wanglab/gogpt-training-data huggingface dataset:
Protein: Ankyrin 2 (A0A5F9ZHL5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSETLSIVCPSIIRSLCVSPAFCPVPHNFRLSQWKAVESAKLLKQLWYLERGWRNIWGILV
Protein: Collagen alpha-1(III) chain (P12105)
Organism: Gallus gallus (Chicken)
Function: Collagen type III occurs in most soft connective tissues along with type I collagen.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Elastin
- Fibronectin
- Aggrecan core protein
- SMB domain-containing protein.
- Decorin
- Actin, cytoplasmic 1
- SPARC
- Albumin
- Serpin H1
- Transforming growth factor beta-1 proprotein
Sequence:
MMSFVQKVSLFILAVFQPSVILAQQDALGGCTHLGQEYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPLGECCPVCPQTTPQPTELPYTQGPKGDPGSPGSPGRTGAPGPPGQPGSPGAPGPPGICQSCPSISGGSFSPQYDSYDVKAGSVGMGYPPQPISGFPGPPGPSGPPGPPGHAGPPGSNGYQGPPGEPGQPGPSGPPGPAGMIGPAGPPGKDGEPGRPGRNGDRGIPGLPGHKGHPGMPGMPGMKGARGFDGKDGAKGDSGAPGPKGEAGQPGANGSPGQPGPGGPTGERGRPGNPGGPGAHGKDGAPGTAGPLGPPGPPGTAGFPGSPGFKGEAGPPGPAGASGNPGERGEPGPQGQAGPPGPQGPPGRAGSPGGKGEMGPSGIPGGPGPPGGRGLPGPPGTSGNPGAKGTPGEPGKNGAKGDPGPKGERGENGTPGARGPPGEEGKRGANGEPGQNGVPGTPGERGSPGFRGLPGSNGLPGEKGPAGERGSPGPPGPSGPAGDRGQDGGPGLPGMRGLPGIPGSPGSDGKPGPPGNQGEPGRSGPPGPAGPRGQPGVMGFPGPKGNEGAPGKNGERGPGGPPGTPGPAGKNGDVGLPGPPGPAGPAGDRGEPGPSGSPGLQGLPGGPGPAGENGKPGEPGPKGDIGGPGFPGPKGENGIPGERGPQGPPGPTGARGGPGPAGSEGAKGPPGPPGAPGGTGLPGLQGMPGERGASGSPGPKGDKGEPGGKGADGLPGARGERGNVGPIGPPGPAGPPGDKGETGPAGAPGPAGSRGGPGERGEQGLPGPAGFPGAPGQNGEPGGKGERGPPGLRGEAGPPGAAGPQGGPGAPGPPGPQGVKGERGSPGGPGAAGFPGARGPPGPPGNNGDRGESGPPGVPGPPGHPGPAGNNGAPGKAGERGFQGPLGPQGAIGSPGASGARGPPGPAGPPGKDGRGGYPGPIGPPGPRGNRGESGPAGPPGQPGLPGPSGPPGPCCGGGVASLGAGEKGPVGYGYEYRDEPKENEINLGEIMSSMKSINNQIENILSPDGSRKNPARNCRDLKFCHPELKSGEYWIDPNQGCKMDAIKVYCNMETGETCLSANPATVPRKNWWTTESSGKKHVWFGESMKGGFQFSYGDPDLPEDVSEVQLAFLRILSSRASQNITYHCKNSIAYMNQASGNVKKALKLMSSVETDIKAEGNSKYMYAVLEDGCTKHTGEWGKTVFEYRTRKTMRLPVVDIAPIDIGGPDQEFGVDVGPVCFL
Protein: Threonine--tRNA ligase, cytoplasmic (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P04801)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Valine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase YHR020W
- Leucine--tRNA ligase, mitochondrial
- Cysteine--tRNA ligase
- Probable proline--tRNA ligase, mitochondrial
Sequence:
MSASEAGVTEQVKKLSVKDSSNDAVKPNKKENKKSKQQSLYLDPEPTFIEERIEMFDRLQKEYNDKVASMPRVPLKIVLKDGAVKEATSWETTPMDIAKGISKSLADRLCISKVNGQLWDLDRPFEGEANEEIKLELLDFESDEGKKVFWHSSAHVLGESCECHLGAHICLGPPTDDGFFYEMAVRDSMKDISESPERTVSQADFPGLEGVAKNVIKQKQKFERLVMSKEDLLKMFHYSKYKTYLVQTKVPDGGATTVYRCGKLIDLCVGPHIPHTGRIKAFKLLKNSSCYFLGDATNDSLQRVYGISFPDKKLMDAHLKFLAEASMRDHRKIGKEQELFLFNEMSPGSCFWLPHGTRIYNTLVDLLRTEYRKRGYEEVITPNMYNSKLWETSGHWANYKENMFTFEVEKETFGLKPMNCPGHCLMFKSRERSYRELPWRVADFGVIHRNEFSGALSGLTRVRRFQQDDAHIFCTHDQIESEIENIFNFLQYIYGVFGFEFKMELSTRPEKYVGKIETWDAAESKLESALKKWGGNWEINAGDGAFYGPKIDIMISDALRRWHQCATIQLDFQLPNRFELEFKSKDQDSESYERPVMIHRAILGSVERMTAILTEHFAGKWPFWLSPRQVLVVPVGVKYQGYAEDVRNKLHDAGFYADVDLTGNTLQKKVRNGQMLKYNFIFIVGEQEMNEKSVNIRNRDVMEQQGKNATVSVEEVLKQLRNLKDEKRGDNVLA
Protein: Psychosine receptor (G-protein coupled receptor 65) (T-cell death-associated gene 8 protein) (Q8IYL9)
Organism: Homo sapiens (Human)
Function: Receptor for the glycosphingolipid psychosine (PSY) and several related glycosphingolipids. Plays a role in immune response by maintaining lysosome function and supporting phagocytosis-mediated intracellular bacteria clearance. May have a role in activation-induced cell death or differentiation of T-cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MNSTCIEEQHDLDHYLFPIVYIFVIIVSIPANIGSLCVSFLQAKKESELGIYLFSLSLSDLLYALTLPLWIDYTWNKDNWTFSPALCKGSAFLMYMNFYSSTAFLTCIAVDRYLAVVYPLKFFFLRTRRFALMVSLSIWILETIFNAVMLWEDETVVEYCDAEKSNFTLCYDKYPLEKWQINLNLFRTCTGYAIPLVTILICNRKVYQAVRHNKATENKEKKRIIKLLVSITVTFVLCFTPFHVMLLIRCILEHAVNFEDHSNSGKRTYTMYRITVALTSLNCVADPILYCFVTETGRYDMWNILKFCTGRCNTSQRQRKRILSVSTKDTMELEVLE
Protein: Procathepsin L (EC 3.4.22.15) (Cathepsin L1) (Major excreted protein) (MEP) (p39 cysteine proteinase) [Cleaved into: Cathepsin L; Cathepsin L heavy chain; Cathepsin L light chain] (P06797)
Organism: Mus musculus (Mouse)
Function: Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter. In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation. Secreted form generates endostatin from COL18A1. Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation. Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:11483509, ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:12782676}. Secreted, extracellular space {ECO:0000269|PubMed:12417635}. Secreted {ECO:0000269|PubMed:10716919}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages (PubMed:12417635). {ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:12782676}.
Interaction partners:
- Cathepsin B
- H-2 class II histocompatibility antigen gamma chain
- Serpin B13
- Apoptosis regulator Bcl-2
- Cathepsin S
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Cathepsin D
- Legumain
- Angiotensin-converting enzyme 2
Sequence:
MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQLHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKNSWGSEWGMEGYIKIAKDRDNHCGLATAASYPVVN
Protein: Clathrin interactor EPSIN 3 (EPSIN-related 3) (Q93YP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin heavy chain 2
- Clathrin coat assembly protein AP180
- AP-2 complex subunit alpha-1
- Protein MODIFIED TRANSPORT TO THE VACUOLE 1
- Adaptin ear-binding coat-associated protein 1 NECAP-1
- Calcium-binding EF hand family protein
- Putative clathrin assembly protein At2g01600
- Putative clathrin assembly protein At2g25430
- AP-2 complex subunit alpha-2
Sequence:
MKKAFGQTVRDLKRGVNKKVLKVPGIEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEHAYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITEVREKAAANRDKYHNSMHRPSGGYGDKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPPSYEEAVSESRSPVYSERDGGETPQVAPPGAAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIPPTVVSTPAPPASINAEMDLLGSLSDVFSPNPLAIVTSDSTSVETNGQANTGLAPSFSTSQSSTQPFDDPFGDSPFKAITSADTETSQHQSFGVPFQPTPPTSNPNNEHNFGFGEAFSAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSEIDILAGILPPSGPPVSLSPQPDSTMPTSQFHPNGNSYESYHHQAAPTDLNMQGQTPFGQASQQFNMVSHSQNHHEGMQFNNGGFTQQPGYAGPATSQPPQYTPGVSSHPPSESFPHQPGSATSASSQTPYATTPNVSAGQFDGGSFMTQQPYGVTQQVHVVPSHIPQRTQSGPVAAFGNNNNIVGDMHQPGSTPSSSSQTPYPTTPNAPSGQFDGGNFMTQQPYGVIPQVHGVPSHIPQRTQSGPVAAHGNSNNVVGDMFSPAGLSSLETSASQPSLTPLTGAIEIVPQNQKKFEPKSTIWADTLSRGLVNFNISGPKTNPLADIGVDFEAINRKEKRLEKPTITQQQVTSTINMGKAMGSGTGLGRAGAGAMRPPTNSMVGSSMPTGMNVGGYGGMNQHQPIGMNQNHPMGMNQNLSMGMNQNYPMGMNQNYPMGMGMNMNMGGYGQGYPMQPQQGMGMAPPGAPQGMTGAYNPMMGQGGYNPQQQQPYGGGYR
Protein: Centrosomal protein of 170 kDa (Cep170) (KARP-1-binding protein) (KARP1-binding protein) (Q5SW79)
Organism: Homo sapiens (Human)
Function: Plays a role in microtubule organization. Required for centriole subdistal appendage assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30354798, ECO:0000269|PubMed:31789463}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:31789463}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15616186}. Note=Associated with the mature mother centriole. Associated with spindle microtubules during mitosis. Localizes to the distal appendage region of the centriole (PubMed:31789463). Localizes at the centriole proximal ends (PubMed:31789463). {ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:31789463}.
Interaction partners:
- Centrosomal protein of 128 kDa
- Centriolin
- Ninein
- Coiled-coil domain-containing protein 68
- Coiled-coil domain-containing protein 120
- Kinesin-like protein KIF2A
- Kinesin-like protein KIFC3
- Outer dense fiber protein 2
- Centlein
- Centrosomal protein CCDC61
Sequence:
MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTNLFTVVQGEMRVPEEALKHEKFTIQLQLSQKSSESELSKSASAKSIDSKVADAATEVQHKTTEALKSEEKAMDISAMPRGTPLYGQPSWWGDDEVDEKRAFKTNGKPEEKNHEAGTSGCGIDAKQVEEQSAAANEEVLFPFCREPSYFEIPTKEFQQPSQITESTIHEIPTKDTPSSHITGAGHASFTIEFDDSTPGKVTIRDHVTKFTSDQRHKSKKSSPGTQDLLGIQTGMMAPENKVADWLAQNNPPQMLWERTEEDSKSIKSDVPVYLKRLKGNKHDDGTQSDSENAGAHRRCSKRATLEEHLRRHHSEHKKLQKVQATEKHQDQAVTSSAHHRGGHGVPHGKLLKQKSEEPSVSIPFLQTALLRSSGSLGHRPSQEMDKMLKNQATSATSEKDNDDDQSDKGTYTIELENPNSEEVEARKMIDKVFGVDDNQDYNRPVINEKHKDLIKDWALSSAAAVMEERKPLTTSGFHHSEEGTSSSGSKRWVSQWASLAANHTRHDQEERIMEFSAPLPLENETEISESGMTVRSTGSATSLASQGERRRRTLPQLPNEEKSLESHRAKVVTQRSEIGEKQDTELQEKETPTQVYQKDKQDADRPLSKMNRAVNGETLKTGGDNKTLLHLGSSAPGKEKSETDKETSLVKQTLAKLQQQEQREEAQWTPTKLSSKNVSGQTDKCREETFKQESQPPEKNSGHSTSKGDRVAQSESKRRKAEEILKSQTPKGGDKKESSKSLVRQGSFTIEKPSPNIPIELIPHINKQTSSTPSSLALTSASRIRERSESLDPDSSMDTTLILKDTEAVMAFLEAKLREDNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTGSPSKDVTKSSSSGAREKMEKKTKSRSTDVGSRADGRKFVQSSGRIRQPSVDLTDDDQTSSVPHSAISDIMSSDQETYSCKPHGRTPLTSADEHVHSKLEGSKVTKSKTSPVVSGSSSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKPPTGRRNISRIDLLAQPRRTRLGSLSARSDSEATISRSSASSRTAEAIIRSGARLVPSDKFSPRIRANSISRLSDSKVKSMTSAHGSASVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRLQSAGSAMPTSSSFKHRIKEQEDYIRDWTAHREEIARISQDLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREELVDRVFDESLNFRKIPPLVHSKTPEGNNGRSGDPRPQAAEPPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSKKIRQSIDKTAGKIRILFKDKDRNWDDIESKLRAESEVPIVKTSSMEISSILQELKRVEKQLQAINAMIDPDGTLEALNNMGFPSAMLPSPPKQKSSPVNNHHSPGQTPTLGQPEARALHPAAVSAAAEFENAESEADFSIHFNRFNPDGEEEDVTVQE
Protein: C-type diheme-containing protein (Conserved hypothetical cytochrome protein) (Q1PVE1)
Organism: Kuenenia stuttgartiensis
Interaction partners:
Sequence:
MKPKGLFYTFGFLSAAVFSCAVLTVVMRPNTASAIEIPKEVTEEGKNVYKKYCAPCHGEEGGGDGLLSRSMLPKPRNFTLGAYKFRTTPSGSLPTDEDIYRTISYGVPNSTMIPWDILTEEQRASVVPVLKSFSEAFEYREPEPSVDVGLPLRPTERTILAGKKIYEEKLECWKCHGVEGRGDGPSASEQEDDFGFPIKPFDFTTGKFKGGNSPTDVYLRFTTGLNGTPMPSFAKELSDDERWYLTHYVMSLVQPEKCRK
Protein: Calcium and integrin-binding family member 3 (Kinase-interacting protein 3) (KIP 3) (Q96Q77)
Organism: Homo sapiens (Human)
Function: Acts a an auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (By similarity). Plays a role in regulating hair cell MET channel localization and function (By similarity).
Interaction partners:
- Transmembrane channel-like protein 1
- Transmembrane channel-like protein 2
- Kinesin-like protein KIF18A
Sequence:
MGNKQTVFTHEQLEAYQDCTFFTRKEIMRLFYRYQDLAPQLVPLDYTTCPDVKVPYELIGSMPELKDNPFRQRIAQVFSEDGDGHMTLDNFLDMFSVMSEMAPRDLKAYYAFKIYDFNNDDYICAWDLEQTVTKLTRGGLSAEEVSLVCEKVLDEADGDHDGRLSLEDFQNMILRAPDFLSTFHIRI
Protein: 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic (AtNCED3) (EC 1.13.11.51) (Protein SALT TOLERANT 1) (Q9LRR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids, in response to water stress.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12834401}. Note=Partially bound to the thylakoid.
Interaction partners:
- Xanthoxin dehydrogenase
- Zeaxanthin epoxidase, chloroplastic
- Abscisic-aldehyde oxidase
- Molybdenum cofactor sulfurase
- Low-temperature-induced 78 kDa protein
- Low-temperature-induced 65 kDa protein
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Protein ABSCISIC ACID-INSENSITIVE 5
- NAC domain-containing protein 72
Sequence:
MASFTATAAVSGRWLGGNHTQPPLSSSQSSDLSYCSSLPMASRVTRKLNVSSALHTPPALHFPKQSSNSPAIVVKPKAKESNTKQMNLFQRAAAAALDAAEGFLVSHEKLHPLPKTADPSVQIAGNFAPVNEQPVRRNLPVVGKLPDSIKGVYVRNGANPLHEPVTGHHFFDGDGMVHAVKFEHGSASYACRFTQTNRFVQERQLGRPVFPKAIGELHGHTGIARLMLFYARAAAGIVDPAHGTGVANAGLVYFNGRLLAMSEDDLPYQVQITPNGDLKTVGRFDFDGQLESTMIAHPKVDPESGELFALSYDVVSKPYLKYFRFSPDGTKSPDVEIQLDQPTMMHDFAITENFVVVPDQQVVFKLPEMIRGGSPVVYDKNKVARFGILDKYAEDSSNIKWIDAPDCFCFHLWNAWEEPETDEVVVIGSCMTPPDSIFNESDENLKSVLSEIRLNLKTGESTRRPIISNEDQQVNLEAGMVNRNMLGRKTKFAYLALAEPWPKVSGFAKVDLTTGEVKKHLYGDNRYGGEPLFLPGEGGEEDEGYILCFVHDEKTWKSELQIVNAVSLEVEATVKLPSRVPYGFHGTFIGADDLAKQVV
Protein: Alpha-keto-acid decarboxylase (KDC) (EC 4.1.1.-) (P9WG37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes.
Interaction partners:
- Probable alcohol dehydrogenase adh
- IscS-like cysteine desulfurase
- Cullin, a subunit of E3 ubiquitin ligase
- Putative acetolactate synthase small subunit
- Coenzyme Q-binding protein COQ10 START domain-containing protein
Sequence:
MTPQKSDACSDPVYTVGDYLLDRLAELGVSEIFGVPGDYNLQFLDHIVAHPTIRWVGSANELNAGYAADGYGRLRGMSAVVTTFGVGELSVTNAIAGSYAEHVPVVHIVGGPTKDAQGTRRALHHSLGDGDFEHFLRISREITCAQANLMPATAGREIDRVLSEVREQKRPGYILLSSDVARFPTEPPAAPLPRYPGGTSPRALSLFTKAAIELIADHQLTVLADLLVHRLQAVKELEALLAADVVPHATLMWGKSLLDESSPNFLGIYAGAASAERVRAAIEGAPVLVTAGVVFTDMVSGFFSQRIDPARTIDIGQYQSSVADQVFAPLEMSAALQALATILTGRGISSPPVVPPPAEPPPAMPARDEPLTQQMVWDRVCSALTPGNVVLADQGTSFYGMADHRLPQGVTFIGQPLWGSIGYTLPAAVGAAVAHPDRRTVLLIGDGAAQLTVQELGTFSREGLSPVIVVVNNDGYTVERAIHGETAPYNDIVSWNWTELPSALGVTNHLAFRAQTYGQLDDALTVAAARRDRMVLVEVVLPRLEIPRLLGQLVGSMAPQ
Protein: DNA repair protein rad14 (XP-A family homolog rhp14) (O59753)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nucleotide excision repair (NER). Functional in repair of ultraviolet radiation induced damages and in mitotic mutation avoidance. Binds damaged DNA. Binds specifically to base-base mismatches or small insertion/deletion loops with unpaired nucleotides. Maintains GT repeat stability. Functions as a part of the short-patch excision repair system.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P28519}.
Interaction partners:
- Mating-type switching protein swi10
- DNA repair protein rad16
- DNA repair protein rad13
- General transcription and DNA repair factor IIH helicase subunit XPD
- DNA repair protein rhp26
- General transcription and DNA repair factor IIH subunit tfb1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- DNA repair protein rhp41
- UV excision repair protein rhp23
- DNA repair protein rhp7
Sequence:
MENSSIVKSPNPTIEEQRNEIEKLKNLTGIEEVHVDGAKVNKRKRTFDEQSEITKDYIEYDFSKIEDTKGGYLLEEKKVEDLREKPAERELREQEERQKKLRLAPLNLDPETAPKCFECDSIELDTKYFDIFHCRVCHTCREKYPDKYSLLTKTECKLDYLLTEPELQDQELLPRLLKANPHQQGWSNMMLYLRYQVEEFAKKKWGSMEALDAEFERREVQKKEMKEKKFEKQLLELRKRTRTSNYSRMSIREKRKHVHSYDEEFEKPNEPGVIVQRCKCGLEIEQLEI
Protein: Cytochrome P450 81F2 (EC 1.14.-.-) (Protein INDOLE GLUCOSINOLATE MODIFIER 1) (Q9LVD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in indole glucosinolate biosynthesis. Catalyzes hydroxylation reactions of the glucosinolate indole ring. Converts indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) intermediates. These hydroxy intermediates are converted to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M) by indole glucosinolate methyltransferase 1 and 2 (IGMT1 and IGMT2). Contributes to defense against the green peach aphid (Myzus persicae), a generalist phloem-feeding herbivore. Required for the biosynthesis of antifungal indole glucosinolate metabolites. Required for the pathogen-induced accumulation of 4MO-I3M, which in turn is activated by the atypical BGLU26/PEN2 myrosinase. Required for the biosynthesis of Trp-derived antifungal compounds and non-host resistance to the necrotrophic fungal pathogen Plectosphaerella cucumerina. Required for resistance to the non-adapted fungal pathogen Colletotrichum gloeosporioides.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcription factor MYB51
- Indole glucosinolate O-methyltransferase 2
- Indole glucosinolate O-methyltransferase 1
- Cytosolic sulfotransferase 16
- Senescence-induced receptor-like serine/threonine-protein kinase
- NDR1/HIN1-like protein 10
- Probable 2-oxoacid dependent dioxygenase
- Probable LRR receptor-like protein kinase At1g51890
- Transcription factor MYB122
- Flavin-containing monooxygenase FMO GS-OX5
Sequence:
MDYVLIVLPLALFLIAYKFLFSSKTQGFNLPPGPTPFPIVGHLHLVKPPVHRLFRRFAEKYGDIFSLRYGSRQVVVISSLPLVRESFTGQNDVILTNRPHFLTAKYVAYDYTTIGTAAYGDHWRNLRRICSLEILSSNRLTGFLSVRKDEIRRLLTKLSREYDGRVVELEPLLADLTFNNIVRMVTGRRYYGDQVHNKEEANLFKKLVTDINDNSGASHPGDYLPILKVFGHGYEKKVKALGEAMDAFLQRLLDECRINGESNTMVSHLLSLQLDQPKYYSDVIIKGLMLSMMLAGTDTAAVTLEWAMANLLKKPEVLKKAKAEIDEKIGEERLVDEPDIANLPYLQNIVSETFRLCPAAPLLVPRSPSEDLKIGGYDIPRGTIVLVNAWAIHRDPRLWDEPEKFMPERFEDQEASKKLMVFGNGRRTCPGATLGQRMVLLALGSLIQCFDWEKVNGEDVDMTENPGMAMRKLVQLRAVCHKRPIMTNLLA
Protein: Cadherin-related family member 2 (Protocadherin LKC) (PC-LKC) (Protocadherin-24) (Q9BYE9)
Organism: Homo sapiens (Human)
Function: Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR5 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation. May also play a role in cell-cell adhesion and contact inhibition in epithelial cells.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409}; Single-pass type I membrane protein {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409}. Cell projection, microvillus membrane {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:32209652}; Single-pass type I membrane protein {ECO:0000269|PubMed:12117771, ECO:0000269|PubMed:24725409}. Cell junction {ECO:0000269|PubMed:12117771}.
Interaction partners:
- Cadherin-related family member 5
- Harmonin
- Unconventional myosin-VIIb
- Ankyrin repeat and SAM domain-containing protein 4B
- Protocadherin-15
Sequence:
MAQLWLSCFLLPALVVSVAANVAPKFLANMTSVILPEDLPVGAQAFWLVAEDQDNDPLTYGMSGPNAYFFAVTPKTGEVKLASALDYETLYTFKVTISVSDPYIQVQREMLVIVEDRNDNAPVFQNTAFSTSINETLPVGSVVFSVLAVDKDMGSAGMVVYSIEKVIPSTGDSEHLFRILANGSIVLNGSLSYNNKSAFYQLELKACDLGGMYHNTFTIQCSLPVFLSISVVDQPDLDPQFVREFYSASVAEDAAKGTSVLTVEAVDGDKGINDPVIYSISYSTRPGWFDIGADGVIRVNGSLDREQLLEADEEVQLQVTATETHLNIYGQEAKVSIWVTVRVMDVNDHKPEFYNCSLPACTFTPEEAQVNFTGYVDEHASPRIPIDDLTMVVYDPDKGSNGTFLLSLGGPDAEAFSVSPERAVGSASVQVLVRVSALVDYERQTAMAVQVVATDSVSQNFSVAMVTIHLRDINDHRPTFPQSLYVLTVPEHSATGSVVTDSIHATDPDTGAWGQITYSLLPGNGADLFQVDPVSGTVTVRNGELLDRESQAVYYLTLQATDGGNLSSSTTLQIHLLDINDNAPVVSGSYNIFVQEEEGNVSVTIQAHDNDEPGTNNSRLLFNLLPGPYSHNFSLDPDTGLLRNLGPLDREAIDPALEGRIVLTVLVSDCGEPVLGTKVNVTITVEDINDNLPIFNQSSYNFTVKEEDPGVLVGVVKAWDADQTEANNRISFSLSGSGANYFMIRGLVLGAGWAEGYLRLPPDVSLDYETQPVFNLTVSAENPDPQGGETIVDVCVNVKDVNDNPPTLDVASLRGIRVAENGSQHGQVAVVVASDVDTSAQLEIQLVNILCTKAGVDVGSLCWGWFSVAANGSVYINQSKAIDYEACDLVTLVVRACDLATDPGFQAYSNNGSLLITIEDVNDNAPYFLPENKTFVIIPELVLPNREVASVRARDDDSGNNGVILFSILRVDFISKDGATIPFQGVFSIFTSSEADVFAGSIQPVTSLDSTLQGTYQVTVQARDRPSLGPFLEATTTLNLFTVDQSYRSRLQFSTPKEEVGANRQAINAALTQATRTTVYIVDIQDIDSAARARPHSYLDAYFVFPNGSALTLDELSVMIRNDQDSLTQLLQLGLVVLGSQESQESDLSKQLISVIIGLGVALLLVLVIMTMAFVCVRKSYNRKLQAMKAAKEARKTAAGVMPSAPAIPGTNMYNTERANPMLNLPNKDLGLEYLSPSNDLDSVSVNSLDDNSVDVDKNSQEIKEHRPPHTPPEPDPEPLSVVLLGRQAGASGQLEGPSYTNAGLDTTDL
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q802Y2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDSSRNRMRFGGFKMSQKVKAGSVVEMQGDEMTRVIWELIKEKLIFPYLELDLHSYDLGMENRDATDDKVTVEAAEAVRRYNVGIKCATITPDEKRVEEFKLKQMWRSPNGTIRNILGGTVFREAIICKNIPRLVPGWIKPIIIGRHAHGDQYKATDFVVPGPGTVEMTYKPKNGGETLKFVVHDFEGTGGVALGMYNTDKSIRDFAHSSFQMGLNKGWPMYLSTKNTILKKYDGRFKDIFQEIYDKEYKAKYEAMGIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGRTVEAEAAHGTVTRHYRMHQQGKETSTNPIASIFAWTRGLLHRAELDKNAELRVFAEALEVVCVETIEAGFMTKDLAICIKGMSGVTRSDYLNTFEFLDKLAENLKIKLSSQPKL