wanglab/gogpt-training-data huggingface dataset:
Protein: Cadherin-like protein 26 (Cadherin-like protein VR20) (Q8IXH8)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Ligand for integrins alpha-E/beta-7, ITGAE:ITGAB7, alpha-4/beta-7, ITGA4:ITGAB7 and alpha-4/beta-1, ITGA4:ITGAB1 through which modulates CD4(+) T cells activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28051089}; Single-pass type I membrane protein {ECO:0000305|PubMed:28051089}.
Interaction partners:
Sequence:
MAMRSGRHPSLLLLLVLLLWLLQVSIIDSVQQETDDLTKQTKEKIYQPLRRSKRRWVITTLELEEEDPGPFPKLIGELFNNMSYNMSLMYLISGPGVDEYPEIGLFSLEDHENGRIYVHRPVDREMTPSFTVYFDVVERSTGKIVDTSLIFNIRISDVNDHAPQFPEKEFNITVQENQSAGQPIFQMLAVDLDEENTPNSQVLYFLISQTPLLKESGFRVDRLSGEIRLSGCLDYETAPQFTLLIRARDCGEPSLSSTTTVHVDVQEGNNHRPAFTQENYKVQIPEGRASQGVLRLLVQDRDSPFTSAWRAKFNILHGNEEGHFDISTDPETNEGILNVIKPLDYETRPAQSLIIVVENEERLVFCERGKLQPPRKAAASATVSVQVTDANDPPAFHPQSFIVNKEEGARPGTLLGTFNAMDPDSQIRYELVHDPANWVSVDKNSGVVITVEPIDRESPHVNNSFYVIIIHAVDDGFPPQTATGTLMLFLSDINDNVPTLRPRSRYMEVCESAVHEPLHIEAEDPDLEPFSDPFTFELDNTWGNAEDTWKLGRNWGQSVELLTLRSLPRGNYLVPLFIGDKQGLSQKQTVHVRICPCASGLTCVELADAEVGLHVGALFPVCAAFVALAVALLFLLRCYFVLEPKRHGCSVSNDEGHQTLVMYNAESKGTSAQTWSDVEGQRPALLICTAAAGPTQGVKDLEEVPPSAASQSAQARCALGSWGYGKPFEPRSVKNIHSTPAYPDATMHRQLLAPVEGRMAETLNQKLHVANVLEDDPGYLPHVYSEEGECGGAPSLSSLASLEQELQPDLLDSLGSKATPFEEIYSESGVPS
Protein: UPF0039 protein C11D3.02c (Q10081)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- UPF0654 protein C11D3.01c
- Uncharacterized transporter C794.04c
- SDO1-like protein C21C3.19
Sequence:
MSNLEFVYKYFNSLDVKELYDIYLLRTNVFVVEQKCAYPEVDEIDLKCGHLMLRNANGKLVAYARLIPEQQQTVRIGRVVVDPDERKNGYGRKLMLQALETSKQEFSSSKTFVLSSQEYAQPLYRSVGFKKCSDAYLEDGIPHVEMRLEL
Protein: Integrin subunit alpha V (H7BZG1)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
XNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVSHWFRQIE
Protein: Pancreatic secretory granule membrane major glycoprotein GP2 (Pancreatic zymogen granule membrane protein GP-2) (ZAP75) (P25291)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Functions as an intestinal M-cell transcytotic receptor specific of type-I-piliated bacteria that participates in the mucosal immune response toward these bacteria. At the apical membrane of M-cells it binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to elicit a mucosal immune response.
Subcellular location: Zymogen granule membrane {ECO:0000269|PubMed:2011597}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2011597}. Secreted {ECO:0000269|PubMed:2011597}. Cell membrane {ECO:0000269|PubMed:2011597}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2011597}. Apical cell membrane {ECO:0000305|PubMed:2011597}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2011597}. Membrane raft {ECO:0000250|UniProtKB:P19218}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2011597}. Endosome {ECO:0000250|UniProtKB:Q9D733}. Note=Secreted, after cleavage, in the pancreatic juice. {ECO:0000269|PubMed:2011597}.
Interaction partners:
- NPC intracellular cholesterol transporter 1.
- Peptidase S1 domain-containing protein
- Repressor of RNA polymerase III transcription MAF1
- Pancreatic polypeptide prohormone
- Glycoprotein VI platelet.
- CUB and zona pellucida like domains 1.
Sequence:
MVGSYVLWLALASCILTLASPEQQGNRNLINTRSYDPCQNYTLLDEPSRSTENTEGSQVCDKDKHGWYRFVGDGGVRMPETCVPMYRCQTDAPLWLNGTHPTLAEGIVNRTACAHWSGNCCLWKTVVQVKACPGEFHVYRLEGTPKCSLRYCTDASTATDKCKNLCRPEEACSFLNGTWDCFCRSDLNSSDVHSLQPRLNCGAKEIQVSLDKCQLGGLGFGDEVIAYLRDWNCSNMMQREERNWISVTSPTQARACGNILERNGTHAIYKNTLSLANEFIIRDTILNINFQCAYPLDMKVSLQTALHPIVSSLNISVDGEGEFTVRMALFQDQSYISPYEGAAAVLAVESMLYVGAILEKGDTSRFNLLLRNCYATPTKDKTDPVKYFIIRNSCPNQYDSTIHVEENGVSSESRFSVQMFMFAGNYDLVFLHCEIHLCDSLNEQCQPCCSRSQQRSEIVALNPARVLDLGPITRRSSASVDITDGTPSTAGFLLAWPMLLLPILLAELF
Protein: Homeobox protein ARX (Aristaless-related homeobox) (A6YP92)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor. Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C. Positively modulates transcription of KDM5C. Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcription regulator ZNF711; synergy may be related to enrichment of histone H3K4me3 in regulatory elements. Required for normal brain development (By similarity). Plays a role in neuronal proliferation, interneuronal migration and differentiation in the embryonic forebrain. May also be involved in axonal guidance in the floor plate (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35137, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
Interaction partners:
Sequence:
MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRTDQEKAMQGSPKGSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELGGPGGVAHPEERLSAASGPGSAPAAGGGTGTEEDEEELLEDEEDEDEEEELLEDDEEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAGSDSEEGLLKRKQRRYRTTFTSYQLEELERAFQKTHYPDVFTREELAMRLDLTEARVQVWFQNRRAKWRKREKAGAQTHPPGLPFPGPLSATHPLSPYLDASPFPPHHPALDSAWTAAAAAAAAAFPSLPPPPGSASLPPSGAPLGLSTFLGAAVFRHPAFISPAFGRLFSTMAPLTSASTAAALLRQPTPAVEGAVASGALADPATAAADRRASSIAALRLKAKEHAAQLTQLNILPGTSTGKEVC
Protein: Signal peptidase complex subunit 3A (Microsomal signal peptidase 22 kDa subunit) (SPC22) (SPase 22 kDa subunit) (Q9MA96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P61008}.
Interaction partners:
- Cyanate hydratase
- Signal peptidase complex subunit 1
- signal peptidase I
- Signal peptidase complex catalytic subunit SEC11
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3B
- At4g03180
- Sec-independent protein translocase protein TATB, chloroplastic
Sequence:
MHTFGYRANALLTFAVTALAFICAIASFSDKFSNQNPSAEIQILNINRFKKQSHGNDEVSLTLDISADLQSLFTWNTKQVFVFVAAEYETPKNSLNQVSLWDAIIPAKEHAKFRIQVSNKYRFIDQGQNLRGKDFNLTLHWHVMPKTGKMFADKIVLPGYSLPDAYR
Protein: Potassium voltage-gated channel subfamily A member 4 (HPCN2) (Voltage-gated K(+) channel HuKII) (Voltage-gated potassium channel HBK4) (Voltage-gated potassium channel HK1) (Voltage-gated potassium channel subunit Kv1.4) (P22459)
Organism: Homo sapiens (Human)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure. Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:8495559}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P15385}.
Interaction partners:
- Disks large homolog 4
- Voltage-gated potassium channel subunit beta-2
- Potassium voltage-gated channel subfamily A member 1
- Voltage-gated potassium channel subunit beta-1
- Potassium voltage-gated channel subfamily A member 2
- Voltage-gated potassium channel subunit beta-3
- Disks large homolog 1
- Disks large homolog 2
- Sigma non-opioid intracellular receptor 1
- A-type potassium channel modulatory protein KCNIP2
Sequence:
MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGSGGSGGGSHHHHQSRGACTSHDPQSSRGSRRRRRQRSEKKKAHYRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEDDHGDECSYTDLLPQDEGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLVMALSAGGHGGLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCAKEEKCQGKGDDSETDKNNCSNAKAVETDV
Protein: Methionine--tRNA ligase, cytoplasmic (EC 6.1.1.10) (Methionyl-tRNA synthetase) (A1ZBE9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tyrosine--tRNA ligase
- leucine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Probable glutamine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- AaRS-interacting multifunctional protein 3
- AaRS-interacting multifunctional protein 1
Sequence:
MIIYTNDGNPLGLQLLMLAKFAKQPVQVQLVNLNDAKYKDLLVLPTLELDNGLRLFSPAAIAKYLFVGKGQQRDEWLEWSATLLAPALAHHMAVGHKADANALPVLNALVKKLDDKLKATPYLAGDKPSAADIAIWSLLAPDGTLKGAQNVDNLRDWYGRVKALPEVQEVLAEQPLKDLSFNALQQSNRYGGLHHVPLKRLSLADASKLLVDTTPTVADTVTNEEISAAKAAFTYTAPKEIKEERTVLPKPGERNVLITSALPYVNNVPHLGNIIGCVLSADIYARYSRSAGYNTLLICGTDEYGTATENKALAENLTPREICDKYFELHNAIYRWFGIGFDYFGRTTTQEQTDIVQEAFKDVLKAGYIITESVEQLLCQKCDRFLADRFVEGTCPHPGCGYEDARGDQCDKCGKLVNATELIRPRCKVCNSAPVLRSSDQLFIDLPKAEPQLKEWVDKSEGGWTHNAKVITRAWLKEGLKPRCITRDLKWGIPVPHEGFEKKVFYVWFDAPFGYVSMTKRYTKEYQQWWQPAKGTDVELFQFMAKDNVPFHSVVWPSVLLAINKGHTLVSHIMATEYLNYEDGKFSKSRGIGVFGNDAQETGIPADVWRFYLASARPEGQDSSFSWNDLAARNNSELLNNLGNFVNRALVFCEKNFSSTVPGVITTQDELVLLALINRELRGYINSMEKAKLRDGVRHLLAISRHGNGYMQSQQPWVLLKGTDDQKTRASTIIGLCVNIACLLANLLFPYMPTTARTLFGQLNAKQTPLNAEKPLVTLLLPAGHQIGKPAPLFAKLEQSFIDELKGKYGGAQATNDAAHSQISAADLEKAVQAQADKVRELKASTKDKAIWQPEVTKLLDLKKQLEEAKKKTATAAAPAATPAPSNGSQSVQDLEKAIQEQGDKVRKLKGSTKDKTVWQPEVNILLDLKKQLEAVQKAAKAAPAANAAPAASPAATADAAKVKALEDKIAQQAEKVRTLKATGDAAVWKPEVDILLSLKNELAALTGTPVAGGQGKGKKKK
Protein: Protein kinase domain-containing protein (Q388T9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
Sequence:
MTDKEDASEFIIVDDDESKRREEDPTQENIQLSLTPQNASDHTVSPTNSHESVLALKRGDIVDGAARTGVSITTNLVFSATVANPIAAAAVAAYESFRAVSDYRRGALNVLGLPMDRTDLALRIGKEVGTAATGLAIGYAIGSLIGLGSIPVVGQVIATTVLSVALNFCVVTLLTRHVDRLILKIKLRRQYGYPRNEQGARRRFEELLEPQHCLLSFETCRIVQHYRDYRVACGWEGLTDISEYRASANIALMPISFQHFAIVQLQRKWGFVNERNECRKVYRALLLVHHPDRGGSGELTGVLNHDFEVYAFCQGWHEDCRRLCQENEEAIHTDGARRPRKRKKNAVVSFLQSLFRTGKNSSQEAQELCDSGLLALEAGTPLELSELEELSVDEPDESVADEEYAVSETKASTTQHSICVVLAAIQRCYQLTTEAVPFSWLKQLHRDCEGWSRLKVNVHMFIRMHVFVHIADEVAARDTATTVLPVERSCCDFRWCTKCEAVAKREDLRRTIVATCFPKHVTGKLIEAFELWKTAQSLAHSFFKQHTGATADVTVVAGTGQTLSALFDIQTAIQALCTGDSDSLEESDETEDERTLEFADEVRIIGLIAGFALSGAHAVDTHQRLRETCKEYYRARDSKMKSVASLRHATHDVGGRTSKSTAKKEKLKSSEQREGDTKESLLFHQVFTEVDAATCELYNIYSVHLPENIGFFKLLPSSCARCAHQKCEIRRYVKYERERTLVSYKHVVVEPRNVLEPHKPATYQGMVLKDGKEISEIEFALLCAEYVDPISGTVTPCWLKRYTFPKYENESSVQTTKVFKTLMERELRLQETCASCRVTSAIEVFGDEHTNQIYFHLPRGGTQVRFSSPQDILKRIKQHGVRWLHGALQAIIDIHSCQVTHGDICMSNFTHDDFGNTTLGFFSNSLKVHKYGTKTAQDDAADFGVTLHAEVLPYLRGTLPQTKSSPHRNASDDRASSGVVTGCGQAEQQIREMFNVFLEVADRLTGKLEPRWSLLDARGFVRRLIKVNYDCDERQYLFTKEVSYPPYWTAQKNMGPVSLFPDNRVLMHRSPQGTAVFLNRNIYLWETYWKYRQQLVLARGCSSFSVPVALREQPHFLPCSDDCEVNERFLWYNCKDEEEAWQICLEGTKEEKCRFAFVPPWMEAKKQTRNDDNPWATWAIVFRVALGAVVSDEDEMETCCVPSAGPDTGLFVVQRCAMVRGSGPAAGQWELSVPSPGTRSYPEYLVRWFHS
Protein: Phospholipid-transporting ATPase dnf2 (EC 7.6.2.1) (Q09891)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32660}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit ivn1
- Phospholipid-transporting ATPase accessory subunit mug89
- Phospholipid-transporting ATPase C4F10.16c
Sequence:
MESVEEKSKQRRWLPNFKALRLKVYRLADRLNIPLADAARVELEEYDGSDPQSLRGLQKLPRTLYFGLPLPDSELDDTGEAKRWFPRNKIRTAKYTPIDFIPKNIFLQFQNVANLFFLFLVILQSISIFGEQVNPGLAAVPLIVVVGITAVKDAIEDFRRTMLDIHLNNTPTLRLSHYQNPNIRTEYISYFRRFKKRISALFRVFLAKQEEKKRAKRLNDAVPLEDMAGSESRPSYDSIFRESFEAKRSFEDSKGKVPLSALDGTATILQSRPMDIIDYEAEATGECHFKKTYWKDVRVGDFVKVMDNDEIPADIVIINSSDPEGICYIETKNLDGETNLKMRHALTCGKNVVDEASCERCRFWIESEPPHANLYEYNGACKSFVHSEAGGSDTSQTVSEPISLDSMLLRGCVLRNTKWVIGVVVFTGDDTKIMLNSGAPPLKRSRITRNLNWNVYLNFIILFSMCFVCAVVEGIAWRGHSRSSYYFEFGSIGGSPAKDGVVTFFTGVILFQNLVPISLYISIEIVKTIQAIFIYFDKDMYYKKLKYACTPKSWNISDDLGQVEYIFSDKTGTLTQNVMEFKKCTINGVAYGEAFTEAMAGMAKREGKDTEELTLQKQSFIERDRMQMISQMRNMHDNKYLVDDNLTFISSQFVHDLAGKAGEEQSLACYEFFLALALCHSVVADRVGDRIVYKAQSPDEAALVGTARDVGFVFLDQRRDIMVTRALGETQRFKLMDTIEFSSARKRMSVIVKGPDNRYVLICKGADSIIFERLEPNEQVELRKTTSEHLRIFALEGLRTLCIAKRELTEEEYYEWKEKYDIAASAIENREEQIEEVADLIESHLTLLGGTAIEDRLQEGVPDSIALLAQAGIKLWVLTGDKMETAINIGFSCNLLDAGMDMIKFDVDQEVSTPELEVILADYLYRYFGLSGSVEELEAAKKDHDTPSGSHALVIDGSVLKRVLDGPMRTKFLLLCKRCKAVLCCRVSPAQKADVVQLVRESLEVMTLAIGDGANDVAMIQKADIGVGIVGEEGRAAAMSADYAIGQFRFLSKLVLVHGRWDYNRVAEMVNNFFYKSVVWTFTLFWYQIYNNFDANYLFDYTYVMLFNLIFSSLPVIVMGVYDQDVNADLSLRIPQLYKRGILQLNSARKIFIGYMLDGFYQSVICFFFSFLVINNVTTAAQNGRDTMAVQDLGVYVAAPTIMVVDTYVILNQSNWDVFSIGLWALSCLTFWFWTGVYSQSLYTYEFYKSASRIFRTPNFWAVLCGTIVSCLFPKFLFMTTQKLFWPYDVDIIRESYRTKRLHELDEEEEIENAEQSPDWASSTLQVPFNASSSSLATPKKEPLRLDTNSLTLTSSMPRSFTPSYTPSFLEGSPVFSDEILNRGEYMPHRGSISSSEQPLRP
Protein: Ecdysone oxidase (EC 1.1.3.16) (Q9VY01)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the inactivation of ecdysteroid molting hormones by converting ecdysteroids into 3-dehydroecdysteroids.
Interaction partners:
- Ecdysone 20-monooxygenase
- Cytochrome P450 315a1, mitochondrial
- FI08446p
Sequence:
MGDQRVHKPRTAKTRTLRVNRILLPMLLLFSGETTSVVTQLFSVDSSGLGISLMQSVAIALNASSLALANNTAWPLQHEPPEDRLEIESYDYIVVGAGSAGSIVASRLSELCQVKVLLLEEGQLPPLESEIFGLTGALHHDERYMFLEEAVPNPKCCQAMASMHGCVWWHGRMMGGGGAINGNIFIPGSRENFRRWNSTGWDWTQVHKTYSRLQQRLNPSYLQPNKLNLKLANLIYSGSAELGVPRMKQPLIAGATFGYTHHVPVTVNQRRRASSARLYLANDQVNRRGNLKVIRGAQVQRVLLNAAGSRATGVIYTLNGVEHTAKTLGEVILSAGTLNSAKLLLLSGIGPREELQRWNITTHQDLPVGRNLQDHGMMPLFLLFGSNCAVNSTRDPTENPYAPVSITQYLLDNQKGPLASGFYMMGYINSSSPSSSRGEPDLHVVAHTLLPKGSTGSFGYLGFRPELIQAQQDILQKGDLLQIMGSLLRPLSHGKVSLSSKNSADQAKIENHYGEAVEDQQTLLRYVRYIQKLSKTRPFRRCGLRLWKPPLHECDTLAADSDDYWLCYIRYFYVGAWHSVGTCRMAPRKGVDSQENGGVVDERLRVHGVKGLRVVDASIMPELPAGNTNGPAMMIGEKGAQMILDDREANNEVIQEC
Protein: Probable tubulin--tyrosine ligase C12B10.04 (EC 6.3.2.25) (Q10438)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable tubulin--tyrosine ligase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- mRNA-decapping enzyme subunit 1
- mRNA decapping complex subunit 2
- LSM complex subunit lsm4
- Tubulin beta chain
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- ADP-ribosylation factor-like protein alp41
- Tubulin alpha-1 chain
Sequence:
MSSTKKDIKVYVNYRDEYAEPKIISALKNSGKELTFTNSAKEANFQWAQYEDIDFDEVYKNPKTKLCCSYVIRKALIRKEYLWRTVITYLAKHPDSILSKSVPEAYSLELDYAEFLDDSLMEAYELRQELEENATKNISEKQWYILKPSMCDRAQGIRLFSTIEELQAIFDSFDDEESESEEAGLEEKGDITVAFNNKIVISQIRNFLVQKYISKPLLLDHRKFHIRAYVLATGALSVYLFNEMLCLLARDKYKKPTPDPDLLFSHLSNTCLQGDNVEQSSIRDFWNTSIENKDDIFKSILNIIGDVFEAAATTQGIHFQPLENCFEIFGVDFLVDCESQVYLLEVNSYPDFKQTGKNLSNIIENLFSAVVETAIIPFFESSTKRNVDSKLTLAKKLQLFGFR
Protein: Peroxisomal ATPase PEX6 (EC 3.6.4.-) (Peroxin-6) (Peroxisomal biogenesis factor 6) (Peroxisome assembly factor 2) (PAF-2) (P54777)
Organism: Rattus norvegicus (Rat)
Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13608}. Peroxisome membrane {ECO:0000250|UniProtKB:Q13608}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q13608}. Note=Associated with peroxisomal membranes; anchored by PEX26 to peroxisome membranes. Localized at the base of the outer segment of photoreceptor cells. {ECO:0000250|UniProtKB:Q13608}.
Interaction partners:
- Peroxisomal ATPase PEX1
- Similar to peroxisome biogenesis factor 26.
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 2 receptor
- Peroxisomal targeting signal 1 receptor.
- Peroxisomal membrane protein PEX16
Sequence:
MALAVLHVLEPFPTETPPLAVLLPPGGPWPVTGVGLVLALRPASESPAGPALLVAAVEGSGAQCEQRGPGPPPLLVSRTLLRVLALSPGARVRARPVRRPPALGWALLGTSPGPGLGPRVGPLLVRRGETLPVPGSRVLETRPALQGLLGPGTRLAVTELQGRTKLDPESRDHNHPPPPPVVSSFAVSHSIRQLRGVLGGTGDALGVSRSCLRSLGLFQGEWVWVARVGELPNTSQPHLAQVQVLEPRWDLSARLGPNSGQPGEPLADGLVFVPATLAFNLGCDPLEVGELRIQRYLEDSTAAEDKGSCSLLPGPPFARELHIEVLPSPHCGVNGKYDHVLYQHFHTPRVVQEGDVLCVSTAGQVEILEGSLERLPRWREVFFKVKKTVGEAPDGPASAFLADTTHTSLYLAGTTLSRVPPLPSGRSPPWDSLSPPGLEALVNELCAVLKPHLQPGGTLLTGTSCVLLQGPPGSGKTTAVTAACSRLGLHLLKVPCSSLCADSSRTVETKLQTTFSRARRCRPVVLLLTALDLLGRDRDGLGEDARVVATLRHLLLDEDPLSRCPPLMVVATTSRVQDLPTDVRTAFPHELEVPVLSESQRLSVLQALTAHLPLGQEVNLSQLARRCAGFVVGDLYALLTHASRAACTRIKAAGLAMSEEDEGELCAAGFPLLAEDFGQALDQLQTAHSQAVGAPKIPSVSWHDVGGLQDVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGASEDRASQLRVLSAITRKFKLEASVSLMNVLDCCPPQLTGADLYSLCSDAMMTALKRRVRDLEEGLEPRSSALLLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC
Protein: Dpr-interacting protein epsilon (IP17937p) (A4IJ70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Defective proboscis extension response 16, isoform C
- Defective proboscis extension response 13, isoform B
- Defective proboscis extension response 14, isoform A
- Defective proboscis extension response 20
- Defective proboscis extension response 3, isoform B
- Defective proboscis extension response 18
- Defective proboscis extension response 19, isoform A
Sequence:
MAYHLEAISSFLYVGLGCLIASSVALSTDTGSEGNAGNVGGSTLNNVISEDPEFTDVIENITVPAGRNVKLACSVKNLGSYKVAWMHFEQSAILTVHNHVITRNPRISVTHDKHDKHRTWFLHINNVQEEDRGRYMCQINTVTAKTQYGFVKVVVPPNIDDALTSSDIIVREGDNVTLRCKAKGSPEPTIKWKRDDGNKIVINKTLEVHDLETDSLELERISRLHMGAYLCIASNGVPPSVSKRIKVSVDFSPMVWIPHQLVGIPIGFNITLECFIEANPTSLNYWTRENDQMITESSKYKTETIPGHPSYKATMRLTITNVQSSDYGNYKCVAKNPRGDMDGNIKLYMSSPPTTQPPPTTTTLRRTTTTAAEIALDGYINTPLNGNGIGIVGEGPTNSVIASGKSSIKYLSNLNEIDKSKQKLTGSSPKGFDWSKGKSSGSHGNLMASSWPLICCILALLTTHSCG
Protein: Pyrimidodiazepine synthase (EC 1.5.4.1) (Protein sepia) (Q9VSL3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates the conversion of 2-amino-4-oxo-6-pyruvoyl-5,6,7,8-tetrahydropteridine (6-PTP; also named 6-pyruvoyltetrahydropterin) to 2-amino-6-acetyl-3,7,8,9-tetrahydro-3H-pyrimido(4,5-b)[1,4]diazepin-4-one (pyrimidodiazepine or PDA), a key intermediate in red eye pigment drosopterin biosynthesis.
Interaction partners:
- Glutathione peroxidase
- glutathione-specific gamma-glutamylcyclotransferase
- Glutathione peroxidase
- glutathione-specific gamma-glutamylcyclotransferase
- 1-Cys peroxiredoxin
- Gamma-glutamyl transpeptidase, isoform A
- RE13973p
- Uncharacterized protein, isoform C
- RE21057p
- Glutathione S transferase O3
Sequence:
MSNGRHLAKGSPMPDVPEDGILRLYSMRFCPFAQRVHLVLDAKQIPYHSIYINLTDKPEWLLEKNPQGKVPALEIVREPGPPVLTESLLICEYLDEQYPLRPLYPRDPLKKVQDKLLIERFRAVLGAFFKASDGGDLEPFWSGLDIYERELARRGTEFFGGEQTGILDYMIWPWCERLELLKLQRGEDYNYDQSRFPQLTLWLERMKRDPAVMAFYMEAEVQAEFLRTRSLGRPNYNLLVKDA
Protein: Interleukin-36 beta (FIL1 eta) (Interleukin-1 eta) (IL-1 eta) (Interleukin-1 family member 8) (IL-1F8) (Interleukin-1 homolog 2) (IL-1H2) (Q9NZH7)
Organism: Homo sapiens (Human)
Function: Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Stimulates production of interleukin-6 and interleukin-8 in synovial fibrobasts, articular chondrocytes and mature adipocytes. Induces expression of a number of antimicrobial peptides including beta-defensins 4 and 103 as well as a number of matrix metalloproteases. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of pro-inflammatory cytokines such as TNF-alpha, IL-8 and IL-6.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32272059}. Secreted {ECO:0000269|PubMed:16646978}. Note=The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000269|PubMed:32272059}.
Interaction partners:
- Interleukin-1 receptor-like 2
- Interleukin-36 receptor antagonist protein
- Interleukin-1 family member 10
- Interleukin-1 receptor accessory protein
- Interleukin-1 alpha
- Interleukin-36 alpha
- Interleukin-1 beta
Sequence:
MNPQREAAPKSYAIRDSRQMVWVLSGNSLIAAPLSRSIKPVTLHLIACRDTEFSDKEKGNMVYLGIKGKDLCLFCAEIQGKPTLQLKLQGSQDNIGKDTCWKLVGIHTCINLDVRESCFMGTLDQWGIGVGRKKWKSSFQHHHLRKKDKDFSSMRTNIGMPGRM
Protein: Bowman-Birk type proteinase inhibitor A7 (HOSPI-A7) (C0HLS8)
Organism: Hyacinthus orientalis (Common hyacinth)
Function: Serine protease inhibitor. Strongly inhibits trypsin (Ki = 7.1 nM) and almost completely inhibits elastase. Also inhibits chymotrypsin (Ki = 19 nM). Does not inhibit bacterial subtilisin.
Interaction partners:
Sequence:
QTWPPVEDRPHCKRCVACTLMWPPEANRCVCGDLVPKCHKGCSQCEKADTRSGRPLYKCLSFEYYNCAAD