wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor MYB88 (Myb-related protein 88) (AtMYB88) (F4IRB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to DNA in promoters cis-regulatory element 5'-GGCGCGC-3' of cell cycle genes, including cyclins, cyclin-dependent kinases (CDKs), and components of the pre-replication complex. Binds to DNA in promoters cis-regulatory element 5'-AGCCG-3' of auxin regulated genes (e.g. PIN3 and PIN7). Together with FAMA and MYB124, ensures that stomata contain just two guard cells (GCs) by enforcing a single symmetric precursor cell division before stomatal maturity. Represses the expression of the mitosis-inducing factors CDKB1-1 and CDKA-1, specifically required for the last guard mother cells (GMC) symmetric divisions in the stomatal pathway. Represses CYCA2-3 in newly formed guard cells. Together with MYB88, regulates stomata spacing by restricting divisions late in the stomatal cell lineage thus limiting the number of GMC divisions. In collaboration with CDKB1-1 and CDKB1-2, restrict the G1/S transition and chloroplast and nuclear number during stomatal formation, and normally maintain fate and developmental progression throughout the stomatal cell lineage. Involved in sensing and/or transducing abiotic stress (e.g. drought and salt), probably via the positive regulation of NAC019. Regulates female reproduction being required for entry into megasporogenesis, probably via the regulation of cell cycle genes. Plays a minor role in lateral roots (LRs) initiation. Involved complementarily in establishing the gravitropic set-point angles of lateral roots by regulating the transcription of PIN3 and PIN7 in gravity-sensing cells of primary and lateral roots.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20675570}.
Interaction partners:
- Transcription factor FAMA
- Retinoblastoma-related protein 1
- Transcription factor MUTE
- Cyclin-A2-3
- Transcription factor SPEECHLESS
- Transcription factor SCREAM2
- Protein EPIDERMAL PATTERNING FACTOR 1
- Cyclin-dependent kinase B1-1
- LRR receptor-like serine/threonine-protein kinase ERL1
- Transcription factor ICE1
Sequence:
MEETTKQNNMKKKKKILLHSDDSKKKERHIVTWSPEEDDILRKQISLQGTENWAIIASKFNDKSTRQCRRRWYTYLNSDFKRGGWSPEEDTLLCEAQRLFGNRWTEIAKVVSGRTDNAVKNRFTTLCKKRAKHEAMAKENRIACCVNSDNKRLLFPDGISTPLKAESESPLTKKMRRSHIPNLTEIKSYGDRSHIKVESTMNQQRRHPFSVVAHNATSSDGTEEQKQIGNVKESDGEDKSNQEVFLKKDDSKVTALMQQAELLSSLAQKVNADNTDQSMENAWKVLQDFLNKSKENDLFRYGIPDIDFQLDEFKDLVEDLRSSNEDSQSSWRQPDLHDSPASSEYSSGSGSGSTIMTHPSGDKTQQLMSDTQTTSHQQNGGELLQDNGIVSDATVEQVGLLSTGHDVLKNSNETVPIPGEEEFNSPVQVTPLFRSLAAGIPSPQFSESERNFLLKTLGVESPSPYPSANPSQPPPCKRVLLDSL
Protein: Solute carrier family 22 member 13 (Organic anion transporter 10) (OAT10) (Organic cation transporter-like 3) (ORCTL-3) (Q6A4L0)
Organism: Mus musculus (Mouse)
Function: Anion antiporter that mediates the transport of orotate and nicotinate in exchange for organic or inorganic anions. Translocates orotate across the apical membrane of proximal tubule epithelial cells. Possibly involved in orotate renal reabsorption and nicotinate intestinal reabsorption. Orotate transport is Cl(-)-dependent (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9Y226}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y226}.
Interaction partners:
Sequence:
MAQFAQVMAEVGDFGRFQVRLTILMGIPNFLAAFFIFGQVFMVLDEAHHCSVSWVKNHTFNLSAAEQLAISIPNDTAGRPESCLMFRPPPDSASLEDILSHRFNETQACDSGWDYPENRPQSLKKEFDLVCDRKNLKKTSQSVFMAGLLVGALVFGPVCDWIGRRPSLLMQVLLSGITSMATAFVSSFELYLALRFVLATANAGFLLSTNVLISEWVGPSWRTQAVVLAQSNVALGQMVLAGLAYGVRNWRLLQITGTAPVLLLFFYFWVLPESPRWLLSQGRTEEAKQLVQKAALVNGRPLSPELLNQLVPEKTGPSGNALDLFRHPHLRKVTLILIAVWFVDSLVYYSLSFQVGDFGLDIYVTQLIFGAVEMPGRFLSVLMMEKLGRKWSQLCTLTLAGIMYIIIIFIPGDLPTVVTVLAVVGKFASAAAFTISYVYTAELFPTIIRQTGMGLVSIFSRVGGIITPLVMLLEQYHQAIPMVIFGSLPIGAGLLCALLPETRGQTLKDTLQDLEQGLPAGSHKTAPQRQDMEALGRTSSVRVAVVKSSYF
Protein: Protein translocase subunit SecY (P25014)
Organism: Cyanophora paradoxa
Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Subcellular location: Plastid, cyanelle thylakoid membrane {ECO:0000269|PubMed:18976493}; Multi-pass membrane protein {ECO:0000269|PubMed:18976493}. Plastid, cyanelle inner membrane {ECO:0000269|PubMed:18976493}; Multi-pass membrane protein {ECO:0000269|PubMed:18976493}.
Interaction partners:
Sequence:
MLSRLIISIFIIFETIYLQIFKPVNKTFKQGEAKLKRTLQTLQSRELSEIRKRAISTLCLIFLIRIGTFLPIPGTALNFDLESFQQNNSRNELANILNLLSGGAFLEIGFFTLGILPYMNASFFLQVLTKILPSLERFQKEQEEIAQREFKKWTRYLTVIWAFIQSIVISWIWIRPYALNWDFFLGLKVVVALTLGAVIVMIIAEQITEIGLTNGSSLLIFINIIARIPNSIEQLFNSNINWTFPMISSLILSLSLSFITMFVIIGLQESGRPVPVLIARQEAERQKFNEPITEAERRKTQAYIFFQLLPAGIMPVIFASTIFDLALPAFTNFLLQQGNWGYQLIKSFPFNSLFKDFCYLITIMLFSSNYALTIMINPKTLAENLNSMNALIPGVRPGSETKVYSEQLIHRLNFIGSFVLALVCILPSIVERSLGLPKLQILSPVSISIALGVAVDTTRRITSYLGSSSPFKRDSSKREPLKRDFSKRRSAN
Protein: lysozyme (EC 3.2.1.17) (Q95V68)
Organism: Ornithodoros moubata (Soft tick) (Argasid tick)
Interaction partners:
Sequence:
MLGKSTVLLVATIFAVGCVVEGKVYDRCSLASELRWKYNLPKDQIADWVCIAEHESSFNTAALGRPNSDGSQDHGLFQINDRYWCSPPGPHNDCGVSCAALRDDNIDDDVKCIRKIYARHGFSAWVAWKNNCRGKNLSKYVAGCKI
Protein: SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4 (EC 3.6.4.-) (ATP-dependent helicase swsn-4) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4) (CeSMARCA4) (SMARCA4) (SWI2/SNF2-like protein) (G5EF53)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000269|PubMed:11030341, ECO:0000269|PubMed:27207389}.
Interaction partners:
- SWI/SNF complex subunit SMARCC2
- HMG box domain-containing protein
- SWI/SNF Subunit INI1 DNA binding domain-containing protein
- SWI/SNF chromatin remodeling complex subunit swsn-7
- ARID domain-containing protein
- Actin-related protein 4
- SWI/SNF chromatin-remodeling accessory subunit 2
- Bromo domain-containing protein
- SWI/SNF chromatin-remodeling accessory subunit 1
- PHD finger protein 10
Sequence:
MSGRPAFEQFTAQPPQPAGEVVAQQAGDGAQGQELTISKLENAITSMEEQGLQNDHRHAKAVLLKQKLQSGLPDAVPGQENGGNQQITPAQLNQLRAQVSAYRLLARNEQVPANLIADAVMLRPKVTTLLPEPYEYPGEAENGEKLPYDLMKIFNLHQIRCNRPTTISVPSGIDPVGMLKQRENMIQNRIGLRMKLLNNLPADIPDHMKLKAEIELRALRLVNLQTQVRSEVMACLKRDTTLETALNPYAYRRTKRQSLREARVTEKLEKQQKMEQERKRRQKHTDLMQAIIQHGKEFKEYHRNNLLKMAKSRKAVMTYHQNNERERKKDEIRNEKLRMQKLMQEDEEGYRALLDEKKDQRLVYLLQQTDEYVDSLCSLVRQHQNTEKKKKKEDKKIEKGNQMDEEARVHVRERSTGKALTGDQAPKTEEIEFWLETHPEYEIVPRDQLSDDEEEEEEEAPVEPEEEKDDQYAGMDEETKAKMILEKARNEEDEYDQKTKKQMADYYATAHKIKEKVVKQHTTMGGGDPNLLLKPYQIKGLEWMVSLYNNNLNGILADEMGLGKTIQTISLVTYLMEVKQNNGPYLVIVPLSTLSNWQNEFAKWAPSVTTIIYKGTKDARRRVEGQIRKGAFNVLMTTYEYVIKEKALLGKIRWKYMIIDEGHRLKNHNCKLTLMLNGFFHAQHRLLLTGTPLQNKLPELWALLNFLLPSIFSSCGTFEQWFNAPFATTGEKVELNQEETMLIIRRLHKVLRPFLLRRLKKEVESQLPDKTEYVIKCDQSALQKVIYRHMQKGLLLDAKMSSGARSLMNTVVHLRKLCNHPFLFPNIEDSCRAYWKVNEVNGTDLMRVAGKLELLDRILPKLKATGHRILMFFQMTSMMNIFEDFLNFRRYTYLRLDGSTKPDERGDLLTQFNAPNSDLFLFMLSTRAGGLGLNLQTADTVIIFDSDWNPHQDMQAQDRAHRIGQKKEVRVLRLITANSVEEKILAAARYKLNVDEKVIQAGKFDQRSTGAERKQMLEQIIQADGEEEEEEEVPDDETVNQMVARSEEEFNIFQSMDIDRRREEANQLHRKPRLLEEHEIPDDILKLSFDYEEMERAREEGREVVDQTPNQRRRRREVDYSSDLLSDEQFMKQVEEVEDENNQAVAERKKQRKRKMAGLDENDDSMDDVVLQHKKKKTDPELAEKINEMLDVILEYKNEDGELIADVFQTLPTRKELPDYYQVISKPMDFDRINKKIETGRYTVMEELNDDMNLLVNNAQTYNEEGSEIYVSSETIGKLWKEQYDKFMNPPKPVEEPVKKKEPSTPSTSSSRPSTSGTPSVSDLQRTQQATAQQMLMLMTHMQSLPPAQAQQFQQALMTQTGGNQALMLQYMQSAMLAQRAQASTKVTPKKDEKKETSSSVKTEEAKKDDEPSTSSASAPPPKKKKESEDSEDPMEEDEEEEIIGQKKEPASSRRKSRPTRRFSNEDEEEEDDE
Protein: Ngt1p (Q5A7S4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Glucosamine-6-phosphate isomerase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylglucosamine kinase 1
- Hgt12p
Sequence:
MEKDQTKMDINSNTSSSNKDLEVQPEHLELKHHTNAEIEASGSWIDKQINILGAKFRFSSAMCQIVLLAFVVFLTPGMFNALSGIGAAISDKKTADLANTALYVTFSTVGFFAGTICNVIGVKMSLVFGGFGYAIYAGSLLSFNHNENKGFVIFAGAFLGFCASLLWAAQGTIIMSYPTEQTKGRAIMVFWVIFNLGAVIGSIIPLAENMHNQGSSASDGTFIAFIILMICGSVLANFMLPISKVWKSDGTRVMTKTHPYWKDELIGLGRTLIKEPKILLMFPMFFASNWFYTYQFNNVNYGRFNLRTRSLNSLLYWLAQMFGAIVLGYILDFKKFKRSTRAKIGWAILFVTSLAIWGGGLKFQMSFTREEVESKPPKISQLDFKDGAYIGPMFLYIFYGVFDAIFQTYTIWVLGAMSNNPKKTALYAGFYKGIQSAGAAIAWRLDSLEVKYMSLFASSWGLVQGSLVLAIPLIFFMIKDHTALEDDNMGEVVDDAELDVVKSTTVHIE
Protein: Photosystem I iron-sulfur center (EC 1.97.1.12) (9 kDa polypeptide) (PSI-C) (Photosystem I subunit VII) (PsaC) (P0C361)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01303}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01303}.
Interaction partners:
- Photosystem I P700 chlorophyll a apoprotein A1
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem II CP47 reaction center protein
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NAD
Sequence:
MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLGPETTRSMALSY
Protein: Ribosomal protein S23, retrogene 1 (Q8C7T0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MQSQQRNIGYFNHLKADSRNITYSMTFSTKSSNQNFIIFLNEVQAAIIGHERCDLLPVLNELHPDALPDGRIWLFGLNPYFFQHNSLCMRGTPKRIGLQGCAQVGFLVLFVMPLLIPSVTAELPGSSETTTLAHLAGATGP
Protein: Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS) (Q6AYQ3)
Organism: Rattus norvegicus (Rat)
Function: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.
Subcellular location: Mitochondrion matrix {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:26553276}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- Phenylalanine--tRNA ligase alpha subunit
- Leucine-rich repeat-containing protein 47
- Tyrosine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Probable arginine--tRNA ligase, mitochondrial
Sequence:
MVCLAFIRAAHEHLYLVRKVSHVCRCHQHRAWGSRPAASQFAVQGAPGRVLELLGKSYPQDDHTNLTQKVLSKVGRNLHNQKFHPLWLIKERVKEHFYQQYMGRSRTPLFSVYDQLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRGHMLRAHTSAHQWDLLHAGLNAFLVVGDVYRRDQIDSQHYPVFHQLEGVRLFSKHELFAGVKDGESLQLFEESSRSAHKQETHTMEAVKLVEFDLKQVLTRLVTHLFGDGLEVRWVDCYFPFTHPSFEMEINFRGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMVLYDIPDIRLFWSEDERFLKQFRLSDINQSVKFQRWFFQEERATGIQRKMGRQLCPFSKYPAVFNDISFWLPSENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRITYRHMERTLSQREVSSVHQAVQEAAVQLLGVEGRF
Protein: Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial (EC 1.6.5.9) (Internal NADH dehydrogenase) (NADH:ubiquinone reductase (non-electrogenic)) (P32340)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidation of NADH generated inside the Mitochondrion.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}; Peripheral membrane protein {ECO:0000269|PubMed:11502169}; Matrix side {ECO:0000269|PubMed:11502169}. Note=Bound to the mitochondrial inner membrane facing the matrix site.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Pro-apoptotic serine protease NMA111
- Cytochrome c isoform 2
- Cytochrome c isoform 1
- Apoptosis-inducing factor 1
- Metacaspase-1
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Mitochondrial oxaloacetate transport protein
Sequence:
MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKHEDGKITEETIPYGTLIWATGNKARPVITDLFKKIPEQNSSKRGLAVNDFLQVKGSNNIFAIGDNAFAGLPPTAQVAHQEAEYLAKNFDKMAQIPNFQKNLSSRKDKIDLLFEENNFKPFKYNDLGALAYLGSERAIATIRSGKRTFYTGGGLMTFYLWRILYLSMILSARSRLKVFFDWIKLAFFKRDFFKGL
Protein: Chromobox protein homolog 2 (Q14781)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (By similarity). Plays a role in the lineage differentiation of the germ layers in embryonic development (By similarity). Involved in sexual development, acting as activator of NR5A1 expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:21282530}. Chromosome {ECO:0000269|PubMed:18927235}. Note=Localized in distinct foci on chromatin and in chromocenters. Localizes to the inactive X chromosome. Seems to be recruited to H3K27me3, H3K9ac and H3K3me2 sites on chromatin. {ECO:0000269|PubMed:18927235}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Polycomb complex protein BMI-1
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 2
- Polyhomeotic-like protein 1
- Polyhomeotic-like protein 2
- E3 SUMO-protein ligase CBX4
- Chromobox protein homolog 8
- Polyhomeotic-like protein 3
- Polycomb complex protein BMI-1
Sequence:
MEELSSVGEQVFAAECILSKRLRKGKLEYLVKWRGWSSKHNSWEPEENILDPRLLLAFQKKEHEKEVQNRKRGKRPRGRPRKLTAMSSCSRRSKLKEPDAPSKSKSSSSSSSSTSSSSSSDEEDDSDLDAKRGPRGRETHPVPQKKAQILVAKPELKDPIRKKRGRKPLPPEQKATRRPVSLAKVLKTARKDLGAPASKLPPPLSAPVAGLAALKAHAKEACGGPSAMATPENLASLMKGMASSPGRGGISWQSSIVHYMNRMTQSQAQAASRLALKAQATNKCGLGLDLKVRTQKGELGMSPPGSKIPKAPSGGAVEQKVGNTGGPPHTHGASRVPAGCPGPQPAPTQELSLQVLDLQSVKNGMPGVGLLARHATATKGVPATNPAPGKGTGSGLIGASGATMPTDTSKSEKLASRAVAPPTPASKRDCVKGSATPSGQESRTAPGEARKAATLPEMSAGEESSSSDSDPDSASPPSTGQNPSVSVQTSQDWKPTRSLIEHVFVTDVTANLITVTVKESPTSVGFFNLRHY
Protein: Protein BTG3 (Abundant in neuroepithelium area protein) (BTG family member 3) (Protein Tob5) (Q14201)
Organism: Homo sapiens (Human)
Function: Overexpression impairs serum-induced cell cycle progression from the G0/G1 to S phase.
Interaction partners:
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 11
- Testis-expressed protein 13A
- Nanos homolog 2
- RIB43A-like with coiled-coils protein 1
- CCR4-NOT transcription complex subunit 6-like
Sequence:
MKNEIAAVVFFFTRLVRKHDKLKKEAVERFAEKLTLILQEKYKNHWYPEKPSKGQAYRCIRVNKFQRVDPDVLKACENSCILYSDLGLPKELTLWVDPCEVCCRYGEKNNAFIVASFENKDENKDEISRKVTRALDKVTSDYHSGSSSSDEETSKEMEVKPSSVTAAASPVYQISELIFPPLPMWHPLPRKKPGMYRGNGHQNHYPPPVPFGYPNQGRKNKPYRPIPVTWVPPPGMHCDRNHWINPHMLAPH
Protein: WD repeat-containing protein 74 (NOP seven-associated protein 1) (Q6RFH5)
Organism: Homo sapiens (Human)
Function: Regulatory protein of the MTREX-exosome complex involved in the synthesis of the 60S ribosomal subunit. Participates in an early cleavage of the pre-rRNA processing pathway in cooperation with NVL. Required for blastocyst formation, is necessary for RNA transcription, processing and/or stability during preimplantation development (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:26456651, ECO:0000269|PubMed:28416111, ECO:0000269|PubMed:29107693}. Nucleus {ECO:0000269|PubMed:28416111}. Note=Nucleolar location depends on active PolI transcription of pre-rRNA. {ECO:0000269|PubMed:28416111}.
Interaction partners:
- Ribosome biogenesis protein BOP1
- Probable rRNA-processing protein EBP2
- Ribosome biogenesis protein WDR12
- Pescadillo homolog
- Protein MAK16 homolog
- mRNA turnover protein 4 homolog
- Ribosome biogenesis protein NSA2 homolog
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- Ribosome production factor 1
- ATP-dependent RNA helicase DDX18
Sequence:
MAAAAARWNHVWVGTETGILKGVNLQRKQAANFTAGGQPRREEAVSALCWGTGGETQMLVGCADRTVKHFSTEDGIFQGQRHCPGGEGMFRGLAQADGTLITCVDSGILRVWHDKDKDTSSDPLLELRVGPGVCRMRQDPAHPHVVATGGKENALKIWDLQGSEEPVFRAKNVRNDWLDLRVPIWDQDIQFLPGSQKLVTCTGYHQVRVYDPASPQRRPVLETTYGEYPLTAMTLTPGGNSVIVGNTHGQLAEIDLRQGRLLGCLKGLAGSVRGLQCHPSKPLLASCGLDRVLRIHRIQNPRGLEHKVYLKSQLNCLLLSGRDNWEDEPQEPQEPNKVPLEDTETDELWASLEAAAKRKLSGLEQPQGALQTRRRKKKRPGSTSP
Protein: Cytochrome c oxidase subunit 4 (Q6TNV0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367145}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Zgc:86599.
- Cytochrome b-c1 complex subunit 6
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 3
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MLATTAFRLVGKRALSTSICLRGAHGVAKVEDYSLPAYFDRRESPLPEIKFVQQLSADQKSLKEKEKGSWAALSKEEKIALYRISFKESFAEMNQGSGEWKSVVAGIFFFVGLTGLVVLWQRKYVYGDVPNTFDPEYKQKEIQRMLDMRINPVQGFAAKWDYENNAWKK
Protein: Trypsin alpha (EC 3.4.21.4) (P04814)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:2414727}.
Interaction partners:
- Trypsin beta
- Trypsin epsilon
- trypsin
- Jonah 65Aiv
- GH01508p
- Uncharacterized protein
- RE12410p
- Bazooka, isoform B
- Zinc carboxypeptidase A 1
- Jonah 74E
Sequence:
MLKIVILLSAVVCALGGTVPEGLLPQLDGRIVGGSATTISSFPWQISLQRSGSHSCGGSIYSANIIVTAAHCLQSVSASVLQVRAGSTYWSSGGVVAKVSSFKNHEGYNANTMVNDIAVIRLSSSLSFSSSIKAISLATYNPANGASAAVSGWGTQSSGSSSIPSQLQYVNVNIVSQSQCASSTYGYGSQIRNTMICAAASGKDACQGDSGGPLVSGGVLVGVVSWGYGCAYSNYPGVYADVAVLRSWVVSTANSI
Protein: Sigma factor AlgU regulatory protein MucB (P38108)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Negative regulator of the sigma factor AlgU. Plays a role in the differentiation of P.aeruginosa into the alginate-producing form. Inactivation of mucB causes conversion to mucoidy.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Sigma factor AlgU negative regulatory protein
- Positive regulator for alginate biosynthesis MucC
- RNA polymerase sigma-H factor
- Probable periplasmic serine endoprotease DegP-like
- AlgW protein
- GDP-mannose 6-dehydrogenase
- Positive alginate biosynthesis regulatory protein
- Alginate biosynthesis transcriptional regulatory protein AlgB
- Phosphomannomutase/phosphoglucomutase
Sequence:
MRTTSLLLLLGSLMAVPATQAADASDWLNRLAEADRQNSFQGTFVYERNGSFSTHEIWHRVESDGAVRERLLQLDGARQEVVRVDGRTQCISGGLADQLADAQLWPVRKFDPSQLASWYDLRLVGESRVAGRPAVVLAVTPRDQHRYGFELHLDRDTGLPLKSLLLNEKGQLLERFQFTQLNTGAAPAEDQLQAGAECQVVGPAKADGEKTVAWRSEWLPPGFTLTRSFMRRSPVTPDPVACLTYGDGLARFSVFIEPLHGAMVGDARSQLGPTVVVSKRLQTDDGGQMVTVVGEVPLGTAERVALSIRPEAAAQK
Protein: Uncharacterized protein (G5EB62)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Uncharacterized protein
- GATA-factor
- Developmental and secondary metabolism regulator veA
- Velvet complex subunit B
- Protein-methionine methyltransferase laeA
- Histidine-containing phosphotransfer protein
Sequence:
MSELPSRSISPRDPSPGETPGRDPSTPSTDAGVGYSASQDAPSFGAYDRVYPIRSLVSLEPPATSEPSSNKSKSPLSPTSGARQFSIIDGHTWTRLRSDSRANSTDYSGGTGLSPESSEAPSSQRMSDSSSARPPSNTTGLRRGDDHTTFTPSSEDSHPQVQEPYELMTTRFRHVVTDDGHAVITGRTVDSFKACEDEPIHIPGAIQSFGALVAVREEPGEQMVVRIVSENSQDILGYSPNDLFSLPTLCDIFPEDQADNFLDHVDFVKEEGYDPSVDGPEVFILTVNQPNGSTIRVWCAIHTNPALNGLVICEFELEDDHVNPLTSSGHISPAVPTNTLDVVPTIEQMAGSTITINQPLRVLRRARRRKGEAAAMEVFSIVSQIQEQLARADNMEALLDTTSGIVKELTGFHRILVYQFDSEFNGKVVSELVDPTMSIDLFKGLHFPAADIPKQARDLYRINKVRLLYDRDHVTARLVCRALEDLETPLDMTHAYLRAMSPIHIKYLANMQIRSSMSISINSMNDLWGLISCHSYGPRGMRVSFPIRKMCRLIGDTVSRNIERLSYASRLQARKLINTVPTDANPSGYIVASSDDLLRLVDADYGALCIRGEVKILAKSPQSQEMLALLEYLKVRKYNSVLTSNHIVKDFQDLNYPPGFKDISGLLYVPLSTDGLDFIVFFRRGQLTEVKWGGNPNEAKFTEGHLEPRKSFQTWRETVLDRCRDWTESEVDTAAVLCLVYGKFIKVWRQQEAALESSSLTKLLLANSAHEVRTPLNAIVNYLEIALEGALDGETRDHLSKSYSASKSLIYVINDLLDLTNVEKGQSLIKDEPFDLPTTFSEATAMFESEAKRKGLNYKVLSQPGIPETVIGDQRRVRQSISNLISNAVQNTSSGGVTVEVWHAPGEGDTDKATVKIAVLDTGRGISSSTLELLFRELEQVSGEDDSHYYGGSEEGEESAPEAKASKDKAVLGLGLALVARIVRNMHGQLTVRSEEGKGSRFQISLQFPIPEGSDTKSPTAEHRPVATGDSAAPFSTGDDVILVDSTTGSKRNSQDSLTRPDVPRKSEPEDTAPADGAGEQASGESEAQTRPKKTGESTASTSHEQSETARSRPSGPSSGPSAPERRPLRVLVAEDDPINAKIIEKRLEKLGHTVQRTVNGEECANAYSAESTQWDVVLMDIQMPILDGIESTKRIRQHESQSEVANLHIPIFAVSASLLEKDVQMYMDIGFDGWIMKPINFVRLNTLLAGIHEERARNGAVYQPGQWEKGGWFTPYTHS
Protein: Thioredoxin domain-containing protein 2 (Spermatid-specific thioredoxin-1) (Sptrx-1) (Thioredoxin-4) (Q6P902)
Organism: Mus musculus (Mouse)
Function: Probably plays a regulatory role in sperm development. May participate in regulation of fibrous sheath (FS) assembly by supporting the formation of disulfide bonds during sperm tail morphogenesis. May also be required to rectify incorrect disulfide pairing and generate suitable pairs between the FS constituents. Can reduce disulfide bonds in vitro in the presence of NADP and thioredoxin reductase.
Subcellular location: Cytoplasm.
Interaction partners:
- Thioredoxin-interacting protein
Sequence:
MTLNNGGKANERGSNENPLQALSKNEAFLVPEFLDTAQSKEKAIASKVSNTLHMSTEESEFPQQVSSTPMFSENTVHPRHEVSPKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGSTLKPATNSTHYREDDIPKSSEDIIQPKKGDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSVPSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEEDVQLSESKLLGLGAEIETLEEGLVRVIKDKEEFEEVLKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGEFSGALVGKLERSISELK