wanglab/gogpt-training-data huggingface dataset:
Protein: Elongation factor 1-gamma 2 (EF-1-gamma 2) (Eukaryotic elongation factor 1Bgamma 2) (eEF1Bgamma 2) (Translation elongation factor 1B gamma 2) (P36008)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Elongation factor 1-beta
- Elongation factor 1-alpha
- Elongation factor 2
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Translationally-controlled tumor protein homolog
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL18
- Valine--tRNA ligase, mitochondrial
Sequence:
MSQGTLYINRSPRNYASEALISYFKLDVKIVDLEQSSEFASLFPLKQAPAFLGPKGLKLTEALAIQFYLANQVADEKERARLLGSDVIEKSQILRWASLANSDVMSNIARPFLSFKGLIPYNKKDVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGLATILGPEWRAKHPHLMRWFNTVAASPIVKTPFAEVKLAEKALTYTPPKKQKAEKPKAEKSKAEKKKDEAKPADDAAPAKKPKHPLEALGKSTFVLDDWKRKYSNDDTRPVALPWFWEHYNPEEYSIWKVGYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDFAPAFDVAPDWESYEYTKLDPTKEEDKEFVNNMWAWDKPVVVNGEDKEIVDGKVLK
Protein: Zinc finger protein 524 (Q96C55)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ribosomal protein S6 kinase-like 1
Sequence:
MDTPSPDPLPSPLPGEEEKPLALSPPVPRGRRGRRPGGATSSNRTLKASLPRKRGRPPKSGQEPPLVQVQGVTAPVGSSGGSDLLLIDDQGVPYTVSEGSAAGPEGSGPRKAPHFCPVCLRAFPYLSDLERHSISHSELKPHQCKVCGKTFKRSSHLRRHCNIHAGLRPFRCPLCPRRFREAGELAHHHRVHSGERPYQCPICRLRFTEANTLRRHAKRKHPEAMGVPLCAPDPGSEPPWDEEGIPATAGAEEEEETEGKGEPA
Protein: Histone deacetylase 5 (HD5) (EC 3.5.1.98) (Antigen NY-CO-9) (Q9UQL6)
Organism: Homo sapiens (Human)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Serves as a corepressor of RARA and causes its deacetylation. In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response.
Subcellular location: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1.
Interaction partners:
- Nuclear receptor corepressor 1
- Histone deacetylase 4
- Nuclear receptor subfamily 2 group E member 1
- Nuclear receptor corepressor 2
- Calcium/calmodulin-dependent protein kinase type IV
- Histone deacetylase 3
- Myocyte-specific enhancer factor 2D
- Myocyte-specific enhancer factor 2A
- Myocyte-specific enhancer factor 2C
- Serine/threonine-protein kinase D1
Sequence:
MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
Protein: Histone H2B type 1-C/E/F/G/I (Histone H2B.1 A) (Histone H2B.a) (H2B/a) (Histone H2B.g) (H2B/g) (Histone H2B.h) (H2B/h) (Histone H2B.k) (H2B/k) (Histone H2B.l) (H2B/l) (P62807)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A type 1
- Histone H2A type 2-A
- Histone H4
- Histone H2A type 2-C
- Histone H2A type 1-C
- Histone H3.1
- Histone H3.2
- Histone H2A type 1-D
- Histone H3.3
- TP53-binding protein 1
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Anti-adapter protein IraD (P39375)
Organism: Escherichia coli (strain K12)
Function: Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Regulator of RpoS
- Anti-adapter protein IraM
- Anti-adapter protein IraP
- RNA polymerase sigma factor RpoS
Sequence:
MMRQSLQAVLPEISGNKTSSLRKSVCSDLLTLFNSPHSALPSLLVSGMPEWQVHNPSDKHLQSWYCRQLRSALLFHEPRIAALQVNLKEAYCHTLAISLEIMLYHDDEPLTFDLVWDNGGWRSATLENVS
Protein: Mitochondrial import inner membrane translocase subunit tim17 (Mitochondrial protein import protein 2) (P87130)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit tim23
- Mitochondrial import inner membrane translocase subunit tim50
- Mitochondrial import inner membrane translocase subunit tim44
- Mitochondrial import inner membrane translocase subunit tim14
- Mitochondrial import inner membrane translocase subunit tim16
- Mitochondrial import inner membrane translocase subunit tim21
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Protein mgr2
- Cytochrome c oxidase subunit 4, mitochondrial
- GrpE protein homolog
Sequence:
MASADHTRDPCPYVILNDFGAAFSMGTIGGAIWHSIKGWRNSPPGEKRISAIAAAKTRAPVLGGNFGVWGGLFSTFDCAVKGVRRKEDPWNAIIAGFFTGGALAVRGGWRATRNGAIGCACILAVFEGLGIALGRMNAEYNRPVAPVIPDAPASGSTSAAPAAV
Protein: Probable thioredoxin TrxA (O53161)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Thioredoxin reductase
- Probable enoyl-CoA hydratase EchA12
- Probable cobalt/nickel-exporting P-type ATPase
- Thioredoxin
- Alkyl hydroperoxide reductase C
Sequence:
MTTRDLTAAYFQQTISANSNVLVYFWAPLCAPCDLFTPTYEASSRKHFDVVHGKVNIETEKDLASIAGVKLLPTLMAFKKGKLVFKQAGIANPAIMDNLVQQLRAYTFKSPAGEGIGPGTKTSS
Protein: Cell wall synthesis protein Wag31 (Antigen 84) (P9WMU1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Important for maintaining cell shape and cell wall integrity by localizing peptidoglycan synthesis to the cell poles. Protects PbpB (PBP3, FtsI) from oxidative stress-induced cleavage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18310019, ECO:0000269|PubMed:7868268}. Note=Localizes to the cell poles.
Interaction partners:
- Serine/threonine-protein kinase PknB
- Cell wall synthesis protein CwsA
- Cell division protein FtsZ
- Cell division protein FtsQ
- Serine/threonine-protein kinase PknA
- Cell division protein SepF
- Probable transmembrane protein
- PASTA domain-containing protein
- Peptidoglycan D,D-transpeptidase PbpA
- Penicillin-binding protein 1A
Sequence:
MPLTPADVHNVAFSKPPIGKRGYNEDEVDAFLDLVENELTRLIEENSDLRQRINELDQELAAGGGAGVTPQATQAIPAYEPEPGKPAPAAVSAGMNEEQALKAARVLSLAQDTADRLTNTAKAESDKMLADARANAEQILGEARHTADATVAEARQRADAMLADAQSRSEAQLRQAQEKADALQADAERKHSEIMGTINQQRAVLEGRLEQLRTFEREYRTRLKTYLESQLEELGQRGSAAPVDSNADAGGFDQFNRGKN
Protein: Two-component response regulator ORR30 (Protein EARLY HEADING DATE 1) (Two-component response regulator EHD1) (Q7Y0W5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional activator that acts as floral inducer to promote short-day (SD) flowering pathway. Activates HD3A and other FT-like genes independently from HD1. May also activate MADS-box transcription factors involved in flowering regulation. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. May directly activate some type-A response regulators in response to cytokinins (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MDHRELWPYGLRVLVIDDDCSYLSVMEDLLLKCSYKVTTYKNVREAVPFILDNPQIVDLVISDAFFPTEDGLLILQEVTSKFGIPTVIMASSGDTNTVMKYVANGAFDFLLKPVRIEELSNIWQHIFRKQMQDHKNNNMVGNLEKPGHPPSILAMARATPATTRSTATEASLAPLENEVRDDMVNYNGEITDIRDLGKSRLTWTTQLHRQFIAAVNHLGEDKAVPKKILGIMKVKHLTREQVASHLQKYRMQLKKSIPTTSKHGATLSSTALDKTQDHPSRSQYFNQDGCKEIMDYSLPRDDLSSGSECMLEELNDYSSEGFQDFRWDSDKQEYGPCFWNF
Protein: Small ribosomal subunit protein uS19m (37S ribosomal protein S19, mitochondrial) (P53733)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein mS33
Sequence:
MQPAARLLSRSVWKGPNIVPLPIREAMTKGTPIRTNARAATILPQFVGLKFQIHNGKEYVPIEISEDMVGHKLGEFAPTRKRFSYTQTKNK
Protein: Chaski, isoform A (Chaski, isoform B) (Chaski, isoform C) (LD30953p) (MIP06944p) (Q8T043)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein, isoform D
Sequence:
MAKLATDPNASNNNSCEAVNNNHNGQNQSQNGGASNYQALPLTPAPANTPLHKAIKHDLFPEVTFCNLSVEELADGAGHSRVVRSSVIELEDGTMTCLMNGNGQVKRRKRLISNESGDSIDSSSTEKKTPKMPDGGYGWVVVFASLVVSLIADGLSFSFGLINVELLEYFGESTSKTAWISSLFFSVPLLMGPIWSNLVDKYGCRKMTILGGVVSAFGFALSSFCNSIEMLMVTFGIISGLGLGIGYVTAVVSIAFWFDKKRTFATGIGASGTGIGTFVYARLTSYLIESYGWRGATLILGGTMLNACVCGALMRDPDWLIEENRLESRSQSVTTFSNSSVCLEEIKKLLDTGITKEAVLDSLVTKNNTEANQQIDDPLDSALKRYRSEIFLPTFLSTQELDSICEVKSLSRRSLRHKEGEEAPSRENLLSMSSGAGAYPPSTAVIGSPDDTLMGGIAHEAAEEAKKAYLASIETLSPSEKRSTGRTPNGSLRSSDEGYLTQKHASSRYSLNENIFMAKHTTPSISNLKVNGLRHNSVDILSEDMHCYYSKDETFALLEPSRRIRPTVIAIPEQEQSVNSELATRRARLDSITGIRRLSRSKKPSHHRSNLRRNISIRNSNFLKDMRIHRNSIHYRGAMLNTHRYRLRASSCPNIYRNSMTTIAKEEEDTWYDNFVDTMKSIFDFSLFLDMKFALFNLSTLFLFIWFIIPYLYLPDYMKQYKYDVSQSAELISDVGIAQTVGMIGLGYLGDLSWMNINICYSLCMLVCGASVFFMPLLITNYMGLMVMCVIFGFTFASSFSFTPSILVSIVDLDDFTCAYGLVLLVQGVGMIAGPPIAGVIYEYTGRWDDTFYYAGIFIALSGVCSYLIEFCEKKAPKESDSDVLETKKAQLLH
Protein: Zygotic DNA replication licensing factor mcm6-B (EC 3.6.4.12) (Zygotic minichromosome maintenance protein 6-B) (zMCM6-B) (zMCM6b) (Q7ZY18)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. The existence of maternal and zygotic forms of mcm3 and mcm6 suggests that specific forms of mcm2-7 complexes may be used during different stages of development. May replace mmcm6 in the mcm2-7 complex.
Subcellular location: Nucleus {ECO:0000250}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250}.
Interaction partners:
Sequence:
MDLVDPSQSAAAAAGTQLVKDEVAEKCQKLFQDFLEEFRGSDGELKYQSDAEELIRPERNTLLVSFVDLEQFNQQLATTIQEEFYRVYPYLCRAVKAFARDHGNIPQNKEFYVAFQELPTRHKIRELTTPRIGSLLRISGQVVRTHPVHPELVSGTFLCLDCQTLVRDVEQQFKYTQPSICRNPVCANRKRFMLDTNKSRFVDFQKVRIQETQAELPRGSIPRSVEVILRAEAVESCQAGDRCDFTGSLIVVPDISQLSTPGVRAETSSRVGGREGYEAEGVQGLRALGVRDLSYKLVFLACYVCPTNPRFGGKDLHEEDMTAESIKNQMSVKEWEKVFEMSQDKNLYHNLCTSLFPTVHGNDEVKRGILLMLFGGVPKSTMEGTSLRGDINVCVVGDPSTAKSQFLKHVEEFSPRAVYTSGKASTAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDTKDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVGGRYDRAKSLKQNVNLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYTLDEVRRYLLFARQFKPKISKESEDFIVEQYKRLRQRDGSGVTKSAWRITVRQLESMIRLSEGMARMHCSDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEDEHEVEEPQEGINGDADVPNGVNGHINGINGHAEETNAAPPKPSLRLNFAEYKRISNLLVLQLRKIEDEDDENETSQRKSELINWYLKEIESEIDSEEELVNRKQIIDKVIHRLVHYDQILIELIQTGLKGTEDENVAKEEDPYLVVNPNYILED
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6ADL5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAALSGGGGSSSGGGGGGGGGGGGGGGGGAEQGQALFNGDMEPEAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGADFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQTPTDVSRNNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPVPQEEAFSAETTLPSGCSSAPPSDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSSSTEDRSRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGEFAAFK
Protein: DNA replication licensing factor Mcm2 (EC 3.6.4.12) (Minichromosome maintenance 2 protein) (DmMCM2) (P49735)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P25205}. Chromosome {ECO:0000250|UniProtKB:P25205}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000250|UniProtKB:P25205}.
Interaction partners:
- DNA replication licensing factor MCM4
- Cell division control protein
- CDC45L
- Double parked, isoform A
- DNA replication complex GINS protein PSF3
- Probable DNA replication complex GINS protein PSF2
- Origin recognition complex subunit 2
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- DNA replication complex GINS protein PSF1
Sequence:
MDNPSSPPPNTPSDAAERRDLRAAMTSPVGDFEPFENEDEILGDQTVRDEAEEEDGEELFGDNMENDYRPMPELDHYDPALLDDEDDFSEMSQGDRFAAESEMRRRDRAAGIHRDDRDLGFGQSDDEDDVGPRAKRRAGEKAAVGEVEDTEMVESIENLEDTKGHSTKEWVSMLGPRTEIANRFQSFLRTFVDERGAYTYRDRIRRMCEQNMSSFVVSYTDLANKEHVLAYFLPEAPFQMLEIFDKVAKDMVLSIFPTYERVTTEIHVRISELPLIEELRTFRKLHLNQLVRTLGVVTATTGVLPQLSVIKYDCVKCGYVLGPFVQSQNTEIKPGSCPECQSTGPFSINMEQTLYRNYQKITLQESPGRIPAGRIPRSKDVILLADLCDQCKPGDELEVTGIYTNNYDGSLNTDQGFPVFATVIIANHVVVKDSKQVVQSLTDEDIATIQKLSKDPRIVERVVASMAPSIYGHDYIKRALALALFGGESKNPGEKHKVRGDINLLICGDPGTAKSQFLKYTEKVAPRAVFTTGQGASAVGLTAYVRRNPVSREWTLEAGALVLADQGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSMTFSENVNLSEPILSRFDVLCVVKDEFDPMQDQQLAKFVVHSHMKHHPSEEEQPELEEPQLKTVDEIPQDLLRQYIVYAKENIRPKLTNIDEDKIAKMYAQLRQESFATGSLPITVRHIESVIRMSEAHARMHLRENVMEADVSMAIRMMLESFIEAQKFSVMKKMRSTFQKYLSFQKDHSELLFFILRQLTLDQLAYIRCKDGPGATHVEIMERDLIERAKQLDIVNLKPFYESDLFRTNGFSYDPKRRIILQIVVDGNTA
Protein: Esculentin-2Ra (P86017)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000269|PubMed:18855342}.
Interaction partners:
Sequence:
GILSLVKGAAKLLGKGLAKEGGKVGLEFIACKVTNQC
Protein: Uncharacterized transcriptional regulatory protein C757.04 (O74915)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}.
Interaction partners:
- FAS1 domain-containing protein fsc1
- Ubiquitin-like-conjugating enzyme ATG10
Sequence:
MSHRIRHLSCLACRRKKVKCNRQYPCTRCLKYGEACTYDERDNRKKRHSLSYLHSLESQLARLESFIMTLKNSDPEGRDEMLKSVVFSDHLTEPNDQEVKSEGPIEYPVFLNVQDSKTVSFYGPTSAYDLSLPDITKDNKTTWNFQASYSPMVSECLKLFFRYQYSQFLFVYRESFLSDYYYNFHDGFYCTEHLIYAICAIGASMSDDENISRHSKSYYDASWQKLLEFGLDRSHLTSVQCLLCLGYYDIGMGNTSLGWLLSGLAFRMGQDLGFQLNPENWYIDNSPAISSADSDIRRRVFWGSYVADKFIGFIMGRPTMLKRSDASIPGSNQLPEFAGLEEFKLNVTDYMSLTDFSVCDAVALFVDLSDIADSILLNMFSPTSKNRATNINCVLSNLGKYNLELMNWHYKLPDTISWRTIDLKKDRIPNLCAVSLYYHLIRICLNRPFLSRKEVTANDLTPKTICTDSINEIVTVIRAHRTANGLRYSTLYIVYAAIVSCSVILLLRDMCTDSELLTLNNDMMFFIEVLKECSQTWKLAQRSIVLIENTLKGKTNSQSTSEFVSPISDTENGSSSQQVSEAKDIVEPSDVLDELQKFDLLPENDDNFQTFQAFYGGPPIILSPNLYEKKLNEKTL
Protein: Retinal dehydrogenase 2 (RALDH 2) (RalDH2) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A2) (ALDH1A2) (Retinaldehyde-specific dehydrogenase type 2) (RALDH(II)) (O93344)
Organism: Gallus gallus (Chicken)
Function: Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. Displays complete lack of activity with citral.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Uncharacterized protein
- Cytochrome P450 26B1
- Alcohol dehydrogenase 1
- Uncharacterized protein.
- NADP-retinol dehydrogenase
- S-
- Uncharacterized protein
- PKS_ER domain-containing protein.
- Uncharacterized protein.
Sequence:
MTSSKIEMPGEVKADPAALMASLHLLPSPTLNLEIKHTKIFINNEWQNSESGRVFPVYNPATGEQICEIQEADKVDTDKAVRAARLAFSLGSVWRRMDASERGQLLDKLADLVERDRAVLATMESLNSGKPFLQAFYVDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGFGPIVGAAIASHVGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIYVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGITEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTVDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGESGLREYSEVKTVTIKIPQKNS
Protein: Probable U6 snRNA-associated Sm-like protein LSm4 (Q19952)
Organism: Caenorhabditis elegans
Function: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y4Z0}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm3
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm2
- Probable small nuclear ribonucleoprotein-associated protein B
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm7
- Probable small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MVLPLSLLKTAQNHPMLVELKNGETYNGHLKACDSWMNIHLVDVIFTSKDGDKFFKMSEAYVRGSTIKYLRIPETVVDLVKTEVNEVRRQQQREQSRGRGGGRGGRGGHRGGGGNRGGRGGAR
Protein: Fatty acid 2-hydroxylase (EC 1.-.-.-) (Q8SXY2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Fatty acid hydroxylase domain-containing protein
- RE26969p)
- Paraplegin, isoform A
- Receptor expression enhancing protein A, isoform I
Sequence:
MPIDMDIPKEAESNDKFIVKYRQQYYDLSRFMHKHPGGINTLKGLNSGDMTARFLKAPPHSDAAMYLMREYKIDPEDSRKPKSSQRETLHHDEDGTLRQRPRETEDKNNNQVDDSMEHLVDWSKAMLPQIANITDCYDEWVHKPVDRPLRLFDPWYLEMCTKTPWWLVPLFWIPVIVKCAVEEFTTAWQDSNQLAVFSGYFLFGVLLWSFLEYTLHRWVFHVKLSNKSGSWLCTFHFMIHGLHHKVPFDPMRLVFPPLPGAVLAAVIYTPLSFVLSHPRVILSGALAGYLCYDMMHYYLHYGNPSLWAFVHMKRYHHHHHFSHQTLGYGISSPLWDVVFKTRIHLRKLRYQLRWS