wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent DNA helicase Q5 (EC 5.6.2.4) (DNA 3'-5' helicase RecQ5) (DNA helicase, RecQ-like type 5) (RecQ5) (RECQL5beta) (RecQ protein-like 5) (Q8VID5)
Organism: Mus musculus (Mouse)
Function: DNA helicase that plays an important role in DNA replication, transcription and repair. Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability. Associates also with POLR1A and enforces the stability of ribosomal DNA arrays. Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress. Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O94762}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. {ECO:0000250|UniProtKB:O94762}.
Interaction partners:
- Fanconi anemia group M protein homolog
- F-box DNA helicase 1
- Structure-specific endonuclease subunit MUS81
- DNA topoisomerase 3-alpha
- DNA repair protein RAD52 homolog
- DNA replication ATP-dependent helicase/nuclease DNA2
- Flap endonuclease 1
- RecQ-mediated genome instability protein 1
- TP53-binding protein 1
- Regulator of telomere elongation helicase 1
Sequence:
MSARPFSTPFDRERRVRSTLKKVFGFDSFKTPLQESATMAVVKGAEDVFVCMPTGAGKSLCYQLPALLASGITIVVSPLIALIQDQVDHLLALKVQVSSLNSKLSVQERKELLSDLERDKPRTKLLYITPEMAASASFQPTLNSLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLAHAPCVALTATATPQVQEDVFAALHLKQPVASFKTPCFRANLFYDVQFKELIPDVYGNLRDFCLKALGQKAENGSSSGCGIVYCRTREACEQLAIELSSRGVNAKAYHAGLKASDRTQVQNEWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKELAKLQEKRGNKPSDKATLLAFDALVTFCEEVGCRHAAIAKYFGDAPPACAKGCDYCQNPAAITKKLDALERSSSWSKTCIGPSQGNGFDPELYEGGRRGYGGFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMSLRKGKEPKIEEFTPPDEDCPLREASSRKIPKLTVKAREHCLRLLEEALISNHQAAGSTHGADLQAKAVELEHETFRNAKMVNLYKASVLKKVAEIHKASKDGQLYDMESGTKSCGAAAEFSEPSDYDIPPTSHVYSLKPKRVGAGFSKGPCSFQTATELLGKSHSQKQAPEAMLEGGQEPPGWVCDLQDEDRSKPHPGYQEKALGSSVNCGDPSPEKKTKGSSQGSAKARASKKQQLLATAARKDSQNITRFLCQRTESPPLPASVPRSEDASPSCGDVPGKCTQEVGAQGHLVAVFQTEGPRERPSTCSLRDQSFPEGQPSPLKETQAEKRPRPQQGNPERRAQKRLRPSTKSSILAEAKDSTLASDRSTENKVAQEPCQLSASGTSLREAADIVVRHLTPFYKEGRFISKDLFKGFARHLSHLLAQQLSPGRSVKEEAQSLIKQFFHNRARCESEADWHSLRGPQR
Protein: Serine/threonine-protein phosphatase PP1 isozyme 4 (EC 3.1.3.16) (Type one protein phosphatase 4) (P48484)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. Acts as positive regulator in the gibberellin (GA) signaling pathway to regulate plant growth and development. Promotes the GA-induced and proteasomal-dependent degradation of the DELLA proteins RGA and GAI by directly binding and dephosphorylating these proteins. Involved in the regulation of phytochrome B (phyB) signaling pathway that controls photomorphogenesis. Promotes the proteasomal-dependent degradation of PIF5 factor by directly binding and dephosphorylating this protein. Involved in the regulation of pavement cell (PC) interdigitation by modulating the auxin efflux carrier PIN1 polarity and endocytic trafficking. Regulates PIN1 polar targeting through direct binding and dephosphorylation. Acts antagonistically with PID in regulating PC development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19329567, ECO:0000269|PubMed:25010794, ECO:0000269|PubMed:25560878, ECO:0000269|PubMed:26704640}. Cytoplasm {ECO:0000269|PubMed:19329567, ECO:0000269|PubMed:25560878}. Note=Localizes predominantly to the nucleus. {ECO:0000269|PubMed:19329567, ECO:0000269|PubMed:25560878}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit INH3
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Flowering time control protein FY
- Transducin/WD40 repeat-like superfamily protein
- Protein ANTHESIS POMOTING FACTOR 1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Cleavage and polyadenylation specificity factor subunit 2
- Peptidyl-prolyl cis-trans isomerase Pin1
- Cleavage and polyadenylation specificity factor subunit 3-I
- Plant/protein
Sequence:
MATTTTTQGQQTAIDSAVLDDIIRRLTEVRLARPGKQVQLSEAEIKQLCTTARDIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPSANYLFLGDYVDRGKQSLETICLLLAYKIKYPGNFFLLRGNHECASINRIYGFYDECKRRFNVRVWKVFTDCFNCLPVAALIDDKILCMHGGLSPDLDHLDEIRNLPRPTMIPDTGLLCDLLWSDPGKDVKGWGMNDRGVSYTFGPDKVSEFLTKHDLDLVCRAHQVVEDGYEFFADRQLVTVFSAPNYCGEFDNAGAMMSVDENLMCSFQILKPAEKKTKFMMSTKI
Protein: Tubulin alpha-3 chain (EC 3.6.5.-) (Alpha-tubulin 3/7) (Alpha-tubulin isotype M-alpha-3/7) (Tubulin alpha-3/alpha-7 chain) [Cleaved into: Detyrosinated tubulin alpha-3 chain] (P05214)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37989994}.
Interaction partners:
- Tubulin beta-4A chain
- Tubulin beta-4B chain
- Tubulin beta-6 chain
- Tubulin beta-1 chain
- Tubulin beta-2A chain
- Tubulin beta-3 chain
- Tubulin beta-5 chain
- Tubulin beta-2B chain
- Microtubule-associated protein
- Cell division control protein 42 homolog
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY
Protein: Peptidyl-prolyl cis-trans isomerase C, mitochondrial (PPIase C) (EC 5.2.1.8) (Cyclophilin C) (PPI-III) (Rotamase C) (P25719)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This isozyme is required for growth on lactate at high temperature.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:7603990}.
Interaction partners:
- FK506-binding protein 1
- Peptidyl-prolyl cis-trans isomerase FPR2
- Ran-specific GTPase-activating protein 1
- Acyl carrier protein, mitochondrial
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL15m
- Putative glycosyltransferase HOC1
- Large ribosomal subunit protein bL17m
Sequence:
MFKRSIIQQSRLFSNSASRLGKKVFFDPAVNGTKIGRIEFELYDNVVPKTAENFRALCTGEKGWGYKGVPFHRIIPDFMIQGGDTDLTNGFGGKSIYGSKFADENFVKKHDKAGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVTKGMDIVKAIESYGTASGKPRAEIVIEEAGEL
Protein: Flagellar biosynthetic protein FliR (P33135)
Organism: Escherichia coli (strain K12)
Function: Role in flagellar biosynthesis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. Bacterial flagellum basal body {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Flagellar protein FliO
- Flagellar biosynthesis protein FlhA
- Flagellum-specific ATP synthase
- Flagellar biosynthetic protein FliQ
- Flagellar biosynthetic protein FlhB
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliN
- Flagellar biosynthetic protein FliP
- Flagellar M-ring protein
- Flagellar FliJ protein
Sequence:
MLQVTSEQWLSWLNLYFWPLLRVLALISTAPILSERSVPKRVKLGLAMMITFAIAPSLPANDVPVFSFFALWLAVQQILIGIALGFTMQFAFAAVRTAGEIIGLQMGLSFATFVDPASHLNMPVLARIMDMLALLLFLTFNGHLWLISLLVDTFHTLPIGGEPLNSNAFLALTKAGSLIFLNGLMLALPLITLLLTLNLALGLLNRMAPQLSIFVIGFPLTLTVGISLMAALMPLIAPFCEHLFSEIFNLLADIISELPLI
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FME2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome K complete sequence
- Transcriptional activator HAP2
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MLTALGSMGENYPVLRPKDSVAEKMAMSKIHISKKWKLPPLRPKGSHERAKPSPSMDAGAKVSPAGDSPTGEDSKHMSGPNRKRLQNREAQRAYRERSRNKLQTLEDNVETLQGMVKMWQSKYKQLASEFDQYKQSSNEKIVELEKTISESKEDSKCYICMKNVDLDGLKENARNEDIKPFFQDEFLSNAIKNFQPMEAVSLKRKQEKNSSSPSITPRSSTTSFAAVLNDVDKGNCGFCNDNTACVCRDITSTLSAKPPQRRSDILLDTMSKSGLSTESIKSNYAVSALRSTHCSENPSKCTKCSDIDTSCLKSVPADNKRSSIYMEELPMEFEVNLNDLFPSPKRQRT
Protein: Ionotropic receptor 48c (A1Z8P2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSLLRIILIIIFLRIVSSIPDTIISHLSAELQIKIQIYFGLGNDLYDFSRLDGNYQKIIISHNISEEFKTYHDEPVLIIIRLERDLNLNLATLDVLRSYLTDRQYNDILLIDNDEENLNSYVDIRKAYWNAGFSQVLIYNSQQRTWSIKPYPYLQIRPTSLKEYIENRNTRNLMGYPLRVLVTNDPPHCFVDKDELPGSPNRYKGSIVTMLKIFADQLNATFQANPFREFRRYSTADCVQMVSDDEIDACGSIFIRTYTYATSQPVRLNRVVIMAPFGNPIEKFYYFFRPFDLYVWIGTGIIVVYIAVMGSLLHRWHFKEWNVGQYLLLAVQTLLNRELSLPQSSSGSKFMLLLLLFAIGFILSNLYVALLSMMLTTKLYQRPIENLADLKAANVNILLQTHNIRPNSVYGSSEELRERFLLVEESQHLEKRNGLDPSYAYVDSEDRMDFYLYQQKFLRRRRMKKLSNPVGYTWAVQVIKQNWVLEKHYNDHVQRFFETGLQNKLVDDVHELAVKAGFLHFFPTQTQTIEPLRLEDIVMAAMVLGGGHALAVICFLVELFA
Protein: Bifunctional pinoresinol-lariciresinol reductase (PhPLR) ((+)-lariciresinol reductase) (EC 1.23.1.2) ((+)-pinoresinol reductase) (EC 1.23.1.1) (B0LL23)
Organism: Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum)
Function: Reductase involved in lignan biosynthesis. Also involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the enantioselective sequential conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis.
Interaction partners:
Sequence:
MAKSRVLIVGGTGYLGRRMVKACLDQGHTTYVLHRQEVGVDIDKIQMLLSFKEQGAHLVEGSFNDHRSLVEAVKLVDVVICTISGVHIRSHQILLQLKLVEAIEEAGNVKRFLPSEFGMDPARMAHAMEPGRATFDEKMVVRKAIEDAKIPHTYASANCFAGYFLGGLCQFGKIIPSKESVILSGDGNVKGIYVDEYDIATYTIKTMDDPRTLNKTIYIRPPANILSQREVVEIWEKLIGKVLDKSSLSEEDFLALMKGLSHGHQAGLTHYYHVSYEGCLTNFEVEDGVDASKLYPQVNYTTVSEYLKRYL
Protein: Accessory gland-specific peptide 26Aa (Male accessory gland secretory protein 355A) [Cleaved into: CP1-N; CP1-C; CP2-N; CP2-C; CP3-N; CP3-C] (P10333)
Organism: Drosophila melanogaster (Fruit fly)
Function: Male seminal protein which enhances ovulation in female Drosophila by stimulating the release of oocytes by the ovary following mating. Acts by increasing octopamine (OA) neuronal signaling in the female genital tract leading to the postmating relaxation of the oviduct muscles. This activation of the OA signaling pathway is likely to indirectly contribute to the mating-dependent increase in the number of OA synaptic sites in the female reproductive tract.
Subcellular location: Secreted {ECO:0000269|PubMed:3142802}. Cytoplasm {ECO:0000269|PubMed:2257979}. Note=In 1 day old virgin males, secreted into the cytoplasm of accessory gland cells (PubMed:2257979). In 5 day old males it localizes to cytoplasmic vesicles of the secondary cells (PubMed:2257979). {ECO:0000269|PubMed:2257979}.
Interaction partners:
- Accessory gland protein Acp76A
- Serpin 28F
- ACP53C14A
- Accessory gland-specific peptide 26Ab
- ACP53C14B
- Serpin 38F, isoform A
- Accessory gland protein Acp36DE
- IP20609p
- Accessory gland-specific peptide 70A
- Accessory gland protein Acp62F
Sequence:
MNQILLCSPILLLLFTVASCDSEQQLDSAMHLKSDSTKSASLKNVAPKNDETQAKIAKDDVALKDAKKGDYIMDIDISDLPLDDYPINRSKSLKSSSIDLNNIPFNKGLDDFPAKEKNQGSNQSALKALQQRLLTEQNNSLLLRNHSIYLMKEIEARKTDIIKVRQLNLDLELELNTVNRRLLELNGQLQNTRKSTKPCKKRSSKDSAPPAANQFQEANVRNTYRNKYLTLLKELSQKINNEIAKVATDVPTETNPSQGNLPTL
Protein: Potassium channel tetramerization domain containing 10 (F5GWA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGESVVSSAVPAAATRTTSFKGTSPSSKYVKLNVGGALYYTTMQTLTKQDTMLKAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGAVPLPESRREIEELLAEAKYYLVQGLVEECQAALQNKDTYEPFCKVPVITSSKEEQKLIATSNKPAVKLLYNRSNNKYSYTRVLFIKDVIGDEICCWSFYGQGRKIAEVCCTSIVYATEKKQTKVEFPEARIYEETLNILLYEAQDGRGPDNALLEATGGAAGRSHHLDEDEERERIERVRRIHIKRPDDRAHLHQ
Protein: GH26207p (Q95SH3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDQTLGTDSEHHYESIRHSGDPIYEEIHEVPPPLPLSAPPLNDAELEKKAARSIFEGASKYDILSYLVDAKERGLAREESFDYGNNPKIIEEEAADTLSDLDKRQAEERERDRDSGQSSMSSLSPPPHNFICGGAGKSSGSDVERQDSGVGSETSKTSRSKYQATPTVLHLCEDCDGAVEMQVGDNGILYAPLVCRKCGKKRVERKEIITEIVETEEKYGRDLQIILEEFCHPMLVAGLLTQEQLSAIFLNTEDLLENNQTLAERMRDALDMSLEQGDDDLLTVNIGRIFLDFTQMLHAFESYCVRQAGASLLLANLEKEKELLRIFLKVSQMENAVLRRMNLNSFLMVPVQRVTKYPLLLARLYKVTPSHLEGRELLKQAQEKIELHLNHINQEAKDVPTKLWRRISSSSPNRRASCEIDMINIKLRKMAIDVLEWNHDEVRFAMEGRLLYTQPTDSNWKKARTIKLTPVNALLVTNGKPSANYRAEKAMSEKLNFPKHTGIREASLLLVKEKCGRYTLIREPLYLDRCVVCSEADWDDYFEVQEISSKDTFIFKAEDGVRTKQWYTQLQYHAQGMGAWRKRRNALANIMINGMLARS
Protein: Porphobilinogen deaminase (PBG) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) (O94048)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Interaction partners:
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- Uroporphyrinogen-III C-methyltransferase
- Uroporphyrinogen decarboxylase
- Ferrochelatase
- Protoporphyrinogen oxidase
- Iron-sulfur assembly protein 1
- coproporphyrinogen oxidase
- 5-aminolevulinate synthase, mitochondrial
- Translation initiation factor RLI1
Sequence:
MPHHIMSINDSNHVQIGGRKSKLAVVQSEIVKKVIEDTFPNLSCSILALSTLGDKVQTQPLYTFGGKSLWTKELEILLLDSVDEFPKLDLIVHSLKDMPTNLPEEFELGCIFQREDPRDAIVMKQGSSYKSLKDLPAGAIVGTSSIRRSSQLIKNYPHLRFESVRGNIQTRLNKLDQPNNEYCCLILASAGLIRLGLGHRITSYLDDMYYAVGQGALGIEIRKGDDNIKSILKKIEDPIATICCLAERSLMRYLEGGCSVPLGVHSDYNESKQELTLKGIIVSPDGTVSIEDEVIKRITCDEDCEQVGIELGDKLKAKGAKEILDKIDMTRNINARPTEV
Protein: Putative hydroxypyruvate isomerase (EC 5.3.1.22) (GIP-like protein) (Transient receptor potential locus C protein) (P36951)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- Alanine--glyoxylate aminotransferase
- Stellate protein CG33247
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- D-amino acid oxidase 2, isoform A
Sequence:
MALKFAANLNFLFTERATSIAERIRLAHQNGFRAVEIPYPEGETSDVVSAVKETGVVVSLVNLAFDKSDDQLRFGSTSVPGSEKLFRSQLDATIDFARQVNCGKIHLTAGLFKGGQESDYTKTYTANLKIAADSLRASKMIGVIEPINKYAVPGYYMNSYSKAAGILADVAADNIQLLADLYHLQHLHGNVSKTLEEYKALIGHFQIAQVPHRHEPDVSGELDYGFVFKALQEFGYDGWIGCEYKPKTTTVEGLGWVSKLGYTL
Protein: Retinol binding protein 1 (A0A0A0MQT0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEMPVDFTGYWKMLVNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ
Protein: Retinitis pigmentosa 9 protein homolog (Pim-1-associated protein) (PAP-1) (P97762)
Organism: Mus musculus (Mouse)
Function: Is thought to be a target protein for the PIM1 kinase. May play some roles in B-cell proliferation in association with PIM1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- U4/U6 small nuclear ribonucleoprotein Prp3
- U4/U6 small nuclear ribonucleoprotein Prp31
- Pre-mRNA-processing factor 6
- U4/U6 small nuclear ribonucleoprotein Prp4
- U5 small nuclear ribonucleoprotein 200 kDa helicase
Sequence:
MSSGAGSRRPREPPEHELQRRREQKRRRHDAQQLQQLKHLESFYEKPPPGFIKEDETKPEDCIPDVPGNEHAREFLAHAPTKGLWMPLGREVKVMQCWRCKRYGHRTGDKECPFFIKGNQKLEQFRVAHEDPMYDIIRENKRHEKDVRIQQLKQLLEDSTSDDDGSSSSSSGDREKRKKRKKKEKHKKRKKEKKKKKKRKHKASKSSESSDSE
Protein: Membrane-anchored junction protein (Q3KP22)
Organism: Homo sapiens (Human)
Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly for the stabilization of telomere attachment on the nucleus inner membrane.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:Q9D992}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D992}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9D992}. Note=In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q9D992}.
Interaction partners:
Sequence:
MSLKPFTYPFPETRFLHAGPNVYKFKIRYGKSIRGEEIENKEVITQELEVPVEKKAVGAVMRKRKHMDEPSSPSRPGLDRAKIGTSSQGPSKKKPPVETRRNRERKTQQGLQETLASDITDVQKQDSEWGHSLPGRIVPPLQHNSPPPKERAATGFFGFLSSLFPFRYFFRKSSHS
Protein: H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7) (P51798)
Organism: Homo sapiens (Human)
Function: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}; Multi-pass membrane protein {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18449189, ECO:0000269|PubMed:21527911}.
Interaction partners:
- Osteopetrosis-associated transmembrane protein 1
- V-type proton ATPase 116 kDa subunit a 3
- Pleckstrin homology domain-containing family M member 1
- Potassium-transporting ATPase alpha chain 1
- Potassium-transporting ATPase alpha chain 2
- Carbonic anhydrase 2
- Tumor necrosis factor receptor superfamily member 11A
- Tumor necrosis factor ligand superfamily member 11
- Sorting nexin-10
Sequence:
MANVSKKVSWSGRDRDDEEAAPLLRRTARPGGGTPLLNGAGPGAARQSPRSALFRVGHMSSVELDDELLDPDMDPPHPFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIDKFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIEAVLVAAVTATVAFVLIYSSRDCQPLQGGSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGVIVDVLSDTASNHNGFPVVEHADDTQPARLQGLILRSQLIVLLKHKVFVERSNLGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT
Protein: Adipose-secreted signaling protein (Q9VSK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RRP12-like protein
- Nucleolar GTP-binding protein 2
Sequence:
MCDESIENVEHQDHHVHFDTNTVKDDFESDSCVTYQRSGDTIVVSLGFLQIRHRYLIELKLPTSLFGDAKTLASKFEPVISATPSLHCRITEFEGTKHDEHDFFEMKIEFFAYKEKLLREVLHIVSSSNAKELLQLVIAARVLGKGKGTPMLRTGIHCIGVERDDDESEASDFAGFDSKP
Protein: HssA/B-like protein 27 (Protein 7E) (P15649)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MTILASICKLGNTKSTSSSIGSSYSSAVSFGSNSVSCGECGGDGPSFPNASPRTGVKAGVNVDGLLGAIGKTVNGMLISPNGGGGGMGMGGGSCGCN
Protein: Endoplasmic reticulum membrane sensor NFE2L1 (Nuclear factor erythroid 2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) (J3QKY3)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004643}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGWESHLTAASADIDLGAGREVFDYSHRQKEQDVEKELRDGGEQDTWAGEGAEALARNLLVDGETGESFPAQFPADISSITEAVPSESEPPALQNNLLSPLLTGTESPFDLEQQWQDLMSIMEMQAMEVNTSASEILYSAPPGDPLSTNYSLAPNTPINQNVSLHQASLGGCSQDFLLFSPEVESLPVASSSTLLPLAPSNSTSLNSTFGSTNLTGLFFPPQLNGTANDTAGPELPDPLGGLLDEAMLDEISLMDLAIEEGFNPVQASQLEEEFDSDSGLSLDSSHSPSSLSSSEGSSSSSSSSSSSSSSASSSASSSFSEEGAVGYSSDSETLDLEEAEGAVGYQPEYSKFCRMSYQDPAQLSCLPYLEHVGHNHTYNMAPSALDSADLPPPSALKKGSKEKQADFLDKQMSRDEHRARAMKIPFTNDKIINLPVEEFNELLSKYQLSEAQLSLIRDIRRRGKNKMAAQNCRKRKLDTILNLERDVEDLQRDKARLLREKVEFLRSLRQMKQKVQSLYQEVFGRLRDENGRPYSPSQYALQYAGDGSVLLIPRTMADQQARRQERKPKDRRK
Protein: Mu-adaptin 3, putative (Q583J1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- AP-3 complex subunit beta
- AP-3 complex subunit delta
- AP complex subunit sigma
- AP-1 complex subunit gamma
- AP-4 complex subunit epsilon
Sequence:
MITGLFFLNKHGEVIIEKEFREKVPRSSLEDFWCTYMTPLRSIEEAPAVITYSRFAFIQIHRNDVVLLAVATSECFPLFVMEVLALAAKVVQKYLKVISESTLRENFSLVYQLLVELIDNGYPLTTEMHVLEELVLPPSLENVFRSALEAPVAIKRRHMGSRAVPWRDPATKHSSNEIFFDIVENLDCIVDCEGNVVQSAVRGAVEVNCRLSGLPEVIMRLTGIDCIEDIAMHRCVRRSRYEVDRMISFIPVDGKFTLLQYRCKMANSVQVPFYVTPQITFNASVGRFNCMVGFRGSGLAARSREYEIQKLIIHLPLPPQTEAVQVHSISHGNTNFKKARNMLVWNVGSLHRGTCSLSGEFTFGTEREKEGLAPCTGGSALVEFSIPNYLLSSIRVDSVQVLNDLTKPYKGVKYVTTAGRFAVRTI
Protein: Transcription factor MYB122 (Myb-related protein 122) (AtMYB122) (Q9C9C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in glucosinolates biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tryptophan N-monooxygenase 1
- Tryptophan N-monooxygenase 2
- Cytosolic sulfotransferase 16
- Transcription factor MYC2
- Transcription factor MYC3
- Transcription factor MYC4
- Dihomomethionine N-hydroxylase
- Methylthioalkylmalate synthase 3, chloroplastic
- Cytosolic sulfotransferase 17
- Cytochrome P450 81F2
Sequence:
MVRTPCCRAEGLKKGAWTQEEDQKLIAYVQRHGEGGWRTLPDKAGLKRCGKSCRLRWANYLRPDIKRGEFSQDEEDSIINLHAIHGNKWSAIARKIPRRTDNEIKNHWNTHIKKCLVKKGIDPLTHKSLLDGAGKSSDHSAHPEKSSVHDDKDDQNSNNKKLSGSSSARFLNRVANRFGHRINHNVLSDIIGSNGLLTSHTTPTTSVSEGERSTSSSSTHTSSNLPINRSITVDATSLSSSTFSDSPDPCLYEEIVGDIEDMTRFSSRCLSHVLSHEDLLMSVESCLENTSFMREITMIFQEDKIETTSFNDSYVTPINEVDDSCEGIDNYFG