wanglab/gogpt-training-data huggingface dataset:
Protein: Vasorin (Protein slit-like 2) (Q6EMK4)
Organism: Homo sapiens (Human)
Function: May act as an inhibitor of TGF-beta signaling.
Subcellular location: Membrane {ECO:0000305|PubMed:15247411}; Single-pass type I membrane protein {ECO:0000305|PubMed:15247411}. Secreted {ECO:0000269|PubMed:15247411}.
Interaction partners:
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-2 proprotein
- Transforming growth factor beta-1 proprotein
Sequence:
MCSRVPLLLPLLLLLALGPGVQGCPSGCQCSQPQTVFCTARQGTTVPRDVPPDTVGLYVFENGITMLDAGSFAGLPGLQLLDLSQNQIASLPSGVFQPLANLSNLDLTANRLHEITNETFRGLRRLERLYLGKNRIRHIQPGAFDTLDRLLELKLQDNELRALPPLRLPRLLLLDLSHNSLLALEPGILDTANVEALRLAGLGLQQLDEGLFSRLRNLHDLDVSDNQLERVPPVIRGLRGLTRLRLAGNTRIAQLRPEDLAGLAALQELDVSNLSLQALPGDLSGLFPRLRLLAAARNPFNCVCPLSWFGPWVRESHVTLASPEETRCHFPPKNAGRLLLELDYADFGCPATTTTATVPTTRPVVREPTALSSSLAPTWLSPTEPATEAPSPPSTAPPTVGPVPQPQDCPPSTCLNGGTCHLGTRHHLACLCPEGFTGLYCESQMGQGTRPSPTPVTPRPPRSLTLGIEPVSPTSLRVGLQRYLQGSSVQLRSLRLTYRNLSGPDKRLVTLRLPASLAEYTVTQLRPNATYSVCVMPLGPGRVPEGEEACGEAHTPPAVHSNHAPVTQAREGNLPLLIAPALAAVLLAALAAVGAAYCVRRGRAMAAAAQDKGQVGPGAGPLELEGVKVPLEPGPKATEGGGEALPSGSECEVPLMGFPGPGLQSPLHAKPYI
Protein: RE18107p (Q7JZN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQLNTLRLALIFLSFVRLEAQANVQNNGWQKVLPDDFRRERDKSSTRTRRNPQEELRLRHEQHHLRLQQHQMAWELDLQRQLQQHLQEQQSEQSEQQSRPVRHHQHKSHTKELAKKPIRRAPSFGDDKAKMVQKRRLHYNEYDNEDLELHTIETGDQGTFTPRQWQQIEIAHRRQKEQHQLQLLAQRQQQRQLLTTTTATATAMAMATTSKATEPNDAKSEDNDVSESKGDSI
Protein: ATP-sensitive inward rectifier potassium channel 8 (Inward rectifier K(+) channel Kir6.1) (Potassium channel, inwardly rectifying subfamily J member 8) (uKATP-1) (P97794)
Organism: Mus musculus (Mouse)
Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family C member 8
- ATP-binding cassette sub-family C member 9
- ATP-sensitive inward rectifier potassium channel 11
- Protein kinase C epsilon type
- Potassium voltage-gated channel subfamily A member 5
Sequence:
MLARKSIIPEEYVLARIAAENLRKPRIRDRLPKARFIAKSGACNLAHKNIREQGRFLQDIFTTLVDLKWRHTLVIFTMSFLCSWLLFAIMWWLVAFAHGDIYAYMEKGTMEKSGLESAVCVTNVRSFTSAFLFSIEVQVTIGFGGRMMTEECPLAITVLILQNIVGLIINAVMLGCIFMKTAQAHRRAETLIFSRHAVIAVRNGKLCFMFRVGDLRKSMIISASVRIQVVKKTTTPEGEVVPIHQQDIPVDNPIESNNIFLVAPLIICHVIDKRSPLYDISATDLANQDLEVIVILEGVVETTGITTQARTSYIAEEIQWGHRFVSIVTEEEGVYSVDYSKFGNTVRVAAPRCSARELDEKPSILIQTLQKSELSHQNSLRKRNSMRRNNSMRRNNSIRRNNSSLMVPKVQFMTPEGNQCPSES
Protein: Chromatin-remodeling ATPase INO80 (EC 3.6.4.-) (O14148)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746}.
Interaction partners:
- Probable actin-related protein 8
- Actin
- RuvB-like helicase 1
- RuvB-like helicase 2
- Actin-related protein 4
- HMG box-containing protein C10F6.08c
- Actin-like protein arp5
- Chromatin-remodeling complex subunit ies6
- INO80 complex subunit 1
- Histone H2A.Z
Sequence:
MDPSRETFDGSTRDSYKPPNGAEMMGQSELNTQNRIPYNTSANNRNWQIPLYWQQRGNEFQASPPPPLGYVTPEYGATGTPVNANNASRVDYATTAANVPEEYANDYSSELAYIHNVNDMPHVDGLSNHSPATQPDLFETPAQSDPILFSSYPHAAQARVDPSISKDLYNMVPRPDANTVSPHAARSASSLPVPKEASETPFRDASTDLFDEHAHAAPMHSSISISTLLSDSDRYEPHVSLTENISPVMAPSIDARLSQTILRGLPPAQKLSPNSSQSQITHNRRKHKLPLNATTNNSVVLTPDTSPLLDSDEVVSDDDSNEQQTMMMKFNYLQHLRNKRDEAVHAEKRRLLDIRGSIHDRLVCRYENRYNKLHASEYNHHHDWAVRQAIREEVAAVEAAKIRADEEKKKKEREEQVRLLQESADKDAEMNEASTATSENEDLKDDLSLADLSSKKTANSQATENNNTPSKAKVKAESKVRSKAKSDKSRAKLSSDTNKDSEKNDNNDASLQSAGVASDGESSPETPLTKASKSKKAKASKLANDTSKNANGETKSTPKKSKKKTSKAQQEANSTTAEGKEKLSGDSTETGNSTNKEASTEDTKANATASAPNKKKKTVETLQQQVIKEIARKEIPRVYKIIQQNQYNRSTNARKTSQLCGREARRWQFRTIKNNKDMQTKAKRAMRETMVFWKRNERVERDLRKKAEREALDRAKKEEELRESRRQARKLDFLITQTELYSHFVGRKMDREQDLPSATNTASVSEINFDSDEEEDIRRLAVESAQEAVQKAREHSQLFDANRQQSPNNSSSDMNEGEMNFQNPTLVNAFEVKQPKMLMCKLKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSISVMAYLAETHNIWGPFLVIAPASTLHNWQQEITRFVPKLKCIPYWGSTKDRKILRKFWCRKNMTYDENSPFHVVVTSYQLVVLDAQYFQSVKWQYMILDEAQAIKSSSSSRWKSLLAFKCRNRLLLTGTPIQNTMQELWALLHFIMPSLFDSHNEFSEWFSKDIESHAQSNTQLNEQQLKRLHMILKPFMLRRVKKNVQSELGEKIEKEVYCDLTQRQKILYQALRRQISIAELLEKAILGGDDTVASIMNLVMQFRKVCNHPDLFEREDVRSPLSLATWSKSIYINREGNFLDVPYNTRNFITFSIPRLLYEQGGILSVPGLNTSRGFETKYLYNLMNIWNPEYTNDSIKSNPEGSPFSWLRFVDESPQTLFQTFQNPVVHYLDEAEASSSLKEEQLCRQEFCYGKDYSNVRKMLLLPKSITKVDVLGSDFKEDSPFYHLTHVLEESDSQLDLTLLDSVLVQRASAPPIDIYCPGSRQFTVLQSRFQRDHLWSHYLYQPLKGEEDLIINNQAVSKLPIPRKPLLPSFGIAKGSYSNVRIPSMLRFIADSGKLSKLDKLLVELKANDHRVLIYFQMTRMIDLMEEYLTFRQYKYLRLDGSSKISQRRDMVTEWQTRPELFVFLLSTRAGGLGINLTAADTVIFYDSDWNPSIDSQAMDRAHRIGQQKQVTVYRFITRGTIEERIVIRAKEKEEVQKVVISGGETRPTKQMDLKGNSREMVSWLLEE
Protein: Interleukin-1 beta (Q0R3N6)
Organism: Ovis aries (Sheep)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU364119}. Secreted {ECO:0000256|RuleBase:RU364119}. Lysosome {ECO:0000256|RuleBase:RU364119}. Secreted, extracellular exosome {ECO:0000256|RuleBase:RU364119}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000256|RuleBase:RU364119}.
Interaction partners:
Sequence:
MATVPEPINEVMAYYSDENELLFEVDGPKQMKSCTQHLDLGSMGDGNIQLQISHQLYNKSFRQVVSVIVAMEKLRSRAYEHVFRDDDLRSILSFIFEEEPVIFETSSDELLCDAAVQSVKCKLQDREQKSLVLDSPW
Protein: Transforming growth factor beta (B2R7T2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAATCERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS
Protein: Uncharacterized protein, isoform D (B7Z0R9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKANPAILLISFSLLAFQSNCVATQKSQLGQPLIQLSHDNNDDDYPEVKDEIHLEDFFWTGSGDGPPDFLKKVHTGITKGKETVFKTETVVATIYVDGNNEIDIPICLDCKPDDGGGTWDMGGPGMPPLNYSATDRRYWLLTVMSGFYTAKDNPTLEEKLARLYRLAFTRQQTRHLGINGAQQIEGVNLPAPRERRKSLTLPTRVETTTGSPADDVEILDMQDEDEQHYIKSVRRLGEDTEWASHSQEEQEQEQSEEQLPLGVTPSTSTESIDYGAYVTLIPWELIQQNGKSEKLREMHETLLTKQPPVQQQQEQQQGAQPPPQTHPQSLPHSQSQSQPLYRDEHVRVVIHNLTQISEADVQKWSTNTNGFGTMEEHNYVNLKFNDRPIANQTELIYTVLVNGRPVLATTAAKDMELVSESEAVKTFGQAVYMKSEPYIREPTATALAPVPRSGQAGFFNSVKNNVALVVISSLAILLLMLLLVAVLLLGRTRSRQRELSAVNRNSSRNELLSDGQSMRPTTSERTEGEPSPGHSQSREAGVRNFSYEREPRISFPAPPQETRSRRESISSSTDNTSDSSVYCPINPPSADVQRILDDKAARLFDAHKRRHQYDRAEGHEETVYTSVVSEKKSDKMRHKSRRRYLNENRVGSLETSPVQGSLAGHSSAEESPEVMRRSYENFQRSEAFNPHNNYHRNKLLTQKTGRGASAEAINSEMIRNIQPSDKSDTASVGSFLSMASVRAFPKSTLPEPLNRVLDPVFVTYYDNVNAVAPHNSTRSLRSHKSQGSKDNTIATIASFPSPKAPPSVRNVRSASHSDNPDPGVVGPVVWERHKKKQTQEAQTYADYNPSPLHNPSAIRNHYEGLLEGALQMYSSQDDIPMPLPTQNFTNNRRATKREHRGSSAGLPSFHPSAEPKSLAERPATAQPEKTSKSAHSTQPPSPTYSAWGGGSMYSSHSTLNRPVSAGPFQRMEARLDATAPSGSRTGTAPLIEAIQSELRKFKQQQE
Protein: Amine oxidase (EC 1.4.3.-) (Q53YE7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004362}.
Interaction partners:
Sequence:
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase) (NMT) (Peptide N-myristoyltransferase) (O43010)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-1 subunit
Sequence:
MDNENNKNTKNSQQDSSFSEGGIRELLDRLALRSLIEKEEAAAPPKTYEDFKFWKTQPVPKFDDECTQEGPIDPNTDINQVPREPYRLLKEFEWATIDVTNDNELSEVHELLTENYVEDATAMLRFAYISEFLRWALMPPGYVKEWHVGVRVKSSRKLVAFISAVPLSIRVRDKIIKKCAEVNFLCIHKKLRSKRLTPLLIKEVTRRCHLENVWQAVYTAGVLLPSPVSLSRYMHRSLNWKKLYDIGFAPFPLGSTEKKETAKYHLPPNTQTPGLRPMELKDVPAVQSLLSQYMERFELAHLFSEEEVRHWFLYTDKVSSGPVVWSYVVENPESKKITDFFSFYSLPSTVIGNPKYKDIQAAYLYYYASDSCPKDLSSESQLAFVERCKLIVNDALILAKKFHFDVFNAVTVLDNNLFLKDLKFGEGDGFLNYYIYNYNCPKIPGGIDASKSVDYSRPSGMGFVMI
Protein: Bcl-2-modifying factor (Q96LC9)
Organism: Homo sapiens (Human)
Function: May play a role in apoptosis. Isoform 1 seems to be the main initiator.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 2
- Bcl-2-like protein 1
- Dynein light chain 2, cytoplasmic
- Induced myeloid leukemia cell differentiation protein Mcl-1
- Bcl-2-interacting killer
- Bcl-2-related protein A1
- Bcl-2-like protein 11
- Mitogen-activated protein kinase 8
- Phorbol-12-myristate-13-acetate-induced protein 1
Sequence:
MEPSQCVEELEDDVFQPEDGEPVTQPGSLLSADLFAQSLLDCPLSRLQLFPLTHCCGPGLRPTSQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAVLPIGEQPPEGQWQHQAEVQIARKLQCIADQFHRLHVQQHQQNQNRVWWQILLFLHNLALNGEENRNGAGPR
Protein: Respiratory supercomplex factor 2, mitochondrial (Altered inheritance of mitochondria protein 38) (P53721)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). May be required for late-stage assembly of the COX12 and COX13 subunits. Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent.
Subcellular location: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Respiratory supercomplex factor 1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 26
Sequence:
MKILTQDEIEAHRSHTLKGGIEGALAGFAISAIIFKVLPRRYPKFKPSTLTWSIKTALWITPPTVLTAICAEEASNNFDATMYGSGSSSEDALDEHRRWKSLSTKDKFVEGLSNNKYKIITGAWAASLYGSWVIVNKDPIMTKAQKIVQARMYAQFITVGLLLASVGLSMYENKLHPNKQKVNEMRRWENALRVAEEEERLEKEGRRTGYVSNEERINSKIFKS
Protein: Corticotropin releasing hormone (Crh protein) (Q5U3N6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLNFLVTTVALLVAFPPPYECRAIESSFNQPAADPDGERQSPPVLARLGEEYFIRLGNRNPTSPRSPADSFPETSQYPKRALQLQLTQRLLEGKVGNIGRLDGSYALRALDSMERERRSEEPPISLDLTFHLLREVLEMARAEQMAQQAHSNRKMMEIFGK
Protein: AT5g54940/MBG8_21 (Translation initiation factor SUI1 family protein) (Translation initiation factor-like protein) (Q9FFT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic translation initiation factor 4C
- Eukaryotic translation initiation factor 4C
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MVELDIQIPSAYDPFAEAKDSDAPGAKENIHIRIQQRNGKKSLTTVQGLKKEYSYERILKDLKKDFCCNGNVVQDKELGKIIQLQGDQRKKVSQFLVQTGIAKKDQIKIHGF
Protein: Isocitrate dehydrogenase [NADP], chloroplastic/mitochondrial (EC 1.1.1.42) (Q8LPJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in response to oxidative stresses.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Mitochondrion {ECO:0000269|PubMed:21841088}.
Interaction partners:
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 3, mitochondrial
- Aconitate hydratase 1
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 1, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 2, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 3, mitochondrial
- Putative isocitrate dehydrogenase subunit-like 4
- Citrate synthase 4, mitochondrial
Sequence:
MLNKLTHGVFTYRASLTAMLSSSTSAGLSSSFVSSRFLSSGIFSSGASRNRVTFPVQFHRASAVRCFASSGGSDRIQVQNPIVEMDGDEMTRVIWSMIKEKLILPYLDLDIKYFDLGILNRDATDDKVTVESAEAALKYNVAIKCATITPDEGRVKEFGLKSMWRSPNGTIRNILDGTVFREPIMCSNIPRLVPGWEKPICIGRHAFGDQYRATDTVIKGPGKLKMVFVPEDGNAPVELDVYDFKGPGVALAMYNVDESIRAFAESSMAMALTKKWPLYLSTKNTILKKYDGRFKDIFQEVYEANWKQKFEEHSIWYEHRLIDDMVAYAVKSEGGYVWACKNYDGDVQSDLLAQGFGSLGLMTSVLLSADGKTLESEAAHGTVTRHFRLHQKGQETSTNSIASIFAWTRGLEHRAKLDKNEKLMDFVKKLESSCVNTVETGKMTKDLALLIHGPKVSRDLFLNTEEFIDAVASKLKTQFKELPLV
Protein: Ankyrin 2 (A0A5F9ZGY1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MMNEDAAQKSDSGEKFNGSSQRRKRPKKVTCPQMKPEAANIEKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Diguanylate cyclase DgcN (DGC) (EC 2.7.7.65) (P46139)
Organism: Escherichia coli (strain K12)
Function: Bifunctional protein that catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress. In the presence of high intracellular c-di-GMP levels, and in response to envelope stress, interacts with cell division proteins and halts cell division, without disassembling the Z ring, but by blocking its further progress toward cytokinesis. Part of a network that regulates cell motility by altering levels of c-di-GMP.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the midcell in a Z ring-dependent manner in response to cell envelope stress. {ECO:0000269|PubMed:27507823}.
Interaction partners:
- Putative lipoprotein YfiB
- Protein YfiR
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeB
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeD
- Cyclic di-GMP phosphodiesterase PdeH
- Oxygen sensor protein DosP
Sequence:
MMDNDNSLNKRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQFSTAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILLASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAKHQRAEKLVR
Protein: Meiotic fizzy-related protein 1 (O94423)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Meiosis-specific activator of the anaphase promoting complex/cyclosome (APC/C). Involved in cdc13 degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11493649}.
Interaction partners:
- Serine/threonine-protein kinase plo1
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 3
- Tyrosine-protein phosphatase CDC14 homolog
- Anaphase-promoting complex subunit cut9
- G2/mitotic-specific cyclin cdc13
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 4
Sequence:
MGDRFIPIRNVSNEFNFSFQSFKECVLSHGSNLRRKTSGTIQRQFMELLSMELFGSQASRSRAFYYGEDKRKIEKKMLDTPDRKSYSLSPISPQSQDMLRQPQKPKRAFPKTPYKILDAPYLKNDFYLNLLDWGQSNVLAVGLASSIYLWSAASGKVVQLHDFGATNHVTSVLWTGKGTQLAVGTDSGVIYIWDIESTKSVRSLKGHSERVAALAWNDNTLTSGGKDEVILHHDLRAPGCCAEMMKVHEQEICGLQWDRSLGQLASGGNDNNLFVWDYRSSRPLHKFEEHTAAVKAIGWSPHQRGILASGGGTIDRCLTIHNTLTGRLQNKLDTGSQVCNMAWSKTSNEIVTTHGFAKNQVSLWKYPSLKNIANLTAHTNRVLYLSMSPDGQSIVTGAGDETLRFWKLFNKKPKEESTLIR
Protein: Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (Q9VL10)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10B
- RE03721p
- Mitochondrial import inner membrane translocase subunit Tim9
- BcDNA.GH07066
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
- Glycerol-3-phosphate acyltransferase 4, isoform D
- Phospholipid/glycerol acyltransferase domain-containing protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Acyltransferase
Sequence:
MNYLRVIRNNWKKCTFGAAVSVYALQALKTHIEIEQHMREFASNIQANWISDRPKKVLVVMNPVANKKRSEKFFKNYCEPVLHLAGYSVEILRTNHIGHAKTYVEELATLPDAIVVAGGDGTSSEVVTGLMRRRGNLCPITILPLGRSVQSASKRINIFGVKDVDYVKSLSKALEPMLKDESQYQSVIRFDVINEEDGSNSQLKPIFGLNGLSWGLLEDIDAAKDKYWYFGPLRHYASAASKSFADNWSLKTDYVYTPPCPGCVDCAATVQRQETAQPSGLFTRGLIKYKNNPGETKRPLVKNDNCSKKFEGSAEASQININCVQNKDNFAELESQFISSLQPGWEFIKQIPEVTCSKILPSLVVKSRTIQLHPDGEMGEKFYSIDGEEYDARPIKVSVVPNAIKVFC
Protein: Ectopic P granules protein 5 homolog (A5WUT8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in autophagy. May play a role in a late step of autophagy, such as clearance of autophagosomal cargo (By similarity).
Interaction partners:
- Synaptosome-associated protein 29.
- Tectonin beta-propeller repeat-containing 2
- Autophagy protein 5
- EI24 autophagy-associated transmembrane protein.
- Ubiquitin-like modifier-activating enzyme ATG7
- Vesicle-associated membrane protein 8
- Syntaxin 17
- Beclin 1-associated autophagy-related key regulator
- Vacuole membrane protein 1
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MLHLQVKKERQSESVRQPSGSSKAVNEPEFTDVPLSLPHVPPDLNTAASQTSLDHHDKAENEQQHVLLCEKPEVVQKSTCHEDKEHELPSQDAAPRLDQTSVLAPSSQSDPKPLSAKLEPFSVPSIYPSIPASLSQPQLSEDSYSISYELLDGSLMPAASERLVAPAVLTLANQESSPPSLVPVEVVDVERSRERLYPELPKTCQSVKPFTSEQLRMWEPGSWLENVELHEAEFQNLAHQEGHELYELLLSYWRCRKQLTQAQTELQAANSDCKNVQNRLWSFKDERLSLQGICADQNKVYGYHCYQQVTLNEAALAELKHLFSAKAEILHQTVALHSYTSILSRLQVESYLYRLLSSNPTTKSVAVQDTSAGNPKSQPSSLQPLKESISVLFIFTRRVLDDSQFQADIHLWLQRLVSVLHQVGSTGDHLFILNHLLCCPAGVGKWAVPFLQIKVLDNPSGVYHFMQALAILMSPARHRPDFLGHMKPSDARGNNSLTEPASGNWTLVDEGGEEDEDPETSWMLLSEDDLVSLFSQFPFDELFKHLLGICSKGDYQPLATTSQKMMKIFAFASSLVELLAVGLQTYNRARYRQFVKRIGHMIRMTLCYVSDHWAQYISLTGVSRTTVQEQSFSMEKLQVEFDHLFLRAVLHVLKAKRLGIWLFMSEMPYGTLSSSMLWKIFYIMQCAETDGLEKLSCSLSAEDCIQRLRESSHQERFQLWLSEINSSDGICLLTTFAHMAQPRRTDVDPEFVRNIVLEIYEVSYVSVTTREIFSKVGRELLAAIAAAHPHIISVLLERLRETIERVGMVSLYLFKELPLHLWMPAQEEVGLIRDWLMNFSLTAVENRLACIILEGLNWGFQPNGCLILPAPLHSDVALLVIEAYQKYLTDKPYGGILSEGIKQVSYLANVVRLGQTPESSFNQWAWDIVLRLKLHANERSPQDAWCPLPSSSAPSVPEITDSPIMHPVFKAVKAGIPIGCFLAIEMTTIGHSLEKFCSEGISLLKTLIQSRHLRAAVHILENILPLVYNCQFYLLKNEQFLSCVQLFLQLDSGTQGVTQQVTQKVAQHLIGPATCENIKLLNSVIQAHVLESSRNGRVGAVAVLEFWLQVLTEQSLWYRDRAVLFLLDHMCRSAFLHQQEECLQKILYQQHKSALGYHGDKGLLSSIMGWIVAGNVTPSFIEGSSLTGEVWFAWMILNMETMFEEDSQLRRCVEHELLSNPACTPDQALKKAQVRLKLQVVPSLQRLMIYRWAQQALATPADHPILPLVWQKFFQLYLRQPGPEFGLEVKGCIGRRYFHSAAHLSLLKSLRQRLVEVSDFHHAASKALKVPCASGDSGDGLLTPGTPITQYMTSPDLHTEIVRLFTVFALWLDDENLQKQEIYLPSLPKQYDTHRLAKIMQRQQEVWMEHVDIERVQHELQEVLDLWSKVKSEPAVSQNSSSSIFTDFINPLAARERILTHLRKHDAPQGSLLPVPMKAPVPDIPTASLTDEKISTTLIQEDLTKLQHQAKLATVRETQQVALDNELLEVLPQLYINREDQLSMQLECRGKSGQPCQGPANITVKYSSMHKLEPVQNQIQSLKSDIKQLQADGIKAPPQSLAEAAVHTENFITALVNVFKQNPSPGVLKVGITAFYQIVSFVCEDTQRHPPTRQFFTSCIEILGQVFIRDVQSECKHMLKTILLNRRLCNLLSPYFTPNASPSELVSLYEEVVNTLHIDSGDVIFMLLTKFDLFQWLSTTQPPFSERSRLMTVIHQALCTCGLEPEPEVLMPFNIFCKHWTELLLYQFPDHYSDFLRLLMQSSSDQLLSPDCWRTSLKALGCSPQTKNKTNKSRSMLLSPQQVDETIEWLSKYFLKLRLSNGDFRSFGLLSKWGPYIEEVKVFWEDLITYVIDLELNHCGKEPVGSPRLLKALENLHRKMAKLFEPWILVLDTDNTSHPRCSPWLESDAAVAASLVGLYTRLTETLHEKFKDRLLPGQRGALWLHLMFYCETCTSPKMPEYLLYTYHTEYSRLPWKDLHPDQTLMNQFFNVERGSPKSCFVFMGELLCEVNWVSVLSDSLSPQLNPSTHTMVVSVLHLMVFLAKEDLSKPESSVLSLLDQSASLPWNLVDFSSYQNVTRYVSTHYPASLVLSHDTSSQQVVRLLRMAAGFEPTTQVLHHKDMTLKCQAFLHLMVQFLTSLDQNGNISLASLETEMEKLLENIVIFNPPETDLQQRHMATCSLFAEMLTLLNEAGISTAEGLGTKLHCWVEKRARGPLLLPLLTAACRCLASVRHMTRTTEACILSYFTDGCVDQYSGWGPILVSLQVPELTVEDFIQESLSLGSFLTLYVYILQRLNLEQTLLNEKKTLMLLNTWISQVFPSGPADEAKLFLWWHKFLELLQIQVDQEDACSLDTLILTLMAFQNRLVQLGEERLNSGILGAIGLGRKSPLSNRFRVVARSMSAFLLVQVPSENQLRLHPGTELQLSAKAQQALSALEAMASNKQYSELHVSVNQACQFIKYPNHCLRDANTLLTLLVNALYTDLHYLDIIR