wanglab/gogpt-training-data huggingface dataset:
Protein: Organic cation/carnitine transporter 2 (AtOCT2) (O64515)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity carnitine transporter involved in the active cellular uptake of carnitine. Also transports organic cations (By similarity).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:18710496}; Multi-pass membrane protein {ECO:0000269|PubMed:18710496}.
Interaction partners:
- GDSL esterase/lipase EXL1
- Probable ADP-ribosylation factor GTPase-activating protein AGD14
- Nucleosome assembly protein 1;4
Sequence:
MAEPTQPLLTDSNSSSPRSLDDTIESYIGSFGWAQFLQAALVSFSGVFDAQQTFISVFTDSEPTWHCTDSNSICHESISNICILPKTAWSWDYSPHVSVISEWGLQCAGSFVKGLPESSFFVGCLIGGLVLSTLADSSLGRKNMLFLSCLVMAISTMLTVFSPNIWVYAVLRFVNGFGRATIGTCALVLSTELVGKKWRGRVGIMSFFGFMLGFLSLPLMAYMNRGSSWRILYAWTSIPTIIYCVLVRFFVCESPRWLFVRGRREEAISILKRVASIPSTDVSSGGAISMSFSSLPFEEDEEKPSTNVNIFTTMKVLVEKRWALKRLSAVMAIAFGIGLVYYGMPLALSNLDFNIYLSAAFNALMDLPANLITLFLVDKLSRRNALIGFTALGGVSSVLIFALHNMRIGNHGALQLALELISYFSACSAFNMEMIYTIELFPTCVRNSAIAMARQALVLGGVFSPIMVAAGRKNAFWSFGLFGLAIGLLGLFAVGLPETRGSDLCDTMDEEECKDRRSKVAVNNVIA
Protein: Rabankyrin-5 (Rank-5) (Ankyrin repeat and FYVE domain-containing protein 1) (Ankyrin repeats hooked to a zinc finger motif) (Q810B6)
Organism: Mus musculus (Mouse)
Function: Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI(3)P). Involved in homotypic early endosome fusion and to a lesser extent in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the subcellular localization of the retromer complex in a EHD1-dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport (By similarity). Involved in macropinocytosis; the function is dependent on Rab5-GTP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10092534}. Endosome membrane {ECO:0000269|PubMed:10092534}; Peripheral membrane protein {ECO:0000269|PubMed:10092534}. Cytoplasmic vesicle {ECO:0000269|PubMed:15328530}. Note=Also associated with endosomal membranes. Localizes to macropinosomes. In kidney proximal tubule cells localizes to vesicle-like structures underneath the apical brush border. {ECO:0000269|PubMed:15328530}.
Interaction partners:
- Sorting nexin-3
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 26A
- Rabenosyn-5
- DENN domain-containing protein 4C
- Sorting nexin-6
- TBC1 domain family member 5
Sequence:
MAEEEVAKLEKHLMLLRQEYVKLQKKLAETEKRCTLLAAQANKENSNESFISRLLAIVAGLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTEEIDLSDANPEVTMTMLRWIYTDELEFREDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSLSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNETDHNGDLALDLALSRRLESIATTLVSHKADVDMVDKNGWSLLHKGIQRGDLFASTFLIKNGALVNAATAGAQETPLHLVALYSPKKYSADVMSEMAQIAEALLQAGANPNMQDSKGRTPLHLSIMARNDCVFSQLLQCKQLDLELKDHEGSTALWLAVQYITVSSDQSVNPFEDLPVVNGTSFDENSFAARLIQRGSNTDAPDVMTGNCLLQRAAGAGNEAAALFLATSGAHANHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEALPVPKESPVLMSSADSIYLQTPLHMAIAYNHPDVVSVILEQKANALHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGASINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVRTQDGETALQLAIKHQLPLVVDAICTRGADMSVPDEKGNPPLWLALASNLEDIASTLVRHGCDATCWGPGPSGCLQTLLHRAVDENNESTACFLIRSGCDVNSPRQPGTNGEGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPVHVAISNQHSVIIQLLISHPNIELSVRDRQGLTPFACAMTYKNNKAAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVQANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRALLTECTVDAEAFNLRGQSPLHILGQYGKENAAAIFDLFLECMPEYPLDKPDAEGNTVLLLAYMKGNANLCRAIVRSGVRLGVNNNQGVNIFNYQVATKQLLFRLLDMLSKEPPWCDGSNCYECTAKFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVLTLGGVS
Protein: Lysyl oxidase homolog 4 (EC 1.4.3.13) (Lysyl oxidase-like protein 4) (Lysyl oxidase-related protein C) (Q924C6)
Organism: Mus musculus (Mouse)
Function: May modulate the formation of a collagenous extracellular matrix.
Subcellular location: Secreted, extracellular space {ECO:0000305}.
Interaction partners:
- Lysyl oxidase homolog 2
- Elastin
- Fibulin-5
- Lysyl oxidase homolog 3
Sequence:
MMWPQPPTFSLFLLLLLSQAPSSRPQSSGTKKLRLVGPTDRPEEGRLEVLHQGQWGTVCDDDFALQEATVACRQLGFESALTWAHSAKYGQGEGPIWLDNVRCLGTEKTLDQCGSNGWGVSDCRHSEDVGVVCHPRRQHGYHSEKVSNALGPQGRRLEEVRLKPILASAKRHSPVTEGAVEVRYDGHWRQVCDQGWTMNNSRVVCGMLGFPSQTSVNSHYYRKVWNLKMKDPKSRLNSLTKKNSFWIHRVDCLGTEPHLAKCQVQVAPGRGKLRPACPGGMHAVVSCVAGPHFRRQKPKPTRKESHAEELKVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGAQLGQGLGPIHLSEVRCRGYERTLGDCLALEGSQNGCQHANDAAVRCNIPDMGFQNKVRLAGGRNSEEGVVEVQVEVNGVPRWGTVCSDHWGLTEAMVTCRQLGLGFANFALKDTWYWQGTPEAKEVVMSGVRCSGTEMALQQCQRHGPVHCSHGPGRFSAGVACMNSAPDLVMNAQLVQETAYLEDRPLSMLYCAHEENCLSKSADHMDWPYGYRRLLRFSSQIYNLGRADFRPKAGRHSWIWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPSGVQRRYACANFGEQGVAVGCWDTYRHDIDCQWVDITDVGPGDYIFQVVVNPTNDVAESDFSNNMIRCRCKYDGQRVWLHNCHTGDSYRANAELSLEQEQRLRNNLI
Protein: Matrix metalloproteinase-C (MMP-C) (MMP-C31) (EC 3.4.24.-) (Zinc metalloprotease 3) (G5EBU3)
Organism: Caenorhabditis elegans
Function: Metalloproteinase.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Putative metalloproteinase inhibitor tag-225
- NTR domain-containing protein
- Cadherin-3
Sequence:
MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSSGGGSRTTARPTTTTRSWFGRFFGDDDDDVRSRTTTRRTTLWPTTQSPFSGDDWGSGSGSSGRGGSSSGSSGGGCPSHIDAYTPSSSFSYAFSGSQVYTISGTKVTKVQSIHDLFPSAPTPVNAALWNPISGSMLLFSSNRVYSYYFSNIRQIFQMDSGFPKTLPSDLGFSVSGALRWINGHQILMSSGDEFAVYDEFWNQVTLKNRISSYFPNLPRGVKGVESPAGSVITAFTSNQVFEYNSRTKSIGRQSGFSSYIAC
Protein: 40S ribosomal protein S24 (E7ETK0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNDTVTIRTRKFMTNRLLQRKQMVIDVLHPGKATVPKTEIREKLAKMYKTTPDVIFVFGFRTHFGGGKTTGFGMIYDSLDYAKKNEPKHRLARHGLYEKKKTSRKQRKERKNRMKKVRGTAKANVGAGKKQ
Protein: RNA-binding motif, single-stranded-interacting protein 3 (Q6XE24)
Organism: Homo sapiens (Human)
Function: Binds poly(A) and poly(U) oligoribonucleotides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10675610}.
Interaction partners:
- Myc proto-oncogene protein
Sequence:
MGKRLDQPQMYPQYTYYYPHYLQTKQSYAPAPHPMAPPSPSTNSSSNNSSNNSSGEQLSKTNLYIRGLPPGTTDQDLIKLCQPYGKIVSTKAILDKNTNQCKGYGFVDFDSPAAAQKAVASLKANGVQAQMAKQQEQDPTNLYISNLPISMDEQELENMLKPFGHVISTRILRDANGVSRGVGFARMESTEKCEVVIQHFNGKYLKTPPGIPAPSEPLLCKFADGGQKKRQNQSKYTQNGRPWPREGEAGMALTYDPTAAIQNGFYSSPYSIATNRMIPQTSITPFIAASPVSTYQVQSTSWMPHPPYVMQPTGAVITPTMDHPMSMQPANMMGPLTQQMNHLSLGTTGTIQSQDRIMILHQLLCQYMTAAAPMQGTYIPQYTPVPPTAVSIEGVVADTSPQTVAPSSQDTSGQQQQIAVDTSNEHAPAYSYQQSKP
Protein: Mast cell protease 8 (mMCP-8) (EC 3.4.21.-) (P43430)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Note=Secretory granules. {ECO:0000250}.
Interaction partners:
- Cell surface glycoprotein CD200 receptor 3
- High affinity immunoglobulin epsilon receptor subunit alpha
- Mast cell carboxypeptidase A
Sequence:
MFLLLVLLVAALPVNAEGGEIIWGTESKPHSRPYMAYIRFNDSKSVYRCGGFLVARDIVMTAAHCNGKVINVTLGIHNLKKKKNTQLIPVSEAIPHESFDNETLVNDIMLLKLERKAQLNSAVDTIALPKSKDWVKPGQVCTVAGWGKLANCTLSDTLQEVNLEVQKGQKCRSMSQTYNDSIQLCVGNPSENKATGKGDSGGPFVCNGVVQGIVSCRLCTGTLPRVFTRISSFMPWIRKTMKLLQQP
Protein: Regulator of G-protein signaling 18 (RGS18) (Q99PG4)
Organism: Mus musculus (Mouse)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i) alpha-1, G(i) alpha-2, G(i) alpha-3 and G(q) alpha.
Subcellular location: Cytoplasm.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
Sequence:
MDMSLVFFSQLNMCESKEKTFFKLMHGSGKEETSIEAKIRAKEKRNRLSLLLQRPDFHGETQASRSALLAKETRVSPEEAVKWAESFDKLLSHRDGVDAFTRFLKTEFSEENIEFWVACEDFKKCKEPQQIILKAKAIYEKFIQNDAPKEVNIDFHTKEVIAKSIAQPTLHSFDTAQSRVYQLMEHDSYKRFLKSETYLHLIEGRPQRPTNLRRRSRSFTYNDFQDVKSDVAIWL
Protein: B3 domain-containing transcription factor FUS3 (Protein FUSCA3) (Q9LW31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription regulator involved in gene regulation during late embryogenesis. Its expression to the epidermis is sufficient to control foliar organ identity by regulating positively the synthesis abscisic acid (ABA) and negatively gibberellin production. Negatively regulates TTG1 in the embryo. Positively regulates the abundance of the ABI3 protein in the seed. Cooperates with KIN10 to regulate developmental phase transitions and lateral organ development and act both as positive regulators of abscisic acid (ABA) signaling during germination.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit B-9
- SNF1-related protein kinase catalytic subunit alpha KIN10
- Ethylene-responsive transcription factor WRI1
- Agamous-like MADS-box protein AGL15
- Nuclear transcription factor Y subunit B-6
- 2S seed storage protein 3
- Protein ABSCISIC ACID-INSENSITIVE 5
- CHD3-type chromatin-remodeling factor PICKLE
- Protein WUSCHEL
- Trihelix transcription factor ASIL1
Sequence:
MMVDENVETKASTLVASVDHGFGSGSGHDHHGLSASVPLLGVNWKKRRMPRQRRSSSSFNLLSFPPPMPPISHVPTPLPARKIDPRKLRFLFQKELKNSDVSSLRRMILPKKAAEAHLPALECKEGIPIRMEDLDGFHVWTFKYRYWPNNNSRMYVLENTGDFVNAHGLQLGDFIMVYQDLYSNNYVIQARKASEEEEVDVINLEEDDVYTNLTRIENTVVNDLLLQDFNHHNNNNNNNSNSNSNKCSYYYPVIDDVTTNTESFVYDTTALTSNDTPLDFLGGHTTTTNNYYSKFGTFDGLGSVENISLDDFY
Protein: Prohibitin 1 (P35232)
Organism: Homo sapiens (Human)
Function: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus. Plays a role in adipose tissue and glucose homeostasis in a sex-specific manner (By similarity). Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:20959514}. Nucleus {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:31899195}. Cytoplasm {ECO:0000269|PubMed:14500729, ECO:0000269|PubMed:31899195}. Cell membrane {ECO:0000269|PubMed:22997079, ECO:0000269|PubMed:24003225}.
Interaction partners:
- Prohibitin-2
- Erlin-2
- Erlin-1
- Stomatin
- RAF proto-oncogene serine/threonine-protein kinase
- Stomatin-like protein 2, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Histone deacetylase 1
- Non-selective voltage-gated ion channel VDAC2
- Mitochondrial import inner membrane translocase subunit TIM14
Sequence:
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Protein: Malectin-A (Q6INX3)
Organism: Xenopus laevis (African clawed frog)
Function: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation. Can bind di- or higher oligomers but not monomers of glucose, including maltose, maltotriose, maltotetraose, maltoheptaose, nigerose, kojibose, cellobiose and isomaltose, although based on their subcellular locations, these are unlikely to all be physiological ligands.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18524852}; Single-pass type I membrane protein {ECO:0000255, ECO:0000269|PubMed:18524852}.
Interaction partners:
Sequence:
MLSIRTVLGPLATILLTVLGPFGAHGSGLADKVIWAVNAGGESHVDVHGIHYRKDPLEGRVGRASDYGMKLPILRSNPEDQVLYQTERYNEDSFGYDIPIKEEGEYVLVLKFAEVYFAQSQQKVFDVRVNGHTVVKDLDIFDRVGHSTAHDEIIPISIKKGKLSVQGEVSTFTGKLSVEFVKGYYDNPKVCALFIMKGTADDVPMLQPHPGLEKKEEEEEEEEEEGSTSKKQINKNRVQSGPRTPNPYASDNSSLMFPILVAFGVFIPTLFCLCRL
Protein: Dermonecrotic toxin LiSicTox-betaID1 (EC 4.6.1.-) (Dermonecrotic toxin 5) (DT5) (LiRecDT5) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 5) (SMD 5) (SMase D 5) (Sphingomyelinase D 5) (Q1W694)
Organism: Loxosceles intermedia (Brown spider)
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with low activity. It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Has no or weak activities in inducing dermonecrosis, hemolysis, inflammatory response, platelet aggregation and increase in vessel permeability. In vivo, shows no lethality when injected at higher dose into mice.
Subcellular location: Secreted {ECO:0000305|PubMed:17296256}.
Interaction partners:
Sequence:
MQLFIILCLAGSAVQLEGTELDGVERADNRRPIWNIAHMVNDKGLIDEYLDDGANSVESDVSFDSNGKPEKMLHGSPCDCGRSCKRQMSFADYLDYMRQLTTPGDPKFRENLILVMLDLKLKKLSSEQAYSAGQEVASQMLDKYWKRGESGARAYIVLSIPTITRVTFVNGFYDKLHSEGFDQYREKVGVDFSGNEDLEDTGKILKSRDILDHIWQSDGITNCLFRIMKRLKAAIRKRDSNGYMVKVYTWSVDKYTTMRKALRAGADGMITNFPKRLVSVLNEREFSGKFRLATYNDNPWERYTG
Protein: Ent-copalyl diphosphate synthase 1, chloroplastic (Ent-CDP synthase 1) (OsCPS1) (OsCPS1ent) (EC 5.5.1.13) (Ent-kaurene synthase A) (OsCPS) (Q6ET36)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- Probable solanesyl-diphosphate synthase 3, chloroplastic
- Solanesyl-diphosphate synthase 2, chloroplastic
- Os07g0580900 protein
- Os02g0668100 protein
- Os04g0561350 protein
- Os01g0265000 protein.
- Ent-kaur-16-ene synthase, chloroplastic
- Os05g0235701 protein
- Ent-kaurene synthase-like 3
Sequence:
MIHLHSPPTAPAAFGGAGSADWRRRRRWSWSSSSRAPVAKGGHLRPCVWRRGGDDGGGEDHHADGGGGGGGGAAWRARATTAGVSSSSSTAKGLQANIIEHETPRITKWPNESRDLDDHQQNNEADEEADDELQPLVEQVRSMLSSMEDGAITASAYDTAWVALVPRLDGEGGTQFPAAVRWIVGSQLADGSWGDEALFSAYDRVINTLACVVALTRWSLHHDQCKQGLQFLNLNLWRLAEEEPDTMPIGFEIAFPSLVEAARGLGIDFPYDHPALKGIYANRELKLKRIPKDMMHIVPTSILHSLEGMPGLDWQRLLKLQCSDGSFLFSPSATAYALMQTGDKKCFAYIDRIIKKFDGGVPNVYPVDLFEHIWVVDRLERLGISRYFQREIEQNMDYVNRHWTEDGICWARNSNVKEVDDTAMAFRLLRLHGYNVSPSVFKNFEKDGEFFCFVGQSTQAVTGMYNLNRASQISFPGEDILQRARNFSYEFLREREAQGTLHDKWIISKDLPGEVQYTLDFPWYASLPRVEARTYIGQYGGNDDVWIGKTLYRMPIVNNATYLELAKQDFNRCQALHQHELQGLQKWFIENGLEAFGMTPEDVLRAYFLAAACIFEPNRASERLAWARVSVLANTISRHFYSDMSSMKRMERFMWSSLYEENGNVLGLEGYAKDGILARTLCQLIDLLSQETPPVREGQKCIHNLIRCAWIEWMMQQINMKDGRYDKGRVMHPGSCTVHNKETCLLIAQIVEICAGRIEEAASMINNTEGSWFIQLASSICDSLHAKMLLSQDTKKNETTINQIDKEIELGMQELAQYLLPRVDDRRINNKTKQTFLSIVKSCYYAANCSPHMLDQHISEVIFEQVI
Protein: Histone H1.3 (Histone H1c) (Histone H1s-2) (P16402)
Organism: Homo sapiens (Human)
Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
Subcellular location: Nucleus. Chromosome. Note=According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin.
Interaction partners:
- Histone H1.4
- Histone H1.5
- Histone H1.2
- Histone H2A type 2-C
- Histone H2B type 2-E
- Histone H2A type 2-A
- DNA fragmentation factor subunit beta
- Testis-specific H1 histone
- Histone H1.8
- Histone H1.1
Sequence:
MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK
Protein: Putative uncharacterized protein YPL205C (Q08958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MYPFYKYIFSFWFFFLVEYVVTFRLFLSLKSGNIFLSTQQRFKDATKMCFHHQMLSSSVEPFFSLYFNHVPYMWSCFNFFSSSPFPRCTKNSPEKKKFKRGLPISSKYTDGKKR
Protein: WASH complex subunit 2 (Family with sequence similarity 21) (A1ZBW7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts at least in part as component of the WASH complex which may regulate wash nucleation-promoting factor (NPF) activity and is required for its membrane targeting during endosomal sorting.
Interaction partners:
- WASH complex subunit 4
- WASH complex subunit 3
- Vacuolar protein sorting-associated protein 35
- WASH complex subunit 1
- WASH complex subunit homolog 5
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 26
- FI18122p1
- LD13361p
- F-actin-capping protein subunit beta
Sequence:
MDISADVDQIIAQAPDWTFAGDCALLALMKRISQNLEERGERTSRNLRDFETSVKQVDIALNNATTSLRSLQFGNQFVEYRVEEVDDADLAMPEEKKKKPELPLKSSEELAKEFLENNLRMFRKNYEPVTIEVPDSDDEDGPVHSTTVFRAKNPYDAIPLPYIIGTKEWQEHKYAGLYDSKENSEDDRSEEFSSSSSDEKEPETKKIATPANKLEEQHLSDSSSLASFAREPAIVSPVINPAVQVAEPVIRTQPRPIINSQRNPHERDMFAALRQSPPSDDPPSTSSSPTSSPAFRNPSSRLPIVSTASLSSSSSSPAQQPPRLFDEAVSTQTPKEAEIKPSQTKRMPVNLFNEDEFKSFMSEIVDKVQSKTPSSSVSPATTISTKEPPKTKKPVEEYPKPGPPKQIVEQTVPKRVNLFDDSPPLSPTPRSEPVFNNTKATGAIPKRSPVVVANNDEDNSLFGSSPAMPKENPSKKPPKPVTKSLFDDDLEDDDFLSSFTPKAKPPEQKLLSKPKPSLFDDDDLDIDDIFTKPSAQPKKLSERVAGKTSLFEDDDQDDVTDLFGSKKAKVIPKETSSGVSPNKNVETPVASKKSLFDDIEDEDLFGTPKAKNLIRSEPDNDPEAVGEDKKQSEIAEQKSKNIETGEKQHQVIAENASVPILRDSPPPMEVTEQKSDDKEWEAVKDDTSAANITKSKDLFSEDLTDDELFSSTSNNMAEPKSANETNEFNKPIEKYTSQTEENVSPVNPPTKLSIKPTDLFNEDFSDDDTFLSASMSKNEPLVGTENEDIKKPSEVQLVKEIKAEELPQQLPENKIYEITAVVEKDELVPEMLSKPQIDEPVSETPPPDDYQSNVDPIISMVADVTNKTSVDTLTPRKPADLAAAQQIMQNYSNLFSDEPPDDSEFFQTLGSSGLSSLSASKIFDNEHDFFEPALPNIPSATKPSPVTPGDQPSVSSDYGAMCLFSDVPPEDNDHAGEEVQKEAEPQKDELASTTRIHTIFYDDFSETARAGAVQPAPKRFPFDDEPPPADETDRSEVKETPELQKPTSPVKKLKMPNININVHALLPGSGSVPKLIRKQESSSSERDEPQATVQTEAEAPSSGQNTVSSADGVLQHVNKSRARGPAKRRPSTRRGRKENYAKSLLDAGQNEGPTASTRDSPEVEHSERSSIKAPSPQYVKPEKLFSTPAQQIQPQLQRPPPSNTGGSFLDSPDEDDSFFNSVPTKTVEGKQGTDPPKSYRSFLDSPDADDKLFSDLENNKAGINVVPVEKKPPKMANSFLASPDEDDFLFDSVKTNATTTAQKAFAAEIMNAFQKVTTAPPKPSNAKEAAKPKSQAAPKLFDDSDDDDDDLFARAPSIQTASKPVQAKQPPKPAATSLFSSDDEEAEVPVKSAPAKKLPVKPSKSLFSDDDDDDDLFGGSSTSKAAAAKKTKPAARTASKPPASKTTTPTATIPSNSGDNPLADLLDFK
Protein: Cysteine proteinase RD21A (EC 3.4.22.-) (Protein RESPONSIVE TO DEHYDRATION 21) (RD21) (P43297)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cysteine protease that plays a role in immunity, senescence, and biotic and abiotic stresses (Probable). Involved in immunity against the necrotrophic fungal pathogen Botrytis cinerea. Involved in elicitor-stimulated programmed cell death (PCD). During infection by the necrotrophic fungal pathogen Botrytis cinerea, functions as PCD-promoting protease that is released from the ER body or vacuole to the cytoplasm. Accumulates in endoplasmic reticulum-derived bodies in epidermal cells and may participate in cell death in stressed or injured cells. Involved in water stress-induced cell death through its protease activity that is released to the cytoplasm after vacuolar collapse. Possesses protease activity in vitro and is involved in cell death in the transmitting tract and septum epidermis during flower development. Possesses peptide ligase activity. Can ligate peptides to unmodified N-termini of acceptor proteins. Probably ligates through a thioester intermediate.
Subcellular location: Vacuole {ECO:0000269|PubMed:11577182, ECO:0000269|PubMed:11743107, ECO:0000269|PubMed:23398119}. Golgi apparatus {ECO:0000269|PubMed:22396764}. Cytoplasm, Stress granule {ECO:0000269|PubMed:26978070}. Cytoplasm, P-body {ECO:0000269|PubMed:26978070}. Note=Specifically accumulates in body structures that directly bud from the endoplasmic reticulum and fuse with the vacuole (PubMed:11577182). Passes through the Golgi on its route to the vacuole (PubMed:22396764). {ECO:0000269|PubMed:11577182, ECO:0000269|PubMed:22396764}.
Interaction partners:
- UPF0235 protein At5g63440
- Zinc finger CCCH domain-containing protein 61
- Developmentally-regulated G-protein 3
- Mitochondrial succinate-fumarate transporter 1
- DNA polymerase epsilon subunit B
- Serpin-ZX
- Protein disulfide isomerase-like 1-1
- At1g49170
- Kunitz trypsin inhibitor 2
- Citrate synthase 3, peroxisomal
Sequence:
MGFLKPTMAILFLAMVAVSSAVDMSIISYDEKHGVSTTGGRSEAEVMSIYEAWLVKHGKAQSQNSLVEKDRRFEIFKDNLRFVDEHNEKNLSYRLGLTRFADLTNDEYRSKYLGAKMEKKGERRTSLRYEARVGDELPESIDWRKKGAVAEVKDQGGCGSCWAFSTIGAVEGINQIVTGDLITLSEQELVDCDTSYNEGCNGGLMDYAFEFIIKNGGIDTDKDYPYKGVDGTCDQIRKNAKVVTIDSYEDVPTYSEESLKKAVAHQPISIAIEAGGRAFQLYDSGIFDGSCGTQLDHGVVAVGYGTENGKDYWIVRNSWGKSWGESGYLRMARNIASSSGKCGIAIEPSYPIKNGENPPNPGPSPPSPIKPPTQCDSYYTCPESNTCCCLFEYGKYCFAWGCCPLEAATCCDDNYSCCPHEYPVCDLDQGTCLLSKNSPFSVKALKRKPATPFWSQGRKNIA
Protein: POU domain, class 3, transcription factor 2 (Brain-specific homeobox/POU domain protein 2) (Brain-2) (Brn-2) (Nervous system-specific octamer-binding transcription factor N-Oct-3) (Octamer-binding protein 7) (Oct-7) (Octamer-binding transcription factor 7) (OTF-7) (P56222)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that plays a key role in neuronal differentiation (By similarity). Binds preferentially to the recognition sequence which consists of two distinct half-sites, ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0, 2, or 3 nucleotides. Acts as a transcriptional activator when binding cooperatively with SOX4, SOX11, or SOX12 to gene promoters (By similarity). The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (By similarity). Acts downstream of ASCL1, accessing chromatin that has been opened by ASCL1, and promotes transcription of neuronal genes (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Myelin transcription factor 1-like protein
- Achaete-scute homolog 1
- Sal-like protein 2
- T-box brain transcription factor 1
- SRY-box transcription factor 2
- Neurogenin 2
- BCL11 transcription factor B
- Paired box protein Pax-6
- Neurogenic differentiation factor 1
- DNA-binding protein SATB
Sequence:
MATAASNHYSLLTSSASIVHAEPPGGMQQGAGGYREAQSLQVQGDYGALQSNGHPLSHAHWITALSHGGSGGGGGGGGGGGGGGGGGGDGSPWSTSPLGQPDIKPSVVVQQGGRGDELHGPGALQQQHQQQQQQQQQQQQQQQQQQQQQQQRPPHLVHHAANNHPGPGAWRSAAAAAHLPPSMGASNGGLLYSQPSFTVNGMLGAGGQPAGLHHHGLRDAHDEPHHADHHPHPHSHPHQQPPPPPPPQGPPGHPGAHHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSSGSPTSIDKIASQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITSLADSLQLEKEVVRVWFCNRRQKEKRMTPPGGTLPGAEDVYGGSRDTPPHHGVQTPVQ