wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-1 beta (IL-1 beta) (P10749)
Organism: Mus musculus (Mouse)
Function: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17284521}. Secreted {ECO:0000269|PubMed:17284521, ECO:0000269|PubMed:17641058}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000269|PubMed:17641058}. 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:0000250|UniProtKB:P01584}.
Interaction partners:
- Caspase-1
- Interleukin-1 receptor type 1
- Interleukin-1 alpha
- Interleukin-1 receptor accessory protein
- Interleukin-1 receptor type 2
- Interleukin-2
- Granulocyte-macrophage colony-stimulating factor
- NACHT, LRR and PYD domains-containing protein 3
- Interleukin-5
- Interferon gamma
Sequence:
MATVPELNCEMPPFDSDENDLFFEVDGPQKMKGCFQTFDLGCPDESIQLQISQQHINKSFRQAVSLIVAVEKLWQLPVSFPWTFQDEDMSTFFSFIFEEEPILCDSWDDDDNLLVCDVPIRQLHYRLRDEQQKSLVLSDPYELKALHLNGQNINQQVIFSMSFVQGEPSNDKIPVALGLKGKNLYLSCVMKDGTPTLQLESVDPKQYPKKKMEKRFVFNKIEVKSKVEFESAEFPNWYISTSQAEHKPVFLGNNSGQDIIDFTMESVSS
Protein: Transcriptional regulatory protein DesR (O34723)
Organism: Bacillus subtilis (strain 168)
Function: Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase DesK
- Sensor histidine kinase YvfT
- Fatty acid desaturase
- Sensor histidine kinase LnrJ
- Sensor histidine kinase LiaS
- Signal transduction histidine-protein kinase/phosphatase DegS
- Sensor histidine kinase YhcY
- Putative transport permease YvfS
- Sensor histidine kinase YxjM
- Sensor histidine kinase YdfH
Sequence:
MISIFIAEDQQMLLGALGSLLNLEDDMEVVGKGTTGQDAVDFVKKRQPDVCIMDIEMPGKTGLEAAEELKDTGCKIIILTTFARPGYFQRAIKAGVKGYLLKDSPSEELANAIRSVMNGKRIYAPELMEDLYSEANPLTDREKEVLELVADGKNTKEIAQELSIKSGTVRNYISMILEKLEVKNRIEAITRSKEKGWFK
Protein: Zinc transporter SLC39A7 (Solute carrier family 39 member 7) (Zrt-, Irt-like protein 7) (A0A024RCX7)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004257}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004257}.
Interaction partners:
Sequence:
MARGLGAPHWVAVGLLTWATLGLLVAGLGGHDDLHDDLQEDFHGHSHRHSHEDFHHGHSHAHGHGHTHESIWHGHTHDHDHGHSHEDLHHGHSHGYSHESLYHRGHGHDHEHSHGGYGESGAPGIKQDLDAVTLWAYALGATVLISAAPFFVLFLIPVESNSPRHRSLLQILLSFASGGLLGDAFLHLIPHALEPHSHHTLEQPGHGHSHSGQGPILSVGLWVLSGIVAFLVVEKFVRHVKGGHGHSHGHGHAHSHTRGSHGHGRQERSTKEKQSSEEEEKETRGVQKRRGGSTVPKDGPVRPQNAEEEKRGLDLRVSGYLNLAADLAHNFTDGLAIGASFRGGRGLGILTTMTVLLHEVPHEVGDFAILVQSGCSKKQAMRLQLLTAVGALAGTACALLTEGGAVGSEIAGGAGPGWVLPFTAGGFIYVATVSVLPELLREASPLQSLLEVLGLLGGVIMMVLIAHLE
Protein: Protein UL40 (P16780)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Plays a role in the protection against host NK-cell cytotoxicity by up-regulating the cell surface expression of HLA-E independent of TAP (HLA-E has an inhibitory effect on the cytotoxic activity of the NK cell). Promotes also cell surface expression of UL18, another viral protein involved in NK-cell evasion.
Interaction partners:
Sequence:
MNKFSNTRIGFTCAVMAPRTLILTVGLLCMRIRSLLCSPAETTVTTAAVTSAHGPLCPLVFQGWAYAVYHQGDMALMTLDVYCCRQTSNNTVVAFSHHPADNTLLIEVGNNTRRHVDGISCQDHFRAQHQDCPAQTVHVRGVNESAFGLTHLQSCCLNEHSQLSERVAYHLKLRPATFGLETWAMYTVGILALGSFSSFYSQIARSLGVLPNDHHYALKKA
Protein: Decaprenyl-diphosphate synthase subunit 1 (EC 2.5.1.91) (All-trans-decaprenyl-diphosphate synthase subunit 1) (Decaprenyl pyrophosphate synthase subunit 1) (O43091)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24911838}.
Interaction partners:
- Farnesyl pyrophosphate synthase
- Squalene synthase
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Geranylgeranyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c-farnesyl diphosphate specific))
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Diphosphomevalonate decarboxylase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- Probable 26S proteasome regulatory subunit rpn3
Sequence:
MIQYVYLKHMRKLWSLGKVRSTVLRFSTTNRNASHLIKNELEQISPGIRQMLNSNSEFLEECSKYYTIAQGKQMRPSLVLLMSKATSLCHGIDRSVVGDKYIDDDDLRSFSTGQILPSQLRLAQITEMIHIASLLHDDVIDHANVRRGSPSSNVAFGNRRSILAGNFILARASTAMARLRNPQVTELLATVIADLVRGEFLQLKNTMDPSSLEIKQSNFDYYIEKSFLKTASLISKSCKASTILGQCSPTVATAAGEYGRCIGTAFQLMDDVLDYTSKDDTLGKAAGADLKLGLATAPVLFAWKKYPELGAMIVNRFNHPSDIQRARSLVECTDAIEQTITWAKEYIKKAKDSLLCLPDSPARKALFALADKVITRKK
Protein: Pyridoxal 5'-phosphate synthase PDX1-like 4 (O80446)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- RNA polymerase II degradation factor-like protein
- RNA polymerase II degradation factor-like protein
- Pentatricopeptide repeat-containing protein At4g33170
Sequence:
MAGTGVVAVYGEGAMTETKQKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARFC
Protein: LIM-domain containing phosphatase (LIM-type zinc finger-containing protein) (Q54MG8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}.
Interaction partners:
- Phosphatidylinositol 3-kinase 2
- Phosphatidylinositol 3-kinase 1
- Phosphatidylinositol 3-kinase VPS34-like
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- phosphoinositide 5-phosphatase
- Phosphatase and tensin homolog
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- PIPK domain-containing protein
- 1-phosphatidylinositol-5-phosphate 4-kinase
- Inositol 5-phosphatase 4
Sequence:
MDLVRKMVSKKKRRFEMYNFDLDLSYITDRVIAMGFPSESLEGLYRNRMRDVQRFFNTLHADHYKVYNLCSERKYEHCRFEDRVSEYPFDDHCPPTLNIISEFCNDMEMWLDQNPENVVAVHCKAGKGRTGTMLACWLLYNKQCQTGSESMRLFANKRTHNSKGVTIPSQIRYVRYFEALLQYGKPIPKPPSITKVLSMIKMNSLPNFNIGGGCEPYLSIVQQGKSVFYSKPVKLKKGTIHQQVELDCGNILLVNDVQIQFFNRNSKGHMFSYCFHTAFIEGTKIHIRRQEIDKAHKDLKHFHSNFSIELIFLEDDRDDDSSSVSEESVEEKRVFNTSYATGLAKLYHNSNSNNKSLTSSTSSTSNLSSSTNNTFEIISNNNNNNNNNNNNNNINSNNNKINDENSNKNNNNNNIINNNSFSAWGNNSKIVKNRGSKLAFICPKCNLPITATDPSINRNSENYHWKCVVCVKCSKPLGGESDCVFENNEMLCTDCGTEFFKSCSGCNLVIKTSDFEELGDHIYHRSCFLCYYCTSYLGGKDFIVENINNIRRFKCSSCIDNKNRQNGDDDDNNNNDNIENILENKIPEICDKLDKEIIKLVIEIDKSTEPSPVSSIDPSMIFNDLEDNGKRRQMTVESMICSKCELAINQSRPIILDCGIYHRECFQCSECFDETPMDPSLYYIRNDKPVCFDCDVNHIMNEAHSEITCYGCKLPIVDEVMMDALNFKWHVACLVCSKCAIQIEGQLGDHQGLIYCKDHFEELVGTKCDQCNQYIDGMFLKVNGKNLCPTCFRCFCCNEVLEGGKYFEKNGESICEKCRNEDILKRKTQIHIQHTLITSLKNSQQISEKSSSSLSTSSTTTTTTTNNVVSSTSSTSTSPSTSPSNSPLSSSIQKDAPLFCLNKSRSLFRNSIKIHLEDLKNSGERKTLLYPSFHRQMRKQTFKTAYPSLRGTRRKDFLNHSKNELDSSNNSLSTLVNAFVPPQQSNNSNTTTTTNTST
Protein: DNA repair and recombination protein RDH54 (EC 3.6.4.12) (RAD homolog 54) (Recombination factor TID1) (Two hybrid interaction with DMC1 protein 1) (P38086)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the recombinational repair of double-strand breaks (DSB) in DNA during mitosis and meiosis. Has DNA dependent ATPase activity. Promotes D-loop (displacement loop) formation with RAD51 recombinase. Modifies the topology of double-stranded DNA during the D-loop reaction to facilitate the invasion of the homologous duplex molecule by the initiating single-stranded DNA substrate. Required for adaptation from G2/M checkpoint arrest induced by a double strand break, by participating in monitoring the extent of single-stranded DNA produced by resection of DNA ends. This role is distinct from its roles in recombination. Promotes colocalization of RAD51 and DMC1 during meiotic recombination. Involved in crossover interference.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA repair protein RAD51
- DNA repair and recombination protein RAD54
- DNA repair protein RAD55
- DNA repair and recombination protein RAD52
- DNA repair protein RAD57
- Meiotic recombination protein DMC1
- DNA repair protein RAD59
- ATP-dependent DNA helicase SRS2
- ATP-dependent helicase SGS1
- Serine/threonine-protein kinase MEC1
Sequence:
MAVISVKPRRREKILQEVKNSSVYQTVFDSGTTQMQIPKYENKPFKPPRRVGSNKYTQLKPTATAVTTAPISKAKVTVNLKRSISAGPTLNLAKKPNNLSSNENTRYFTIMYRKPTTKKHKTWSGDGYATLKASSDKLCFYNEAGKFLGSSMLPSDSDSLFETLFKAGSNEVQLDYELKENAEIRSAKEALSQNMGNPSPPTTSTTETVPSTKNDGGKYQMPLSQLFSLNTVKRFKSVTKQTNEHMTTVPKTSQNSKAKKYYPVFDVNKIDNPIVMNKNAAAEVDVIVDPLLGKFLRPHQREGVKFMYDCLMGLARPTIENPDIDCTTKSLVLENDSDISGCLLADDMGLGKTLMSITLIWTLIRQTPFASKVSCSQSGIPLTGLCKKILVVCPVTLIGNWKREFGKWLNLSRIGVLTLSSRNSPDMDKMAVRNFLKVQRTYQVLIIGYEKLLSVSEELEKNKHLIDMLVCDEGHRLKNGASKILNTLKSLDIRRKLLLTGTPIQNDLNEFFTIIDFINPGILGSFASFKRRFIIPITRARDTANRYNEELLEKGEERSKEMIEITKRFILRRTNAILEKYLPPKTDIILFCKPYSQQILAFKDILQGARLDFGQLTFSSSLGLITLLKKVCNSPGLVGSDPYYKSHIKDTQSQDSYSRSLNSGKLKVLMTLLEGIRKGTKEKVVVVSNYTQTLDIIENLMNMAGMSHCRLDGSIPAKQRDSIVTSFNRNPAIFGFLLSAKSGGVGLNLVGASRLILFDNDWNPSVDLQAMSRIHRDGQKKPCFIYRLVTTGCIDEKILQRQLMKNSLSQKFLGDSEMRNKESSNDDLFNKEDLKDLFSVHTDTKSNTHDLICSCDGLGEEIEYPETNQQQNTVELRKRSTTTWTSALDLQKKMNEAATNDDAKKSQYIRQCLVHYKHIDPARQDELFDEVITDSFTELKDSITFAFVKPGEICLREQ
Protein: ParB/Sulfiredoxin domain-containing protein (O93707)
Organism: Sulfolobus sp. NOB8H2
Interaction partners:
Sequence:
MSKLKEYKEISIEEIKEVEEFKNFVPENNMYDKIKEDIAKNGIKVPLIVNQNYELINGYTRLKIARELGIKEVPVAIYETEGRADEYDLLVSTNLTQRQLNRAQALALIEKAVEEKMKMSKKNQNNDNNTKVLKVESGETQLSATESKKIEKSESKERKVESPGDSTFSNNEKKIENITEIKNAIKEELKKHNIKIDDNTLNKYIRIKQNSHWLTDYILKGKIGITTAYELYTKLQEMGLLEAVAKLPPYERNALLTDGRKIILNGRKDLLEEIVNHRMAVSQAISKLKTDEKLEKLQRSKKKPRAKEENLEDEEEEEIESEGEQREDNVSDNDEEYDFVGEWQKAQEEEEKEKQLTRLDDEAPPTKLEIYTPKADLESLYRAMPSIKKLVDEGKLTEKDAEKVYEIWRNMEAIYKQASLLWYNTVDLLLKRIGLSEKEREEIFYEMVRPYFRLFSREEVFPKEVLEGKL
Protein: Casein kinase II subunit beta (CK II beta) (P43639)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of casein kinase II/CK2 (By similarity). As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity).
Interaction partners:
- rRNA biogenesis protein RRP36
- U3 small nucleolar ribonucleoprotein protein IMP4
- Nucleolar protein 19
- Casein kinase II subunit alpha'
- Casein kinase II subunit beta'
- U3 small nucleolar RNA-associated protein 21
- U3 small nucleolar ribonucleoprotein protein IMP3
- Ribosome biogenesis protein SLX9
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar RNA-associated protein 6
Sequence:
MSQEFVEDYSRTGSSDDEDSGAYDEWIPSFCSRFGHEYFCQVPTEFIEDDFNMTSLSQEVPHYRKALDLILDLEAMSDEEEDEDDVVEEDEVDQEMQSNDGHDEGKRRNKSPVVNKSIIEHAAEQLYGLIHARFILTKPGLQAMAEKFDHKEFGTCPRYYCNGMQLLPCGLSDTVGKHTVRLYCPSCQDLYLPQSSRFLCLEGAFWGTSFPGVFLKHFKELEEYVERKSKESYELKVFGFRINDEAVSGPRMKWLRQYPSTEEDWEEFAKCEFETPAV
Protein: CLAVATA3/ESR (CLE)-related protein 45 [Cleaved into: CLE45p] (Q6IWA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Represses protophloem differentiation in a BAM3-dependent manner. BRX, BAM3, and CLE45 act together to regulate the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 and involves MAKR5 for its transduction/amplification. Triggers the accumulation of MAKR5 in developing sieve elements in a BAM3-dependent manner. Prevents, in a dose-dependent manner, auxin response in the root meristem thus leading in the repression of protophloem differentiation and periclinal sieve element precursor cell division. Promotes pollen tube growth prolongation in a SKM1 and SKM2-dependent manner, especially under relatively high temperature (at 30 degrees Celsius), thus conferring tolerance against high temperature probably through the maintenance of mitochondrial activity. Alleviates mitochondrial decay pollen tube in vitro culture.
Subcellular location: [CLE45p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- Protein CLAVATA 3
- CLAVATA3/ESR
- Membrane-associated kinase regulator 5
- Leucine-rich repeat receptor-like serine/threonine-protein kinase RGI4
- Protein BREVIS RADIX
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- Type IV inositol polyphosphate 5-phosphatase 6
- CLAVATA3/ESR
Sequence:
MLGSSTRSMFFLLVCIGLLADNRYNVSAMRHREFFLKETQAEKAGVQTEEISKLRSIGVQFKHTLEDQEMLNKNRRVLEEVNKDKIKAEETQERKNKTEDSFKSSKRRVRRGSDPIHNKAQPFS
Protein: RT03118p (TweedleJ) (Q9VBD6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform O
- Cuticular protein 67Fa1
Sequence:
MRQFSVVLCLCLAVLARADKLGYNYQPVAHSPSGLSFQPSGSASSDAPAFAPAPSESFGPGPSSIADALEGSQSAAAPNYAAPQAQLEKEFFTYTADEGDFYDPAASDRVANAVNKGLRVVFIKGPENRGLEDAALALAKQAAQQETAIYVLNKQADIGDLANKLNSIRNNNNNKPEVHFVKYRTPEDAANAQSAIQGQYDQLGGSSQAQDGGVASTLNFASQPAPVQAASSQAPAQFLPASQPEATAPISSYVPPATPGSSYLPANILRRLRF
Protein: Neutral cholesterol ester hydrolase 1 (NCEH) (EC 3.1.1.-) (Acetylalkylglycerol acetylhydrolase) (2-acetyl MAGE hydrolase) (EC 3.1.1.71) (Arylacetamide deacetylase-like 1) (Chlorpyrifos oxon-binding protein) (CPO-BP) (Q8BLF1)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q6PIU2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6PIU2}. Microsome {ECO:0000269|PubMed:18782767}.
Interaction partners:
- Monoglyceride lipase
- Sterol O-acyltransferase 1
Sequence:
MRSSCVLLAALLALAAYYVYIPLPSAVSDPWKLMLLDATFRGAQQVSNLIHSLGLNHHLIALNFIITSFGKQSARSSPKVKVTDTDFDGVEVRVFEGSPKPEEPLRRSVIYIHGGGWALASAKISYYDQLCTTMAEELNAVIVSIEYRLVPQVYFPEQIHDVIRATKYFLQPEVLDKYKVDPGRVGISGDSAGGNLAAALGQQFTYVASLKNKLKLQALVYPVLQALDFNTPSYQQSMNTPILPRHVMVRYWLDYFKGNYDFVEAMIVNNHTSLDVERAAALRARLDWTSLLPSSIKKNYKPIMQTTGNARIVQEIPQLLDAAASPLIAEQEVLEALPKTYILTCEHDVLRDDGIMYAKRLESAGVNVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRNSYIKWLDQNL
Protein: glutathione transferase (EC 2.5.1.18) (B3KNR3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
Protein: Hydrogenobyrinate a,c-diamide synthase (EC 6.3.5.9) (Hydrogenobyrinic acid a,c-diamide synthase) (P9WP97)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Interaction partners:
- Probable cob
- Precorrin-8X methylmutase
- Uncharacterized protein Rv2850c
- Cobalamin biosynthesis protein CobN
- UPF0039 protein Rv2851c
- Cobyric acid synthase
- Adenosylcobinamide-GDP ribazoletransferase
- Histidinol-phosphate aminotransferase Rv2231c
- Cobalamin biosynthesis protein CobIJ
- Precorrin-4 C
Sequence:
MRVSAVAVAAPASGSGKTTIATGLIGALRQAGHTVAPFKVGPDFIDPGYHALAAGRPGRNLDPVLVGERLIGPLYAHGVAGADIAVIEGVLGLFDGRIGPAGGAPAAGSTAHVAALLGAPVILVVDARGQSHSVAALLHGFSTFDTATRIAGVILNRVGSARHEQVLRQACDQAGVAVLGAIPRTAELELPTRYLGLVTAVEYGRRARLAVQAMTAVVARHVDLAAVIACAGSQAAHPPWDPVIAVGNTARQPATVAIAAGRAFTFGYAEHAEMLRAAGAEVVEFDPLSETLPEGTDAVVLPGGFPEQFTAELSANDTVRRQINELAAAGAPVHAECAGLLYLVSELDGHPMCGVVAGSARFTQHLKLGYRDAVAVVDSALYSVGERVVGHEFHRTAVTFADSYQPAWVYQGQDVDDVRDGAVHSGVHASYLHTHPAATPGAVARFVAHAACNTPRA
Protein: MIP14426p (TBP-associated factor 30kD subunit alpha-2) (Q9VR21)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP01149p
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 13
Sequence:
MDSNMEPWSFALNFDDSDKSSDNESHSSTRSSSRSSDTSIDTSSVEKEPASVIESQSVPGGSYDIISKTNMLQFVQKIDANSSLDDQGCDMMARIADAFVNDISMRIVKLAKYRKSDVSVLDLKFILKREFNMEFPIE
Protein: NADP-dependent 3-hydroxy acid dehydrogenase (L-allo-threonine dehydrogenase) (EC 1.1.1.381) (Q9P7B4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000250|UniProtKB:Q05016}.
Interaction partners:
- Probable low-specificity L-threonine aldolase
- L-2-aminoadipate reductase
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Uncharacterized mitochondrial carrier C17H9.08
Sequence:
MSRLDGKTILITGASSGIGKSTAFEIAKVAKVKLILAARRFSTVEEIAKELESKYEVSVLPLKLDVSDLKSIPGVIESLPKEFADIDVLINNAGLALGTDKVIDLNIDDAVTMITTNVLGMMAMTRAVLPIFYSKNKGDILNVGSIAGRESYVGGSVYCSTKSALAQFTSALRKETIDTRIRIMEVDPGLVETEFSVVRFHGDKQKADNVYKNSEPLTPEDIAEVILFALTRRENVVIADTLVFPSHQGGANHVYRKQA
Protein: Acid-sensing ion channel 3 (ASIC3) (Amiloride-sensitive cation channel 3) (Dorsal root ASIC) (DRASIC) (Q6X1Y6)
Organism: Mus musculus (Mouse)
Function: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UHC3}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15051137}. Note=Preferentially expressed at the plasma membrane of the soma and cellular processes of neurons (By similarity). In part cytoplasmic in cochlea cells (PubMed:15051137). Localized in specialized sensory nerve endings (PubMed:11754838). {ECO:0000250|UniProtKB:O35240, ECO:0000269|PubMed:11754838, ECO:0000269|PubMed:15051137}.
Interaction partners:
- Stomatin
- Transient receptor potential cation channel subfamily V member 1
- Stomatin-like protein 3
- P2X purinoceptor
- Acid-sensing ion channel 1
- P2X purinoceptor 3
- Transient receptor potential cation channel subfamily A member 1
Sequence:
MKPPSGLEEAQRRQASDIRVFANSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAQGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHGQEEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASVDPDFDPEPSDPLGSPSSSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSETYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSSQRRSGNTLLQEELNGHRTHVPHLSLGPRPPTAPSAVTKTLAASHRTCYLVTRL
Protein: Protein kinase C (EC 2.7.11.13) (A0A1D5PUY5)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Serine/threonine-protein kinase TOR
- Protein kinase C delta type
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- sphingosine kinase
- Integrin beta-1
- Uncharacterized protein.
- Inositol 1,4,5-trisphosphate receptor
- Phosphoinositide phospholipase C.
Sequence:
MAEPPAAPGPEGEEGPVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIRADIEKDVLTVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIKCSLNPEWNETFRFQLKEADKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKSGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGTGSKAADEKTTNAISKFDNNGSRDRMKLSDFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYQIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPAKRLGCGPEGERDIKEHAFFRYIDWDKLERKEIQPPFKPKACGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFFNSEFFKPEAKS