wanglab/gogpt-training-data huggingface dataset:
Protein: Protein TORMOZ EMBRYO DEFECTIVE (Q9LFE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein involved in the regulation of cell division planes during embryogenesis which defines cell patterning, especially longitudinal division planes of the proembryo, probably via the regulation of embryo patterning genes expression patterns.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:17616738}. Nucleus, nucleolus {ECO:0000269|PubMed:17616738}.
Interaction partners:
- U3 small nucleolar ribonucleoprotein protein IMP3
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- U3 small nucleolar RNA-associated protein 18 homolog
- WD repeat-containing protein PCN
- Transducin family protein / WD-40 repeat family protein
- Uncharacterized protein At3g06530
- Protein SLOW WALKER 1
- Nucleolar protein
- Putative U3 small nucleolar ribonucleoprotein
- At4g28200
Sequence:
MAPHSLKKNYRCSRSLKQFYGGGPFIVSSDGSFIACACGDVINIVDSTDSSVKSTIEGESDTLTALALSPDDKLLFSAGHSRQIRVWDLETLKCIRSWKGHEGPVMGMACHASGGLLATAGADRKVLVWDVDGGFCTHYFRGHKGVVSSILFHPDSNKNILISGSDDATVRVWDLNAKNTEKKCLAIMEKHFSAVTSIALSEDGLTLFSAGRDKVVNLWDLHDYSCKATVATYEVLEAVTTVSSGTPFASFVASLDQKKSKKKESDSQATYFITVGERGVVRIWKSEGSICLYEQKSSDITVSSDDEESKRGFTAAAMLPSDHGLLCVTADQQFFFYSVVENVEETELVLSKRLVGYNEEIADMKFLGDEEQFLAVATNLEEVRVYDVATMSCSYVLAGHKEVVLSLDTCVSSSGNVLIVTGSKDKTVRLWNATSKSCIGVGTGHNGDILAVAFAKKSFSFFVSGSGDRTLKVWSLDGISEDSEEPINLKTRSVVAAHDKDINSVAVARNDSLVCTGSEDRTASIWRLPDLVHVVTLKGHKRRIFSVEFSTVDQCVMTASGDKTVKIWAISDGSCLKTFEGHTSSVLRASFITDGTQFVSCGADGLLKLWNVNTSECIATYDQHEDKVWALAVGKKTEMIATGGGDAVINLWHDSTASDKEDDFRKEEEAILRGQELENAVLDAEYTKAIRLAFELCRPHKVFELFSGLCRKRDSDEQIVKALQGLEKEEFRLLFEYVREWNTKPKLCHIAQFVLYKTFNILPPTEIVQVKGIGELLEGLIPYSQRHFSRIDRFVRSSFLLDYTLGEMSVIDPETVETEYPKDEKKKEKDVIAAMEQDTDELKQETPSRKRKSQKSKGKSNKKRLIAEAQGSVIAV
Protein: Solute carrier family 15 member 2 (Kidney H(+)/peptide cotransporter) (Oligopeptide transporter, kidney isoform) (Peptide transporter 2) (Q9ES07)
Organism: Mus musculus (Mouse)
Function: Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Can also transport the aminocephalosporin antibiotic cefadroxil (By similarity). Also able to transport carnosine (By similarity). Involved in innate immunity by promoting the detection of microbial pathogens by NOD-like receptors (NLRs). Probably acts by mediating transport of bacterial peptidoglycans across the plasma membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q63424}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q16348}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11027540, ECO:0000269|PubMed:29784761}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with the cell membrane in resting macrophages and enriched in phagocytic cups and phagosomes after particle internalization. {ECO:0000250|UniProtKB:Q16348}.
Interaction partners:
Sequence:
MNPFQKNESKETLFSPVSTEEMLPGPPSPPKKSTPKLFGSSYPLSIAFIVVNEFCERFSYYGMKAVLTLYFLYFLHWNEDTSTSVYHAFSSLCYFTPILGAAIADSWLGKFKTIIYLSLVYVLGHVFKSLGAIPILGGKMLHTILSLVGLSLIALGTGGIKPCVAAFGGDQFEEEHAEARTRYFSVFYLSINAGSLISTFITPMLRGDVKCFGEDCYALAFGIPGLLMVLALVVFAMGSKMYRKPPPEGNIVAQVTKCIWFAICNRFRNRSEDIPKRQHWLDWAAEKYPKHLIMDVKALTRILFLYIPLPMFWALLDQQGSRWTLQANKMDGDLGFFVLQPDQMQVLNPFLVLVFIPLFDLVIYRLISKCGVNFSSLRKMAVGMILACLAFAVAALVEIKINGMIHPQPASQEIFLQVLNLADGEIEVTVQGNRNNPLLVESISSFQNTTHYSKLRLETKSQDLHFHLKYNNLSVHNEYSVEEKNCYQLVVHENGESLSSMLVKDTGIKPANGMTAIRFINTLHKDMNISLDANAPLSVGKDYGVSEYRTVQRGKYPAVHCETEDNVFSLNLGQLDFGTTYLFVITNITNRGLQAWKAEDIPANKLSIAWQLPQYVLVTAAEVMFSVTGLEFSYSQAPSSMKSVLQAAWLLTVAVGNIIVLIVAQFSGLVQWAEFVLFSCLLLVVCLIFSVMGYYYVPLKSEGIHEATEKQIPHIQGNMINLETKNTRL
Protein: HTLV-1 basic zipper factor (HBZ) (P0C745)
Organism: Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A) (HTLV-1)
Function: Enhances viral infectivity and persistence, and facilitates proliferation of HTLV-1-infected lymphocytes. Mechanistically, inhibits Tax-mediated viral replication and NF-kappa-B activation. Plays a role in allowing infected T-cells to escape the cytotoxic T-lymphocyte response by maintaining low levels of viral protein production. Inhibits also host EP300 histone acetyltransferase (HAT) activity, reducing levels of acetylated histone H3 at 'Lys-18' (H3K18ac) in infected cells. Contributes to the accumulation of chromosomal abnormalities by inhibiting double-stranded DNA breaks (DSB) repair through the NHEJ pathway. Participates in the modulation of host immune response at multiple levels contributing to abnormal interferon signaling and viral pathogenesis.
Subcellular location: Host nucleus {ECO:0000269|PubMed:22434882, ECO:0000269|PubMed:28768861}.
Interaction partners:
Sequence:
MVNFVSVGLFRCLPVPCPEDLLVEELVDGLLSLEEELKDKEEEETVLDGLLSLEEESRGRLRRGPPGGKAPPRGETHRDRQRRAEEKRKRKKEREKEEEKQIAEYLKRKEEEKARRRKRAEEKAADFARRKQEEQERRERKWRQGAEKAKQHSARKEKMQELGVDGYTRQLEGEVESLEAERRRLLQEKEDLMGEVNYWQGRLEAMWLQ
Protein: E-selectin (CD62 antigen-like family member E) (Endothelial leukocyte adhesion molecule 1) (ELAM-1) (Leukocyte-endothelial cell adhesion molecule 2) (LECAM2) (CD antigen CD62E) (Q00690)
Organism: Mus musculus (Mouse)
Function: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1375914}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16581}.
Interaction partners:
- P-selectin glycoprotein ligand 1
- Golgi apparatus protein 1
- CD44 antigen
- Leukosialin
- L-selectin
- Integrin beta-2
- Cadherin-5
- Alpha-
- Platelet endothelial cell adhesion molecule
- Vascular cell adhesion protein 1
Sequence:
MNASRFLSALVFVLLAGESTAWYYNASSELMTYDEASAYCQRDYTHLVAIQNKEEINYLNSNLKHSPSYYWIGIRKVNNVWIWVGTGKPLTEEAQNWAPGEPNNKQRNEDCVEIYIQRTKDSGMWNDERCNKKKLALCYTASCTNASCSGHGECIETINSYTCKCHPGFLGPNCEQAVTCKPQEHPDYGSLNCSHPFGPFSYNSSCSFGCKRGYLPSSMETTVRCTSSGEWSAPAPACHVVECEALTHPAHGIRKCSSNPGSYPWNTTCTFDCVEGYRRVGAQNLQCTSSGIWDNETPSCKAVTCDAIPQPQNGFVSCSHSTAGELAFKSSCNFTCEQSFTLQGPAQVECSAQGQWTPQIPVCKAVQCEALSAPQQGNMKCLPSASGPFQNGSSCEFSCEEGFELKGSRRLQCGPRGEWDSKKPTCSAVKCDDVPRPQNGVMECAHATTGEFTYKSSCAFQCNEGFSLHGSAQLECTSQGKWTQEVPSCQVVQCPSLDVPGKMNMSCSGTAVFGTVCEFTCPDDWTLNGSAVLTCGATGRWSGMPPTCEAPVSPTRPLVVALSAAGTSLLTSSSLLYLLMRYFRKKAKKFVPASSCQSLQSFENYHVPSYNV
Protein: Galactolipase DONGLE, chloroplastic (EC 3.1.1.26) (EC 3.1.1.32) (Phospholipase A1 DONGLE) (Phospholipase A1-Ialpha1) (Q9MA46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sn-1-specific phospholipase that releases free fatty acids from phosphatidylcholine. Has a higher galactolipase activity than phospholipase A1 activity when digalactosyldiacylglycerol (DGDG) is used as substrate. Catalyzes the initial step of jasmonic acid biosynthesis. Required for the biosynthesis of basal-level endogenous jasmonate in vegetative tissues. Regulates leaves growth. Not essential for jasmonate biosynthesis after wounding or upon pathogen infection.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:20348210}. Note=PubMed:20348210 shows a localization in lipid droplets.
Interaction partners:
- Phospholipase A I
- AICARFT/IMPCHase bienzyme family protein
- Protein DETOXIFICATION 43
Sequence:
MAAKVFTQNPIYSQSLVRDKTPQQKHNLDHFSISQHTSKRLVVSSSTMSPPISSSPLSLPSSSSSQAIPPSRAPAVTLPLSRVWREIQGSNNWENLIEPLSPILQQEITRYGNLLSASYKGFDLNPNSKRYLSCKYGKKNLLKESGIHDPDGYQVTKYIYATPDINLNPIKNEPNRARWIGYVAVSSDESVKRLGRRDILVTFRGTVTNHEWLANLKSSLTPARLDPHNPRPDVKVESGFLGLYTSGESESKFGLESCREQLLSEISRLMNKHKGEEISITLAGHSMGSSLAQLLAYDIAELGMNQRRDEKPVPVTVFSFAGPRVGNLGFKKRCEELGVKVLRITNVNDPITKLPGFLFNENFRSLGGVYELPWSCSCYTHVGVELTLDFFDVQNISCVHDLETYITLVNRPRCSKLAVNEDNFGGEFLNRTSELMFSKGRRQALHFTNAATNAAYLLCSISNHMLYYNIF
Protein: Protein DETOXIFICATION (Multidrug and toxic compound extrusion protein) (F4JTB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDPTAPLLTHGGEVEEDYAPARSWTDVKRVLSTESAKLWMIAAPVGFNIICQYGVSSVTNIFVGHIGEVELSAVSISLSVIGTFSFGFLLGMGSALETLCGQAYGAGQVNMLGVYMQRSWIILFVSCFFLLPIYIFATPVLRLLGQAEEIAVPAGQFTLLTIPQLFSLAFNFPTSKFLQAQSKVVAIAWIGFVALSLHVIMLWLFIIEFGWGTNGAALAFNITNWGTAIAQIVYVIGWCNEGWTGLSWLAFKEIWAFVRLSIASAVMLCLEIWYMMSIIVLTGRLDNAVIAVDSLSICMNINGLEAMLFIGINAAISVRVSNELGLGRPRAAKYSVYVTVFQSLLIGLVFMVAIIIARDHFAIIFTSSKVLQRAVSKLAYLLGITMVLNSVQPVVSGVAVGGGWQGLVAYINLGCYYIFGLPFGYLLGYIANFGVMGLWSGMIAGTALQTLLLLIVLYKTNWNKEVEETMERMKKWGGSETTSKDILASGWPSGLRRQTQVLVFVRGRGFKPHF
Protein: Sister chromatid cohesion protein PDS5 homolog B (Androgen-induced proliferation inhibitor) (Androgen-induced prostate proliferative shutoff-associated protein AS3) (Q9NTI5)
Organism: Homo sapiens (Human)
Function: Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin. May couple sister chromatid cohesion during mitosis to DNA replication. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Plays a role in androgen-induced proliferative arrest in prostate cells.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
Interaction partners:
- Wings apart-like protein homolog
- Double-strand-break repair protein rad21 homolog
- Structural maintenance of chromosomes protein 1A
- Structural maintenance of chromosomes protein 3
- Cohesin subunit SA-2
- Cohesin subunit SA-1
- Sororin
- Nipped-B-like protein
- Sister chromatid cohesion protein PDS5 homolog A
- Breast cancer type 2 susceptibility protein
Sequence:
MAHSKTRTNDGKITYPPGVKEISDKISKEEMVRRLKMVVKTFMDMDQDSEEEKELYLNLALHLASDFFLKHPDKDVRLLVACCLADIFRIYAPEAPYTSPDKLKDIFMFITRQLKGLEDTKSPQFNRYFYLLENIAWVKSYNICFELEDSNEIFTQLYRTLFSVINNGHNQKVHMHMVDLMSSIICEGDTVSQELLDTVLVNLVPAHKNLNKQAYDLAKALLKRTAQAIEPYITNFFNQVLMLGKTSISDLSEHVFDLILELYNIDSHLLLSVLPQLEFKLKSNDNEERLQVVKLLAKMFGAKDSELASQNKPLWQCYLGRFNDIHVPIRLECVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVSIVTAAKKDILLVNDHLLNFVRERTLDKRWRVRKEAMMGLAQIYKKYALQSAAGKDAAKQIAWIKDKLLHIYYQNSIDDRLLVERIFAQYMVPHNLETTERMKCLYYLYATLDLNAVKALNEMWKCQNLLRHQVKDLLDLIKQPKTDASVKAIFSKVMVITRNLPDPGKAQDFMKKFTQVLEDDEKIRKQLEVLVSPTCSCKQAEGCVREITKKLGNPKQPTNPFLEMIKFLLERIAPVHIDTESISALIKQVNKSIDGTADDEDEGVPTDQAIRAGLELLKVLSFTHPISFHSAETFESLLACLKMDDEKVAEAALQIFKNTGSKIEEDFPHIRSALLPVLHHKSKKGPPRQAKYAIHCIHAIFSSKETQFAQIFEPLHKSLDPSNLEHLITPLVTIGHIALLAPDQFAAPLKSLVATFIVKDLLMNDRLPGKKTTKLWVPDEEVSPETMVKIQAIKMMVRWLLGMKNNHSKSGTSTLRLLTTILHSDGDLTEQGKISKPDMSRLRLAAGSAIVKLAQEPCYHEIITLEQYQLCALAINDECYQVRQVFAQKLHKGLSRLRLPLEYMAICALCAKDPVKERRAHARQCLVKNINVRREYLKQHAAVSEKLLSLLPEYVVPYTIHLLAHDPDYVKVQDIEQLKDVKECLWFVLEILMAKNENNSHAFIRKMVENIKQTKDAQGPDDAKMNEKLYTVCDVAMNIIMSKSTTYSLESPKDPVLPARFFTQPDKNFSNTKNYLPPEMKSFFTPGKPKTTNVLGAVNKPLSSAGKQSQTKSSRMETVSNASSSSNPSSPGRIKGRLDSSEMDHSENEDYTMSSPLPGKKSDKRDDSDLVRSELEKPRGRKKTPVTEQEEKLGMDDLTKLVQEQKPKGSQRSRKRGHTASESDEQQWPEEKRLKEDILENEDEQNSPPKKGKRGRPPKPLGGGTPKEEPTMKTSKKGSKKKSGPPAPEEEEEEERQSGNTEQKSKSKQHRVSRRAQQRAESPESSAIESTQSTPQKGRGRPSKTPSPSQPKKNVRVGRSKQAATKENDSSEEVDVFQGSSPVDDIPQEETEEEEVSTVNVRRRSAKRERR
Protein: Calpain-like cysteine peptidase, putative (Q57UN7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDITYENGSPTYTGNTVLKCFRENGNGLLFRIVNDEEKKWAFYNDTKDYNMVVKVAFGKDSTVQPLGNTKMEKDTATGEFKCEVKIAPLATEMFIEGVPNGYKISYEADPIPQWKSVPT
Protein: Zinc finger protein 275 (Q9NSD4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMSHPCVSLLGVPVLNPALVPHLAQGQVLLVSDPSPNTDPAKYSESTSATRHQMKGEDAQPQEMASTSFPRASGPSPEFRQHGDSDGKRGSPQNLPIEHHFACKECGDTFRLKVLLVQHQRVHSEEKGWECGDCGKVFRGVAEFNEHRKSHVAAEPQPGPSRALENAAEKREQMEREAKPFECEECGKRFKKNAGLSQHLRVHSREKPFDCEECGRSFKVNTHLFRHQKLHTSEKPFACKACSRDFLDRQELLKHQRMHTGHLPFDCDDCGKSFRGVNGLAEHQRIHSGAKPYGCPHCGKLFRRSSELTKHRRIHTGEKPYACGQCGKAFRQSSSLLEHARIHSGERPYACGECGKAFRGPSDLIKHRRIHSGLKPYECDKCGKAFRRSSGLSRHRRIHSGARRCECSQCGRVFKRRSALQKHQPTHHE
Protein: COP9 signalosome complex subunit 2 (Signalosome subunit 2) (Q5B3U7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 7
- Uncharacterized protein
- RING-box protein 1
- Ubiquitin-like domain-containing protein
- Ubiquitin ligase subunit CulD, putative
Sequence:
MSDDDDFMHDSADEEYDFEYEDADDDETGDIGIENKYYNAKQIKVDNPEEAIDEFLGVPALEQDKGDWGFKGLKQAIKLEFKLGRYSDAVEHYRELLTYVKSAVTRNYSEKSINNMLDYIEKGSDDEKAYQCMEEFYSLTLNSFQNTNNERLWLKTNIKLARLWLERREYGQLSKKVRELHRACQREDGSDDPSKGTYLLELYALEIQMYAETKNNKRLKALYQRALRVRSAVPHPKIMGIIRECGGKMHMSEENWEEAQSDFFESFRNYDEAGSMQRIQVLKYLVLTTMLMKSDINPFHSQETKPYKTDPRISAMTDLVDAFQRDDIHAYEEVLSKNPDVLADPFIAENIDEVSRNMRTKAILKLIAPYTRFTLSFISKHIKISVTEAQDILSFLILDKKLNAKIDQESGTVVVESASDVERLRSVEEWNESLRTLWQVTLKDGDGFKNDDVSQPTGIGMRGPLLYQSGLDDDTAGLLRSSGHRFRRGGKGSKAGGGLGMKTGLF
Protein: F-actin-capping protein subunit beta (P13517)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:1315784}. Bud {ECO:0000269|PubMed:1315784}. Bud tip {ECO:0000269|PubMed:1315784}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9HGP5}. Note=Found at cortical actin spots at the site of bud emergence and at the tips of growing buds and shmoos.
Interaction partners:
- F-actin-capping protein subunit alpha
- Twinfilin-1
- Fimbrin
- Actin-binding protein
- Nuclear migration protein JNM1
- Actin-interacting protein 1
- Thiamine biosynthesis regulatory protein
- Endoplasmic reticulum membrane protein complex subunit 10
- Actin
- Cofilin
Sequence:
MSDAQFDAALDLLRRLNPTTLQENLNNLIELQPNLAQDLLSSVDVPLSTQKDSADSNREYLCCDYNRDIDSFRSPWSNTYYPELSPKDLQDSPFPSAPLRKLEILANDSFDVYRDLYYEGGISSVYLWDLNEEDFNGHDFAGVVLFKKNQSDHSNWDSIHVFEVTTSPSSPDSFNYRVTTTIILHLDKTKTDQNSHMMLSGNLTRQTEKDIAIDMSRPLDVIFTSHVANLGSLIEDIESQMRNLLETVYFEKTRDIFHQTKNAAIASSAEEANKDAQAEVIRGLQSL
Protein: Lysine-specific demethylase JMJ15 (EC 1.14.11.-) (Jumonji domain-containing protein 15) (AtJMJ15) (Protein JUMONJI 15) (Lysine-specific histone demethylase JMJ15) (Protein MATERNAL EFFECT EMBRYO ARREST 27) ([histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ15) (O64752)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3. No activity on H3K4me2, H3K4me1, H3K9me3/2, H3K27me3/2 and H3K36me3/2. Involved in the control of flowering time by demethylating H3K4me3 at the FLC locus and repressing its expression. The repression of FLC level and reduction in H3K4me3 at the FLC locus results in induction of the flowering activator FT, which is a downstream target of FLC. Promotes salt tolerance by down-regulating the expression of several transcriptions factors involved in stress responses via H3K4me3 and H3K4me2 demethylation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit O, mitochondrial
- ATPase, F1 complex, OSCP/delta subunit protein
- ATP synthase subunit delta, chloroplastic
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- ATP synthase subunit a-1
- ATP synthase subunit a-2
- ATP synthase subunit a.
- ATP synthase subunit a, chloroplastic
Sequence:
MEPFSAAQNKEDKDTSVEPPRRRCHRKNKGTNVEPPSSPYHPKVLARWDPANEKRPDIGEAPVFHPTSEEFEDTLAYIEKIRPLAESFGICRIVPPSNWSPPCRLKGDSIWKNKNFPTRVQFVDLLQNRGPVKKKTPKGRKRKRGKYSRTVAPKKRNGSVSKSVSTPKATEEENFGFESGPEFTLEKFEKYAQDFKDSYFERKDNVGDPSVEEIEGEYWRIIEKETNEVKVLYGTDLENPILGSGFSKGVKIPTRRNDMDKYISSGWNLNNLARLQGSLLSFEDCEISGVQVPWLYVGMCFSTFCWHVEDNHLYSLNYHHFGEPKVWYGVPGSHATGLEKAMRKHLPDLFDEQPDLLHELVTQFSPTILKNEGVPVYRAVQNAGEYVLTFPRAYHSGFNCGFNCAEAVNVAPVDWLAHGQNAVEIYSQETRKTSLSHDKILLGAAFEAVKSLSAHGEDNTKRFSWKRFCGKDGIITKAIEARLRMEEKRIEALGNGFSLVKMDKDFDSNCERECISCFSDLHLSATGCKNCSSLEEYGCTKHDICSCEGKDRFIFLRYTIDELSSLVRALEGESDDLKAWLSKVMEGCSETQKGESSGIIVKEKQVQEECFDLNGECNKSSEICEDASIMDLAAYHVEPINLGFLVVGKLWCNKHAIFPKGFKSRVKFYNVQDPMRISYYVSEIVDAGLLGPLFKVTLEESQDESFSYASPQKCWEMVLLRVKEEIMRRSNQKQDVHMLESIDGLKMFGFRSPFIVQATEALDPNHGQVEYWNHKNEKDSLEMKDCFMSNSSQSLSKARLFGVDLN
Protein: Solute carrier family 25 member 20 (C9JPE1)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFRKTLFREIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDVPASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPNL
Protein: Cilia- and flagella-associated protein 20 (Basal body up-regulated protein 22) (Bug22p) (Flagellar-associated protein 20) (A8IU92)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the control of flagellar beating in an asymmetric and planar waveform. Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6. Not essential for flagellar assembly.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9Y6A4}. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes predominantly along the length of all nine axonemal outer doublet microtubules (DMTs). Localizes to the inner junction (IJ) between A- and B-tubules of the DMTs. Associates to the basal bodies in a microtubule-dependent manner. Enters into the flagella through diffusion.
Interaction partners:
Sequence:
MFKNAFQSGFLSVLYSIGSKPLEIWDKQVSNGHIKRITDADIQSSVLEIMGQNVSTTYITCPADPNKTLGIKLPFLVLIIKNLNKYFSFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDSGWNQIQFNLSDFTRRAYGTNYIETLRVQVHANCRIRRIYFSDRLYSEEELPAEFKLFLPIQKS
Protein: ATPase AAA-type core domain-containing protein (Q386H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- IST1 homolog
Sequence:
MSSLTCEELYRRALDDLTAIWREDVNVSKMKVMPTGRQRYDQLLLCWASLYVQYLRTGRRLVIVHDAQLQPQKRYDVRTVLDACMARMLELRALLSTNCGEFVKLDECILDLKMTPDELEVPIPRYFVEDNASVMQERRRQIASLQQYYKETEPDAPVTKALTASSVPPQKKSTEAAAGNVMSMDEALMLLKINERGRQARERAKFQLSMYAQKRHSVELASVYNHPTGRERAATVLQSAVQAYLTRKHIFSDHQEELQLLGMAPSADSTNREEAVQAEARLDEQKARQRMNEANFRQKTLEIESRIKTEEGPRTMELMLNEALTRMAYARMEGKDDQGMLQAADVSGSRRLADSSNQAGSLAPIITDSFRSPAPNISGTFPSAGGTGNDARNAMRRTGSVSARRRGEEDETVPAMPPSVLWETIRAEDERYSSLWKPRFEQTYVREVDLEQSADLVLLRQQLLEGPRGVMEELRHVVDELILMEVENLKKRLEQERRSGKRKGAKKKKGPRKPRAPKLKDPTKGSTVETLMNTAVHQNVLKLPDSEVVLSGYLGCVAVHESPLDALLRAQKPDDDMRKKWQRILNNWDANVEKVMKMKKDAFQKVFDKYLQQSTWLAEPTAAHVRQSVTEYAILPLGSQVIHDLAPSSKTLLLYGFHGTGKTHLVHAVCNHSGANFFDLSPANFETDTGLAGIIQTVFYLAKVMAPSVIYIDNVEKLFLRKKRKGPKDPLMKRGRKMKKEVLKGIASISPTDRVIVIGCTCAPYDAEFNAMVNNFAHMVYCGCPDYASRVVVLQELAGSHTGDVWSLKPEHYHELALLTEGFTCGDISAVFEEVLTKRRLRRIEQRPLTADDFLSAVARAKPPSVEDRALMKEFTARLPLHLRRVNPIADIPLPEKETAAKKRPKKKE
Protein: Uncharacterized protein C630.12 (Q9UUH0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKVGRFLVIIAFCFYVLYLEKIIHTRPHKKCDWRSWEQWESTGNPVRIALVADPQLVDDLTYDYPRPLIGIVKWISDQFLRRHWRYLHKSLKPDITFIMGDLMDTGREFATEEFKKDYFRMMNVLDPKFTNKLEIYPGNHDIGFGNHAIVKDIQRFESLFGPTSRSIDVGNHTLVIVDGIRLSNNVNPQVYQPARDFLKSFETNKDNSRPRILLSHVPLFRPAINSCGELREKDDVIKYGLGYQYQNLLLPELSESILKAVEPIAAFAGDDHDYCEVVHNYQVDTREAATTEYNVKAFSMTSGILYPGYQLLSLNYPYDNPKADQKSSYQTKLCILPNQIQIYVWYGASISIFFALILLRTAIFFFGTDRYSLPLYKTHARRFSLSTTIHLFKKIVRITLSTFISYTWIPFLLFIFLNIFII
Protein: Farnesyl pyrophosphate synthase (NvFPPS) (NvIDS2) (EC 2.5.1.68) (Farnesyl diphosphate synthase) (A0A386JVA3)
Organism: Nezara viridula (Southern green stink bug) (Cimex viridulus)
Function: Farnesyl pyrophosphate synthase involved in pheromone biosynthesis by catalyzing the formation of (2Z,6E)-farnesyl diphosphate.
Interaction partners:
Sequence:
MPLAKLCAKKLSSPLMKLCYPNLNGKLPFSNLSNILDNSSLKFHSCNPHITCRGLSTVALRPQTITKDDKRDFMAVFPDIVRDLTQLNPGISDLSTLISKIMQYNVSGGKKVRGLTVVYSYRMLAPDHALTPENIRLAQILGWCVEMLQGFFLVIDDLADQSITRRGRPCWYRNPDVGLRAGSDALLIQSGTFQLLQQHCKDREFYIDLVELFLDAVRRTTYGQTLDHVSSFPNITHLTMDRYNFITKYKTSYYTFHLPVATAMYMAGIYNTELHRQAKSVLLEMGHYFQVQDDYLDVFGDEEVIGKIGTDIQEGKCTWLAIVAFQRASPSQREILESCYGSKDPEKIKKVKDTFIEIGVPAVFHAYEEETYNLITRQIQQLSQGLPHELFLTLLHKTYGRKQ
Protein: Small proline-rich protein 2E (SPR-2E) (Small proline-rich protein II) (SPR-II) (P22531)
Organism: Homo sapiens (Human)
Function: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane.
Subcellular location: Cytoplasm.
Interaction partners:
- Small proline-rich protein 2D
- Cornifin-B
- Small proline-rich protein 2A
- Small proline-rich protein 2G
- Small proline-rich protein 2F
- Late cornified envelope protein 3E
- Cornifin-A
- Late cornified envelope protein 3D
- Small proline-rich protein 3
- Late cornified envelope protein 1C
Sequence:
MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPCPPQQCQQKCPPVTPSPPCQPKCPPKSK
Protein: At1g71070/F23N20_6 (Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein) (Glycosyltransferase) (Q9C9A1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
- Arabinogalactan O-methyltransferase 2
Sequence:
MGAEKKWLFTLFSVVFLSVFLLLLYSISAFTSKPFPSSIRHGAHYPPAFAYYITGGRGDNDRISRLLLAVYHPRNRYLIHLGAEATDAERLALLSDLKSVPAVNAFGNVDVLGKVDRLSENGASKIASTLHAVSILLKLDPTWNWFIELSALDYPLITQDDLSHVFASVNRSLNFIDHTSDLAWKESQRIKPIVVDPALYLARRTQLFTATEKRPTPDAFKVFTGSPWIVLSRPFLEYCIFGWDNLPRILLMYFNNVILSEECYFHTVICNAPEFSNTTVNGDLRYMIWDSPPKMEPHFLTISDFDQMAQSGAAFARQFKKDDPVLDMVDREILKRGRYRVTPGAWCSSHSSWWTDPCSEWDEVNIVKAGPQAKKLDETITNFLDDLNSQSNQCK
Protein: CCAAT/enhancer-binding protein (Q7ZU07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005879}.
Interaction partners:
Sequence:
MEVAGFYEGDYLAFHSTNASSSPVSDGVCKQPVNGSMTKLHDISEHEKAIDFSIYLDSLPQYQHLASQDESHRHRALGIYSDFLSEGNKSKRAALQNYKNYISLTERDPNQLAYPELQETRIDAVFSPDFMGSFAKSNGRHEETPMDGPGGYDMRSYLPYQTAPSGSLGNISTASSSCSSPPGTPAPSGKGRSPQAGGKMTSSGKGKKRLDKDSDEYRQRRERNNLAVRKSRDKAKMRNLETQHKVLELAAENDRLQKRVEQLSRELATLRNLLSATGQC