wanglab/gogpt-training-data huggingface dataset:
Protein: Phorbol-12-myristate-13-acetate-induced protein 1 (Protein Noxa) (Q9JM54)
Organism: Mus musculus (Mouse)
Function: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1 (By similarity). Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10807576}.
Interaction partners:
- Induced myeloid leukemia cell differentiation protein Mcl-1 homolog
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Bcl-2-like protein 2
- Bcl-2-related protein A1
- Bcl-2-like protein 11
- Bcl-2-binding component 3
- Bcl-2-interacting killer
- BH3-interacting domain death agonist
- Cellular tumor antigen p53
Sequence:
MPGRKARRNAPVNPTRAELPPEFAAQLRKIGDKVYCTWSAPDITVVLAQMPGKSQKSRMRSPSPTRVPADLKDECAQLRRIGDKVNLRQKLLNLISKLFNLVT
Protein: Chromosome 1 open reading frame 48 variant (Chromosome 1 open reading frame 48, isoform CRA_a) (Q53FM2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGSPELVVLDPPWDKELAAGTESQALVSATPREDFRVRCTSKRAVTEMLQLCGRFVQKLGDALPEEIREPALRDAQWTFESAVQENISINGQAWQEASDNCFMDSDIKVLEDQFDEIIVDIATKRKQYPRKILECVIKTIKAKQEILKQYHPVVHPLDLKYDPDPAPHMENLKCRGETVAKEISEAMKSLPALIEQGEGFSQVLRMQPVIHLQRIHQEVFSSCHRKPDAKPENFITQIETTPTETASRKTSDMVLKRKQTKDCPQRKWYPLRPKKINLDT
Protein: Calcium release-activated calcium channel protein 1 (Protein orai-1) (Transmembrane protein 142A) (Q5M848)
Organism: Rattus norvegicus (Rat)
Function: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT. Plays a prominent role in Ca(2+) influx at the basolateral membrane of mammary epithelial cells independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May mediate transepithelial transport of large quantities of Ca(2+) for milk secretion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96D31}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8BWG9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Note=Colocalizes with STIM1 in membrane punctate structures at ER-PM junctions. {ECO:0000250|UniProtKB:Q96D31}.
Interaction partners:
- Stromal interaction molecule 1
- Stromal interaction molecule 2
- Short transient receptor potential channel 1
- Short transient receptor potential channel 3
- Protein orai-3
- Short transient receptor potential channel 4
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Transient receptor potential Ca2+ channel 6A
Sequence:
MHPEPAPPPNNSNPELPLSGGSSTSGSRRSRRRSGDGEPTGAPPLPPPPAVSYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDTDHDYPPGLLIVFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKRQAGQPSPTKPPTEPAVVVANSSNNGGITPGEAAAIASTAIMVPCGLVFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHSLTPGTHYA
Protein: Testican-3 (SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycan 3) (Q8BKV0)
Organism: Mus musculus (Mouse)
Function: May participate in diverse steps of neurogenesis. Inhibits the processing of pro-matrix metalloproteinase 2 (MMP-2) by MT1-MMP and MT3-MMP. May interfere with tumor invasion (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MLKVSALLCVCAAAWCSQTLAAAAAVAVAGGRSDGGNFLDEKQWLTTISQYDKEVGQWNKFRDEVEDDYFRTWNPGKPFDQALDPAKDPCLKTKCSRHKVCITQDAQTALCISHRRLTHSMKEVGGSHKQWRGLPSSTCKPCPIAYASPVCGSDGHSYSSQCKLEYQACVLGKQISIKCEGRCPCPSDKSMNIGRNVKRACSDLEFREVANRLRDWFKALHESGSQNKKTKALLRPERSRFDTSILPICKDSLGWMFNRLDTNYDLLLDQSELGSIYLDKNEQCTKAFFNSCDTYKDSLISNNEWCYCFQRQQDPPCHTELSNIQKRQGIKKLLGQYIPLCDEDGYYKPTQCHGSVGQCWCVDRYGNEVVGSRINGVADCAIDFEISGDFASGDFREWTDDEGEEDDIMNDKDDIEDDDEDEGDDDDDGDVHDGYI
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IBW8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MAPPGGSVGAGSGGEEDAKHMFDRIGEEVYKEVKNGGAEKYFYELHGTLSKARFENEPEGLQTQGNPCQLDHRYHTNATNVRSYPCRAGKEERFSQVHGGECDKNKIRDNEDDRVGACAPFRRLHLCVRNLENINIKKKIDNDNLLADVCLAAKYEGDLIKTHYTPYEHKYGDSPSQLCTMLARSFADIGDIVRGKDLYLGNSREKEKLQTNLKSIFQNIYKNLKKPAQKHYSDPHANFYKLREDWWYANRQQVWYAITCGAEGYQYFRKTACNGGKSSTPNKCRCTTHDVPTYFDYVPQYLRWFEEWAEDFCRKRKKQLTDAIKNCREEDENGENRYCDLNGYDCKNTAKGKNKYKHDQECIKCSSVCIPFGPWIKNQKQEFEKQKNKYENEILGKSRRKRSIGSDTYDGYIEQFYDILKREYRDVDKFLDLLSKETACKQQPYDEPRTIDISFKNPEGIDIFSSTKYCQACPWCGIEEQKVNGRWIAKGDEDCNNKEIIKFNNEDTTDISILSTDRGKTKILEKLGSFCRNGEKIKKDDWKCHYDDNDKSDNCILQNDNKNTKNQEIESFNSLFWHWINEMLKDSILWSKELDRCIKKDDKSKCISGCKKNCECFKNWVAQKQQEWKQIEQHYEKEDFELSGPYGILEGNLQIYYLPMIQEAHPKDEAVQKMEDIIEKNKPNMLSVKEHDNSITKFLQHEEEDANKCTGIHNDAKCNQQKKQKTPGGGDDARSDTSHDGARPQPPPITNHHEEHDDDEDDDPNKIRSIKFEDEKHIQPKFKEHPDEVKETEEAEETEEGTDGGGEIPQKETQPAEATTEDGTGETTQITKEDGVKPCDIVSKLFQNPNDFSDACTLKYVTGKNYGWKCIPSGDKTATSSGNGERPSRSKRGAEPTSDGVPTTGGKDGATGGSICVPPRRRRLYVTPLTRLAGGDGNTQAGETTQGNGASTETPEASLRRAFVESAAVETFFLWHKYKEEKKTPATQNGALPLPLAPDVSPPSENPQTKLEGGNIPEEFLRQMFYTLGDYRDILVRGGDVNSDSEKKDGDSNSDRNIVLNAGGDKASMEKIQQEIDEIIKQSGNNKGTSGTTSRGPQIGSHSPNPDKQQTEREKWWDKHAPSIWNGMICALTYEEKTNSASGSESKIEQNQKLKDKLWDNDGNKPKNDNYTYDKVELKEENSGPKGQTESSSPSGDNTPLSHFISRPTYFRYLEEWGQNFCKERKKRLEKIKEECRSGNYGKEHCSGDGHYCKTSDLKHHKMFQDFVCRDCYKQCRKYKKWIDIKFDEYQNQKHKYQGEYDKLTKVDCPNNGDKKFCEEIKKHSSAAEFLKSLKHCKDGQNNNDQNNIIDFENTKTTFGPLDYCKTCPLNGVNCNVIRGTNGCIENRQKWKDVFDKIHKDNEKITENITVEMIDRRGINIDKKFEQLFKESYLFKSVREQNWECKVINNDTDVCKLTNFDETIDLNDYTTFKVFLEYWLDDFLYGYYLLKKRKIIEKCTQKEGKTCNENSKNDCACVGKWVQQKGKEWESIKDHFQKRQYGNGDDIKSKVKMFLEKLQSLTELNKIMKPCTSLDKFKASLKCNSTENSEKGGKDGKKSDIIECMLEDLDTKIKTGSCLTQPSGEKQAECEKYTPPDDEDLLLEEENENQVEAPKICEGVIKPETKVVDEHACKTDAPQPDVKEEEEEKEEEIVQPATTGDEGTKELPLTPPAPAPAAPSSTPATPNHQPLPSDNTSDILKTTIPFGIALALTSIALLFLKKKTKSSVGNLFQILQIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSESEYEEMDINDIYVPDSPKYKTLIEVVLEPSGNNTTASGKNTPSDTQNDIQSDGIPSSKITDNEWNTLKKDFISNMLQNTQNTEPNILRDNVDNNTHPTTSHHNVEEKPFIMSIHDRNLFSGEEYNYDMFNSGNNPINISDSTNSMDSLTSNNHSPYNDKNDLYSGIDLINDALSGNHIDIYDEMLKRKENELFGTNHVKHTSTHSVAKNTNSDPILNQINLFHKWLDRHRDMCEKWKNNHERLPKLKELWENETHSGDINSGIPSGNHVLNTDVSIQIHMDNPKPKNEFKNMDTTPNKSTMDTMLDDLEKYNEPYYYDFYKNDIYYDVNDDDKTSMDNNNNLVDKNNPVDNNNSTYNHRNPADINKNFVHKNNQNQHPIEKPTKIQIEMNSNNREVVEQQYPIADIWNI
Protein: Platelet-derived growth factor subunit A (PDGF subunit A) (PDGF-1) (Platelet-derived growth factor A chain) (Platelet-derived growth factor alpha polypeptide) (P20033)
Organism: Mus musculus (Mouse)
Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB.
Subcellular location: Secreted. Note=Released by platelets upon wounding.
Interaction partners:
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Platelet-derived growth factor subunit B
- Platelet-derived growth factor C
- Platelet-derived growth factor D
- Pro-epidermal growth factor
- Insulin-like growth factor 1
- Epidermal growth factor receptor
- Protransforming growth factor alpha
- Insulin-1
Sequence:
MRTWACLLLLGCGYLAHALAEEAEIPRELIERLARSQIHSIRDLQRLLEIDSVGAEDALETSLRAHGSHAINHVPEKRPVPIRRKRSIEEAIPAVCKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACATSNLNPDHREEETGRRRESGKKRKRKRLKPT
Protein: tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+] (EC 1.3.1.90) (mRNA-dihydrouridine synthase DUS4) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 4) (Q06063)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U20a and U20b in cytoplasmic tRNAs. Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- 18S rRNA aminocarboxypropyltransferase
- tRNA
Sequence:
MHTMHIPSGDVLIPKPKLITEETDPLHIIKTRQKTHGRPVTIAGPMVRYSKLPFRQLCREYNVDIVYSPMILAREYVRNEHARISDLSTNNEDTPLIVQVGVNNVADLLKFVEMVAPYCDGIGINCGCPIKEQIREGIGCALIYNSDLLCSMVHAVKDKYGDKLRIETKIRIHEALDETVELCRKLCDAGVDWITIHGRTRRTRSSQPANLDAIKYIIENISDKNVPVIANGDCFKLSDLERITKYTGAHGVMAVRGLLSNPALFAGYTTCPWGCIEKFCYWALEFGGLPFQLAQHHLYCMLENMELKKSLLKKMMNLKNYISLIDWFNKTFEFKRYGEDGFGMGVEIPYKANSCVQRSASVVERQE
Protein: L-tyrosine decarboxylase (TDC) (EC 4.1.1.25) (Levodopa decarboxylase) (L-dopa decarboxylase) (EC 4.1.1.-) (A0A481NV25)
Organism: Enterococcus faecium (Streptococcus faecium)
Function: Catalyzes the decarboxylation of L-tyrosine to produce tyramine. Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecium (By similarity).
Interaction partners:
- Amino acid permease
- Na+/H+ antiporter
- APC family permease
- Isochorismatase
- Tyrosine--tRNA ligase
- Amino acid decarboxylase
- EntA
Sequence:
MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLHVDAAYGGYARSLFLNEAGEFVPYASLAEFFEEHHVFHHYVTIDKEVYEGFRAISEADSVTIDPHKMGYVPYAAGGIVIKHKNMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNVTGYGQLIGASIEAAQRFREFLEQLHFTVKGKTIEVYPLNHPDFNMVNWVFKVQDCTDLNAINELNEKMFDRSSYMDGDVYGERFITSHTTFTQEDYGDSPIRFIERMGLSKEEWQKEQQITLLRAAIMTPYLNDDRIFNFYTKEIAKAMEKKLNEIIK
Protein: UPF0461 protein C5orf24 (Q7Z6I8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMHPVASSNPAFCGPGKPSCLNEDAMRAADQFDIYSSQQSKYSHTVNHKPMVCQRQDPLNETHLQTTSGRSIEIKDELKKKKNLNRSGKRGRPSGTTKSAGYRTSTGRPLGTTKAAGFKTSPGRPLGTTKAAGYKVSPGRPPGSIKALSRLADLGYGCGTAAFPYPMMHGRAVHGVEETSSEVKPPNE
Protein: Succinyl-CoA:glutarate CoA-transferase (EC 2.8.3.-) (Dermal papilla-derived protein 13) (Dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase SUGCT) (Succinate--hydroxymethylglutarate CoA-transferase) (EC 2.8.3.13) (Q9HAC7)
Organism: Homo sapiens (Human)
Function: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23893049, ECO:0000269|PubMed:34492704}.
Interaction partners:
- M-phase-specific PLK1-interacting protein
- Hydroxysteroid dehydrogenase-like protein 2
- Glutaryl-CoA dehydrogenase, mitochondrial
- Iodotyrosine deiodinase 1
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Riboflavin kinase
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Citramalyl-CoA lyase, mitochondrial
- 2-hydroxyacyl-CoA lyase 1
- 2-hydroxyacyl-CoA lyase 2
Sequence:
MLATLARVAALRRTCLFSGRGGGRGLWTGRPQSDMNNIKPLEGVKILDLTRVLAGPFATMNLGDLGAEVIKVERPGAGDDTRTWGPPFVGTESTYYLSVNRNKKSIAVNIKDPKGVKIIKELAAVCDVFVENYVPGKLSAMGLGYEDIDEIAPHIIYCSITGYGQTGPISQRAGYDAVASAVSGLMHITGPENGDPVRPGVAMTDLATGLYAYGAIMAGLIQKYKTGKGLFIDCNLLSSQVACLSHIAANYLIGQKEAKRWGTAHGSIVPYQAFKTKDGYIVVGAGNNQQFATVCKILDLPELIDNSKYKTNHLRVHNRKELIKILSERFEEELTSKWLYLFEGSGVPYGPINNMKNVFAEPQVLHNGLVMEMEHPTVGKISVPGPAVRYSKFKMSEARPPPLLGQHTTHILKEVLRYDDRAIGELLSAGVVDQHETH
Protein: Vacuolar segregation protein 7 (O94262)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the PI(3,5)P2 regulatory complex that regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Directly involved in vacuolar membrane scission. Required for normal vacuole acidification, inheritance and morphology (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Inclusion body clearance protein IML2
- Large ribosomal subunit protein eL20B
- Vacuolar protein sorting-associated protein atg6
- Vacuolar protein sorting-associated protein 3
- Vacuolar fusion protein mon1
- Vitamin H transporter 1
- Pterin-4-alpha-carbinolamine dehydratase
- PtdIns3K complex I subunit atg38
- Protein VAC14 homolog
- Phosphatidylinositol 3-kinase pik3
Sequence:
MSEPKPMQMSVETETVLNVSQVQIPSSCDRKASLETLKTKKNAQKKKKISLPNVMTSKAAMFAARVASAVDQDPNDEESENFVYENLIPTNDDELHSPSASIHSFQTYNLPLEMLPTINHVPYYGSAGTNALNGGPLSNSRKLIPKRSAKFSSMVGSSDTRCNSPTTARGLATSPLQINPTTSKSPLLNKKLSSTSQEPFRTSRRSGQESGDVTTKMLRNLLHKRLWISFFFACFVVLSLVYFHYAVQPLL
Protein: At5g01075 (Glycosyl hydrolase family 35 protein) (Q8LEW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40 homolog
Sequence:
MKTSSFVFLLVVIILSFSLLASSSEMKVGLEDYNFPVDPTPTTKASIKPGPIEHGTPLNPYIPKPPSPSSSPPPQQSQDGG
Protein: Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein) (P06733)
Organism: Homo sapiens (Human)
Function: Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10802057}. Cell membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.; SUBCELLULAR LOCATION: [Isoform MBP-1]: Nucleus.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Plasminogen
- Pyruvate kinase PKM
- Phosphoglycerate mutase 1
- Phosphoglycerate kinase 1
- Glucose-6-phosphate isomerase
- Probable phosphoglycerate mutase 4
- Fructose-bisphosphate aldolase A
- Pyruvate kinase PKLR
Sequence:
MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK
Protein: Subtilisin-like protease SBT5.4 (EC 3.4.21.-) (Subtilase subfamily 5 member 4) (AtSBT5.4) (F4JXC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position (By similarity). Interferes with CLAVATA 3 (CLV3) signaling, but does not cleave CLV3.
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:19588163}. Cell membrane {ECO:0000305|PubMed:19588163}.
Interaction partners:
- Glycoprotein membrane GPI-anchored
- Probable beta-1,3-galactosyltransferase 8
- Kunitz trypsin inhibitor 2
- Subtilisin-like protease SBT6.1
- S-protein homolog 12
- Putative B3 domain-containing protein At5g58280
Sequence:
MSMTRRYSSTQYSNKMSLQSLSSLLLLVTLFFSPAFALKKSYIVYLGSHAHLPQISSAHLDGVAHSHRTFLASFVGSHENAKEAIFYSYKRHINGFAAILDENEAAEIAKHPDVVSVFPNKGRKLHTTHSWNFMLLAKNGVVHKSSLWNKAGYGEDTIIANLDTGVWPESKSFSDEGYGAVPARWKGRCHKDVPCNRKLIGARYFNKGYLAYTGLPSNASYETCRDHDGHGSHTLSTAAGNFVPGANVFGIGNGTASGGSPKARVAAYKVCWPPVDGAECFDADILAAIEAAIEDGVDVLSASVGGDAGDYMSDGIAIGSFHAVKNGVTVVCSAGNSGPKSGTVSNVAPWVITVGASSMDREFQAFVELKNGQSFKGTSLSKPLPEEKMYSLISAADANVANGNVTDALLCKKGSLDPKKVKGKILVCLRGDNARVDKGMQAAAAGAAGMVLCNDKASGNEIISDAHVLPASQIDYKDGETLFSYLSSTKDPKGYIKAPTATLNTKPAPFMASFSSRGPNTITPGILKPDITAPGVNIIAAFTEATGPTDLDSDNRRTPFNTESGTSMSCPHISGVVGLLKTLHPHWSPAAIRSAIMTTSRTRNNRRKPMVDESFKKANPFSYGSGHVQPNKAAHPGLVYDLTTGDYLDFLCAVGYNNTVVQLFAEDPQYTCRQGANLLDFNYPSITVPNLTGSITVTRKLKNVGPPATYNARFREPLGVRVSVEPKQLTFNKTGEVKIFQMTLRPLPVTPSGYVFGELTWTDSHHYVRSPIVVQLSS
Protein: Protein-lysine N-trimethyltransferase SMYD5 (EC 2.1.1.-) (SET and MYND domain-containing protein 5) ([histone H3]-lysine20 N-trimethyltransferase SMYD5) (EC 2.1.1.372) ([histone H4]-lysine36 N-trimethyltransferase SMYD5) (EC 2.1.1.359) (F1RET2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 to form trimethylated histone H4 lysine 20 (H4K20me3) which represents a specific tag for epigenetic transcriptional repression (By similarity). Plays a crucial role in hematopoiesis during embryogenesis by negatively regulating expression of genes related to both primitive and definitive hematopoiesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6GMV2}.
Interaction partners:
- Protein-lysine N-methyltransferase SMYD4
- SET and MYND domain-containing 3.
- [histone H3]-lysine
- Mitogen-activated protein kinase kinase kinase 2
- Actin-histidine N-methyltransferase
Sequence:
MAAPVDDMFSRCVDSAKASNCVDVRFINNVKGKGLFAKKPFKKGDTIFIERPLVSSQFLWNALYKYRACEYCLRALETAEENARRLSGLPALILPHPELCKVRPDRHQACPQCQVMYCSSECRQAAMDQYHKILCLGPSNDDPDHPVNKLQDAWRSVHFPPETSSVMILAKMVATIKQTQDKERWQRLFTNFCSRTANEEEEIVHKLLGEKFQGQLGLLRNLFTTALYEDRLSQWFTPEGFRSLFSLVGTNGQGIGTSSLSQWVHACDALELPRQQREQLDAFIDQLYKDIDKETGDFLNCEGSGLFLLQSSCNHSCVPNAEASFPENNFLLHLTALGDIGPGEEICISYLDCCQRDRSRHSRHKILRENYLFICSCQKCLSQMDDADMTSEDEEEVEGEGETEGEDMEDEMTDV
Protein: Cystatin-B (Stefin-B) (Q76LA1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF
Protein: Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2) (Q9Z2Y2)
Organism: Mus musculus (Mouse)
Function: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Trans cisternae of Golgi stack. {ECO:0000250}.
Interaction partners:
- Beta-galactoside alpha-2,6-sialyltransferase 2
- Alpha-lactalbumin
- Beta-1,3-galactosyltransferase 1
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- Alpha-
- Beta-galactoside alpha-2,6-sialyltransferase 1
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
Sequence:
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSTRSPAHALYPAASSSTNCSRPNATAASSGLPEVPSARPGPTAPVIPPCPDVPPGLVGRVVIEFTSPMPLERVQRENPGVLLGGRYSPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPMLRRQRLRYGVYVINQHGEETFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYASYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDVRIGRYRMIKHDRDKHNEPNPQRFNKIQNTKMSMKWDGIGSVRYRVLEVSRQPLFTNITVDIGQPMSWLTQG
Protein: Myb family transcription factor PHL13 (Protein PHR1-LIKE 13) (F4J3P7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Vesicle-associated protein 1-3
- Cold shock protein 1
- Sulfate transporter 1.3
Sequence:
MTLASDFGFPSAISSSFTILEERYHNNFPNTLCVSSGQESMNNNPVPCQVFPLVSGGSSGGNLFSSSSGFCNGVYVSSSSQARPSVSTVPRDRITVAHVSGEGQRQECPVETHSLQLINQPQEQKIMTWSSDQIRGFFDFPVPDPQAASSRTMVSSKEVLSKCEWPDWADQLISDDSLEPNWSELLGDPNVLNLYSKIETQSSDIARQEIVFRNQHQVDPSMEPFNAKSPPASSMTSKQRMRWTPELHEAFVEAINQLGGSERATPKAVLKLINSPGLTVYHVKSHLQKYRTARYKPELSKDTEEPLVKNLKTIEDIKSLDLKTSIEITEALRLQMKVQKQLHEQLEIQRSLQLQIEEQGRYLQMMIEKQQKMQENKKDSTSSSSMPEADPSAPSPNLSQPFLHKATNSEPSITQKLQNGSSTMDQSESTSGTSNRKRVRED
Protein: GATA-type transcription factor sreA (Siderophore uptake regulator sreA) (G5EB20)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: GATA-type transcription repressor that regulates iron- acquisition genes through specific binding GATA sequence elements of target promoters. Iron acquisition regulation is critical for survival under both iron-limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity). SreA targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Siderophore iron transporter mirB
- Nitrite reductase [NAD
- HapE
- PTAB
- BZIP domain-containing protein
- Siderophore iron transporter mirC
- CPCA
- 5-aminolevulinate synthase, mitochondrial
- Cytochrome c
- Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase
Sequence:
MLASIPHMETLRSLPRNPDVVARHPSAEDLDAAQQLISSAQAGREHPQDRHYTDNGSRKSEAGAPHSHHEGEYPIVQTSETPMNGHHVEKTSPKSQKDTSFLGHSCSNCGTKSTPLWRRSPTGAMICNACGLYLKARNVARPTKRNRTQASPEAYHPQNQSVGSQPDPAVTGSEGCTGSCPGGGNCNGTGGAEGCDGCPAYNNRVYKSTARGNVAAHALNRAGNSDAVPSPEAEAPARNSGQPEGNMLVACQNCGTTVTPLWRRDENGHPICNACGLYYKLHGSYRPTTMKKTIIKRRKRVVPALRENSPTAATHSSHGSSASPEASSPATLAYSHDERHRYYSSEPVDQYHRISPAAQRPFGFAPPPVDFTNFNSGAVTLPHHPPPPRLLEPGHPPLSQFARRSISPSSSGNSKKRTLAEAGANTDTGPVPTTLEAGSNQLPPIVSSANPPPPARLSSISSILNHAHARDESRLDPSLAALGRQQQSQPHHPQSSPLAPTQAASQSLPGVSNMDNHVEDRRAKLQREAEEMREQLRAKERELAELAGQ