wanglab/gogpt-training-data huggingface dataset:
Protein: Wings apart-like protein homolog (Friend of EBNA2 protein) (WAPL cohesin release factor) (Q7Z5K2)
Organism: Homo sapiens (Human)
Function: Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.
Subcellular location: [Isoform 2]: Nucleus.; SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000269|PubMed:26299517}. Cytoplasm. Note=Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase.
Interaction partners:
- Sister chromatid cohesion protein PDS5 homolog A
- Double-strand-break repair protein rad21 homolog
- Structural maintenance of chromosomes protein 3
- Cohesin subunit SA-1
- Sister chromatid cohesion protein PDS5 homolog B
- Nipped-B-like protein
- Sororin
- Cohesin subunit SA-2
- Structural maintenance of chromosomes protein 1A
- N-acetyltransferase ESCO1
Sequence:
MTSRFGKTYSRKGGNGSSKFDEVFSNKRTTLSTKWGETTFMAKLGQKRPNFKPDIQEIPKKPKVEEESTGDPFGFDSDDESLPVSSKNLAQVKCSSYSESSEAAQLEEVTSVLEANSKISHVVVEDTVVSDKCFPLEDTLLGKEKSTNRIVEDDASISSCNKLITSDKVENFHEEHEKNSHHIHKNADDSTKKPNAETTVASEIKETNDTWNSQFGKRPESPSEISPIKGSVRTGLFEWDNDFEDIRSEDCILSLDSDPLLEMKDDDFKNRLENLNEAIEEDIVQSVLRPTNCRTYCRANKTKSSQGASNFDKLMDGTSQALAKANSESSKDGLNQAKKGGVSCGTSFRGTVGRTRDYTVLHPSCLSVCNVTIQDTMERSMDEFTASTPADLGEAGRLRKKADIATSKTTTRFRPSNTKSKKDVKLEFFGFEDHETGGDEGGSGSSNYKIKYFGFDDLSESEDDEDDDCQVERKTSKKRTKTAPSPSLQPPPESNDNSQDSQSGTNNAENLDFTEDLPGVPESVKKPINKQGDKSKENTRKIFSGPKRSPTKAVYNARHWNHPDSEELPGPPVVKPQSVTVRLSSKEPNQKDDGVFKAPAPPSKVIKTVTIPTQPYQDIVTALKCRREDKELYTVVQHVKHFNDVVEFGENQEFTDDIEYLLSGLKSTQPLNTRCLSVISLATKCAMPSFRMHLRAHGMVAMVFKTLDDSQHHQNLSLCTAALMYILSRDRLNMDLDRASLDLMIRLLELEQDASSAKLLNEKDMNKIKEKIRRLCETVHNKHLDLENITTGHLAMETLLSLTSKRAGDWFKEELRLLGGLDHIVDKVKECVDHLSRDEDEEKLVASLWGAERCLRVLESVTVHNPENQSYLIAYKDSQLIVSSAKALQHCEELIQQYNRAEDSICLADSKPLPHQNVTNHVGKAVEDCMRAIIGVLLNLTNDNEWGSTKTGEQDGLIGTALNCVLQVPKYLPQEQRFDIRVLGLGLLINLVEYSARNRHCLVNMETSCSFDSSICSGEGDDSLRIGGQVHAVQALVQLFLERERAAQLAESKTDELIKDAPTTQHDKSGEWQETSGEIQWVSTEKTDGTEEKHKKEEEDEELDLNKALQHAGKHMEDCIVASYTALLLGCLCQESPINVTTVREYLPEGDFSIMTEMLKKFLSFMNLTCAVGTTGQKSISRVIEYLEHC
Protein: Interleukin-18 (IL-18) (E0AFT5)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR015162}.
Interaction partners:
Sequence:
MSCEEIAVCAVRLRENLCLYFEDDELECDAFCKDKTIKRFFRNVNSQLLVVRPDLNVAAFEDVTDQEVKSGSGMYFDIHCYKTTAPSAGMPVASSVQVEDKSYYMCCEKEHGKMVVRFREGEVPKDIPGESNIIFFKKTFTSCSSKAFKFEYSLEQGMFLAFEEEDSLRKLILKKLPREDEVDETTKFVTSHNERHNL
Protein: Tubulinyl-Tyr carboxypeptidase 1 (EC 3.4.17.17) (Tubulin carboxypeptidase 1) (Tyrosine carboxypeptidase 1) (TTCP 1) (Vasohibin-1) (Q7L8A9)
Organism: Homo sapiens (Human)
Function: Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis. This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15467828, ECO:0000269|PubMed:27879017}. Secreted {ECO:0000269|PubMed:15467828, ECO:0000269|PubMed:16707096, ECO:0000269|PubMed:20736312, ECO:0000269|PubMed:27879017}. Note=Mainly localizes in the cytoplasm (PubMed:27879017). Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion (PubMed:27879017). {ECO:0000269|PubMed:27879017}.
Interaction partners:
- Small vasohibin-binding protein
- Tubulin alpha-1A chain
- Tubulin beta-3 chain
- Protein angel homolog 1
Sequence:
MPGGKKVAGGGSSGATPTSAAATAPSGVRRLETSEGTSAQRDEEPEEEGEEDLRDGGVPFFVNRGGLPVDEATWERMWKHVAKIHPDGEKVAQRIRGATDLPKIPIPSVPTFQPSTPVPERLEAVQRYIRELQYNHTGTQFFEIKKSRPLTGLMDLAKEMTKEALPIKCLEAVILGIYLTNSMPTLERFPISFKTYFSGNYFRHIVLGVNFAGRYGALGMSRREDLMYKPPAFRTLSELVLDFEAAYGRCWHVLKKVKLGQSVSHDPHSVEQIEWKHSVLDVERLGRDDFRKELERHARDMRLKIGKGTGPPSPTKDRKKDVSSPQRAQSSPHRRNSRSERRPSGDKKTSEPKAMPDLNGYQIRV
Protein: Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1) (A0A2R8YDP2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU369118}.
Interaction partners:
Sequence:
MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ
Protein: AFF4 protein (Q8TAX5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPKLVAIPKPTVPPSADEKSNPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRTSAGSSSGTNSSGQRHDRESYNNSGSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLNSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSTQSFPPSLMSKSNSMLQKPTAYVRPMDGQESMEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSQPLDASASGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGTGEQRLK
Protein: IP08064p (MCPH1 isoform A) (Microcephalin, isoform C) (A5YTR9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTNEPSITNKLRSLLLDDQAARDRLMLKPALAVSKAISQHRSEFHQDENEAGAEGSAAKPDPPIGAATPTRQEGHWARLQQDLNSPNAALRLRAIRALKSPTKSAYNTFDVPLAEQSIITMEERNPQEPPSLPELLKDIVVYVEVRTGNDNRSEGVKSIIAKMGAQVKDRLTRTTTHVVFKDGLLSTYKKATEWNIPVVSILWIEACKVQLKICDPKQFPISNIRMYEYPELFGKMPRVKFMQPDSELNQRPRKRQGTPTSSKDNEPGSTNKRAQTGTPTTTTPKNDISRFFRAINHNKPSDDEAIESPATKLLNRISSGCYTPLPAGGTPQLMGTNGSGDAVAQKVQAQKSLQFGEQTDSNTPQAKPSSTSRPRRSTVDPPPVMTPPVRTTRRRSCVAEISSPAATDTRMTRRRSSLLTSTVIHEADPTQTAVAEPRMTRRRSSLLGIAKQAEETAQRQTIQPITEELAPVEENRNSIIMAETNIINNTNCLEQSIEITAVEAEASFKADRRGTLYASELMDISSPRRRSVAKSSLELRQENLAPRARQSLSNVTTQTSFLDVEQQVTPLFSSTRLPTGQTTGNRRRTIFNMDMDVINESIERMNQSHRMSLALANKAELGESCQVHEQEPPQAEPVPSQEPKRRRLFNPNDEVVISPAMSNRKSRLSITGSGSSSSVQKRRRSLATPAKSSSSELCATTPLSKAVTNKEAEKSKSNTEISEASLDAVPEVKKSTSNAGEENEKPKGKSRTRIRTLVHTNMHQEQINVIRKALRKLRGMRLDPTVTQHTTHLVSLEPRRTLNLLRGLMRGVWIVSYQWVLASIRAGKWINEEPYELTRFSRAIEICRTERQAFGVHYQCELFRFMEPFYVSSLCRPVQFNNMKELLLLGGATLTENRFKAKYIIGDKRRAEDDRVYLDPYWVLDSITNMQIQRFGKYLMKSAIISADGIRYEDPRDRDEDKTQRRHLHDFVDPPFVLDK
Protein: Leucine-rich repeat protein lrrA (Q54AX5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cytoskeleton remodeling, which is needed for normal chemotactic aggregation and efficient cell sorting during multicellular morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16051212}.
Interaction partners:
- Latrophilin receptor-like protein A
- Severin
- Probable serine/threonine-protein kinase DDB_G0288795
- RAC family serine/threonine-protein kinase homolog
Sequence:
MGGNLSSELKSTKYRKREIVDLRKMNIDKLPPTIGALQCKELLLSENDLITIPEEIGKLSKVEIIDFAKNRINYIPPEIGSLATLKQLFLSNNKLFYTPITPNIGALKNLTRLDLSSNQLDDLPVEISNCEALEYLDISDNQLQSFPLEFGKLYNLQVFNCSKNSLKSLPSEISGWVKLEELNVSNNQLAFLPNQICLLGLLSTLNVGFNKLQQLPEELSSMVSLTNLDLKVNPPLQYVPQLSNLRQLKILSIRNLQITHLPLGLGLLSELIELDIRDNPQLKEIPYDIATLINLQKLDLFGNNMRIVPREVGNLINLQTLDLRQNKLTIDNIPSEIGKLVNLKKLLLSNNLLIALPPEIASMKALKEFEASNNQLQAIPTEIGELSGLTKINLSGNKLTSIPASFGNLSELQICDLKSNEIAELPTTLDGLKSCTKIDLSHNMLTELPWEFGDLIGLTILDVGHNPLTIPPNPIVMKGTESIIQWLKKNEKEGRKGKVSGLGIQQDNEK
Protein: Apoptosis regulator Bcl-2 homolog (F5HGJ3)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays a role in the protection against apoptosis mediated by cytotoxic cells during the immune response to acute and persistent viral infection. Contributes therefore to latency establishment. Plays also a role in the inhibition of host starvation-induced autophagy which ultimately contributes to the viral chronic infection. Participates also in the viral genome replication within host nucleus.
Subcellular location: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host mitochondrion {ECO:0000269|PubMed:20042497, ECO:0000269|PubMed:28053098}. Host nucleus, host nucleolus {ECO:0000269|PubMed:20042497}. Host nucleus {ECO:0000269|PubMed:28053098}.
Interaction partners:
Sequence:
MDEDVLPGEVLAIEGIFMACGLNEPEYLYHPLLSPIKLYITGLMRDKESLFEAMLANVRFHSTTGINQLGLSMLQVSGDGNMNWGRALAILTFGSFVAQKLSNEPHLRDFALAVLPVYAYEAIGPQWFRARGGWRGLKAYCTQVLTRRRGRRMTALLGSIALLATILAAVAMSRR
Protein: Acetylcholine receptor subunit beta-type unc-29 (Uncoordinated protein 29) (P48181)
Organism: Caenorhabditis elegans
Function: Non-alpha subunit of nicotinic acetylcholine receptor (nAChR). Involved in nAChR sensitivity to nicotine and levasimole.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein {ECO:0000255}. Note=Co-localizes with unc-38 and lev-1 at nerve cord synapses. {ECO:0000269|PubMed:15990870}.
Interaction partners:
- Acetylcholine receptor subunit alpha-type unc-38
- Acetylcholine receptor subunit alpha-type unc-63
- Acetylcholine receptor subunit beta-type lev-1
- AcetylCholine Receptor
- Protein unc-50
- Resistance to inhibitors of cholinesterase protein 3
- AcetylCholine Receptor
- Acetylcholine-gated chloride channel subunit acc-2
- CUB domain-containing protein
Sequence:
MRTNRLSWILVLSVVIFLVIINTINASDDEERLMVDVFRGYNSLIQPVRNSSELPLIVKMALQLVLLINVDEKDQVMHTNVWLTLQWHDFQMKWNPVNYGEIKQIRVSPDKVWLPDIVLFNNADGNYEVSFMCNVVINHKGDMLWVPPAIYKSSCIIDVEFFPFDEQVCTLVFGSWTYNENEIKLEFVQAELVDVSEYSASSIWDVIDVPASLVNKRSRIEFQVRIRRKTLFYTVVLIIPTVLMAFLSMAVFFLPTDSGEKITLTISVLLSIVVFLLLVSKILPPTSSTIPLMAKYLLLTFVLNVITILVTVIIINVYFRGPRTHRMPQWVRVVFLQFLPKLVCMKRPKSASERSAVRSGMAQLPGVGQFTLSPSAHHPLCPSADDRTTTIRNTASNETSAYYPLSTDALRAIDAIEYITEHLKRDEQHKSFRDDWKYVAMIIDRLLLYVFFGITVGGTCGILFSAPHVFQRIDQQEMLDRLKEKYDTASNIP
Protein: RING finger protein 17 (Mad member-interacting protein 2) (Mmip-2) (Q99MV7)
Organism: Mus musculus (Mouse)
Function: Seems to be involved in regulation of transcriptional activity of MYC. In vitro, inhibits DNA-binding activity of Mad-MAX heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly found in the cytoplasm. Component of a nuage in male germ cells (an electron-dense spherical cytoplasmic body present in late pachytene and diplotene spermatocytes and in elonging spermatids).
Interaction partners:
- Piwi-like protein 2
- Piwi-like protein 1
- Piwi-like protein 4
- ATP-dependent RNA helicase DDX4
- Serine/threonine-protein kinase 31
Sequence:
MAAEASSTGLASCHLVESKSGAQGASGCQCTRCGRKVSVASGDHHKFPCGHAFCELCLLAPQEYTTSKCTDCEVHTTVSMNQGHYPVDGFIEEDSSLEALPPKMVNNCSSDLEKTVDQLINDLEHSSSIHRNVSNPSAVMSETEEIDEALKIAGCNFEQLSNAIKMLDSTQDQTRQETHSLTEAVEKQFDTLLASLDSRKKSLCEELIRRTDDYLSKLVTVKSYIEEKKSDLDAAMKIAKELRSAPSLRTYCDLTQIIRTLKLTFESELSQVSSIIPRNTPRLDINCSEAICMFSSMGKIEFEDSTKCYPQENEDGQNVQKKFNNRKELCCDVYSSLEKKKVDAAVLTDETPEPPLQAEAPDRHLEGKKKQPTKEMVVVTSPKTIAVLPQLGSSPDVIIEEIIEENLESCFTDDPIETSGYPKKPPQKEQSAPVGSKAGCPELVFVSHVIHPCHFYVRKYSQIKDATILEKKMKQVCNRSLHLDPSDILELGARIFVNSIKNRMWCRGIITEIIPSKTKNIRKPCSPTKFSVCEISLIQIFMVDFGNSEVLIITGVGDTHEGPEHDGEQHITLSDFCLLLMKSEPYSEELLKDIPHLAHLCSLKDIVPYNSTEGWEKEAKVEFLKMVNKKAVLMKVFGEEDDVLIVDLQKPPTNKISSDMPVSLRDALVFMELARFRSQSPRSHSEKNTTLCYHPPILPEEMTEVSVMVCHINSPTDFYLQLMENLDFLSLLKTIEEFYKGEDGENLEILCPLQNQACVAKFEDGIWYRAKVIGLPGHREVEVKYVDFGNTAKITLKDMRKIKDEFLEPPEKAIKCKLAYVEPSKKSQWSKKAKEKFEEKTQDKFVTCSVIKILENNVLLVELFDSRAPGKSAVSINDQLVKEGLASYEAGYTLKDNSKKHLEVWDPSPEEIITSEINNLSPLSVKSLPNENFQSLYNKELPVNICNVISPEKIYVQWLLTENLLNSLEEKMVAAYEHSEWKPVKWECDMHCAVKVPAKNQWRRGQILRMVTDKLVEVLLYDVGVELVVNIHCLRELQENLKTMGRLSLECSLVDIRPTGGSDKWTATACDCLSLHLTGAIATIILQESNTTWPLPVKIFCRDEKGERVDVSKYLIKKGLALRERRVSKSSNSHSPEKSLEIPLEQGDSVVTKCFKINFDTNKKIADKVNEHKVPDSKGKKSESRSTGCYRPPAVPNTSSFEAIVTCIGDDGTIFVVPKLSEFELIKMMDEIQSNLKCLGLLEPYSWKKGEPCAVRGSDTLWYRGKVMEVVGGTIRVQYLDHGFTEKIPQCHLYPILLYPDTPQFCIPCQLYQTLPVGNTWQPDAIELLQELLSKREVDIHIMELPNNSWGKLSVHLYFDGMSLSHFMAHHKYCIFEHTEEIFKEKPRGQNKKYEDENWKIRFEDLLLPEMEAPVLPPYLSSLLPPPEELFAVQVKHIVSPDEMYICLDSEDSYTQFNHHGDTDDSGVSWESESENLEEALQRFNKNVETFPPLTDFSSEMPCLAEYADGLWYRAKIISIKEFNPLSVLVLFVDYGCTEKLTINRLRQIPVQLMQYPAQAIKVLLAGFKPPLSDSGKTRIPYCPKWSMEALWTMIDCLQGKQLYASSVAQAPEQIVTLYEDEQYPVHMSLVEMGLADKDE
Protein: NOPS domain-containing protein (B3GWA0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MIPRTPGLSKERELGPRFPTPNSFEYVYGMKWKELYVVEQKRRAQLDEELRESRRRLESDMELAYQDYQAQMLREDLQRRQQELERLEAARRERMRGLGGPPPGMPGGVPPQAQPFNPHGGSMFGGPGGPGGPPPFGQPFQQAPQGMFNVPTGPPPLMGGGGDPRGPPGGMGGPPGHGGMGGPPGHGGQGGPPGHGGMGGPPPGQGGPGGPGGPGGPGGMLPKSHGRSNMIEGVQRLLQIFKSDNGPPGGMPGRDYPPQQGPGGMFGSYGDGGYPPEKKQRR
Protein: E3 ubiquitin-protein ligase BRE1 (EC 2.3.2.27) (Brefeldin A-sensitivity protein 1) (RING-type E3 ubiquitin transferase BRE1) (Q07457)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.
Subcellular location: Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- Transcriptional regulatory protein LGE1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone H2B.1
- RNA polymerase-associated protein RTF1
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone H2B.2
- COMPASS component SWD2
- Histone H3
Sequence:
MTAEPATKKIKLELSDPSEPLTQSDVIAFQKEALFRCINRRRVDFEALRKQYELSRRECIDVSRKLANIMALIVTLARFIETFCTDANEKQLCREIAQGDETLIVQRSDSFMKLLTKYGKPNTTDSNTNSNASDHIQELTTELKNLRKSKEELFYENSQLTEEISALKEYYTNIIRKYDRDESFTIKRVFKEDKTDAVKELREDEKESNENNIKSGNKDSSAINGDNTSKKSEKGDELVQAEDERKEDAENEKLELDLKFSDLRAEINSLSSTIKDLENIRRENEEELIKTRSEVSNLKKQQIAAADQDPDFKSYDHESLLAKIQHLTEQNAELSEINSSFLSKFQVLAKEKEIYTKKVREEFQKSLDSLVEMNSSLEKDVVRIRTARDDLLSKIAILEAEKSKTEVLSDLQHAIDILKEQWTKIDQRSNDTKSSSTQDALIKEIQDLEKGFRELSDLTHKKYSEIINHESVISKLTVEKTKADQKYFAAMRSKDSILIEIKTLSKSLSKSNELILQLKDSDRLLQQKIGNLHKQLDLSQNNERRLIDSSKTETLKIIDLNNTSTKLKRSLEKLQEESNKSIADMTHLETKLNDTEIELKHFKQKASHLESKCEKLHDTLFRGNNKNKGSSDEALVEELANFRTLVYCSLCSKNWKNMAIKTCGHVFCENCCKERLAARMRKCPTCNKAFSSNDLLTVHL
Protein: Geminin (Q709D5)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTSSGKLQKNHQRSNENIKTFLAPSQKQMEFNRKSLQILQPSAANTDLRAAQAGKGIPKRKQWLAEQTRGPKRVKVEVKSTQTEDDCLPPDGVSSEAYDLMIKETPPASYWKEIAEERRKALFNVLQENEKLHKDLEVRDEQIRKLQSENEDLQELAQHVQYMADMIERLTGKCPDNLDELKGITLDVVDSYEHAEGEAEDHSGEEGDQDLRDGHDYDEVSDNDWEGPSGKLG
Protein: Lipase preproprotein (B1Q560)
Organism: Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Interaction partners:
Sequence:
MVSFISISQGVSLCLLVSSMMLGSSAVPVSGKSGSSNTAVSASDNAALPPLISSRCAPPSNKGSKSDLQAEPYNMQKNTEWYESHGGNLTSIGKRDDNLVGGMTLDLPSDAPPISLSSSTNSASDGGKVVAATTAQIQEFTKYAGIAATAYCRSVVPGNKWDCVQCQKWVPDGKIITTFTSLLSDTNGYVLRSDKQKTIYLVFRGTNSFRSAITDIVFNFSDYKPVKGAKVHAGFLSSYEQVVNDYFPVVQEQLTAHPTYKVIVTGHSLGGAQALLAGMDLYQREPRLSPKNLSIFTVGGPRVGNPTFAYYVESTGIPFQRTVHKRDIVPHVPPQSFGFLHPGVESWIKSGTSNVQICTSEIETKDCSNSIVPFTSILDHLSYFDINEGSCL
Protein: Homeobox-containing protein 1 (Q8BJA3)
Organism: Mus musculus (Mouse)
Function: Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA (By similarity). Associates with the telomerase complex at sites of active telomere processing and positively regulates telomere elongation (By similarity). Important for TERT binding to chromatin, indicating a role in recruitment of the telomerase complex to telomeres. Also plays a role in the alternative lengthening of telomeres (ALT) pathway in telomerase-negative cells where it promotes formation and/or maintenance of ALT-associated promyelocytic leukemia bodies (APBs) (By similarity). Enhances formation of telomere C-circles in ALT cells, suggesting a possible role in telomere recombination (By similarity). Might also be involved in the DNA damage response at telomeres (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23685356}. Cytoplasm {ECO:0000250|UniProtKB:Q6NT76}. Chromosome, telomere {ECO:0000269|PubMed:23685356}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q6NT76}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6NT76}. Note=Predominantly detected in cytoplasm. Localizes in a dynamic manner to actively processed telomeres. Localizes to the periphery of Cajal bodies. Associates with PML nuclear bodies in telomerase-negative cells. {ECO:0000250|UniProtKB:Q6NT76}.
Interaction partners:
Sequence:
MLSSFPVVLLETMSHYTDEPRFTIEQIDLLQRLRRTGMTKHEILHALETLDRLDQEHSDKFGRRSSYGGSSYGNSTNNVPASSSTATASTQTQHSGMSPSPSNSYDTSPLPCTTNQNGRENNDRLSTSNGKMSPSRYHANSMGQRSYSFEASEEDLDVDDKVEELMRRDSSVIKEEIKAFLANRRISQAVVAQVTGISQSRISHWLLQQGSDLSEQKKRAFYRWYQLEKTNPGATLSMRPAPIPIEDPEWRQTPPPVSATPGTFRLRRGSRFTWRKECLAVMESYFNENQYPDEAKREEIANACNAVIQKPGKKLSDLERVTSLKVYNWFANRRKEIKRRANIAAILESHGIDVQSPGGHSNSDDVDGNDYSEQDDSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD
Protein: Toll-like receptor 8 (CD antigen CD288) (P58682)
Organism: Mus musculus (Mouse)
Function: Endosomal receptor that plays a key role in innate and adaptive immunity. Controls host immune response against pathogens through recognition of RNA degradation products specific to microorganisms that are initially processed by RNASET2. Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction. In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q9NR97}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9NR97}. Note=Endosomal localization confers distinctive proteolytic processing. {ECO:0000250|UniProtKB:Q9NR97}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 7
- Protein unc-93 homolog B1
- Toll-like receptor 9
- Toll-like receptor 3
- Toll-like receptor 2
- Nucleotide-binding oligomerization domain-containing protein 2
- Interferon regulatory factor 5
- Interferon beta
- Interleukin-1 receptor-associated kinase 4
Sequence:
MENMPPQSWILTCFCLLSSGTSAIFHKANYSRSYPCDEIRHNSLVIAECNHRQLHEVPQTIGKYVTNIDLSDNAITHITKESFQKLQNLTKIDLNHNAKQQHPNENKNGMNITEGALLSLRNLTVLLLEDNQLYTIPAGLPESLKELSLIQNNIFQVTKNNTFGLRNLERLYLGWNCYFKCNQTFKVEDGAFKNLIHLKVLSLSFNNLFYVPPKLPSSLRKLFLSNAKIMNITQEDFKGLENLTLLDLSGNCPRCYNAPFPCTPCKENSSIHIHPLAFQSLTQLLYLNLSSTSLRTIPSTWFENLSNLKELHLEFNYLVQEIASGAFLTKLPSLQILDLSFNFQYKEYLQFINISSNFSKLRSLKKLHLRGYVFRELKKKHFEHLQSLPNLATINLGINFIEKIDFKAFQNFSKLDVIYLSGNRIASVLDGTDYSSWRNRLRKPLSTDDDEFDPHVNFYHSTKPLIKPQCTAYGKALDLSLNNIFIIGKSQFEGFQDIACLNLSFNANTQVFNGTEFSSMPHIKYLDLTNNRLDFDDNNAFSDLHDLEVLDLSHNAHYFSIAGVTHRLGFIQNLINLRVLNLSHNGIYTLTEESELKSISLKELVFSGNRLDRLWNANDGKYWSIFKSLQNLIRLDLSYNNLQQIPNGAFLNLPQSLQELLISGNKLRFFNWTLLQYFPHLHLLDLSRNELYFLPNCLSKFAHSLETLLLSHNHFSHLPSGFLSEARNLVHLDLSFNTIKMINKSSLQTKMKTNLSILELHGNYFDCTCDISDFRSWLDENLNITIPKLVNVICSNPGDQKSKSIMSLDLTTCVSDTTAAVLFFLTFLTTSMVMLAALVHHLFYWDVWFIYHMCSAKLKGYRTSSTSQTFYDAYISYDTKDASVTDWVINELRYHLEESEDKSVLLCLEERDWDPGLPIIDNLMQSINQSKKTIFVLTKKYAKSWNFKTAFYLALQRLMDENMDVIIFILLEPVLQYSQYLRLRQRICKSSILQWPNNPKAENLFWQSLKNVVLTENDSRYDDLYIDSIRQY
Protein: Pyrophosphate-energized membrane proton pump 2 (EC 7.1.3.1) (AVP1-like protein 1) (Pyrophosphate-energized inorganic pyrophosphatase 2) (H(+)-PPase 2) (Vacuolar proton pyrophosphatase 2) (Q56ZN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pyrophosphatase active in both inorganic pyrophosphate hydrolysis and H(+) translocation.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Sodium/hydrogen exchanger 5
- Endoplasmic reticulum transmembrane protein
Sequence:
MMMDEDVEQASLMSFNDRPRAFPNMRSKTYSPLIFRIIRKLNVRVLSIILLFCFGAIFYMGASTSPIIVFVFTVCIISFLLSIYLTKWVLAKDEGPPEMVEISDAIRDGAEGFFRTQYSTISKMAILLAFVILCIYLFRSLTPQQEAAGLGRAMSAYITVAAFLLGALCSGIAGYVGMWVSVRANVRVSSAARRSAREALQIAVRAGGFSALVVVGMAVIGIAILYSTFYVWLGVGSPGSMNVTDLPLLLVGYGFGASFVALFAQLGGGIYTKGADVGADLVGKVEQGIPEDDPRNPAVIADLVGDNVGDCAARGADLFESIAAEIISAMILGGTMAKKCKIEDPSGFILFPLVVHSFDLIISSIGILSIKGTRDASVKSPVEDPMAVLQKGYSLTIILAVITFGASTRWLLYTEQAPSAWFNFALCGLVGIITAYIFVWISKYYTDYKHEPVRTLALASSTGHGTNIIAGVSLGLESTALPVLTISVAIISAYWLGNTSGLVDENGIPTGGLFGTAVATMGMLSTAAYVLTMDMFGPIADNAGGIVEMSQQPESVREITDLLDAVGNTTKATTKGFAIGSAALASFLLFSAYMDEVSAFANVSFKEVDIAIPEVFVGGLLGAMLIFLFSAWACAAVGRTAQEVVNEVRRQFIERPGIMEYKEKPDYSRCVAIVASAALREMIKPGALAIASPIVVGLVFRILGYYTGQPLLGAKVVASMLMFATVCGILMALFLNTAGGAWDNAKKYIETGALGGKGSEAHKAAVTGDTVGDPFKDTAGPSIHVLIKMLATITLVMAPVFL
Protein: Probable folylpolyglutamate synthase (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) (O74742)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Folic acid synthesis protein fol1
- Dihydrofolate reductase
- Probable thymidylate synthase
- Probable dihydrofolate synthetase
- C-1-tetrahydrofolate synthase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methylenetetrahydrofolate dehydrogenase [NAD
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MHTAKPVKRYFNLKSSRIGMNPQTKTFEGAINRLNSLQSNAKVLEVLRKRGKIPNDQSMVEMRHWLRCIGYQPSDLNRLNVIHVAGTKGKGSTCAFTSSILQQIQKSGERSIPKCIGMYTSPHLRSVCERIQLNGKPISQELFTKYFFDVWERLENAVGSDSEKPMYFRFLTLMAWHVFISENVDAAIIEVGIGGEYDSTNLIEKPYATAVTSLGLDHTSLLGNTIAEIAWQKAGIYKESAIALTCEQAPEAMNVLKNRAAERNTSLKVVIPPAELTPDMIGLSGVHQLGNTSLAVSLVQEFYEKAGCPFDRDPYQDPAILDGLKYVKWPGRCQIEEINNIKWCFDGAHTKESLEATGLWLASKKNLYEDADARILLFNQQSRDDPIALLRSFLKGLESSGTGISFTHVIFSTNVTWKDAGYNPELLSINTITDNKPVLHVQEDLCKWWKESKGTTSEATVAPTIQEAIETVMSIKQKSRNTFVCVTGSLHLTGGVFVVLDQAVF
Protein: Phage shock protein D (P0AFV8)
Organism: Escherichia coli (strain K12)
Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12562786}. Cell inner membrane {ECO:0000269|PubMed:12562786}; Peripheral membrane protein {ECO:0000269|PubMed:12562786}; Cytoplasmic side {ECO:0000269|PubMed:12562786}.
Interaction partners:
- Phage shock protein B
- Phage shock protein C
- Phage shock protein A
- Thiosulfate sulfurtransferase PspE
- Psp operon transcriptional activator
- Phage shock protein G
Sequence:
MNTRWQQAGQKVKPGFKLAGKLVLLTALRYGPAGVAGWAIKSVARRPLKMLLAVALEPLLSRAANKLAQRYKR