wanglab/gogpt-training-data huggingface dataset:
Protein: C3H1-type domain-containing protein (Q38B87)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYRPTNRCVADVGQGNPPNLQQVMYSGSVPQTAPVQMQLHPHPQSQSHMVMRPQAHTMATAVNSKPKVHVVSRSPPSRSGASQGERSGTVRFVCPRTNTIVCARYNRTVHTRAKLQHGAVICEDYMHKLHCPEGDQCLKVHVAAEHTWNYILPHIGAPQGIFQHGFTVRCFHPSMTEYFNIPSELVYYTKGSMEYIYDYNEHGDNSKKKFVLCEEMINNRICMSGMACEDVHAVMDDFSSVGRNSTHIVDEKLLPLYPRLRPDVVVRVFEQNSTEEYKDYTGDQILVTDGARQYLLALDVEGAIPRKKMQHCAHFRTKHLCRMGSGCNFIHVLQGLVANAEISPRSTSRSDSPTSELSISVRNRPIALRQSGSQVAEMLAEKYGLSRDENSQVGRHASPFVKQPPNEMASLPLCDGGLFQSNTKSQGNAVINSNINGNYNKEYCRNDDLFPCGAADAGDERVTQRNQQGEQIHDGTQPVAVCSRFRQISPPRRNNPYASPVLSQQASPHPRETI
Protein: Platelet-activating factor acetylhydrolase 2, cytoplasmic (EC 3.1.1.47) (PAF:lysophospholipid transacetylase) (PAF:sphingosine transacetylase) (Platelet-activating factor acetyltransferase PAFAH2) (EC 2.3.1.149) (Serine-dependent phospholipase A2) (SD-PLA2) (hSD-PLA2) (Q99487)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolyze of the acetyl group at the sn-2 position of platelet-activating factor (PAF) and its analogs, leading to their inactivation. Hydrolyzes propionyl and butyroyl moieties approximately half as effectively as PAF (By similarity). Also catalyzes transacetylation of the acetyl group from platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine, producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9494101}. Membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to intracellular membranes and cytoplasm. Translocates from the cytoplasm to intracellular membranes upon oxidative stress. {ECO:0000250|UniProtKB:P79106}.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Lysophosphatidylcholine acyltransferase 2
- Choline/ethanolaminephosphotransferase 1
- Lysophosphatidylcholine acyltransferase 1
- Cholinephosphotransferase 1
- Platelet-activating factor acetylhydrolase
- Lysophospholipid acyltransferase LPCAT4
- 85/88 kDa calcium-independent phospholipase A2
Sequence:
MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKHLDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL
Protein: Hedgehog interacting protein (Hedgehog-interacting protein precursor) (A1A5I0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKHLKFVLLLAIAANFWECGDAKFGEKGELSPRRRRCYDGSLPRRLKKKERKLSLEGSGGGEVCHRLYPRVSCCPSRRAPYQILHRKDARTFSTNNTECSRLLEEIKCAHCSPNAQMLFHSPKLEKAPHREQDLPHLCHDYCQEFYYTCRGHVPELFQADVDEFCQYYGRMDGGLCFPDFHRKQLRRDSNYLLDEKTEAINRKHKHNCYCAQEIHSGLQQPVGVVHCGDGSQRLFILEREGFVWILTHDMELLKEPFLDIHKLVQSGLKGGDERGLLSLAFHPNYKKNGKLYVSYTTNQERWTIGPHDHILRVVEYTVSRKNPNQVDTRTPRVLMEVAELHRKHLGGQLLFGPDGLLHIFLGDGMITLDNMEEMDGLSDFTGSVLRVDVDTECCSTPYSIPRNNPYFNSTNQPPEIFAHGLHDPGRCAVDKLRMDTNGSLLILCTDTVGKNTTTGRILQVIKGKDYENEPSMFDLGSSGGTTPVGGFIYRGCQSRRLYGSYVFGDKNGNFRILQRPLEDRLWQEKPLCLGTSSSCGSSLVGHILGFGEDELGEVYILVSSKSTAKQSHGKIYKLVDPKRPQVPKECRRPVEDPEMLSTACSRECKNGHCTPTGKCCCNAGWEGPFCLRAKCELACRNGGVCVEPNKCLCKEGFSGNQCSKGERGTKGDGEKDSILEHIIDMTTYLLDLTSYIV
Protein: Hydrolase Rv0480c (EC 3.5.-.-) (P9WJ01)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0479c
- Uncharacterized protein Rv0481c
Sequence:
MRIALAQIRSGTDPAANLQLVGKYAGEAATAGAQLVVFPEATMCRLGVPLRQVAEPVDGPWANGVRRIATEAGITVIAGMFTPTGDGRVTNTLIAAGPGTPNQPDAHYHKIHLYDAFGFTESRTVAPGREPVVVVVDGVRVGLTVCYDIRFPALYTELARRGAQLIAVCASWGSGPGKLEQWTLLARARALDSMSYVAAAGQADPGDARTGVGASSAAPTGVGGSLVASPLGEVVVSAGTQPQLLVADIDVDNVAAARDRIAVLRNQTDFVQIDKAQSRG
Protein: Aminoaldehyde dehydrogenase 1, peroxisomal (PsAMADH1) (EC 1.2.1.-) (Aminobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.19) (Gamma-guanidinobutyraldehyde dehydrogenase AMADH1) (EC 1.2.1.54) (Q8VWZ1)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 3-aminopropanal to beta-alanine. Catalyzes the oxidation of 4-aminobutanal to 4-aminobutanoate. Catalyzes the oxidation of 4-guanidinobutanal to 4-guanidinobutanoate.
Subcellular location: Peroxisome {ECO:0000255}.
Interaction partners:
Sequence:
MAITVSSRQLFIDGEWRVPILNKRIPNINPSTENIIGDIPAATKEDVDLAVDAAKRAISRKNGRDWSAASGSLRARYLRAIAAKIKEKKDELGKLESIDCGKPLEEALADLDDVVACFEYYAGLAEELDSKQKAPISLPMDTFKSYILKEPIGVVALITPWNYPFLMATWKIAPALAAGCAAILKPSELASVTCLELGEICKEVGLPRGVLNIVTGLGHEAGASLASHPDVDKISFTGSSATGSKIMTTAAQLVKPVSLELGGKSPIVVFEDVDLDKVAEWTVFGCFFTNGQICSATSRLIVHESIAVEFVDKLVKWAENIKISDPLEEGCRLGPIVSEAQYKKVLNCISSAKSEGATILTGGRRPEHLKKGYFVEPTIITDVTTSMQIWREEVFGPVLAVKTFSTEEEAINLANDTHYGLGSAVMSNDLERCERLSKALQAGIVWINCAQPSFIQAPWGGIKRSGFGRELGEWGLENYLSVKQVTRYTSDEPWGWYQPPSKL
Protein: Interferon gamma (BoIFNG) (IFN-gamma) (P07353)
Organism: Bos taurus (Bovine)
Function: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01579}.
Interaction partners:
- Interferon gamma receptor 1
- Interferon gamma receptor 2
- Granulocyte-macrophage colony-stimulating factor
- Tyrosine-protein kinase
- Interferon alpha/beta receptor 1
- Tyrosine-protein kinase
- Interleukin-1 beta
- Interleukin-13
- Interleukin-10
- Interleukin-2
Sequence:
MKYTSYFLALLLCGLLGFSGSYGQGQFFREIENLKEYFNASSPDVAKGGPLFSEILKNWKDESDKKIIQSQIVSFYFKLFENLKDNQVIQRSMDIIKQDMFQKFLNGSSEKLEDFKKLIQIPVDDLQIQRKAINELIKVMNDLSPKSNLRKRKRSQNLFRGRRASM
Protein: Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha) (P26450)
Organism: Mus musculus (Mouse)
Function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (By similarity). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement.
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Insulin receptor substrate 1
- E3 ubiquitin-protein ligase CBL
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Epidermal growth factor receptor
- Growth factor receptor-bound protein 2
Sequence:
MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQQALPLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDAASVDLEMIDVHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQELQSPEDCIQLLKKLIRLPNIPHQCWLTLQYLLKHFFKLSQASSKNLLNARVLSEIFSPVLFRFPAASSDNTEHLIKAIEILISTEWNERQPAPALPPKPPKPTTVANNSMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNHDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
Protein: Uncharacterized protein At4g28025 (Q9C5F3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVVTSFSSAPPIFFLPGADAQFSSSNGRFAIPSSSLVKGLRRHQDAKLVGNRARVGVVRVLANPNVSPPPPPGKAKVKKEVIMVDPLEAKRLASKQMEEIKGREKQQRRREIEAINGAWAIIGLMIGLVIEAQTGKGILAQLAGYWSAVVHLFTPST
Protein: Ahnak protein (Q8BKS2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PHIDVPDVDVHGPDWHLKMPKVKMPKFSMPGFKGEGPEVDVNLPKADLDVSGPKVDIDVPDVNVEGPDMKVTGPKFRMPEINIKAPKISMPDVDLELKGPKVKGAFDGSVPKIEGTLKGPEIDMKGPGLDFEGPDAKLSGPNLKMPSLEVSVPKITGPDANVHLKTPKVGISAPKLGGGEVDLKGPKVDLETPSLDVHMESPDINIEGPDVKVPKFKKPKFGFGAKSPKADIKTPTVDVTVPEAELNVDSPEINIGGKSKKSKFKMPKIHMSGPKVKAKKQGFDLNIPGGEIDTSLKAPDVDVSVAGPDAALKAEVKSPKVKKTMFGKMYFPDVEFDIKSPKFKAEAPLPSPKLEGEIKVPDVDISSPGINVEAPDIHMKAPKFKVPGVEASGPKIEGNLKGPKVQANLDTPDINIEGPEAKIKAPSFSVSAPQVSIPDVNVNLKGPKIKGDVPSVGLEGPNIDLQGPEGKIKFPKFSLPKISAPGVKMEGGSTEIGAQMPSLEGGLSTSDMKLEGPHLSLKGPGVDLPSVDLSMPKVSGPDLDMNLKGPSLKGDLGASSPSMKLHAPGLDLKGVGGKVHIGADGVKMSGIDATTALSVGAPDVTLKGPSLQGDLAVSGDIKCPKVSVATPDVSLEASEGAVKLPHMKLPQFGISTPGSDLDINIKGPQVCGELKGSGMDVNLKGPQISAPSMDFNLEGPKVKGSLGAAGELKGPAIGGALPGISIQGPEGNLQMPGIKASGCDVKLSSGQISGPEIKGDLKGSGLGLHGAVPDIGVKGPSFNVASPESDFGVSLKGPKVKGGVDVSGGVSVPDINLGEGHMSVKGSGVEWKGPQVSSSLNLDTSKLAGNLHFSGPKIEGDVKGGQTGLQGPGLSVSGPQGHLESESGKVTFPKMKIPKFTFSGRELIGREVGVDVNFPKVEANVQAGAGEGKWEESEV
Protein: Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK) (Two pore potassium channel KT4.1) (K2P4.1) (Two pore K(+) channel KT4.1) (Q9NYG8)
Organism: Homo sapiens (Human)
Function: Voltage-insensitive potassium channel. Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the perception of pain caused by heat (By similarity). Plays a role in the sensory perception of pain caused by pressure (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}; Multi-pass membrane protein {ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}. Cell projection, axon {ECO:0000250|UniProtKB:G3V8V5}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000250|UniProtKB:G3V8V5}.
Interaction partners:
- Keratin, type II cytoskeletal 2 oral
- Potassium channel subfamily K member 2
- Potassium channel subfamily K member 12
- Potassium channel subfamily K member 13
- Piezo-type mechanosensitive ion channel component 1
- Potassium channel subfamily K member 9 channel 3)
- Potassium channel subfamily K member 18
Sequence:
MRSTTLLALLALVLLYLVSGALVFRALEQPHEQQAQRELGEVREKFLRAHPCVSDQELGLLIKEVADALGGGADPETNSTSNSSHSAWDLGSAFFFSGTIITTIGYGNVALRTDAGRLFCIFYALVGIPLFGILLAGVGDRLGSSLRHGIGHIEAIFLKWHVPPELVRVLSAMLFLLIGCLLFVLTPTFVFCYMEDWSKLEAIYFVIVTLTTVGFGDYVAGADPRQDSPAYQPLVWFWILLGLAYFASVLTTIGNWLRVVSRRTRAEMGGLTAQAASWTGTVTARVTQRAGPAAPPPEKEQPLLPPPPCPAQPLGRPRSPSPPEKAQPPSPPTASALDYPSENLAFIDESSDTQSERGCPLPRAPRGRRRPNPPRKPVRPRGPGRPRDKGVPV
Protein: Centrosome and spindle pole-associated protein 1 (Q1MSJ5)
Organism: Homo sapiens (Human)
Function: May play a role in cell-cycle-dependent microtubule organization.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15580290, ECO:0000269|PubMed:16826565}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15580290, ECO:0000269|PubMed:16826565}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16826565}. Cell projection, cilium {ECO:0000269|PubMed:36606424}. Note=Associated with mitotic spindles. {ECO:0000269|PubMed:15580290, ECO:0000269|PubMed:16826565}.
Interaction partners:
- Protein FAM110B
- Protein FAM110A
- Protein FAM110C
- Coiled-coil domain-containing protein 14
- Pericentriolar material 1 protein
- Dynactin subunit 2
- Centriole and centriolar satellite protein OFD1
- Dynactin subunit 4
- Dynactin subunit 5
Sequence:
MLFPLQVAAVTSSVRDDPLEHCVSPRTRARSPEICKMADNLDEFIEEQKARLAEDKAELESDPPYMEMKGKLSAKLSENSKILISMAKENIPPNSQQTRGSLGIDYGLSLPLGEDYERKKHKLKEELRQDYRRYLTQGITQGKRKKNFLSTSETDPSTLGVSLPIGERLSAKERLKLERNKEYNQFLRGKEESSEKFRQVEKSTEPKSQRNKKPIGQVKPDLTSQIQTSCENSEGPRKDVLTPSEAYEELLNQRRLEEDRYRQLDDEIELRNRRIIKKANEEVGISNLKHQRFASKAGIPDRRFHRFNEDRVFDRRYHRPDQDPEVSEEMDERFRYESDFDRRLSRVYTNDRMHRNKRGNMPPMEHDGDVIEQSNIRISSAENKSAPDNETSKSANQDTCSPFAGMLFGGEDRELIQRRKEKYRLELLEQMAEQQRNKRREKDLELRVAASGAQDPEKSPDRLKQFSVAPRHFEEMIPPERPRIAFQTPLPPLSAPSVPPIPSVHPVPSQNEDLRSGLSSALGEMVSPRIAPLPPPPLLPPLATNYRTPYDDAYYFYGSRNTFDPSLAYYGSGMMGVQPAAYVSAPVTHQLAQPVVNTVGQNELKITSDQVINSGLIFEDKPKPSKQSLQSYQEALQQQIREREERRKKEREEKEEYEAKLEAEMRTYNPWGKGGGGAPLRDAKGNLITDLNRMHRQNIDAYHNPDARTYEDKRAVVSLDPNLATSNAENLEDAANKSSGHMQTQSSPFARGNVFGEPPTELQIKQQELYKNFLRFQIEEKKQREEAERERLRIAEEKEERRLAEQRARIQQEYEEEQEKKREKEEEQRLKNEEHIRLAEERQKEAERKKKEEEEKYNLQLQHYCERDNLIGEETKHMRQPSPIVPALQNKIASKLQRPPSVDSIIRSFIHESSMSRAQSPPVPARKNQLRAEEEKKNVIMELSEMRKQLRSEERRLQERLLHMDSDDEIPIRKKERNPMDIFDMARHRLQAPVRRQSPKGLDAATFQNVHDFNELKDRDSETRVDLKFMYLDPPRDHHTLEIQQQALLREQQKRLNRIKMQEGAKVDLDAIPSAKVREQRMPRDDTSDFLKNSLLESDSAFIGAYGETYPAIEDDVLPPPSQLPSARERRRNKWKGLDIDSSRPNVAPDGLSLKSISSVNVDELRVRNEERMRRLNEFHNKPINTDDESSLVDPDDIMKHIGDDGSNSVATEPWLRPGTSETLKRFMAEQLNQEQQQIPGKPGTFTWQGLSTAHG
Protein: Cell division cycle protein 20 homolog B (Q86Y33)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm. Note=Tightly associated to mature deuterosomes. {ECO:0000269|PubMed:30405130}.
Interaction partners:
- Cilia- and flagella-associated protein 107
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Ubiquitin-conjugating enzyme E2 C
- Serine/threonine-protein kinase PLK1
- Mitotic spindle assembly checkpoint protein MAD2A
- Cyclin-dependent kinase 6
- Protein boule-like
- Cell division cycle-associated protein 3
- Cell division cycle protein 16 homolog
- Cell division cycle protein 27 homolog
Sequence:
MEWKLERTAPRRVRTEEEMLWESIMRVLSKDLKQKRSQDSANVLDSVNATYSDFKSNFAKRLSAEVPVASSPITTRWQQSQTRALSSDSFGEEQSTTYLPEASGSVLKTPPEKETLTLGSRKEQLKTPSKGISETSNSALHFCKAPHAMDRDWKESVASKGQKCLKQLFVTQNVVQQANGKMQLCEQSECVWKGCKDGVRDESFHLKSSGDINDSILQPEVKIHITGLRNDYYLNILDWSFQNLVAIALGSAVYIWNGENHNGIENIDLSLTCNYISSVSWIKEGTCLAVGTSEGEVQLWDVVTKKRLRNMLGHLSVVGALSWNHFILSSGSRLGRVYHHDVRVAQHHVGTLRHKQAVCALKWSPDGRLLSSGCSDGLLTIWPHDPGASAQGQPLKVITQSTAVKAMDWCPWQSGVLAIGGGMKDGRLHILDINAGKSIQTPSTNSQICSLIWLPKTKEIATGQGTPKNDVTVWTCPTVSRSGGFFGHRGRVLHLSLSPDQTRVFSAAADGTASVWNCY
Protein: Sialyltransferase-like protein 3 (OsSTLP3) (EC 2.4.99.-) (Q7FA29)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses sialyltransferase-like activity in vitro. Transfers sialic acid to the glycoprotein asialofetuin. The transferred sialic acid is linked to galactose of Gal-beta-1,3-GalNAc through alpha-2,6-linkage.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9SGD2}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKRRHWSHPSCGLLLLVAVFCLLLVFRCSQLRHSGDGAAAAAPDGGAGRNDGDDVDERLVELAAVDPAAMAVLQAAKRLLEGNLARAPERHRDVALRGLREWVGKQERFDPGVMSELVELIKRPIDRYNGDGGGGGEGEGRRYASCAVVGNSGILLAAEHGELIDGHELVVRLNNAPAGDGRYARHVGARTGLAFLNSNVLSQCAVPRRGACFCRAYGEGVPILTYMCNAAHFVEHAVCNNASSSSSGAADATAAAPVIVTDPRLDALCARIVKYYSLRRFARETGRPAEEWARRHEEGMFHYSSGMQAVVAAAGVCDRVSVFGFGKDASARHHYHTLQRRELDLHDYEAEYEFYRDLESRPEAIPFLRQRNSGFRLPPVSFYR
Protein: Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) (A0A5F9ZHD4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAVLAALLRSGARSRSPLLRRLVQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
Protein: Protein ALTERED SEED GERMINATION 2 (Q94BQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as a substrate adapter for CUL4-DDB1 E3 ubiquitin-protein ligase complex (Probable). Negative regulator of fatty acid biosynthetic process and accumulation. Acts as an abscisic acid (ABA) negative regulator. Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26147561}. Cytoplasm, cytosol {ECO:0000269|PubMed:26147561, ECO:0000269|PubMed:28663238}. Note=Excluded from the nucleus when farnesylated at Cys-754. {ECO:0000269|PubMed:26147561}.
Interaction partners:
- DNA damage-binding protein 1a
- DNA damage-binding protein 1b
- Cullin-4
- Transducin/WD40 repeat-like superfamily protein
- DET1- and DDB1-associated protein 1
- Katanin p80 WD40 repeat-containing subunit B1 homolog KTN80.2
- Protein DAMAGED DNA-BINDING 2
- AT3g05090/T12H1_5
- WD-40 repeat-containing protein MSI4
- Protein DWD HYPERSENSITIVE TO UV-B 1
Sequence:
MDNLSFHDGNIFNLLHTRSQDPSHEVDQRMQFHSSLVRRLSQEQELEGHQGCVNALAWNSNGSLLISGSDDLRINIWNYSSRKLLHSIDTGHTANIFCTKFVPETSDELVVSGAGDAEVRLFNTSRLSGRAEDDNAIIPSALYQCHTRRVKKLAVEPGNPNVVWSASEDGTLRQHDFRESTSCPPAGTAHQECRSVLLDLRSGAKRALADPPKQTLSLKSCDISATRPHLLLVGGSDAFARLYDRRMLPPLASSRKRMPPPPCVNYFCPMHLSERGRTNLHLTHVTFSPNGEEVLLSYSGEHVYLMNVNNGICSTGIMQYTPGDVDNLFSFSNNLHDVESPPQVSTTPQNGFHRSSNAATVKKCTELVEIAKWSLEEGTDVFYAIEAANEVLDAHSNDIESALRHECLCTRAALLLKRKWKNDAHMAVRDCHNARRIDASSFKAHYYMSEALQQLGKCKEALDFATAAQHMNPSDADIVAKVESIKRDLQAAGAEKNEETGAGTTRVLSLSDILYRSEANSDSSHDMSRSEREDSDYDEELELDIQTSLSDDEGRDTDSNSMRGSLNLRIHRVGDDKPMENTVDNASSGTASSSQNDRTSYQPEGAIDMKRRYVGHCNVGTDIKQASFLGQRGEYIASGSDDGRWFIWEKQTGRLMKVLVGDESVLNCIQCHPFDSVVATSGIDNTIKIWSPTASVPSIVAGGSAGPATANVVEVMESNQQKLSRNRENPLSVELMQRFRMQEFAEGNFHPFECTQS
Protein: Protein FLC EXPRESSOR (AtFLX) (Protein SUPPRESSOR OF FRI 5) (F4IMQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transactivator required for FRIGIDA-mediated activation of FLC and for the expression of the repressors of flowering AGL27/MAF1 and AGL31/MAF2. Does not alter expression of known activators of FLC expression. Not required for the photoperiod response or for the vernalization response. Not redundant with FLXL4.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18156133, ECO:0000269|PubMed:21282526}. Nucleus {ECO:0000269|PubMed:18156133, ECO:0000269|PubMed:21282526}. Note=homodimers present in the cytosol and heterodimers with FRI and FES1 detected only in the nucleus. {ECO:0000269|PubMed:21282526}.
Interaction partners:
- FRIGIDA-like protein 1
- Protein FRIGIDA-ESSENTIAL 1
- Transcription initiation factor TFIID subunit 14
- Inactive protein FRIGIDA
- Calcineurin-like metallo-phosphoesterase superfamily protein
- Protein SUPPRESSOR OF FRI 4
- Uncharacterized mitochondrial protein AtMg00320
- Transcription initiation factor TFIID subunit 15b
- U2 small nuclear ribonucleoprotein B''
- Protein PAF1 homolog
Sequence:
MAGRDRYIPSSAVSTSSSSRLLESQLIESDRNRARSVILEDRIAIQHREIQSLLNDNQRLAVAHIGLKDQLNVAKRELERLLETAVKVKAEGEAKVREVYQNALRMEAEARVIDGLGAELGQVRSDVQRLGSDRQELATELAMFDDEMAKAKPNSDRAIEVKLEIEILRGEIRKGRAALELEKKTRASNLHHERGMEKTIDHLNREIVKLEEELVDLETKAREANAAAEAAPTPSPGLAASYGNNTDDIYGGQGRQYPEANGTHELVLREKSYVHRLVSVQLVQVSVG
Protein: DNA replication licensing factor Mcm7 (EC 3.6.4.12) (Minichromosome maintenance 7 protein) (DmMCM3) (Q9XYU0)
Organism: Drosophila melanogaster (Fruit fly)
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. 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.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication licensing factor Mcm6
- DNA replication complex GINS protein SLD5
- DNA replication complex GINS protein PSF1
- Probable DNA replication complex GINS protein PSF2
- DNA replication complex GINS protein PSF3
- Double parked, isoform A
- CDC45L
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm2
Sequence:
MARRDYAQDRESIKTFLSEFCKCDDDGKKEFVYGSQLVKLAHREQVLITIDLDDLAEFNESLAEAVVDNCRRYTSIFSDVIAELLPSYKQQEVHAKDALDVYIEHRLMMESRTRNPMEQRDERNSFPSELMKRFEVGFKPLSTEKAHSIREVKAQHIGKLVTVRGIVTRCTEVKPMMVVATYTCDRCGSETYQPVNSLSFTPVHDCPSDDCRVNKAGGRLYLQTRGSKFVKFQEVKMQEHSDQVPVGHIPRSMTIMCRGEVTRMAQPGDHIVVSGVFLPLMRTGFAQMIQGLLSETFLQAHRIICINKNDEISDKDAELTPEELEELAQDDFYERLATSLAPEIYGHLDVKKALLLLLVGGVDKRPDGMKIRGNINICLMGDPGVAKSQLLGYISRLAVRSQYTTGRGSSGVGLTAAVMKDPLTGEMTLEGGALVLADQGVCCIDEFDKMADQDRTAIHEVMEQQTISIAKAGIMTTLNARVSILAAANPAFGRYNPRRTVEQNIQLPAALLSRFDLLWLIQDKPDRDNDLRLAKHITYVHSHSKQPPTRVKALDMNLMRRYINLCKRKNPTIPDELTDYIVGAYVELRREARNQKDMTFTSARNLLGILRLSTALARLRLSDSVEKDDVAEALRLLEMSKDSLNQIHEHQKGHVPNTSDRIFAIVRELAGSGKAVKISDIMDRCTTKGFKPDQVDKCIDDYEELNVWQVNMGRTKITFM