wanglab/gogpt-training-data huggingface dataset:
Protein: U2 small nuclear ribonucleoprotein A' (U2 snRNP A') (P09661)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- ATP-dependent RNA helicase DHX15
- Splicing factor 3B subunit 2
- SNW domain-containing protein 1
- Splicing factor 3B subunit 3
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein F
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U4/U6 small nuclear ribonucleoprotein Prp31
- Protein BUD31 homolog
Sequence:
MVKLTAELIEQAAQYTNAVRDRELDLRGYKIPVIENLGATLDQFDAIDFSDNEIRKLDGFPLLRRLKTLLVNNNRICRIGEGLDQALPCLTELILTNNSLVELGDLDPLASLKSLTYLSILRNPVTNKKHYRLYVIYKVPQVRVLDFQKVKLKERQEAEKMFKGKRGAQLAKDIARRSKTFNPGAGLPTDKKKGGPSPGDVEAIKNAIANASTLAEVERLKGLLQSGQIPGRERRSGPTDDGEEEMEEDTVTNGS
Protein: Membrane-bound O-acyltransferase GUP1 (Glycerol uptake protein 1) (P53154)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Acts as an acyltransferase for GPI anchors that adds C26 fatty acids to the sn2 position of lyso-PI-containing GPI anchors. PER1 first deacylates, GUP1 subsequently reacylates the anchor lipid, thus replacing a shorter fatty acid (C16:0 or C18:0) by C26:0. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Together with GUP2, has an influence on the chemical composition of the yeast extracellular matrix (yECM) in yeast multicellular aggregates, such as biofilms and colonies. Involved in cell integrity and apoptosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15813700}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15813700}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:30184078}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- Lysophospholipid acyltransferase
- L-2-aminoadipate reductase
- Protein PER1
- Putative aldehyde dehydrogenase-like protein YHR039C
- Protein CWH43
Sequence:
MSLISILSPLITSEGLDSRIKPSPKKDASTTTKPSLWKTTEFKFYYIAFLVVVPLMFYAGLQASSPENPNYARYERLLSQGWLFGRKVDNSDSQYRFFRDNFALLSVLMLVHTSIKRIVLYSTNITKLRFDLIFGLIFLVAAHGVNSIRILAHMLILYAIAHVLKNFRRIATISIWIYGISTLFINDNFRAYPFGNICSFLSPLDHWYRGIIPRWDVFFNFTLLRVLSYNLDFLERWENLQKKKSPSYESKEAKSAILLNERARLTAAHPIQDYSLMNYIAYVTYTPLFIAGPIITFNDYVYQSKHTLPSINFKFIFYYAVRFVIALLSMEFILHFLHVVAISKTKAWENDTPFQISMIGLFNLNIIWLKLLIPWRLFRLWALLDGIDTPENMIRCVDNNYSSLAFWRAWHRSYNKWVVRYIYIPLGGSKNRVLTSLAVFSFVAIWHDIELKLLLWGWLIVLFLLPEIFATQIFSHYTDAVWYRHVCAVGAVFNIWVMMIANLFGFCLGSDGTKKLLSDMFCTVSGFKFVILASVSLFIAVQIMFEIREEEKRHGIYLKC
Protein: Heterogeneous nuclear ribonucleoprotein H1 (G8JLB6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MMLGTEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVELFLNSTAGASGGAYEHRYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYGNQGAVNSSYYSSGSRASMGVNGMGGLSSMSSMSGGWGM
Protein: RNA-editing ligase 1, mitochondrial (RNA ligase 1) (EC 6.5.1.3) (TbMP52) (P86927)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P86926}.
Interaction partners:
- RNA-editing complex protein nuclease, putative KREPB1
- RNA-editing ligase 2, mitochondrial
- DNA ligase
- DNA ligase, putative
- RNA editing complex protein MP63
- Mitochondrial RNA binding complex 1 subunit
- REH2-associated factor 1
- RNA editing associated helicase 2
- MP18 RNA editing complex protein
- Metallo-beta-lactamase domain-containing protein
Sequence:
MQLQRLGAPLLKRLVGGCIRQSTAPIMPCVVVSGSGGFLTPVRTYMPLPNDQSDFSPYIEIDLPSESRIQSLHKSGLAAQEWVACEKVHGTNFGIYLINQGDHEVVRFAKRSGIMDPNENFFGYHILIDEFTAQIRILNDLLKQKYGLSRVGRLVLNGELFGAKYKHPLVPKSEKWCTLPNGKKFPIAGVQIQREPFPQYSPELHFFAFDIKYSVSGAEEDFVLLGYDEFVEFSSKVPNLLYARALVRGTLDECLAFDVENFMTPLPALLGLGNYPLEGNLAEGVVIRHVRRGDPAVEKHNVSTIIKLRCSSFMELKHPGKQKELKETFIDTVRSGALRRVRGNVTVISDSMLPQVEAAANDLLLNNVSDGRLSNVLSKIGREPLLSGEVSQVDVALMLAKDALKDFLKEVDSLVLNTTLAFRKLLITNVYFESKRLVEQKWKELMQEEAAAQSEAIPPLSPAAPTKGE
Protein: Alternative oxidase (EC 1.-.-.-) (A2QWD9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004292}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004292}; Matrix side {ECO:0000256|ARBA:ARBA00004292}.
Interaction partners:
Sequence:
MNSLTATAPIRAAIPKSYMHIATRNYSNVIAMSGLRCSGSLVANRHQTAGKRFISTTPKSQIKEFFPPPTAPHVKEVETAWVHPVYTEEQMKQVAIAHRDAKNWADWVALGTVRMLRWGMDLVTGYRHPPPGREHEARFKMTEQKWLTRFIFLESVAGVPGMVGGMLRHLRSLRRMKRDNGWIETLLEEAYNERMHLLTFLKLAEPGWFMRLMVLGAQGVFFNGFFLSYLMSPRICHRFVGYLEEEAVITYTRAIKEIEAGSLPVWEKTEAPEIAVQYWKMPEGQRSMKDLLLYVRADEAKHREVNHTLGNLNQAIDPNPYAAKYKDPTKAHPNKGIADLKPMGWEREEVI
Protein: Probable phosphomannomutase PmmB (Phosphomannose mutase) (O53360)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- mannose-6-phosphate isomerase
- Mannose-1-phosphate guanylyltransferase
- Purine nucleoside phosphorylase
- Probable phosphomannomutase PmmA
- Putative glycosyltransferases
- Deoxyribose-phosphate aldolase
- Possible N-acyl-L-amino acid amidohydrolase AmiA1
- Peptidase M20 domain-containing protein 2
Sequence:
MTPENWIAHDPDPQTAAELAACGPDELKARFSRPLAFGTAGLRGHLRGGPDAMNLAVVLRATWAVARVLTDRGLAGSPVIVGRDARHGSPAFAAAAAEVLAAAGFSVLLLPDPAPTPVVAFAVRHTGAAAGIQITASHNPATDNGYKVYVDGGLQLLAPTDRQIEAAMATAPPADQIARKTVNPSENRASDLIDRYIQRAAGVRRCAGSVRVALTPLHGVGGAMAVETLRRAGFTEVHTVATQFAPNPDFPTVTLPNPEEPGATDALLTLATDVDADVAIALDPDADRCAVGIPTVSGWRMLSGDETGWLLGDYILSQTDDRASPPETRVVASTVVSSRMLAAIAAHHAAVHVETLTGFKWLARADANLPGTLVYAYEEAIGHCVDPTAVRDKDGISAAVLVCDLVAALKGQGRSVTDALDELARCYGVHEVAALSRPVSGAVETTDLMRRLREDPPRRLAGFPATVTDIGDTLILTGGDDNMLVRVAVRPSGTEPKLKCYLEIRCAVTGDLPAARQLVRARIDELSASVRRWW
Protein: Major capsid protein (Gene product 10A) (Gp10A) (Major head protein) (P19726)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Assembles with the minor capsid protein to form an icosahedral capsid with a T=7 symmetry, about 60 nm in diameter, and consisting of 415 capsid proteins. The major and minor capsid proteins are incorporated into the capsid in about a 90/10 ratio respectively. Once the capsid is formed, encapsidates one single copy of the viral genome.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04119, ECO:0000269|PubMed:20962334, ECO:0000269|PubMed:23884409}.
Interaction partners:
Sequence:
MASMTGGQQMGTNQGKGVVAAGDKLALFLKVFGGEVLTAFARTSVTTSRHMVRSISSGKSAQFPVLGRTQAAYLAPGENLDDKRKDIKHTEKVITIDGLLTADVLIYDIEDAMNHYDVRSEYTSQLGESLAMAADGAVLAEIAGLCNVESKYNENIEGLGTATVIETTQNKAALTDQVALGKEIIAALTKARAALTKNYVPAADRVFYCDPDSYSAILAALMPNAANYAALIDPEKGSIRNVMGFEVVEVPHLTAGGAGTAREGTTGQKHVFPANKGEGNVKVAKDNVIGLFMHRSAVGTVKLRDLALERARRANFQADQIIAKYAMGHGGLRPEAAGAVVFKVE
Protein: Uncharacterized protein (Q57UP5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCGTFCDVLEDPYTKDTWRLHDKMLYLVWWSHRPTSCTNCGTQDAWLPSEDSELKCWNCGTGAGTTADHDIVEERFDEANMSEEEEGGPDRSMVEGETSGGFATGDNNAVVATGGSAVSLYSFFYEWISVLQSTKQLSGIRLPKGECLSQVLRAAYDLAMLFVLPGTPGSGAMAMWGGALFLSLTLYRYAVPFPLFQLGGQLYDLRESPKASSDNRERIENLQWVDVELLSSLIGVVLPDFFESCSVGEQYMCNVMTVTAQFGVPSCIWHPRRISWYQDSILLMKKRRRLPTQTHGTPFPSEISPEHTAMIALLELARLFDSKPSSASVSARVGKWLDENGLYPQRTSYRSKECGDENLNDDNQQPNAAEAAGNASIPAAEEDTAWACGSLTTTSSPFAGAMHHVLQSPCANALLYMFAEVFSIPALELADMASSSGMYGGPVRTFEVLRDSACSGNYGLVPLSRRISPIVSPWTSVYFAIHSNDRLPFLAALQHVRSATSREKEIHFVRLIQAILRKHQSTRRYQFNYTINVKSEKSMSQIDGTYFLCYVAEQFAVFAAIGSAQRTLTFDSTNKSITFNSPQLRDVEVELIPEKRMSSSAKSEKPHEEASQASVGQSPHFRGHHHDKFQNNQYQSLPGAARPQSQRDAHRIHIKFSGPVIANVESSSAKCVIDCARQDLGSVQWQSVVRRLERCGRIRRRMRVPMLASRLDALASVRESTAMTSHPMNGSSTLGWRDTESLFGSTHHMLYVSQKYTATTLRREVQQDVLSLLRPSLVFGMSESRVVTMYAALIALLEITDRQLGSQARTSPRVPGGPPARTWLDELLSKEEWNFDDRPTQKTLNDTPSPPYPNRDTNGGGDAMVLPASTAAVQREQQDAKHRNSSDGQQRCPNGSRHSTQCNATTEAFPSYEEVLMGRVKMITNGAGGRNSGTRFLRFTKSQKQRRPCTEGSAGGVSVDNPSASAVDDPSNLNFTSFNLFKAEICRRRLYRLLCFIDEYKRKGHAELKRPPHEIRADTHMAVKAEDHKAFKREDSPPLYSAQTPNVCANRSPRHSFTSARKSNTPLLGPQPNKTTPTTPPRHATSPIVEPIKLPPQAEQSVWGCRSSGSSGHRNGDNTNHTHNRIYHTGVGDRPPQSRASSNDGGSIENRKPMGEWSSKKFRRTK
Protein: DUP240 protein DFP4 (P38727)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:12101299}; Multi-pass membrane protein {ECO:0000269|PubMed:12101299}.
Interaction partners:
- Putative UPF0377 protein YHL045W
- Uncharacterized protein YHL049C
- Putative uncharacterized protein YHL046W-A
- Uncharacterized protein YHL048C-A
- Uncharacterized protein YHL041W
- Uncharacterized protein YHL050C
- Putative UPF0377 protein YKL223W
- Putative uncharacterized protein YAR070C
- Putative uncharacterized protein YAR069C
- Protein COS8
Sequence:
MSSELLISNSKPRPEGLRKLCEGETVILPRDITPSKCAYFLKQNIVFISYIFIHIIITIILNRLALSAHGNTLIIILAALLITISLFLLLLLPYLSCSRYKLRCLDDDCKFKLLAEVITHKPNMDLSTWDRIAYDMNQFVYDRRICADRSFFYDGSYCYQVFKKLVATPYLVNSNMNSIYADLEMRSNGATNINDSGNSSLHIELGTYIFKALAVFRNSVDKYWEDKYPEMGVTV
Protein: SUF system FeS assembly ATPase SufC, putative (Q72DA7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- SUF system FeS cluster assembly SufBD core domain-containing protein
- Nitrogen fixation protein NifU
- Quinone oxidoreductase
Sequence:
MLEIRDLHVCIGDVEVLKGINLHIRPGETFILFGPNGSGKTTLLMTLMGFANYKVTQGQILFKGHDITNAPMYERARLGMGMSFQRPPTIHGLKTGHLVRMCGRGREVDVEGLAQRVNFDRFLERDVNAGFSGGEIKRSELLQLMAQQPDLVLFDEPESGVDLENMSLIGQTARQLLDGIAPASCASIKQRKAACKTAGLIITHTGYILEYVNADRGQVMYDGHLCCEARPRDILEHIGKHGYQECLRCLDSDIKGGL
Protein: Phosphatidylinositol glycan anchor biosynthesis class C, isoform B (Q9VZR1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVKNGQSKRQPWVKNLYSNREYPDNYTDASFLKDLRTNLHCRIYTFGEAIAGITVLNNQISCITGFLILYQLMLSDSVSPTTILVPSCGITGIGYLCYRGRSLSWALLGEDSKTLVTVVLFGYLFSPMLHTLTQAISTDTIYTMTFFVLLGNLIFGHYGLDVAMVSKAVSLNAAIFGAICLASRLPTSYHAFVLLVEAAVFFVLYPIMTEANWHAGFMLPIFAICCMALYCISRPVLYLYASTTIFINFVCPFIFVWQQQYKFNIHGPWDEAIVEENTEENLDGNL
Protein: Lysozyme (EC 3.2.1.17) (B1B1Z5)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Interaction partners:
Sequence:
MNYSQKAIDLCKKYSNFSLKAVAGRNGILSIGYGHFTNEKHPIKPGMVITESQATQILRDDLNEHAALISKLLAIKATQNQFDALVSFSHSKGLGFLPSSDIMHFTNNKEFNSAAREMKLYVYDIGSIKLPKLVERRNAETALYLEGASGNEETTNHARIGFDVMIRWMEQKKAQHITYSMDYRLGPNSYDCSSAVYFALKEAGFIDPSTFPGNTDSLFGQLERVGWSQVPLVGGKYHVQRGDIFIWGIRGNSGGELGHTGIFIDDKDNIIHCTCGWDGNKCSINGISVDNHDQVWVASGRPPVTIYRFGGASKPYPGDSSGSKGDSVNPSAGVFYPSMRLPVSGDTDPNSPALDYYEAGQAIVYDSYVFANGYAWISYVAGSGLRRYVAVGPDDGRTDTVWGTGFLNNTPSGSGSNTGSALSGVFYPSMRLPVSGDTDPNSPALAYYEAGQAIIYDSYVFANGYAWISYIAGSGLRRYVAVGPDDGRTDTVWGTGFFDNGGDPGSQAHPNSIGLVPKAGNFVPNRKLPVSADTDPNSAALDYYEAGQSIGYDSYIFANGYAWISYIAGSGLRRYVAVGPDDGRTDTVWGKGFFN
Protein: Beta-1,3-galactosyltransferase 4 (Beta-1,3-GalTase 4) (Beta3Gal-T4) (Beta3GalT4) (GalT4) (b3Gal-T4) (EC 2.4.1.62) (Gal-T2) (Ganglioside galactosyltransferase) (UDP-galactose:beta-N-acetyl-galactosamine-beta-1,3-galactosyltransferase) (O96024)
Organism: Homo sapiens (Human)
Function: Involved in GM1/GD1B/GA1 ganglioside biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z0F0}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
- Beta-galactosidase
- Lactosylceramide 4-alpha-galactosyltransferase
- WD repeat-containing protein 46
- Small ribosomal subunit protein uS13
- Beta-1,4-galactosyltransferase 6
Sequence:
MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPNQEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPVWGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYVNVPELVSELVLRGGRWGQWERSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTPGGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARRGGLAPTQCVKLAGATHYPLDRCCYGKFLLTSHRLDPWKMQEAWKLVGGSDGERTAPFCSWFQGVLGILRCRAIAWLQS
Protein: Protein O-glucosyltransferase 2 (EC 2.4.1.-) (Endoplasmic reticulum resident protein 58) (ER protein 58) (ERp58) (KDEL motif-containing protein 1) (Protein O-xylosyltransferase POGLUT2) (EC 2.4.2.-) (Q9JHP7)
Organism: Mus musculus (Mouse)
Function: Protein glucosyltransferase that catalyzes the transfer of glucose from UDP-glucose to a serine residue within the consensus sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of xylose from UDP-xylose but less efficiently. Specifically targets extracellular EGF repeats of proteins such as NOTCH1, NOTCH3, FBN1, FBN2 and LTBP1. May regulate the transport of NOTCH1 and NOTCH3 to the plasma membrane and thereby the Notch signaling pathway.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:11167020}.
Interaction partners:
- Glucoside xylosyltransferase 2
- Glucoside xylosyltransferase 1
Sequence:
MFSISLLSCLFLGTVPALAQTGGERRLSPEKSEIWGPGLKAHVVLPARYFYIRAVDTSGEQFTSSPGEKVFQVKISAPDEQFTRVGVQVLDRKDGSFIVRYRMYASYRNLKIEVKHHGQHVAESPYVLRGPVYHENCDCPLEDSAAWLREMNCSETISQIQKDLAHFPTVDPEKIAAEIPKRFGQRQSLCHYTLKDNKVYIKTHGEHVGFRIFMDAILLSLTRKVRMPDVEFFVNLGDWPLEKKKSNSNIQPIFSWCGSTESRDIVMPTYDLTDSVLETMGRVSLDMMSVQANTGPPWESKNSTAVWRGRDSRKERLELVKLSRKHPELIDAAFTNFFFFKHDESLYGPIVKHISFFDFFKHKYQINIDGTVAAYRLPYLLVGDSVVLKQDSIYYEHFYNELQPWKHYIPVKSNLSDLLEKLKWAKEHDAEAKKIAKAGQEFARNNLMGDDIFCYYFKLFQGYANLQVSEPQIREGMKRVEPQSEDDLFPCTCHRRKAKDEL
Protein: NudC domain containing 2 (E5RFP0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAPFEERSGVVPCGTPWGQWYQTLEEVFIEVQVPPGTRAQDIQCGLQSRHVALSVGGREILKGKLFDSTIADEGTWTLESEYAADPWVQDQMQRKLTLERFQKENPGFDFSGAEISGNYTKGGPDFSNLEK
Protein: Treslin (TopBP1-interacting checkpoint and replication regulator) (TopBP1-interacting, replication-stimulating protein) (D3IUT5)
Organism: Xenopus laevis (African clawed frog)
Function: Regulator of DNA replication and S/M and G2/M checkpoints. Regulates the triggering of DNA replication initiation via its interaction with topbp1 by participating in cdk2-mediated loading of cdc45l onto replication origins. Required for the transition from pre-replication complex (pre-RC) to pre-initiation complex (pre-IC). Required to prevent mitotic entry after treatment with ionizing radiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20116089}. Note=Associates with chromatin.
Interaction partners:
Sequence:
MAPSHNVVLLVDTAESSDKSRLRRVSLRLLNFLACRAGLGQVRWSYRFLNSSGGRCRPPRRSDLRELGPRGWEEFEDELEACWERARNCRPSSTQSSRAQLLQTALMETLADFQWDRPDITSPTKPTLLRSRRGRIVAADEPLKDDSPDNFINPHSRNSIFLLSSCPHSGTELGQFAATSGDFSTQKVMDKLLPKSLQKIVSSKRVRVYWLDTSDWTQFGSSSDHSGYWTMVELMHQVEGRILPSESILGSSCQKAKTLPSFSVPPINIPFESVLNYLIFSEPDYQLWFPRRDGILFLTGKDGTKQLDCAVSLEPVSMIQKLSTSLMTIELKGTMQNCNLPLAGLRVETWLLHNSDCVQLQKLTKELMLKELHMIATVTLEDDVLPRTGILSPLSETAAVLNVICSERTLGLDNLHVQGSVHETDKETFSDLPDIVMSVLNHVYSSEDNTLAPDFPVPEWIKQELSQSSRWTSSVTARWYPLSGVSGASCNLMESFRLINAASSNCDEHLKFDQELTNYLSEFYQKKSVDDAGLGVHRENQKKSGLPRTPVRQKMKTLPRALQMLNAARLNVKAQKADSTLPVPNEKNSQMKRRSSGKQDNKPKQLKPTEFQSEDGLISYIKENYEEAVSLVDHSTMTWARDTLTTIKSYLKSIGSEQIETEAIDKVKLLFKTSKVIRQNYRNNQDKEVKLKECQLQVFLRLEMFVQCPVIQMDSDELELIIEEITDILRIVSLTEDPLFLTKFLEVDVLTQYIASVPKILADIYFSLGTQIPEVLVLVLPSDGDDSIMHEEKSVKSQPSTSRVPSVAPIGAETDQLEDLRTRSAKKRRSTALARHRSVAESSQSFRQIEVPKRQPNKENVQSNAVVVLEKLKLPLPAQPQKDAEAKVRRNLFIQETRSPSKRCSKMPRSQSVSAVESLKRKRSKSHDGSKDHHKLLTKKVSETPVHKQTANRLLLRQIKGRPSESNSNISIVEESPEKEIRDIDLRRSPRIKQLSLTRRNSSSFYASQPKSRNLERVNSATQLQQSRERPGSCLISEVKTPKRLLFGEVLGMISPPTTKRSRRILDMVNPVYKTPGKTPRKTPSKNIPNFEDQSGNMLVKSPCTPYTPRTPSRTPKRLKTPSKGSTERKKAAKNLGKLFSPSKPEEKSPLKLWGRRSERLAQMTPGKDGSPYKQSVCQTLMEVKTPQKLQRLESKDFRTPSRTPTRSNNTTPAKQSMQISNTPRKSDLKHPQEHESRGPSGYILWTPQKRILASVPHTPILQTPQKPISASVPRTPVCRTPQKAILSSVPSTPVCQTPNKAILTSVSRTPVYQTPQKAILASVMSTPVYQTPQKPVLASVPTTPILKTPQRSALASVSHTPSPKKYIMKELTVAITRMRECTPEKVLGSNLSSSATPSSALKSFCSEKTTSVCQTPKKSSIALLKPCDSLEFSGAPERLMDSLCSNKDSTKAETACTVPSQISTQMQNVINAGECTDSLSQTSVSSPSIPFTDKSLSPDLKDALSDVTSSKAEGVTIVSEKLDSSSMDSQEATDSFINSSQTEESIDISEARVVSTEASELKMKVLITRKPSGSGVSYLPTTPKCLGNVCSTSTYGLRCTPDRRQREAAARLGTPEIPAKFSTPKSHCKMIPQSIYEVELEMQESGLPKLRFKRTDSNSTIDMDVNKTPKISRKRKGDESPFNEKWCSKHAVRTEPACVSPSCVRTSHYTPGKSGIQTFICQSYTPNRCLSAAASPSQSDAGVPWTPSPKEKLSTDVINSWPRKKKASALCTNLLKCDKIPEYAEEDGGDFELEGVSKLLEKSPVIEQQSKVDGGTFGLRSRKRVFSLVSPTKETENPVKRVCTFNRHEDSSTATHRHQTKEEMEIFSSDQSRSSYLSSSQQSICDDVFNMSDFTPPSKVPKNPLSACGLLTLTQSPLLYKGKTPSSKRKEKIQDVFSDGDSDHGTPTLKRPTNPAAVSDDSPFRKVNPLRSISKTYSRKKLIT
Protein: RGS domain-containing serine/threonine-protein kinase A (EC 2.7.11.1) (RGS domain-containing serine/threonine-protein kinase 1) (Q54XQ2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Serine/threonine kinase involved in negative regulation of chemotaxis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12686622}. Cell membrane {ECO:0000269|PubMed:12686622}. Note=Translocates very rapidly to the plasma membrane upon stimulation by chemoattractant, but no polarized localization to the leading edge in aggregating cells.
Interaction partners:
- Probable stress-associated endoplasmic reticulum protein
Sequence:
MKTSKDSSNSNSNNNNNNNNNNNNNNNNNNGLNGTYSSKSLSPPTSPKQMSGNSIISNSTGNLSSGSGSGSSSGGNKKFINRSFNTFIDFIKKPARRNSKAHNTPPPYPEVDTGFGYFLELDSKPPKPFDEKDDPIHNSTGSTDSWEGDLNSSGGGGKQPQQTQQQSSGENLNNSSDRNNNSNENNQIVDDNSNVFNKGVVVQTVPMTEIGLFPVSLMMAQQRAEHPINVEDIESDVQTCSIPNSKPLYSSLGCSTNSSNSGSSISAPNITFQSFGISPVNNNNNNNNNSNNNSNSNSNSNSNSNNNNNNNNNNNNNNNNNNNNNNNNNSTVNSNNSSLNNSPRYLNSSSSPRSMQHLSSKITTTTTTTTTTTTTTSDDNNGNTNNNISNNNNIINNSNNNSNSNNNNNNNINNTNHKFKTMEKYFSSKENFPIPFPKLKDELGVIIENSSNKGYVGGNKGSEDRRKKIEQKKKQVPAPEMKATKEKFIETITDPTTLNSFRSFMENTQSNENLEFFLEVKRFNTIQDQVLLKHTCDDIWRRFFDDLAVTQLCVESSLKKLINNRRENPTHSMFNEVLDLLLDDIVCDAFRNYISSPFNPEWKSEFKKKFTNNTYSTTTQPINNFNNTNNNNNNNCSTPPNNYSSSPIKQSNINNNNNNASSSNIASSSNVNNNNNNSNGSNTSSSHHRERLDNIKGNRERVDSNGKERSIDNKDILSLLESNLSNHSNSSSNSNGKDKDKDKDKNENTTDNSNNNNNSNNNLNNLIIKNNFNNILQSPQIVSKINEIFKDSNNSQLSISITLDNDEDPTIFHLDESDMESLIEEVVKDNISVHTEISYSDVSIHKWIASGSSGRVYNGQYKGKDVAIKVLGPEVCVHFDLNEFKREVALMSIFKHDNLARCLGAGQYDDKYFHLTEYCHNGSLFSYLRDQRNNISFGQRLHFALGIARGMRYLHSMSIIHRDLKSMNILLTKRLKIKIVDFGTSRVANKYNMTTHVGTQAWMAPEIFTSRTYTNKVDVYSYAIILFEIFTRKSAYDENANINIPNMVMKGERPELPKDMQTSISNIIKKCWQQKPSNRPSFIKIVAYLESIIYPSVSNSLGLVASTSFSSSALWSGQILAQPKN
Protein: Large ribosomal subunit protein bL28m (54S ribosomal protein L24, mitochondrial) (O60091)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000250|UniProtKB:P36525}.
Interaction partners:
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein bL9m
Sequence:
MASKLLRKLAYPTLPVKGKIYDPFSKFQQNLYGGSKTEAGNNKIPKFGHKTRRVWIPNGHSKWLYSNVLEEKFHLYVTSRVLRTIDKEGGLDEYLVKSTPSRLKSLGLRGVELRALVLHKLGAKNPILEKLPSDSGAQKRYLEKVKDVVLKLNRSKKLYQQIKSLVGKERSVNTSV
Protein: Hydroxyproline O-galactosyltransferase GALT2 (AtGALT2) (EC 2.4.1.-) (Beta-1,3-galactosyltransferase 20) (A7XDQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23430255}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,6-galactosyltransferase GALT31A
- Beta-1,6-galactosyltransferase GALT29A
- Beta-glucuronosyltransferase GlcAT14A
- Fucosyltransferase 6
- Hydroxyproline O-galactosyltransferase HPGT3
- Probable fucosyltransferase 4
- Beta-1,3-galactosyltransferase 7
- Hydroxyproline O-galactosyltransferase HPGT2
- Beta-arabinofuranosyltransferase RAY1
- Beta-glucuronosyltransferase GlcAT14C
Sequence:
MKRVKSESFRGVYSSRRFKLSHFLLAIAGFYLVFLAFKFPHFIEMVAMLSGDTGLDGALSDTSLDVSLSGSLRNDMLNRKLEDEDHQSGPSTTQKVSPEEKINGSKQIQPLLFRYGRISGEVMRRRNRTIHMSPFERMADEAWILGSKAWEDVDKFEVDKINESASIFEGKVESCPSQISMNGDDLNKANRIMLLPCGLAAGSSITILGTPQYAHKESVPQRSRLTRSYGMVLVSQFMVELQGLKTGDGEYPPKILHLNPRIKGDWNHRPVIEHNTCYRMQWGVAQRCDGTPSKKDADVLVDGFRRCEKWTQNDIIDMVDSKESKTTSWFKRFIGREQKPEVTWSFPFAEGKVFVLTLRAGIDGFHINVGGRHVSSFPYRPGFTIEDATGLAVTGDVDIHSIHATSLSTSHPSFSPQKAIEFSSEWKAPPLPGTPFRLFMGVLSATNHFSERMAVRKTWMQHPSIKSSDVVARFFVALNPRKEVNAMLKKEAEYFGDIVILPFMDRYELVVLKTIAICEFGVQNVTAPYIMKCDDDTFIRVESILKQIDGVSPEKSLYMGNLNLRHRPLRTGKWTVTWEEWPEAVYPPYANGPGYIISSNIAKYIVSQNSRHKLRLFKMEDVSMGLWVEQFNASMQPVEYSHSWKFCQYGCTLNYYTAHYQSPSQMMCLWDNLLKGRPQCCNFR
Protein: Antithrombin (Q8IZZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KVYLLSLLLIGFWDCVTCHGSPVDICTAKPRDIHMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLME
Protein: Transcription factor SOX-14 (Protein SOX-28) (O95416)
Organism: Homo sapiens (Human)
Function: Acts as a negative regulator of transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Transcription factor SOX-2
Sequence:
MSKPSDHIKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPYIDEAKRLRAQHMKEHPDYKYRPRRKPKNLLKKDRYVFPLPYLGDTDPLKAAGLPVGASDGLLSAPEKARAFLPPASAPYSLLDPAQFSSSAIQKMGEVPHTLATGALPYASTLGYQNGAFGSLSCPSQHTHTHPSPTNPGYVVPCNCTAWSASTLQPPVAYILFPGMTKTGIDPYSSAHATAM