wanglab/gogpt-training-data huggingface dataset:
Protein: CLP protease regulatory subunit CLPX1, mitochondrial (Q9FK07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates (By similarity). Can perform chaperone functions in the absence of ClpP (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11352464}.
Interaction partners:
- Chloroplastic ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease proteolytic subunit 2, mitochondrial
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 4, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 2, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 6, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 4, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 3, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
Sequence:
MAAALRSNTSRETASLTLSHFRYFIFNRIHTARTATSPPHCNHRSKSDEKFPYKISSLGTSFLDNRGGGERRNSTKCYAAQKKLSGVGSSVVILSSQGDPPDLWQPPGDGVSVRVNGSSVNLGRGGGGGGSSPGGPGNGTGSNSKEDCWGGSNLGSDFPTPKEICKGLNKFVIGQERAKKVLSVAVYNHYKRIYHESSQKRSAGETDSTAAKPADDDMVELEKSNILLMGPTGSGKTLLAKTLARFVNVPFVIADATTLTQAGYVGEDVESILYKLLTVADYNVAAAQQGIVYIDEVDKITKKAESLNISRDVSGEGVQQALLKMLEGTIVNVPEKGARKHPRGDNIQIDTKDILFICGGAFVDIEKTISERRHDSSIGFGAPVRANMRAGGVTNAAVASNLMETVESSDLIAYGLIPEFVGRFPVLVSLSALTENQLMQVLTEPKNALGKQYKKMYQMNSVKLHFTESALRLIARKAITKNTGARGLRALLESILMDSMYEIPDEGTGSDMIEAVVVDEEAVEGEGRRGSGAKILRGKGALARYLSETNSKDSPQTTKEGSDGETEVEAEIPSVVASM
Protein: NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1) (P03886)
Organism: Homo sapiens (Human)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH-ubiquinone oxidoreductase chain 6
- Cytochrome c oxidase subunit 1
Sequence:
MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEPLKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSGWASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWPLAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTTIFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLALLMWYVSMPITISSIPPQT
Protein: Uncharacterized protein YKR078W (P36158)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Carboxypeptidase Y-deficient protein 8
- PX domain-containing protein LEC1
- Sorting nexin MVP1
- Sorting nexin-41
Sequence:
MENDKASHASPSIGVNEFVVQGEISIDDSERSVKSVSVSISDDEDSKTDVQDNMATPSTRSKFQTDLAIDNRLLEKDPKYKKLFTEKRRRRRPESCINLMTKGKGTGQKDNINDQIFSLRILPGSDLNSLKDSLWIIKISTQPDVEKTIARAFSDFYWLYHQLQNNHWGKTIPPPTRSNILVEKDEFAINHLFMIRNNEKYDPIFNFKPEYIISLQLMAMIKHIFNDKVLRLDSNFIDFISWDDDLPESLQIVVDDSTFTGDKILMTSSQFRELKEFHKQSKKVESITNSHASLIPVTELTEIYISPTKLFSRKDYQRLFQPQSTDNTFNNNDPLIQEWIPKSKTLFTSLSFGSSAPTYQEASTEIQACHDWVSISKEQWKQLLYHVLQYIVDEAVKVNSVINEFTECLKQISLDEVIRANSELFLKFSKLNESFLKKFKGASRQDILKLIILFDENVRFCESFESILNQRLKLGKILSIIEVDLDKKKNFLDKLSPGNNNSNNEDLKIRTAEDEYRIVLKRYNRVKQSWEKIMEDILNERKEFEKREAAEVNSCLKSIRDLNMDEKKHYLQLWQDFVPDEHISQ
Protein: Cell wall protein IFF5 (Adhesin-like protein IFF5) (Q5A1E0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:21841123}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MKLFQNILISIALLTQLIFAIEIAENKVDRGSITLNLGDIIIYTGATWSIIDNAYTNFVGKLDVRADAGLYITSTSHLLALQVSLTTILHSITNNGIISFDSRISRTSSSYDLRGISFTNNGEMYFGSSGESSSSTSLTSASWSNTGLLSFFQNQRTSGTVNLGVSMGSITNDGQICLNNQVYEQTTQIKGSGCFTAKGDSTIYIANVVLAVSSKQNFYLTDKGSSMIVQAVSTTQTFNVYGFGDGNKIGLTLPLVGTIFNSAFTYDTASGILTLRNTLLEQKFNIGTGYEPSKFQVVTDSGSGTPSTVLGSVAYYGHVPTRTLPKSCQIPCKPIPKAPGTQPTEYTTTITKTNTAGNTVTETGVVNISTDKAGSWFTTTSIFPTLTTAIAAPTSTAMSTDLSSSVNIPVETSSNESSSITLASSESSAVQTSSIEIPVSSHISANQESSSIGESSVNGSTMISSESALESASEFTIAQSSDVESYSSSEHSITHESSAITSSSTTIETHVTESSVVVDSFTSDSLFVSETQDPKASSFSIVTPSDSIIVNESSIPELSTSVGAVSTSTSSSEISSNSYFPSETHISKVSSSAEPTFVTPSESIIINISEPAVSTDSVQPSTEPQPDMSSVIAESLISSTVSASEIELSSTMELSHSESLLAKQSETINQSESNYISETSAVPTAKSTISDSKLTSTWESSSLVNMESTYSVVISESEITPIPVHTSESATESAAESSDIQTQFTSTWTATKSDGSFVTESGVISQSGTSFTTIATFPPLYTSSDITTEFISTWTATNSDGSVTTEIGVVSQSGTSLTTIATFPPSSTESGITSEFISTWTTTSSDGSVATKSGVVIQSGTSLTTIATFPPMSTSSDIITEFTSTWTTTNSDGSITTESGIVSQSGTSLTTLTIFEPVTSLAVPSYTVIETEFTSTWTTTKSDGSIVTGSGIVSQSGTSLTTLSTFAPSSSSSEIAPEFTSTWEIGSSNESNVVESSIVNQSNESLTNSVSSYEPATESAIVSPSDQVLTSSATSFVSASEFSAVTTTTVDSASASSSTDINNDVTVLVSPSESEINTSSSIWNNENNVSGAVSTSESTSIANNHDGSLSMTKTESEINGFYSTESSTMFVTATITSCNKSDCFENVVTYVSNDSYTTVTTGHSNDNTSVDNNNVPSTLIENVSNTETIPVVTNTEEVSTTVYNPLTSTSTSNIVESSNTSIVDNENNGVHINSDDMTAMVTAVETGNGITNGTNFVSPSTIPNEISETGSPATSIVGTLPYENGSNQLSIENIKYLILVVFGLMMIM
Protein: Calpain-11 (EC 3.4.22.-) (Calcium-activated neutral proteinase 11) (CANP 11) (Q9UMQ6)
Organism: Homo sapiens (Human)
Function: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}.
Interaction partners:
- Calpastatin
- Calpain small subunit 1
Sequence:
MLYSPGPSLPESAESLDGSQEDKPRGSCAEPTFTDTGMVAHINNSRLKAKGVGQHDNAQNFGNQSFEELRAACLRKGELFEDPLFPAEPSSLGFKDLGPNSKNVQNISWQRPKDIINNPLFIMDGISPTDICQGILGDCWLLAAIGSLTTCPKLLYRVVPRGQSFKKNYAGIFHFQIWQFGQWVNVVVDDRLPTKNDKLVFVHSTERSEFWSALLEKAYAKLSGSYEALSGGSTMEGLEDFTGGVAQSFQLQRPPQNLLRLLRKAVERSSLMGCSIEVTSDSELESMTDKMLVRGHAYSVTGLQDVHYRGKMETLIRVRNPWGRIEWNGAWSDSAREWEEVASDIQMQLLHKTEDGEFWMSYQDFLNNFTLLEICNLTPDTLSGDYKSYWHTTFYEGSWRRGSSAGGCRNHPGTFWTNPQFKISLPEGDDPEDDAEGNVVVCTCLVALMQKNWRHARQQGAQLQTIGFVLYAVPKEFQNIQDVHLKKEFFTKYQDHGFSEIFTNSREVSSQLRLPPGEYIIIPSTFEPHRDADFLLRVFTEKHSESWELDEVNYAEQLQEEKVSEDDMDQDFLHLFKIVAGEGKEIGVYELQRLLNRMAIKFKSFKTKGFGLDACRCMINLMDKDGSGKLGLLEFKILWKKLKKWMDIFRECDQDHSGTLNSYEMRLVIEKAGIKLNNKVMQVLVARYADDDLIIDFDSFISCFLRLKTMFTFFLTMDPKNTGHICLSLEQWLQMTMWG
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (G8B6C6)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSLTEDKMVNTKEEIEYIATEDESGLSEEHKQYLIAKHGTYDLVPLPSMNDDDPLNWSNGFKHLQLAMVAFHAFMATFMASGLVPVIGMYSEIYQMSTPDVAYLVSVQIVLIGGFPLLWVPLMERYGKRLLLIISTLGTMCFSLGSVFSTTYGTMMAMRCLQAIFISPGLAVGGAVVNETTFSHQRGSRSGIWAIAVNLGTMVGALLMGIVAQHQDPKYIHVVFTCINFGQVVCYVFFGKESLYNHKDLSRNETNRFKQLRFRAIFPENRITLKDTFYPMVFFTNWRIFIPTFAYSMCFLHGNIALNIEIPEVMYIKFGLGPQALGLQFISFIVGAAIGEVGGYMSDKLVAWGQKRGRGPSFRLWITYPGFATCIIGLVVFGVQIDAATSWNVTPLIGCALASFGLQIMTSPFIAYCIDMDHKQAGAIILFITVVRQTLAFIGPFYFPVMFAKLGFTVAYSVMAGIIAGLAFIPTLVLQIKDAKSGK
Protein: Alpha-parvin (Actopaxin) (CH-ILKBP) (Calponin-like integrin-linked kinase-binding protein) (Matrix-remodeling-associated protein 2) (Q9NVD7)
Organism: Homo sapiens (Human)
Function: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishment of cell polarity, cell adhesion, cell spreading, and directed cell migration.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:11331308, ECO:0000269|PubMed:35259013}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}.
Interaction partners:
- Paxillin
- Scaffold protein ILK
- LIM and senescent cell antigen-like-containing domain protein 1
- Ras suppressor protein 1
- Beta-parvin
- LIM and senescent cell antigen-like-containing domain protein 2
- Dual specificity testis-specific protein kinase 1
- Actin, cytoplasmic 1
- Vinculin
- Talin-2
Sequence:
MATSPQKSPSVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSELQEEGMNAINLPLSPIPFELDPEDTMLEENEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRNVE
Protein: FI24210p1 (Usf, isoform B) (Usf, isoform C) (Q9W4J8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LP12374p
- histone acetyltransferase
- Net, isoform B
- Transcription factor btd
- Mediator of RNA polymerase II transcription subunit 1
- Taiman, isoform G
- 14-3-3 protein zeta
- 14-3-3 protein epsilon
- Max-binding protein MNT
- CCAAT/enhancer-binding protein
Sequence:
MNVHKRPRLNMEFGSSTSNTNTSTSPSSVNISNANPTAGPGLMTITNHHTADLSEALVHSSFANGQQSLILTSDTGNPLMNSQGAQIFLTICGDENSDDSQEYYTIKQEPGCDLDIHSLLPSNLQLPNNLQLPTGCEIYLVKETGSLMGEPPTKAAIKLELDTLSEKPLLPSVTTSSSTQSAVITAQTVNPPIPGNINTTTSTTSTTTTTSVLYGSHGNGHGHGHAHAQARSQPESAGQTPSSKLEAYKKRDDKRRATHNEVERRRRDKINSWIFKLKEMLPSLSSSSSFSEASTSPSTSGSTSTNGSSHSKGNASSSSGRAPPNDSKSQILIKACEYIKSMQGEIDTLRDCLRETDSLRASNQALREELDRLKRQQQLQERFHTAGGRSTFNVTLNSLNSSATSDLFEGIDTTPNLAAVSSLGFGKRGLLISDFDE
Protein: Alpha-xylosidase 1 (EC 3.2.1.177) (Q9S7Y7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycoside hydrolase releasing xylosyl residues from xyloglucan oligosaccharides at the non-reducing end. Has alpha-xylosidase activity against xylan oligosaccharides. Also has alpha-glucosidase activity against p-nitrophenyl-alpha-D-glucopyranoside. No activity against p-nitrophenyl-D-xyloside.
Subcellular location: Secreted, cell wall. Secreted, extracellular space, apoplast.
Interaction partners:
- Alpha-L-fucosidase 2
- Beta-galactosidase 10
- Prolyl endopeptidase
- F-box protein At1g67130
- Alpha-L-fucosidase 3
- Glycosyl transferase family 1 protein
- 11-beta-hydroxysteroid dehydrogenase-like 2
- Nucleotide binding protein
- Glucosidase 2 subunit beta
- Berberine bridge enzyme-like 26
Sequence:
MASSSSSLAFSLSLLLALILCFSPTQSYKTIGKGYRLVSIEESPDGGFIGYLQVKQKNKIYGSDITTLRLFVKHETDSRLRVHITDAKQQRWEVPYNLLPREQPPQVGKVIGKSRKSPITVQEISGSELIFSYTTDPFTFAVKRRSNHETLFNTTSSLVFKDQYLEISTSLPKEASLYGLGENSQANGIKLVPNEPYTLYTEDVSAINLNTDLYGSHPMYMDLRNVGGKAYAHAVLLLNSNGMDVFYRGDSLTYKVIGGVFDFYFIAGPSPLNVVDQYTQLIGRPAPMPYWSLGFHQCRWGYHNLSVVEDVVDNYKKAKIPLDVIWNDDDHMDGHKDFTLNPVAYPRAKLLAFLDKIHKIGMKYIVINDPGIGVNASYGTFQRAMAADVFIKYEGKPFLAQVWPGPVYFPDFLNPKTVSWWGDEIKRFHDLVPIDGLWIDMNEVSNFCSGLCTIPEGKQCPSGEGPGWVCCLDCKNITKTRWDDPPYKINATGVVAPVGFKTIATSATHYNGVREYDAHSIYGFSETIATHKGLLNVQGKRPFILSRSTFVGSGQYAAHWTGDNQGTWQSLQVSISTMLNFGIFGVPMVGSDICGFYPQPTEELCNRWIEVGAFYPFSRDHANYYSPRQELYQWDTVADSARNALGMRYKILPFLYTLNYEAHMTGAPIARPLFFSFPEYTECYGNSRQFLLGSSFMISPVLEQGKTEVEALFPPGSWYHMFDMTQAVVSKNGKRVTLPAPLNFVNVHLYQNTILPTQQGGLISKDARTTPFSLVIAFPAGASEGYATGKLYLDEDELPEMKLGNGQSTYVDFYASVGNGTMKMWSQVKEGKFALSKGWVIEKVSVLGLRGAGQVSEIQINGSPMTKKIEVSSKEHTYVIGLEDEEENKSVMVEVRGLEMLVGKDFNMSWKMGIN
Protein: Flavonol 3-O-glucosyltransferase UGT71C4 (EC 2.4.1.91) (Flavonol 7-O-beta-glucosyltransferase UGT71C4) (EC 2.4.1.237) (UDP-glycosyltransferase 71C4) (Q9LML6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses quercetin 3-O-glucosyltransferase and 7-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives.
Interaction partners:
- Mucin-like protein
- Hydroxyproline-rich glycoprotein family protein
- F-box/kelch-repeat protein At1g55270
- At2g29210/F16P2.41
Sequence:
MVKETELIFIPVPSTGHILVHIEFAKRLINLDHRIHTITILNLSSPSSPHASVFARSLIASQPKIRLHDLPPIQDPPPFDLYQRAPEAYIVKLIKKNTPLIKDAVSSIVASRRGGSDSVQVAGLVLDLFCNSLVKDVGNELNLPSYIYLTCNARYLGMMKYIPDRHRKIASEFDLSSGDEELPVPGFINAIPTKFMPPGLFNKEAYEAYVELAPRFADAKGILVNSFTELEPHPFDYFSHLEKFPPVYPVGPILSLKDRASPNEEAVDRDQIVGWLDDQPESSVVFLCFGSRGSVDEPQVKEIARALELVGCRFLWSIRTSGDVETNPNDVLPEGFMGRVAGRGLVCGWAPQVEVLAHKAIGGFVSHCGWNSTLESLWFGVPVATWPMYAEQQLNAFTLVKELGLAVDLRMDYVSSRGGLVTCDEIARAVRSLMDGGDEKRKKVKEMADAARKALMDGGSSSLATARFIAELFEDGSSC
Protein: C-type lectin domain family 4 member D (C-type lectin superfamily member 8) (CD antigen CD368) (Q69FH1)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of pathogen-associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs include alpha-mannans on C.albicans hypheas and mycobacterial trehalose 6,6'-dimycolate (TDM) (By similarity). Interacts with signaling adapter Fc receptor gamma chain/FCER1G, likely via CLEC4E, to form a functional complex in myeloid cells. Binding of mycobacterial TDM or C.albicans alpha-mannans to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. The heterodimer formed with CLEC6A is active against fungal infection. Functions as an endocytic receptor. May be involved in antigen uptake at the site of infection, either for clearance of the antigen, or for processing and further presentation to T-cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:23921530}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 4 member E
- High affinity immunoglobulin epsilon receptor subunit gamma
- C-type lectin domain family 9 member A
- C-type lectin domain family 1 member A
- C-type lectin domain family 5 member A
Sequence:
MWLEESQMKSKGALHPRRIPWVCAVVSISFLSACFISTCVVTHYFLLWKRGSALKFSDYHTRLTCILEEPQPGATGGTWTCCPVSWRAFQSNCYFALNDNQTWHESERNCSGMSSHLVTINTEAEQDFVTQLLDEQFSYFLGLSYEKVEGQWQWVDKTPFNPNVVFWKVGEPKDSMEEDCVVLVYDQDKWVWNDFPCHFEMGRICKLPGATFDWNPSK
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (A0A060WBM3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
- Elongation of very long chain fatty acids protein 6
- Elongation of very long chain fatty acids protein
- Elongation of very long chain fatty acids protein 6
- 3-oxo-5-alpha-steroid 4-dehydrogenase C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Steroid 5-alpha reductase C-terminal domain-containing protein
- 3-oxo-5-alpha-steroid 4-dehydrogenase C-terminal domain-containing protein
- 3-oxo-5-alpha-steroid 4-dehydrogenase C-terminal domain-containing protein
- 3-oxo-5-alpha-steroid 4-dehydrogenase C-terminal domain-containing protein
Sequence:
MEAFNHKLNTYIDSWMGPRDERVQGWLLLDNYPPTFALTLMYLLIVWLGPKYMRHRQPVSCQGLLVLYNLALTLLSFYMFYEMVSAVWQGGYNFYCQDTHSAGETDTKIINVLWWYYFSKVIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFIHVLMYSYYGLSAVPAIRPYLWWKRYITQGQLIQFFLTMSQTICAVIWPCGFPRGWLFFQIFYMASLIALFSNFYIQTYKKHRVSQKKAYHQNGSVDSLNGHANGVTPTETITHRKVRAD
Protein: Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (Q9CQE6)
Organism: Mus musculus (Mouse)
Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51. Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y294}. Chromosome {ECO:0000250|UniProtKB:Q9Y294}.
Interaction partners:
- Ubinuclein-1
- Protein HIRA
- Calcineurin-binding protein cabin-1
- Nuclear autoantigenic sperm protein
- Serine/threonine-protein kinase tousled-like 2
- Chromatin assembly factor 1 subunit B
- DNA replication licensing factor MCM2
- Histone H3.2
- Histone H3.3
- Histone acetyltransferase type B catalytic subunit
Sequence:
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNAGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
Protein: Aspartate carbamoyltransferase catalytic subunit (EC 2.1.3.2) (Aspartate transcarbamylase) (ATCase) (P9WIT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Carbamoyl phosphate synthase small chain
- Dihydroorotase
- Carbamoyl phosphate synthase large chain
- Bifunctional protein PyrR
- Orotidine 5'-phosphate decarboxylase
- Probable export or membrane protein
- Dihydroorotate dehydrogenase
- 6,7-dimethyl-8-ribityllumazine synthase
- Adenylosuccinate synthetase
- Putative asparagine synthetase
Sequence:
MTPRHLLTAADLSRDDATAILDDADRFAQALVGRDIKKLPTLRGRTVVTMFYENSTRTRVSFEVAGKWMSADVINVSAAGSSVGKGESLRDTALTLRAAGADALIIRHPASGAAHLLAQWTGAHNDGPAVINAGDGTHEHPTQALLDALTIRQRLGGIEGRRIVIVGDILHSRVARSNVMLLDTLGAEVVLVAPPTLLPVGVTGWPATVSHDFDAELPAADAVLMLRVQAERMNGGFFPSVREYSVRYGLTERRQAMLPGHAVVLHPGPMVRGMEITSSVADSSQSAVLQQVSNGVQVRMAVLFHVLVGAQDAGKEGAA
Protein: BRWD3 (Q9VC96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histone H3
- ATP-dependent helicase brm
- DNA damage-binding protein 1
- Jetlag, isoform A
- Cullin-4A
Sequence:
METRQPSSGDDLKPELYFLISKFLAAGPLEETAKVLIRELEEKKVLPRRLDWQGNEHEQTFEELERKYKHIGANHLLEICSRLGPLVDRELPPSVPGINSLLGTGRQNLLRTKETVYCHRSLRDYCTRLNGVSLPDSVLTKPTHNLDRVLTGREHGGEVRRKLLVPTDLYRRTKLLRRTVGHLSSVYCVLFDRTGRYIITGADDLLIKIWSAADGRLLATLRGASSEITDIAINLDNTMLAAGSLDHILRVWDMQTTSPIAVLSAHTGMITSVNFCPSPRSDLKYLVTTSTDGSIAFWQYSTPRGQKITFAPKPTQYHEKLRPGQAQMMCTTFSPGGIFLAAGSADHHVRVYMMGEDGPKRILETEAYTDAVDSVQWSHRGLRFISGSKDGTAHIWTFESQQWKSSKLCMTERLASCPEPEEGKRLKVTMVAWDASDRYVITAVNDFTIKIWDSKSAKLHRVLRGHKDELYVLESNPRDEHVLLSAGHDGQVFLWDIEQGVCVANFLNDIDGQGHGSVFDAKWSPDGTMIAATDSHGHILIFGLGVCIEKYKMLPTELFFHTDFRPLLRDAQHHVVDEQTQIMPHLMPPPFLVDADGNPHPSRFQRFVPGRESCSLDQLIPNLTVGVDGVVIDDGGAGGDAVVAAAPAEAPPAALPPAAAGGPQGANYSHIDRMIAALANRQSVNVNANDANPTNGNQSFERLTNRQMPDSNGRQSSRGNVLGSRLSTPRQGWGAAAAAPVEDQAGPSQPPAEPAAEPGQAQVQQALPLKFIRRTYVRPMKYPQLQNLKQTIYSAGQFEKQEYKREMRRRPIMINTASAASSQQPGSVGRPRNTRGNGGGARAGRRRGPQPAGGQPQPAYRTRAVRDQEPEHYDEVAPPPEEEEEDVSSNSSGDTSYSNVEENLEDSSDESETDSSDYSDWVADTPGPNLEPPKRSKRKPLSRRPRSSDDSSDDERAGRSRGGQVTARKVGRKTVLFPPTDANGEIPELYRPAEWLSEVIPRKAPYYPQMGDEVVYFRQGHAKYLDAVRLKKVYKLSHSSEPWNFHTLRDHELVRVIGIKYEIRPPRLCCLKLAIIDEEGNMTGTTFKIKYHDMPDVLDFLVLRQTFDLAVQRNWSIGDRFRCMIVDGWWMGQIESRHALSADFPDSSFMCFRVRWDNGEYEFMSPWDMEPIDQQRVPDEVGGAVPVLPEEIRATLYQPKSEEWHRGDRDGTCRRIINGLEQVMRLSIAEHFLAPVDLNIYPDYAYLIEYPIDLTTIKSRFENHFYRRITSAQFDVRYLATNAEQYNRRHAIIVKHSRIVTDLCLRIIREPDEIDVAAVYHQLADVYHSSESENEVDSDVVPSTSTGPTTSAAAAAARQRVSSARRSTRIHSEGDWRADCRQLLDLMWARTDSAPFREPVDTIDFPDYLEIIATPMDLRTVKEDLLGGNYDDPLDFAKDVRLIFQNSKNYNTNKRSRIYAMTLRLSALFESHIKTVVTSWKAALRRANKNKSGSSGGGRGGSSSSPNKRVKKERSTRRNQKPTAAARRLPVANSSEDEDEEDDDDDDDDDDEEEASTRGRSRRRNGVAVSASSSGSNRVTSSSAAQQRRGKSSSSEEEEEEETSAQATSDASSDEEERAQSNDSSPQQTRTRRARQRQRLSDDSNINDSEDSYNPNEGRGSRRRPGAARPSSNRQTNGHSSKRRRLNKSPANAAPGPSLPRRTRRIAGSSAEEAASHSQHDESTQDSQIGRRKGRSASSRSIGNGPSTSAAAAANSSLESPSRNTRANGTRTSSHLGAENDHSYHLPVRNGRIIESDTDSPVIRPTRQSAKRALMDWGRGSDIEEEEEEEEEDSEEAEEILPTPTKDDLPSTSRAALAQAAAGPSRQLRTNRNTVVRPAQSDDDDDDDSDNEPLANNQQKNYQSPAKSSSTATVAPHPLSLRRRLASPPERNTHMTRSHATSTTSSAAASRAEQQPAVSTHDHNYLGNVNSSRAPRRILSRHQRNADELDTSLDVLENSRLLSAIANHRRPTSTTNSNSASNVVTRRLRGRASQANSHDEDHEEEEAAASDEGTDGGSSSQSYEDEDEDSDSEDNQPLTSYVSPSNGRPRRKAKTSSSSATTQERPLRRTRRPPSNNSIANDNDDDDDYVVPRSRRANRGGNQRAGRNQKRPRYNEQSEEEEAAAGYSHRSKRIRNGDAHASSQERSQASTERDQEEEEDGTSVDSEEQQVNVSSRGRVRKPSAKARGIFKE
Protein: Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 7A (TED7-1) (C1PGW1)
Organism: Zinnia elegans (Garden zinnia) (Zinnia violacea)
Function: Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19383897}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19383897}.
Interaction partners:
Sequence:
MASPLSQSVFPHFPPPSPAATPPPAPTTPSTPPPHFISPPPHSVPPPSPPHSVPPPLHPVPPPSPPHPVSPPPHTVPPPSPPHPVSPPPHTVPPPSPPHPVFPPPHTVPPPSPHFVPPPPNMVPPPSPPHANPPPPPPPHSVPPPPHTVPPPPPPPHIIPPPAHALSPPPPHIIPPPPPSPSNHSTTIVVIFVSCGGVFFLAFAMAALWCFLKKKKKKMVQKAENIHFDEHRKVTERIEQGPHGTETAILSVEDDIHIEEDIKKSELENFRKGLHLNYGNTYNIDTGKPSSSFGHHYLHG
Protein: Psilocybin synthase (EC 2.1.1.-) (EC 2.1.1.345) (Psilocybin biosynthesis methyltransferase) (P0DPA9)
Organism: Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis)
Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin.
Interaction partners:
Sequence:
MHIRNPYRTPIDYQALSEAFPPLKPFVSVNADGTSSVDLTIPEAQRAFTAALLHRDFGLTMTIPEDRLCPTVPNRLNYVLWIEDIFNYTNKTLGLSDDRPIKGVDIGTGASAIYPMLACARFKAWSMVGTEVERKCIDTARLNVVANNLQDRLSILETSIDGPILVPIFEATEEYEYEFTMCNPPFYDGAADMQTSDAAKGFGFGVGAPHSGTVIEMSTEGGESAFVAQMVRESLKLRTRCRWYTSNLGKLKSLKEIVGLLKELEISNYAINEYVQGSTRRYAVAWSFTDIQLPEELSRPSNPELSSLF