleoside-diphosphate reductase subunit alpha
- Vitamin B12-dependent ribonucleoside-diphosphate reductase
- Probable transcriptional regulatory protein
- Ribonucleoside-diphosphate reductase subunit beta nrdF2
- Ribonucleoside-diphosphate reductase subunit beta nrdF1
- Protein NrdI
- Adenylate kinase
- Thymidylate kinase
- Cytidylate kinase
- Nucleoside diphosphate kinase
Sequence:
MTRTRSGSLAAGGLNWASLPLKLFAGGNAKFWHPADIDFTRDRADWEKLSDDERDYATRLCTQFIAGEEAVTEDIQPFMSAMRAEGRLADEMYLTQFAFEEAKHTQVFRMWLDAVGISEDLHRYLDDLPAYRQIFYAELPECLNALSADPSPAAQVRASVTYNHIVEGMLALTGYYAWHKICVERAILPGMQELVRRIGDDERRHMAWGTFTCRRHVAADDANWTVFETRMNELIPLALRLIEEGFALYGDQPPFDLSKDDFLQYSTDKGMRRFGTISNARGRPVAEIDVDYSPAQLEDTFADEDRRTLAAASA
Protein: B-cell scaffold protein with ankyrin repeats (Protein AVIEF) (Q80VH0)
Organism: Mus musculus (Mouse)
Function: Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2 (By similarity).
Interaction partners:
- Tyrosine-protein kinase Lyn
- B-lymphocyte antigen CD20
- B-cell receptor CD22
Sequence:
MLPVASGTRGSTQDLFQVGLAPPGNAKDILLLYEEDAEEWALYLREIFMRVVEREAILLYPLHSFSSSHLEMLNFYAYKCKLLIISNSLLKDLTPKKCQFLEKILHSTGNVVTLLCGMESSDPFYQLLSIPRKRWEISTEQDPDGYISVIRQILDQGPEDYLEVSIPTDSRAKYPEDTSGQKGTDVLASLRPSVPRVLVLPGEIPCEKPGEIFILLKDELIGEILEVEFISTNKRLRARPARWNKSVWHMKAADFPAGSVTVNIHCDGIIKATTEIKYCSAAKATESPFRVSDPGKSLCQKSIEELDNVLASIFKREIPYYEFKHLQAETYPQKERTHTTELPTLLHCAAKFGLKNLALHLLQCSGATRAARMKATDGSDLLHIAERHGHEELKEVFEDFLSQNTGRNSKQENDYEEDVISFSTYSPSMPSPASLHELRKTHRRNTDRSEEPERSVEMKEEEAGAEARRSLSEGERESSENQYDDLYVFIPGFDTEGNSEEPLPHCRPPLLPPRPGTAASQLERPHFTSQGKVLEDQMERSQNWNDLNARPETREESSREEKKEEAQEEEEEEENPYAFAETEDNEYDLILASKSVKKRTGNRSFIINRPPAPTPRPTHIPPKEETTPYIAQVFQQKAARRQSDGDKFYSLPKKPDKTRMEGPTFPSTRDYLTTGQEELILLQERVKNGKMSVDEALEKFKHWQMGKSGLEMIQQEKLRQLRDNIIGKRPEDENAYDKLTIVHHPSGNTAHNENMLYNSPFNSKFPARIQVEKEFGFCCKKDH
Protein: Phosphoenolpyruvate-dependent phosphotransferase system (EC 2.7.3.9) (Enzyme I-Ntr) (EINtr) (Phosphotransferase system, enzyme I) (P37177)
Organism: Escherichia coli (strain K12)
Function: Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins. Enzyme I-Ntr is specific for NPr.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphocarrier protein NPr
- Multiphosphoryl transfer protein
- PTS system glucose-specific EIIA component
- Nitrogen regulatory protein
- Phosphocarrier protein HPr
- RNA pyrophosphohydrolase
Sequence:
MLTRLREIVEKVASAPRLNEALNILVTDICLAMDTEVCSVYLADHDRRCYYLMATRGLKKPRGRTVTLAFDEGIVGLVGRLAEPINLADAQKHPSFKYIPSVKEERFRAFLGVPIIQRRQLLGVLVVQQRELRQYDESEESFLVTLATQMAAILSQSQLTALFGQYRQTRIRALPAAPGVAIAEGWQDATLPLMEQVYQASTLDPALERERLTGALEEAANEFRRYSKRFAAGAQKETAAIFDLYSHLLSDTRLRRELFAEVDKGSVAEWAVKTVIEKFAEQFAALSDNYLKERAGDLRALGQRLLFHLDDANQGPNAWPERFILVADELSATTLAELPQDRLVGVVVRDGAANSHAAIMVRALGIPTVMGADIQPSVLHRRTLIVDGYRGELLVDPEPVLLQEYQRLISEEIELSRLAEDDVNLPAQLKSGERIKVMLNAGLSPEHEEKLGSRIDGIGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFNDKPVTLRTLDVGADKQLPYMPISEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAATGNLNILLPMVTSLDEVDEARRLIERAGREVEEMIGYEIPKPRIGIMLEVPSMVFMLPHLAKRVDFISVGTNDLTQYILAVDRNNTRVANIYDSLHPAMLRALAMIAREAEIHGIDLRLCGEMAGDPMCVAILIGLGYRHLSMNGRSVARAKYLLRRIDYAEAENLAQRSLEAQLATEVRHQVAAFMERRGMGGLIRGGL
Protein: N-acetylhexosamine 1-kinase (EC 2.7.1.162) (N-acetylgalactosamine/N-acetylglucosamine 1-kinase) (E8MF12)
Organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Function: Phosphorylates both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Also accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate several GlcNAc and GalNAc derivatives.
Interaction partners:
Sequence:
MTESNEDLFGIASHFALEGAVTGIEPYGDGHINTTYLVTTDGPRYILQQMNTSIFPDTVNLMRNVELVTSTLKAQGKETLDIVPTTSGATWAEIDGGAWRVYKFIEHTVSYNLVPNPDVFREAGSAFGDFQNFLSEFDASQLTETIAHFHDTPHRFEDFKAALAADKLGRAAACQPEIDFYLSHADQYAVVMDGLRDGSIPLRVTHNDTKLNNILMDATTGKARAIIDLDTIMPGSMLFDFGDSIRFGASTALEDEKDLSKVHFSTELFRAYTEGFVGELRGSITAREAELLPFSGNLLTMECGMRFLADYLEGDIYFATKYPEHNLVRTRTQIKLVQEMEQKASETRAIVADIMEAAR
Protein: Oo18 RNA-binding protein, isoform B (Oo18 RNA-binding protein, isoform D) (Q8IMZ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLGVEKPYVVEPAMAVAQDSFEFGSNGDGSSTNSHTSNASSKDLGRLTSGDGAQNFAQDSSANSIDQDSTDNTNSDCNPITLNDLLGLCGASTANEVVGTGQTPSTSAPILGAGGGGRANGVTAGAATATGVGVGAGGTLPGPGVPSIQGGGGGGVVGQQTNASCNTSAANPSASFGGNGSSSDVNNLLLASAAAAAAAAAGDGAQLSANAAAYAPLTPSSTHSSASPGTKSNFDYFQFENVAQSNPLKAFQRTNISFDCSAPLSPSTPTSIYNRSFHSSPLVSDSSNSSSGIGLSMDSINMFYNQQQQQQQPEQQGYTSLGNSMGSGLGLSLANASTRSNSPESQNSSNSTTEQNLLDMINLLSVNSNKIPHQQQQQQQQQQQQQQQQQQNQQQLQVQQQHQLQQQFVNLNRNYEQQISANLGSQQHGFEHNGVGVGASSSGNENCFSQYNLENITSVDMELAKLQNLQRINTLKLLHAQAQQMPLINQLLQSYAGNAIGSVGGSNLGNLMSAGGSSLMTEMAGNVGGIITTNDGHLDRVAKFYKSSAALCDATCTWSGHLPPRSHRMLNYSPKVFLGGIPWDISEQSLIQIFKPFGSIKVEWPGKEQQAAQPKGYVYIIFESDKQVKALLSACVLQVDDSHCGRNYFFKISSRRIKSKDVEVIPWIIADSNFVRSSSQKLDPTKTVFVGALHGKLTAEGLGNIMDDLFDGVLYAGIDTDKYKYPIGSGRVTFSNFRSYMKAVSAAFIEIRTTKFTKKVQVDPYLEDALCSICGVQHGPYYCRELSCFRYFCRSCWQWQHSCDIVKNHKPLTRNSKSQSLVGIGPSSSNVSLPFSGQRSIRDNRMGNGQHQQHQQHQYQQQKHRQLQEYSQPHSLNVMGNSGAANAAATSMVTLQQRQIHKVRIQRQQHQAI
Protein: LPS-assembly protein LptD (Q9I5U2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01411}.
Interaction partners:
- LPS-assembly lipoprotein LptE
- Chaperone SurA
- Lipopolysaccharide export system protein LptC
- Outer membrane protein assembly factor BamA
- Outer membrane protein assembly factor BamD
- Lipopolysaccharide export system protein LptH
- Outer membrane protein assembly factor BamE
- Outer membrane protein assembly factor BamB
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Outer-membrane lipoprotein carrier protein
Sequence:
MAVKSLVFRRKFPLLVTGSLLALQPVAALTVQAADQFDCKVSATGGWDCSPLQNANANLPPRPAHTATSVSTAAAGSSVSGSGGETVEAEPTQRLVTESGGRALKSRSADYSHLDWIPREKLTAAQLAEIGPYCGGSYIEPVRPGMDDGAPSDESPTYVSAKASRYEQEKQIATLAGDVVLRQGSMQVEGDEANLHQLENRGELVGNVKLRDKGMLVVGDHAQVQLDNGEAQVDNAEYVIHKAHARGSALYAKRSENAIIMLKDGTYTRCEPSSNAWTLKGNNVKLNPATGFGTATNATLRVKDFPVFYTPYIYFPIDDRRQSGFLPPSFSSTSDTGFTLVTPYYFNLAPNYDATLYPRYMAKRGMMLEGEFRYLTHSSEGIVNAAYLNDKDDHREGFPDYSKDRWLYGLKNTTGLDSRWLAEVDYTRISDPYYFQDLDTDLGVGSTTYVNQRGTLTYRGDTFTGRLNAQAYQLATTTDVTPYDRLPQITFDGFLPYNPGGMQFTYGTEFVRFDRDLDENIYFNDDGSIRGKRPDASLQGLARATGDRMHLEPGMSLPMTRSWGYVTPTLKYLYTKYDLDLDSQGKTDLNKRDESFDSNQDRSLPLVKVDSGLYFDRDTTFAGTPFRQTLEPRAMYLYVPYKDQDSLPVFDTSEPSFSYDSLWRENRFTGKDRIGDANQLSLGVTSRFIEENGFERASISAGQIYYFRDRRVQLPGLTEKDLKRLNLDPSGLDNDSWRSPYAFAGQYRFNRDWRINSDFNWNPNTSRTESGSAIFHYQPEVDPGKVVNVGYRYRADARRFDSSRGTFRYGNENDIIKQHDFSVIWPLVPQWSVLARWQYDYNKNRTLEAFGGFEYDSCCWKLRLINRYWLDVDDDAFLVQSEKADRGIFLQIVLKGLGGIVGNKTEMFLDKGIQGYRQREDQAM
Protein: NADPH dehydrogenase 3 (EC 1.6.99.1) (Old yellow enzyme 3) (P41816)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive (By similarity). Has a prooxidant activity, increasing reactive oxygen species (ROS) levels when overexpressed. Formation of OYE2-OYE3 heterodimers contribute to the induction of programmed cell death upon oxidative stress.
Interaction partners:
- Glutathione S-transferase 2
- Probable electron transfer flavoprotein subunit beta
- Probable aryl-alcohol dehydrogenase AAD4
Sequence:
MPFVKGFEPISLRDTNLFEPIKIGNTQLAHRAVMPPLTRMRATHPGNIPNKEWAAVYYGQRAQRPGTMIITEGTFISPQAGGYDNAPGIWSDEQVAEWKNIFLAIHDCQSFAWVQLWSLGWASFPDVLARDGLRYDCASDRVYMNATLQEKAKDANNLEHSLTKDDIKQYIKDYIHAAKNSIAAGADGVEIHSANGYLLNQFLDPHSNKRTDEYGGTIENRARFTLEVVDALIETIGPERVGLRLSPYGTFNSMSGGAEPGIIAQYSYVLGELEKRAKAGKRLAFVHLVEPRVTDPSLVEGEGEYSEGTNDFAYSIWKGPIIRAGNYALHPEVVREQVKDPRTLIGYGRFFISNPDLVYRLEEGLPLNKYDRSTFYTMSAEGYTDYPTYEEAVDLGWNKN
Protein: Microtubule-associated protein RP/EB family member 3 (EB1 protein family member 3) (EBF3) (End-binding protein 3) (EB3) (RP3) (Q9UPY8)
Organism: Homo sapiens (Human)
Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:19255245, ECO:0000269|PubMed:28814570}. Note=Associated with the microtubule network. Detected at the plus end of microtubules. {ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:19255245, ECO:0000269|PubMed:28814570}.
Interaction partners:
- Microtubule-associated protein RP/EB family member 1
- Dynactin subunit 1
- Drebrin
- CAP-Gly domain-containing linker protein 1
- Cytoskeleton-associated protein 5
- Tubulin beta-2B chain
- Tubulin beta-3 chain
- Tubulin alpha-1B chain
- SRC kinase signaling inhibitor 1
- Sperm flagellar protein 1
Sequence:
MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYDGKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAPPCILRKNPPSARNGGHETDAQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEHESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY
Protein: Solute carrier family 41 member 2 (Q8BYR8)
Organism: Mus musculus (Mouse)
Function: Acts as a plasma-membrane magnesium transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96JW4}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transient receptor potential cation channel subfamily M member 6
- Transient receptor potential cation channel subfamily M member 7
- Magnesium transporter MRS2 homolog, mitochondrial
Sequence:
MTHSKGRPVTYKTSASPESGGGFVDWTLNLNTIQSDKFLNLLLSMVPVIYQKNQEDRHKKVNGIWQDGLSGAAQTFSKRSEPHLDYHEFSEQAFHSSSSGHTPASCSPKYDDYAGYNYCDGREASETTAMLQDEDLSSEGDDVIVETSQRIPKESSGVMALQILVPFLLAGFGTVSAGMVLDIVQHWEVFKNVTEVFILVPALLGLKGNLEMTLASRLSTAVNVGKMDSPIEKWNLIIGNLALKQVQATVVGFLAAVAAIILGWIPEGKYYLSHSILLCSSSVATAFIASLLQGIIMVGVIVGSKKTGINPDNVATPIAASFGDLITLAILAWISQGLYSCLETYYYISPLVCAFFLALTPIWIIIAAKHPATRTVLHSGWEPVITAMVISSIGGLILDTTVSDPNLVGIVVYTPVINGIGGNLVAIQASRISTYLHLHSIPGELPEEPKGCSYPFRTFFGSGVNNKSAQVLLLFVIPGHLIFLYTIHLMKSGHTSLTVVFVVVYLFAAVLQVFTLLWIADWMVHRFWRKGKDPDSFSIPYLTALGDLLGTALLALSFHFLWLIGDRDGDVGD
Protein: Ran-binding protein 10 (RanBP10) (Q6VN19)
Organism: Mus musculus (Mouse)
Function: May act as an adapter protein to couple membrane receptors to intracellular signaling pathways (Probable). Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Enhances dihydrotestosterone-induced transactivation activity of AR, as well as dexamethasone-induced transactivation activity of NR3C1, but does not affect estrogen-induced transactivation (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for RAN GTPase. May play an essential role in hemostasis and in maintaining microtubule dynamics with respect to both platelet shape and function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18347012}. Nucleus {ECO:0000269|PubMed:18347012}. Note=Predominantly cytoplasmic. Associates with cytoplasmic microtubules in mature megakaryocytes and platelets.
Interaction partners:
- WD repeat-containing protein 26
- Ran-binding protein 9
- Armadillo repeat-containing protein 8
- Glucose-induced degradation protein 8 homolog
- Muskelin
- E3 ubiquitin-protein transferase RMND5B
- Glucose-induced degradation protein 4 homolog
- Protein yippee-like 5
- E3 ubiquitin-protein transferase MAEA
- E3 ubiquitin-protein ligase RMND5A
Sequence:
MAAATADPGAGNPQAGDSSGGDSGGGLPSPGEQELSRRLQRLYPAVNQHETPLPRSWSPKDKYNYIGLSQGNLRVHYKGHGKNHKDAASVRATHPIPAACGIYYFEVKIVSKGRDGYMGIGLSAQGVNMNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINGTCFYTKNGHSLGIAFTDLPANLYPTVGLQTPGEIVDANFGQQPFLFDIEDYMREWRAKVQGTVHGFPISARLGEWQAVLQNMVSSYLVHHGYCSTATAFARMTETPIQEEQASIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSEVRSLSSRSPKSQDSYPGSPSLSPRHGPSSSHIHNTGADSPSCSNGVASTKNKQNHSKYPAPSSSSSSSSSSSSSSPSSVNYSESNSTDSTKSQPHSSTSNQETSDSEMEMEAEHYPNGVLESVSTRIVNGAYKHDDLQTDESSMDDGHPRRQLCGGNQAATERIILFGRELQALSEQLGREYGKNLAHTEMLQDAFSLLAYSDPWSCPVGHQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECLRLMARAGLGSCSFARVDDYLH
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (P15682)
Organism: Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04070}.
Interaction partners:
Sequence:
MATKGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVDGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMVDQVRESRNPGNAEFEDLIFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGTKVVPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASSGQISIQPTFSVQRNLPFDRPTIMAAFTGNTEGRTSDMRTEIIRLMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDN
Protein: Semaphorin-3C (Semaphorin-E) (Sema E) (Q99985)
Organism: Homo sapiens (Human)
Function: Binds to plexin family members and plays an important role in the regulation of developmental processes. Required for normal cardiovascular development during embryogenesis. Functions as attractant for growing axons, and thereby plays an important role in axon growth and axon guidance (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Neuropilin-1
- Neuropilin-2
- Plexin-D1
- Plexin-A1
- Plexin-A2
- Plexin-A3
- Transcription factor GATA-6
- Plexin-A4
Sequence:
MAFRTICVLVGVFICSICVKGSSQPQARVYLTFDELRETKTSEYFSLSHHPLDYRILLMDEDQDRIYVGSKDHILSLNINNISQEALSVFWPASTIKVEECKMAGKDPTHGCGNFVRVIQTFNRTHLYVCGSGAFSPVCTYLNRGRRSEDQVFMIDSKCESGKGRCSFNPNVNTVSVMINEELFSGMYIDFMGTDAAIFRSLTKRNAVRTDQHNSKWLSEPMFVDAHVIPDGTDPNDAKVYFFFKEKLTDNNRSTKQIHSMIARICPNDTGGLRSLVNKWTTFLKARLVCSVTDEDGPETHFDELEDVFLLETDNPRTTLVYGIFTTSSSVFKGSAVCVYHLSDIQTVFNGPFAHKEGPNHQLISYQGRIPYPRPGTCPGGAFTPNMRTTKEFPDDVVTFIRNHPLMYNSIYPIHKRPLIVRIGTDYKYTKIAVDRVNAADGRYHVLFLGTDRGTVQKVVVLPTNNSVSGELILEELEVFKNHAPITTMKISSKKQQLYVSSNEGVSQVSLHRCHIYGTACADCCLARDPYCAWDGHSCSRFYPTGKRRSRRQDVRHGNPLTQCRGFNLKAYRNAAEIVQYGVKNNTTFLECAPKSPQASIKWLLQKDKDRRKEVKLNERIIATSQGLLIRSVQGSDQGLYHCIATENSFKQTIAKINFKVLDSEMVAVVTDKWSPWTWASSVRALPFHPKDIMGAFSHSEMQMINQYCKDTRQQHQQGDESQKMRGDYGKLKALINSRKSRNRRNQLPES
Protein: Intraflagellar transport protein 80 homolog (WD repeat-containing protein 56) (Q9P2H3)
Organism: Homo sapiens (Human)
Function: Component of the intraflagellar transport (IFT) complex B, which is essential for the development and maintenance of motile and sensory cilia.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Note=Basal body and ciliary axoneme. {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 172 homolog
- Clusterin-associated protein 1
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 70B
Sequence:
MRLKISLLKEPKHQELVSCVGWTTAEELYSCSDDHQIVKWNLLTSETTQIVKLPDDIYPIDFHWFPKSLGVKKQTQAESFVLTSSDGKFHLISKLGRVEKSVEAHCGAVLAGRWNYEGTALVTVGEDGQIKIWSKTGMLRSTLAQQGTPVYSVAWGPDSEKVLYTAGKQLIIKPLQPNAKVLQWKAHDGIILKVDWNSVNDLILSAGEDCKYKVWDSYGRPLYNSQPHEHPITSVAWAPDGELFAVGSFHTLRLCDKTGWSYALEKPNTGSIFNIAWSIDGTQIAGACGNGHVVFAHVVEQHWEWKNFQVTLTKRRAMQVRNVLNDAVDLLEFRDRVIKASLNYAHLVVSTSLQCYVFSTKNWNTPIIFDLKEGTVSLILQAERHFLLVDGSSIYLYSYEGRFISSPKFPGMRTDILNAQTVSLSNDTIAIRDKADEKIIFLFEASTGKPLGDGKFLSHKNEILEIALDQKGLTNDRKIAFIDKNRDLCITSVKRFGKEEQIIKLGTMVHTLAWNDTCNILCGLQDTRFIVWYYPNTVYVDRDILPKTLYERDASEFSKNPHIVSFVGNQVTIRRADGSLVHISITPYPAILHEYVSSSKWEDAVRLCRFVKEQTMWACLAAMAVANRDMTTAEIAYAAIGEIDKVQYINSIKNLPSKESKMAHILLFSGNIQEAEIVLLQAGLVYQAIQININLYNWERALELAVKYKTHVDTVLAYRQKFLETFGKQETNKRYLHYAEGLQIDWEKIKAKIEMEITKEREQSSSSQSSKSIGLKP
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (Enhancer of zeste homolog 2) (Q08BS4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Polycomb group (PcG) protein. Catalytic subunit of the prc2/eed-ezh2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. May regulate the circadian clock via histone methylation at the promoter of the circadian genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15910}.
Interaction partners:
- Polycomb protein suz12-B
- Polycomb protein suz12-A
- Polycomb protein eed
- Histone-binding protein RBBP4
- Zinc finger protein AEBP2
- E3 ubiquitin-protein ligase RING2
- Histone-binding protein RBBP7
- DNA
- Polycomb complex protein BMI-1-A
- Histone H3.3
Sequence:
MGLTGRKSEKGPVCWRRRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTDILNQEWKLRRIQPVHIMTPVSSLRGTRECTVDSGFSEFSRQVIPLKTLNAVASVPVMYSWSPLQQNFMVEDETVLHNIPYMGDEILDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALNQYSDNEEDDEEDDHHDYKFEKMDLCDGKDDAEDHKEQLSSESHNNDGSKKFPSDKIFEAISSMFPDKGSTEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFQATPNTYKRKNMENLVDSKPCGIYCYMYMVQDGMVREYPAGVVPERAKTPSKRSTGRRRGRLPNSNSRPSTPTVNSETKDTDSDREGGADGNDSNDKDDDDKKDETTSSSEANSRCQTPVKLKLSSEPPENVDWSGAEASLFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIARAPAVDENTPQRKKKRKHRLWATHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVTAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAAEHWDSKNVSCKNCSIQRGAKKHLLLAPSDVAGWGIFIKEPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP