wanglab/gogpt-training-data huggingface dataset:
Protein: FK506-binding protein 39 kDa (EC 5.2.1.8) (Histone proline isomerase) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (O74191)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10544281, ECO:0000269|PubMed:14981505}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome production factor 2 homolog
- Nucleolar protein 58
- Histone H2A.Z-specific chaperone chz1
- Ribosome biogenesis protein erb1
- 25S rRNA
- ERAD-associated E3 ubiquitin-protein ligase doa10
- Peptidyl-prolyl cis-trans isomerase
- H/ACA ribonucleoprotein complex subunit nhp2
- AdoMet-dependent rRNA methyltransferase spb1
- Uncharacterized NOC2 family protein C1142.04
Sequence:
MSLPIAVYSLSVKGKDVPAVEESTDASIHLTMASIDAGEKSNKPTTLLVKVRPRIPVEDEDDEELDEQMQELLEESQREFVLCTLKPGSLYQQPLNLTITPGDEVFFSASGDATIHLSGNFLVDEEDEEEEESDEDYDLSPTEEDLVETVSGDEESEEESESEDNSASEEDELDSAPAKKAQVKKKRTKDESEQEEAASPKKNNTKKQKVEGTPVKEKKVAFAEKLEQGPTGPAAKKEKQQASSNAPSSPKTRTLKGGVVVTDVKTGSGASATNGKKVEMRYIGKLENGKVFDKNTKGKPFAFILGRGEVIRGWDVGVAGMQEGGERKITIPAPMAYGNQSIPGIPKNSTLVFEVKLVRVH
Protein: Nucleolar protein 3 (Apoptosis repressor with CARD) (Q9D1X0)
Organism: Mus musculus (Mouse)
Function: Apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (By similarity). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I. Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia. Inhibits too myoblast differentiation through caspase inhibition (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q62881}. Mitochondrion {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q62881}. Membrane {ECO:0000250|UniProtKB:O60936}; Lipid-anchor {ECO:0000250|UniProtKB:O60936}. Note=Phosphorylation at Thr-149 results in translocation to mitochondria. Colocalized with mitochondria in response to oxidative stress. {ECO:0000250|UniProtKB:Q62881}.
Interaction partners:
Sequence:
MGNVQERPSETIDRERKRLVETLQADSGLLLDALVARGVLTGPEYEALDALPDAERRVRRLLLLVQSKGEAACQELLRCAQQTVRMPDPAWDWQHVGPGYRNRSYDPSCPGHWTPEAPSSGTTCPELPRASEQEEVGGPEGSEALQPRTPEEPELEAEATEGDEPDLEQEMNPEQEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPDFQEEDESEDS
Protein: Calcium-activated chloride channel N-terminal domain-containing protein (Q8C9E1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKSEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDRPFYISRKNTIEATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTENNHNAEAPNLQNKMCNRRSTWDVIKASADFQNSPPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLT
Protein: Isochorismate synthase MenF (EC 5.4.4.2) (Isochorismate hydroxymutase) (Isochorismate mutase) (P38051)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of chorismate to isochorismate. Can also catalyze the reverse reaction, but with a lower efficiency.
Interaction partners:
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- 1,4-dihydroxy-2-naphthoyl-CoA synthase
- o-succinylbenzoate synthase
- Enterobactin synthase component B
- 2-succinylbenzoate--CoA ligase
- Chorismate synthase
- Bifunctional protein TrpGD
- Isochorismate synthase EntC
- 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
- Chorismate pyruvate-lyase
Sequence:
MQSLTTALENLLRHLSQEIPATPGIRVIDIPFPLKDAFDALSWLASQQTYPQFYWQQRNGDEEAVVLGAITRFTSLDQAQRFLRQHPEHADLRIWGLNAFDPSQGNLLLPRLEWRRCGGKATLRLTLFSESSLQHDAIQAKEFIATLVSIKPLPGLHLTTTREQHWPDKTGWTQLIELATKTIAEGELDKVVLARATDLHFASPVNAAAMMAASRRLNLNCYHFYMAFDGENAFLGSSPERLWRRRDKALRTEALAGTVANNPDDKQAQQLGEWLMADDKNQRENMLVVEDICQRLQADTQTLDVLPPQVLRLRKVQHLRRCIWTSLNKADDVICLHQLQPTAAVAGLPRDLARQFIARHEPFTREWYAGSAGYLSLQQSEFCVSLRSAKISGNVVRLYAGAGIVRGSDPEQEWQEIDNKAAGLRTLLQME
Protein: Beta-soluble NSF attachment protein (SNAP-beta) (Brain protein I47) (N-ethylmaleimide-sensitive factor attachment protein beta) (P28663)
Organism: Mus musculus (Mouse)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Subcellular location: Membrane; Peripheral membrane protein.
Interaction partners:
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein 25
- Syntaxin-1A
- Vesicle-associated membrane protein 8
- Synaptosomal-associated protein 23
- Vesicle-fusing ATPase
- Syntaxin-4
- Syntaxin-7
- Syntaxin-5
- Syntaxin-3
Sequence:
MDNAGKEREAVQLMAEAEKRVKASHSFLRGLFGGNTRIEEACEMYTRAANMFKMAKNWSAAGNAFCQAAKLHMQLQSKHDSATSFVDAGNAYKKADPQEAINCLNAAIDIYTDMGRFTIAAKHHITIAEIYETELVDIEKAIAHYEQSADYYKGEESNSSANKCLLKVAAYAAQLEQYQKAIEIYEQVGANTMDNPLLKYSAKDYFFKAALCHFIVDELNAKLALEKYEEMFPAFTDSRECKLLKKLLEAHEEQNSEAYTEAVKEFDSISRLDQWLTTMLLRIKKSIQGDGEGDGDLK
Protein: Extensin-1 (AtExt1) (AtExt4) (Extensin-1/4) (Q38913)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Structural component which strengthens the primary cell wall.
Subcellular location: Secreted, primary cell wall.
Interaction partners:
- Leucine-rich repeat extensin-like protein 1
- Cytoplasmic tRNA 2-thiolation protein 1
- Extensin-2
- Proline-rich extensin-like family protein
- Extensin-like protein
- OBP3-responsive protein 4
- Leucine-rich repeat extensin-like protein 6
- 2-isopropylmalate synthase 1, chloroplastic
- Leucine-rich repeat extensin-like protein 2
Sequence:
MASFLVLAFSLAFVSQTTANYFYSSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVKHYSPPPVYKSPPPPVKYYSPPPVYKSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPVHYSPPPVVYHSPPPPKKHYEYKSPPPPVHYSPPTVYHSPPPPVHHYSPPHQPYLYKSPPPPHY
Protein: tRNA(His) guanylyltransferase 2 (EC 2.7.7.79) (F4ISV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:20660484}.
Interaction partners:
- RNA-binding
- Histidine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, chloroplastic/mitochondrial
- GPN-loop GTPase 3
- F17H15.1/F17H15.1
- KH domain-containing protein
- KH domain-containing protein
- Nucleotidyltransferase
- RNA-binding
- Protein BTR1
Sequence:
MANSKYEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKASRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVVSCASVEVLQAYLAWRQHDCHISNQYDTCLWMLVKSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKVIFSIISFFYFLLEETVKHDENGKPVKRLRRRETLVHSENVAGRSFWNEHSSLHKDLGHFAKDIGKIEPDYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKSELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYPTSDILLDYLAWRQVDCHINNQYNTCFWMLVKSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQEGVTEENGEVSGKQVEAEVGVDYSNIIDQCFWQQHPHILSFS
Protein: Collagen type XV alpha 1 chain (F1SSE8)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MASGRDAQCWRLLLLLSISALLPAVTRTRSATELASQGHLDLTELIGVPLPSSVSFVTGYGGFPAYSFGPGANVGRPARTLIPPTFFRDFAISVTVKPSSARGGVLFAITDAFQKVIYLGLRLSAVEDGRQRVILYYTEPGSQVSHEAASFPVPVMTHRWNRFAVVVQGEEASLLVECEEQGHVSFPRSSQALAFEPSAGIFVGNAGATGLERFTGSIQQLTVHSDPRTPEELCEAEESSASGEASGLQETDGVAEMVEAVTYTQAPSEPAEVEPINMPPTPSPLSEDAELSGEPVPEGTQGTTNLSAFPHSSPEQGSGEILNDTLERVHTVDGAPVTDTGSGDGAFLHVIEESLAATAAAVESEVTISTAGEAETESVPTEGPTLSMSTKDPGEEVTLGPDDEEGSAVTAAEEAEVLVSSPGEAEAGSVPTGELTLSMSTQDPGEGGPVHEESLTTAVTAKAPLSTFEEEASRVPTDGLAPLIPTVAPEQVFTSGPGDDDLAAAATEEPLISSGAEELSGVPPEGPPLPLPTVAPERGGAPGEEGEGLPGPPPPTRPAGPTAGAEAEGSSLGWGLDIGSGSGDPVRSEELLRGPPGPPGPPGLPGIPGRPGTDVFVGPPGSPGEDGPAGEPGPPGPEGKPGLDGASGLPGMKGEKGARGPDGSVGEKGDPGSRGLPGPPGKNGQVGTPGVMGPPGPPGPPGPPGPGCAMGQGFEDTEGSGSIRLLHEPRISGPVASVGPKGEKGDQGPKGERGMDGASIVGPPGPRGPPGRIEVLSSSLINITHGFMNLSDIPELVGPPGPEGIPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGAILTGDVPLERLRGKKGEPGEHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGVMMPGPPGLPGPPGPPGPPGAVINIKGAVFPIPVRPHCKTPVGTTHPGNSELITFHGVKGEKGSWGLPGSKGEKGDQGAQGPPGPPVDPAYLRHFLNSLKGENGDRGMKGEKGDTYEGFSVSGPPGLPGSPGLVGQKGETVIGPQGPPGVPGLPGPPGFGRPGSPGPPGPPGPPGPPAILGAAVALPGPPGPPGQPGLPGSRNLVTAFSNMDDMLQKAHLVIEGTFIYLRDSTEFFIRVRDGWKKLQLGELIPLPADSLPPPALSGNPHQPQLPLTSISSVNYDRPALHLVALNTPSSGDLRADFQCFQQARAAGLLSTYRAFLSSHLQDLSTIVRKAERYSLPIVNLKGQVLFNNWDSIFSGHGGQFNTHVPIYSFDGRDVMTDPSWPQKVVWHGSSTHGVRLVDQYCEAWRTADVAVMLGSPLSTGKILDQKAYSCADRLIVLCIENSFMTDARK
Protein: Tyrosine-protein phosphatase YVH1 (PTPase YVH1) (EC 3.1.3.48) (Q02256)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be directly involved in signal transduction and/or cell cycle regulation. It is necessary for maintaining growth rate or spore germination. Could show both activity toward tyrosine-protein phosphate as well as with serine-protein phosphate.
Interaction partners:
- 60S ribosomal export protein NMD3
- Large subunit GTPase 1
- Probable metalloprotease ARX1
- Cytoplasmic 60S subunit biogenesis factor REI1
- Ribosome assembly factor MRT4
- Eukaryotic translation initiation factor 6
- Ribosome biogenesis protein RLP24
- Large ribosomal subunit protein eL24A
- Large ribosomal subunit protein uL18
- Nucleolar GTP-binding protein 1
Sequence:
MAGNANSVDEEVTRILGGIYLGGIRPIIDHRPLGAEFNITHILSVIKFQVIPEYLIRKGYTLKNIPIDDDDVTDVLQYFDETNRFIDQCLFPNEVEYSPRLVDFKKKPQRGAVFAHCQAGLSRSVTFIVAYLMYRYGLSLSMAMHAVKRKKPSVEPNENFMEQLHLFEKMGGDFVDFDNPAYKQWKLKQSIKLDPSGSELVSNSGMFKDSESSQDLDKLTEAEKSKVTAVRCKKCRTKLALSTSFIAHDPPSKESSEGHFIKRAANSHRIIDIQESQANCSHFFIEPLKWMQPELQGKQELEGKFSCPGCSSKVGGYNWKGSRCSCGKWVIPAIHLQTSKVDQFPLQSTALPNMVNFESEKVNR
Protein: Lysine-specific demethylase JMJ13 (EC 1.14.11.-) (Jumonji domain-containing protein 13) (AtJMJ13) (Protein JUMONJI 13) (Lysine-specific histone demethylase JMJ13) ([histone H3]-trimethyl-L-lysine(27) monodemethylase JMJ13) (F4KIX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone demethylase that demethylates 'Lys-27' (H3K27me) of histone H3 with a specific activity for H3K27me3 and involved in the regulation of gene expression. Acts as a temperature and photoperiod dependent flowering repressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- Histone H3.1
- ATP synthase subunit d, mitochondrial
- Lysine-specific demethylase JMJ31
- ATP synthase subunit delta, chloroplastic
- ATP synthase subunit O, mitochondrial
- ATPase, F1 complex, OSCP/delta subunit protein
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit a-1
Sequence:
MAERRICLSKEAKDGLEFLKRKKLQKMRSDSVNETVGFSTMARSGGDALRPTSASCGMRLRVTSSDTVSKVHGASTVRGGLMKEKVEKLETDDLKWTERLPECPVYRPTKEEFEDPLTYLQKIFPEASKYGICKIVSPLTATVPAGAVLMKEKSNFKFTTRVQPLRLAEWDSDDKVTFFMSGRTYTFRDYEKMANKVFARRYCSGGSLPDSFLEKEFWKEIACGKTETVEYACDVDGSAFSSAPGDPLGSSKWNLNKVSRLPKSTLRLLETSIPGVTEPMLYIGMLFSMFAWHVEDHYLYSINYQHCGASKTWYGIPGSAALKFEKVVKECVYNDDILSTNGEDGAFDVLLGKTTIFPPKTLLDHNVPVYKAVQKPGEFVVTFPRAYHAGFSHGFNCGEAVNFAMGDWFPFGAIASCRYAHLNRVPLLPHEELICKEAMLLNSSSKSENLDLTPTELSGQRSIKTAFVHLIRFLHLARWSLMKSGLCTGLVSNTYGTIVCSLCKRDCYLAFINCECYSHPVCLRHDVKKLDLPCGTTHTLYLRDNIEDMEAAAMKFEKEDGVSDLITTDEDLYKYPSSITLPAAKEDGYTPYSTIYFDFYTEVEMTSHDQLQSGNPVMSYEANASCISSVADDYECSDYVNRRANCSSSSDSKLSEEVACSSSKKTRFFPVVQDEQLVADQESDGSDSECFRVKRRSSLKFENRTVVLDTRESDHHQELKRLKKSHHHEGRYSSSSSVSRQEEEEDELVISNRKETQQQSDVKMQKKRIENHFGGFKRLKVKGLIKP
Protein: UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (BGnT-7) (Beta-1,3-Gn-T7) (Beta-1,3-N-acetylglucosaminyltransferase 7) (Beta3Gn-T7) (EC 2.4.1.-) (Q8NFL0)
Organism: Homo sapiens (Human)
Function: N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Involved in biosynthesis of N-linked keratan sulfate proteoglycans in cornea, with an impact on proteoglycan fibril organization and corneal transparency (By similarity). May play a role in the maintenance of tissue architecture by suppressing cellular motility and invasion (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Keratocan
Sequence:
MSLWKKTVYRSLCLALALLVAVTVFQRSLTPGQFLQEPPPPTLEPQKAQKPNGQLVNPNNFWKNPKDVAAPTPMASQGPQAWDVTTTNCSANINLTHQPWFQVLEPQFRQFLFYRHCRYFPMLLNHPEKCRGDVYLLVVVKSVITQHDRREAIRQTWGRERQSAGGGRGAVRTLFLLGTASKQEERTHYQQLLAYEDRLYGDILQWGFLDTFFNLTLKEIHFLKWLDIYCPHVPFIFKGDDDVFVNPTNLLEFLADRQPQENLFVGDVLQHARPIRRKDNKYYIPGALYGKASYPPYAGGGGFLMAGSLARRLHHACDTLELYPIDDVFLGMCLEVLGVQPTAHEGFKTFGISRNRNSRMNKEPCFFRAMLVVHKLLPPELLAMWGLVHSNLTCSRKLQVL
Protein: Pectinesterase A (EC 3.1.1.11) (Pectin methylesterase A) (Q5B7U0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in maceration and soft-rotting of plant tissue. Active against citrus pectin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- 3'-5' exonuclease/helicase
- Pectate lyase H
- Pectate lyase A
- Meiotic recombination protein
- Pectate lyase E
- Endopolygalacturonase B
- Probable pectate lyase G
- Probable pectate lyase F
- Pectate lyase plyB
- Probable pectate lyase D
Sequence:
MRVQSYLSLFSLVGAALCAPREHFKRTARTSAPAGCLTVGGSGTYSTIGAAFAALGSSSSEACIYISAGTYKEQLTFQYAGPLTLYGETTDTSSYKKNTVTITHTISSPEAGSLVASATVNAAMDNFTMYNINVVNGYGKGAQAVALAASGERQGYYGCQFLGYQDTLYARVGVQYYSNCYIEGAVDYIFGDASAWFGECDIVSNGAGYITAMSRETASDPAWYCFDHCNIYGKSGLDLTGDVYLGRPWRVLARVIYQNSELSDIINAAGWTTMAEGATPLYYEIGNTGDGADTSKRLYLSEISAAVTKATVLGSDWTDWLDWSY
Protein: Signal transducing adaptor molecule (A0A8I6A2K6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469}.
Interaction partners:
Sequence:
MESVRNWQNVLEKATSELNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGKIFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTDEFKNDPQLSLISAMIKNLKEQGVTFPAIGSQAAEQAKASPALVAKDPGTVATKKEEEDLAKAIELSLKEQRQQAAPLSTLYPSTSSLLTNHQHEGRKVRAVYDFEAAEDNELTFKAGEVITVLDDSDPNWWKGETHQGMGLFPSNFVTADLTAEPEMIKTEKKTVQFSDDVQIETIEPEPEPEPAFIDEDKMDQLLQMLQSTDPSDNQPDLPELLHLEAMCHQMGPLIDEKLEDIDRKHSELSELNVKVMEALSLYTKLMNEDPVYSVYAKSQSQQYYVQASGVSAPQVYPGPAQSGAYLVAGNAQMTHLQSYSLPPEQLASISQGAVPPSATPALPNQQAQASYPNAMVSSVQGNSYPSQASIYSPAAAAAAVAVTAVPVPADVTIYQNPGPNMSQVPNYTLTSSTLPHTGGSQQPPQPQQAYSQKALL
Protein: RNA-binding protein 42 (RNA-binding motif protein 42) (Q9VND7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Augmin complex subunit dgt3
- Augmin complex subunit dgt6
- RE23632p)
- LD36006p
- RE11167p
- PHD and RING finger domain-containing protein 1
- Precursor RNA processing 3, isoform A
- U4/U6 small nuclear ribonucleoprotein Prp31
- Small nuclear ribonucleoprotein F
- LIM domain-containing protein jub
Sequence:
MGTKRRNIEDELSRFEAEISKPPARNLFVPNQVRPIIAANTYQNSQHKLQHHQGNGGSRLTVPPPPMPPPPTFMSTFVPTGSGGGSSKAMSATPVVLSSAPKLYQCRQSVHVPTVAAAPSIDINAVSFDVTQKLKKLKAEKSGPNPIAEEAIKAARASSALQSFQTTERKKKDRKTVRIAGGTVWEDTSLADWPDDDFRIFCGDLGNDVNDEVLTRTFNKFPSFQRARVVRDKRTGKSKGFGFVSFREPADFIRAMKEMDGRYVGSRPIKLRKSTWRQRSLDVVKKKEREKQVLLQAFNSMT
Protein: Kunitz-type serine protease inhibitor DrTI (P83667)
Organism: Delonix regia (Royal poinciana) (Poinciana regia)
Function: Inhibits bovine trypsin and human plasma kallikrein.
Subcellular location: Secreted.
Interaction partners:
Sequence:
SDAEKVYDIEGYPVFLGSEYYIVSAIIGAGGGGVRPGRTRGSMCPMSIIQEQSDLQMGLPVRFSSPEESQGKIYTDTELEIEFVEKPDCAESSKWVIVKDSGEARVAIGGSEDHPQGELVRGFFKIEKLGSLAYKLVFCPKSSSGSCSDIGINYEGRRSLVLKSSDDSPFRVVFVKPRSGSETES
Protein: UPF0494 membrane protein C1348.07 (Q9P3V3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized transporter SPAC750.02c
Sequence:
MVRDTRNVDLERGLELCKPEKVNKQNLFTNIVKPQKDKINIKTDKIKFFLNNLFTEFSKFHDSCYPDGRISTRSKLRWPLLIIWCILIVFAIDKNFEVKDFLSIWINESFINENRFYSEIWGPIAIYICLFILLLLGLIYCSKIVVKAIPLISIVIAAVVVIIAVAMVKILYICHWLIYKILILAFGIKVKPLGDTLPTHNGETGSHSKATVGSDIEQIEFQNMPTPVKK
Protein: ISPsy5, Orf1 (Q877K1)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- ISPsy5, transposase
Sequence:
MMRPDAKVEKVYLYPKPVDFRKSIDGLAALVELDIKVAVFDPVLFVFLNKSRNRVKILYWERNGFCLWLKRLESERFKISPDDVDEAIVLTVQELNWLLDGFDLWRNRPHKILTPRFVA
Protein: Killer cell lectin-like receptor subfamily B member 1 (C-type lectin domain family 5 member B) (HNKR-P1a) (NKR-P1A) (Natural killer cell surface protein P1A) (CD antigen CD161) (Q12918)
Organism: Homo sapiens (Human)
Function: Plays an inhibitory role on natural killer (NK) cells cytotoxicity. Activation results in specific acid sphingomyelinase/SMPD1 stimulation with subsequent marked elevation of intracellular ceramide. Activation also leads to AKT1/PKB and RPS6KA1/RSK1 kinases stimulation as well as markedly enhanced T-cell proliferation induced by anti-CD3. Acts as a lectin that binds to the terminal carbohydrate Gal-alpha(1,3)Gal epitope as well as to the N-acetyllactosamine epitope. Binds also to CLEC2D/LLT1 as a ligand and inhibits NK cell-mediated cytotoxicity as well as interferon-gamma secretion in target cells.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 2 member D
- NKG2-D type II integral membrane protein
- Granzyme A
- Early activation antigen CD69
- Granzyme K
- T-cell surface antigen CD2
- T-cell surface glycoprotein CD3 zeta chain
- C-C chemokine receptor type 6
- Sphingomyelin phosphodiesterase
- T-cell surface glycoprotein CD8 alpha chain
Sequence:
MDQQAIYAELNLPTDSGPESSSPSSLPRDVCQGSPWHQFALKLSCAGIILLVLVVTGLSVSVTSLIQKSSIEKCSVDIQQSRNKTTERPGLLNCPIYWQQLREKCLLFSHTVNPWNNSLADCSTKESSLLLIRDKDELIHTQNLIRDKAILFWIGLNFSLSEKNWKWINGSFLNSNDLEIRGDAKENSCISISQTSVYSEYCSTEIRWICQKELTPVRNKVYPDS
Protein: RING finger protein 37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RNF37) (U-box domain-containing protein 5) (UbcM4-interacting protein 5) (hUIP5) (Ubiquitin-conjugating enzyme 7-interacting protein 5) (O94941)
Organism: Homo sapiens (Human)
Function: May have a ubiquitin-protein ligase activity acting as an E3 ubiquitin-protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates.
Subcellular location: Nucleus {ECO:0000269|PubMed:11274149, ECO:0000269|PubMed:11435423}. Note=Enriched in nuclear bodies. {ECO:0000269|PubMed:11274149}.
Interaction partners:
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Transitional endoplasmic reticulum ATPase
- Ubiquitin thioesterase OTU1
- Sorting nexin-15
Sequence:
MVINLCLPQFRPRIHCNKISADGYEVENLISEDLTKRSHGFRTEYFIKPPVYVTVSFPFNVEICRINIDLTAGGGQNVTGLEMYTSASSSRVSWNTPQCRTLGPAEPSVPDKEAFTLVGKVLLKNQSQVVFSHRGFKARPPFGAMEATLPSPAVVAQELWNKGALSLSHVAHLRICITHVTGGGIPCIKRLEVWGQPAKTCSQEVIDSILLVTSENLPQDVALQAPALPMESDCDPGDQPESQQAPSSLQKLAEIIQDVPEEFLDPITLEIMPCPMLLPSGKVIDQSTLEKCNRSEATWGRVPSDPFTGVAFTPHSQPLPHPSLKARIDHFLLQHSIPGCHLLGRAQTALAVIPSSIVLPSQKRKIEQAEHVPDSNFGVNASCFSATSPLVLPTTSEHTAKKMKATNEPSLTHMDCSTGPLSHEQKLSQSLEIALASTLGSMPSFTARLTRGQLQHLGTRGSNTSWRPGTGSEQPGSILGPECASCKRVFSPYFKKEPVYQLPCGHLLCRPCLGEKQRSLPMTCTACQRPVASQDVLRVHF
Protein: Hephaestus, isoform C (Hephaestus, isoform S) (Hephaestus, isoform T) (Hephaestus, isoform U) (Polypyrimidine tract binding protein) (Q8IMF8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRGSDELLSQAAVMAPASDNNNQDLATKKAKLEPGTVLAGGIAKASKVIHLRNIPNESGEADVIALGIPFGRVTNVLVLKGKNQAFIEMADEISATSMVSCYTVTPPQMRGRMVYVQFSNHRELKTDQGHNNSTAHSDYSVQSPASGSPLPLSAAANATSNNANSSSDSNSAMGILQNTSAVNAGGNTNAAGGPNTVLRVIVESLMYPVSLDILHQIFQRYGKVLKIVTFTKNNSFQALIQYPDANSAQHAKSLLDGQNIYNGCCTLRIDNSKLTALNVKYNNDKSRDFTNPALPPGEPGVDIMPTAGGLMNTNDLLLIAARQRPSLSGDKIVNGLGAPGVLPPFALGLGTPLTGGYNNALPNLAAFSLANSGALQTTAPAMRGYSNVLLVSNLNEEMVTPDALFTLFGVYGDVQRVKILYNKKDSALIQMAEPQQAYLAMSHLDKLRLWGKPIRVMASKHQAVQLPKEGQPDAGLTRDYSQNPLHRFKKPGSKNYQNIYPPSATLHLSNIPSSCSEDDIKEAFTSNSFEVKAFKFFPKDRKMALLQLLSVEEAVLALIKMHNHQLSESNHLRVSFSKSNI