wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 28 homolog (Caspase-activated DNase inhibitor that interacts with ASK1) (CIIA) (ESCRT-I complex subunit VPS28) (Q9D1C8)
Organism: Mus musculus (Mouse)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process.
Subcellular location: Cell membrane {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Tumor susceptibility gene 101 protein
- Vacuolar protein-sorting-associated protein 36
- Ubiquitin-associated protein 1
- Vacuolar protein sorting-associated protein 37B
- Vacuolar protein sorting-associated protein 37A
- Multivesicular body subunit 12A
- Vacuolar protein-sorting-associated protein 25
- Multivesicular body subunit 12B
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 37C
Sequence:
MFHGIPATPGVGAPGNKPELYEEVKLYKNAREREKYDNMAELFAVVKTMQALEKAYIKDCVTPNEYTAACSRLLVQYKAAFRQVQGSEISSIDEFCRKFRLDCPLAMERIKEDRPITIKDDKGNLNRCIADVVSLFITVMDKLRLEIRAMDEIQPDLRELMETMHRMSHLPPDFEGRQTVSQWLQTLSGMSASDELDDSQVRQMLFDLESAYNAFNRFLHA
Protein: CUGBP Elav-like family member 2 (CELF-2) (Bruno-like protein 3) (CUG triplet repeat RNA-binding protein 2) (CUG-BP2) (CUG-BP- and ETR-3-like factor 2) (ELAV-type RNA-binding protein 3) (ETR-3) (Neuroblastoma apoptosis-related RNA-binding protein) (hNAPOR) (RNA-binding protein BRUNOL-3) (O95319)
Organism: Homo sapiens (Human)
Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity). May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF1, negatively regulates the processing to mature miRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:33131106}. Cytoplasm {ECO:0000250|UniProtKB:Q7T2T1, ECO:0000250|UniProtKB:Q9Z0H4}. Note=Accumulates in the cytoplasm after ionizing radiation (By similarity). Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments. {ECO:0000250}.
Interaction partners:
- CCAAT/enhancer-binding protein delta
- Troponin T, cardiac muscle
- Muscleblind-like protein 1
- Polypyrimidine tract-binding protein 2
- Prostaglandin G/H synthase 2
Sequence:
MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: A-type voltage-gated potassium channel KCND3 (Potassium voltage-gated channel subfamily D member 3) (Voltage-gated potassium channel subunit Kv4.3) (Q9UK17)
Organism: Homo sapiens (Human)
Function: Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23280837, ECO:0000269|PubMed:23280838}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q62897}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q62897}. Note=Interaction with palmitoylated KCNIP2 and KCNIP3 enhances cell surface expression. {ECO:0000250|UniProtKB:Q62897}.
Interaction partners:
- A-type potassium channel modulatory protein KCNIP2
- A-type potassium channel modulatory protein KCNIP1
- Inactive dipeptidyl peptidase 10
- Calsenilin
- Kv channel-interacting protein 4
- Potassium voltage-gated channel subfamily E member 3
- A-type potassium channel modulatory protein DPP6
- A-type voltage-gated potassium channel KCND2
- Ubiquitin-like protein FUBI
- Sodium channel regulatory subunit beta-1
Sequence:
MAAGVAAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDDELAFYGILPEIIGDCCYEEYKDRKRENAERLMDDNDSENNQESMPSLSFRQTMWRAFENPHTSTLALVFYYVTGFFIAVSVITNVVETVPCGTVPGSKELPCGERYSVAFFCLDTACVMIFTVEYLLRLFAAPSRYRFIRSVMSIIDVVAIMPYYIGLVMTNNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPASFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRVAKTGSSNAYLHSKRNGLLNEALELTGTPEEEHMGKTTSLIESQHHHLLHCLEKTTGLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPSTRSPSLSSHPGLTTTCCSRRSKKTTHLPNSNLPATRLRSMQELSTIHIQGSEQPSLTTSRSSLNLKADDGLRPNCKTSQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSIASNVVKVSAL
Protein: Ets-family transcription factor ELF1 (Transcription factor Elf-1) (Q9EQY3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MAAVVQQNDLVFDFASNVMEDEQQLGDPAIFPAVIVEHVPGADILNGYAGLACVEEPNDMITESSLDVAEEEIIEDDDDDITLTVEASCHNGDETIETIGAAEALLNMDSPGPVLDEKRINNNIFSSSEDDIVAPITHVSVTLDGIPEVMETQQVQESNADSPGASSPDQPKRKKGRKTKPPRPDSPATTPNISVKKKSKDGKGNTIYLWEFLLALLQDKATCPKYIKWTQREKGIFKLVDSKAVSRLWGKHKNKPDMNYETMGRALRYYYQRGILAKVEGQRLVYQFKEMPKDLIYIDDEGPSSSTESSDQSLSSTTTSSRNQANRTRMSSSPGIKGGATTILKPGNPKVAKPKDTVEVGQPSEVLRTVQPSQAPYPTQLFRTVHVVQPVQAIPEEATITSTMQEEAAGSSVQGIRTIQASTQVPVVVSPGNQQLHTVTLQTVPLTTVIASTDPSSGAGPQKFILQAIPSSQPMTVLKENVLLQSQKPGSPPSIVFSPTPVQQVLTGSVQSLGNGAVSMASPPNFSATAPVVTFSRSSQLAAHPPGTVITSVIKAQETKTPKAEVEKKAEGHLNGDPEEIEQQPQPYVMVVSSSNGFSSQVAITQNELLEPSSF
Protein: Rho guanine nucleotide exchange factor 2, isoform G (A0A0B4K7T7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDDPSIKKRLLDLYTDEHEYDEVQEIPEESSIQPPETSTSHTSTNGSSHSGPGTATGPGATSAGPSAGAPQSPVIVVDSVPELPAPKQKSVKNSKSKQKQKQLANKSKIPRSPSLASSLSSLASSLSGHRDRDKDRDKDRENQNAVPPQTPPLPPSYKQNQMNGDSTAAAGGGVSAPATPTTANNNNASHNNGSIMGGGVQLNQSDNSNPVLQAPGERSSLNLTPLSRDLSGGHTQESTTPATTPSTPSLALPKNFQYLTLTVRKDSNGYGMKVSGDNPVFVESVKPGGAAEIAGLVAGDMILRVNGHEVRLEKHPTVVGLIKASTTVELAVKRSQKLTRPSSVSVVTPSTPILSGRDRTASITGPQPVDSIKRREMETYKIQTLQKMLEQEKLNLERLKSDQNNPSYKLSEANIRKLREQLHQVGAEDAPTVKLQAAAGNKNTALLTPNQIQHLSASATHSNQQFHHLHHHHNLHNNNYPPQQQPASTSPAFLSLLPRSLSSLSLGTRKNKTEKDLTTSSPFGLTTDFLQQQRMSHQAESMSQSMHQHTSTPTSQQFFHPHQQQHRFKETGPTSKGKNKFLISRSLIEEDVPPPLPQRNPPRQLNLDLKNGNASPGGSHLVAPVSDLDRATSPQLNRSQQQQLPSSTDNSPSNAKSKRSKIKTKALSDPKMSTQMFLQMESASAAGAAGGSIEVDGGPPPLPPRLPGMMTEDMSRGSCQNLAQPNSVGTAFNYPLVSTTTAVQNDNLNIAFPLSQRPNIVQQLQQYQQQQQHQMSGGQATGALGQTPNLGKNKHRRVGSSPDNMHPRHPDRITKTTSGSWEIVEKDGESSPPGTPPPPYLSSSHMTVLEDPNENNRGAAAAGPGVFIESHQFTPMAGASSPIPISLHSSHMHAAQSNDTQKEIISMEDENSDLDEPFIDENGPFNNLTRLLEAENVTFLAIFLNYVISNSDPAPLLFYLITELYKEGTSKDMRKWAYEIHSTFLVPRAPLSWYRQDESLAREVDNVLQLEYDKVEILRTVFLRSRKRAKDLISEQLREFQQKRTAGLGTIYGPTDDKLAEAKTDKLREQIIDKYLMPNLHALIEDENGSPPEDVRKVALCSALSTVIYRIFNTRPPPSSIVERVHHFVSRDKSFKSRIMGKNRKMNVRGHPLVLRQYYEVTHCNHCQTIIWGVSPQGYHCTDCKLNIHRQCSKVVDESCPGPLPQAKRLAHNDKISKFMGKIRPRTSDVIGNEKRSRQDEELDVELTPDRGQASIVRQPSDRRPDANISIRSNGNTSCNTSGLNTTDLQSSFHGSCANDSINPGGGAGCNMDLSTSVASTTPSTSGSVAAGLSAFAELNALDTVDKEARRERQHPKHKSAPVSVNRSESYKERLSNKRNRNSRRKTSDPSLSSRPNDEQLDLGLSNATYVGSSNSSLSSAGGSESPSTSMEHFAAPGAAGGVQVPPMGLNQNQHPHLLIQQHAQQYCQQDSFQAGLAGAAGSSAASNSSFWNAGHPLPVARWTLESEDEDDVNEADWSSMVAAEVLAALTDAEKKRQEIINEIYQTERNHVRTLKLLDRLFFLPLYESGLLSQDHLLLLFPPALLSLREIHGAFEQSLKQRRIEHNHVVNTIGDLLADMFDGQSGVVLCEFAAQFCARQQIALEALKEKRNKDEMLQKLLKKSESHKACRRLELKDLLPTVLQRLTKYPLLFENLYKVTVRLLPENTTEAEAIQRAVESSKRILVEVNQAVKTAEDAHKLQNIQRKLDRSSYDKEEFKKLDLTQHHLIHDGNLTIKKNPSVQLHGLLFENMIVLLTKQDDKYYLKNLHTPLSITNKPVSPIMSIDADTLIRQEAADKNSFFLIKMKTSQMLELRAPSSSECKTWFKHFSDVAARQSKNRSKNASSNHDTSISDPALAAIPHSNTKESLELSTDTVQPLAATATLTTTPLAPMLPIATVTPAPATNNSNVSSLTGVQLRNPQRDATASESDADYVNTPKPRSSQNEVNRTMSIRSTGEPIQKYSANGTEANDVTLRHSQSTRESVRPGSTGEERNSTYGMVGGNSKRDSASIVCSNNSNNTRTLLMQSPLVDPTAIQVSISPAHTAEPVLTPGEKLRRLDASIRNDLLEKQKIICDIFRLPVEHYDQIVDIAMMPEAPKDSADIALAAYDQIQTLTKMLNEYMHVTPEQEVSAVSTAVCGHCHEKEKLRKKVAPSSSFSSSPPPLPPPNRQHAQAQAQIPPSRLMPKLQTLDLDEVAIHEDDDGYCEIDELRLPAIPSKPHERPTTPLAPFNTEPKTSQSVIDASKRQSTDAVPEGLLEQEPLEGDKTETKGEDNEVKTVPSDKLSESCNEERQCVEADITKEVADPTTSKNEAAASVDELPSQSREIKTAENASKSVADKKEDNEETIEEGVASTVDSSTQTSPTESPKETDKLTGGSSSTCGPNRIQHASVLEPSVPCHALSSIVTILNEQISMLLPKINERDMERERLRKENQHLRELLSALHDRQRVDEVKETPFDLKKLMHAEDVEFDDDIDAISNSSLTPTPTPIPTASPSASGQVETAEAMRITSTEDEE
Protein: Antitoxin HigA (P67701)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents HigB-mediated cessation of cell growth and inhibition of cell proliferation.
Interaction partners:
- mRNA interferase toxin HigB
- mRNA interferase toxin RelE
- Antitoxin HicB
- Antitoxin RelB
- Probable mRNA interferase toxin HicA
- Antitoxin MqsA
- Endoribonuclease toxin MazF
- Antitoxin MazE
- mRNA interferase toxin YafQ
- Antitoxin YefM
Sequence:
MIAIADILQAGEKLTAVAPFLAGIQNEEQYTQALELVDHLLLNDPENPLLDLVCAKITAWEESAPEFAEFNAMAQAMPGGIAVIRTLMDQYGLTLSDLPEIGSKSMVSRVLSGKRKLTLEHAKKLATRFGISPALFID
Protein: Glucose-6-phosphatase catalytic subunit 1 (EC 3.1.3.9) (Glucose-6-phosphatase) (G-6-Pase) (G6Pase) (P43428)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35575}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hexokinase-2
- Hexokinase-3
- Phosphoglucomutase-1
- Glucose-6-phosphate 1-dehydrogenase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Glucose-6-phosphate isomerase
- Galactose mutarotase
- Lactase/phlorizin hydrolase
- Fructose-bisphosphate aldolase B
- Glucose-6-phosphatase 3
Sequence:
MEERMNVLHDFGIQSTRYLQVNYEDSQDWFVLVSVIADLRNAFYVLFPIWFHIQETVGINLLWVAVVGDWFNLVFKWILFGQRPYWWVLDTDYYSNSSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLAIFRGKKKSTYGFRCLNVVLWLGYWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIRGIYNASLQRYCLITFFLFGFALGFYLLLKGLGVDLLWTLEKAKRWCERPEWVHLDTTPFASLFKNLGTLLGLGLALNSSMYRKSCKGELRKSLPFRLACIVASLGLLHLFDSLKPPSQIESIFYILSFCKSATVPFASVSLIPYCLARLLGQTHKKSL
Protein: 60S ribosomal protein L13 (A8K4C8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPSRNGMVLKPHFHKDWQRRVATWFNQPARKIRRRKARQAKARRIAPRPASGPIRPIVRCPTVRYHTKVRAGRGFSLEELRVAGIHKKVARTIGISVDPRRRNKSTESLQANVQRLKEYRSKLILFPRKPSAPKKGDSSAEELKLATQLTGPVMPVRNVYKKEKARVITEEEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK
Protein: Uncharacterized protein YjaA (P09162)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Ankyrin repeat protein A
- Tryptophan synthase alpha chain
- ATP synthase gamma chain
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
- Fumarate hydratase class II
- Prophage lipoprotein Bor homolog
- Adenylate kinase
- Probable autotransporter YfaL
Sequence:
MSVLYIQIRRNQITVRDLESKREVSGDAAFSNQRLLIANFFVAEKVLQDLVLQLHPRSTWHSFLPAKRMDIVVSALEMNEGGLSQVEERILHEVVAGATLMKYRQFHIHAQSAVLSDSAVMAMLKQK
Protein: Sodium/hydrogen exchanger 9 (Na(+)/H(+) exchanger 9) (NHE-9) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 9) (F7B113)
Organism: Equus caballus (Horse)
Function: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A9 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Regulates organellar pH and consequently, endosome maturation and endocytic trafficking of plasma membrane receptors and neurotransporters (By similarity). Promotes the recycling of transferrin receptors back to the cell surface to facilitate additional iron uptake in the brain (By similarity). Regulates synaptic transmission by regulating the luminal pH of axonal endosomes. Regulates phagosome lumenal pH, thus affecting phagosome maturation, and consequently, microbicidal activity in macrophages. Can also be active at the cell surface of specialized cells, e.g., in the inner ear hair bundles uses the high K(+) of the endolymph to regulate intracelular pH (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8IVB4}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Cell membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q8BZ00}; Multi-pass membrane protein {ECO:0000269|PubMed:33118634}. Note=Localized to the plasma membrane in inner ear hair cell bundle. {ECO:0000250|UniProtKB:Q8BZ00}.
Interaction partners:
Sequence:
MERQRRFMSEKDEYQFQHQGAVELLVFNFLLILTILTIWLFKNHRFRFLHETGGAMVYGLIMGLILRYATAPTDIESGTVYDCGKLAFSPSTLLINITDQVYEYKYKREISQHNINPHLGNAILEKMTFDPEIFFNVLLPPIIFHAGYSLKKRHFFQNLGSILTYAFLGTAISCIVIGLIMYGFVKAMVYAGQLKNGDFHFTDCLFFGSLMSATDPVTVLAIFHELHVDPDLYTLLFGESVLNDAVAIVLTYSISIYSPKENPNAFDAAAFFQSVGNFLGIFAGSFAMGSAYAVVTALLTKFTKLCEFPMLETGLFFLLSWSAFLSAEAAGLTGIVAVLFCGVTQAHYTYNNLSLDSKMRTKQLFEFMNFLAENVIFCYMGLALFTFQNHIFNALFILGAFLAIFVARACNIYPLSFLLNLGRKHKIPWNFQHMMMFSGLRGAIAFALAIRDTESQPKQMMFSTTLLLVFFTVWVFGGGTTPMLTWLQIRVGVDLDEDLKERPSSHQEANNLEKSTTKTESAWLFRMWYGFDHKYLKPILTHSGPPLTTTLPEWCGPISRLLTSPQAYGEQLKEDDAECIVNQDELAMNYQEQAASPCSPPTRLGLDQKAAPQTPGKENIYEGDLGLGGYELKLEQTPGQSQLN
Protein: Coiled-coil domain-containing protein 157 (Q569K6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHLLGSQACMESLRTDLTDLQGAIVDVFSRAGPVRFPSWKFPDRMACDLDMVALLEHYDHVPGDPEFTQLSHAVLLELVIDRLLLLLQSCMSYLENLGSEQMMPPAQAAGPCMSVGLTVRRFWDSLLRLGTLHQQPLPQKGANQRETPTSKPTTKGEPARSPEYLTTKLIKPSSPVLGLPQTCQEPESIPVRASLQFPATTFKNTRSVHSQTIETALVPCDACASVQGSLQKVGKVVISLCQSQNLPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELERELEELKERERLLVAFPDLHRPTETQIHGGRSSSVESQITCPTDSGNVTDHMERQVQSNDIRIRVLQEENGRLQSMLSKIREVAQQGGLKLIPQDRLWSPSSKGTQGATPPVQAKSTSPGPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQPSKSLLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERPM
Protein: DNA primase small subunit (EC 2.7.7.102) (DNA primase 1) (O14215)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11160827}.
Interaction partners:
- DNA polymerase alpha subunit B
- DNA polymerase alpha catalytic subunit
- DNA primase large subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon subunit B
- Replication factor C subunit 2
- DNA replication licensing factor mcm10
- DNA replication licensing factor mcm5
- Replication factor A protein 2
Sequence:
MTVQIDELDDKDLDEIIANGTLDGAKQGAVDSETMIQYYRHLFPWKYLFQWLNHGPVVTNDFAHREFAFTLPNDAYIRYLSFSNWEELKKEALNLCPSRFEVGPVYSANPRDRKTIRKSTFHPLKKELVFDIDMTDYDDVRTCCSKTNICEKCWPFITIAVQVLDICFHEDFGFKHILWVYSGRRGIHAWICDEIACSLDDRSRRMIASYLQVVVGNPQGGVRLINNLKRPLHPHLTRSLNILKSAFVKIVLEDQDPWASKEGAENLLKLLPDKDLASALRKKWEVDPERSSKNKWSDIDTVLASGSIASISPSVIAIAKQDIVLTYLYPRLDVEVSRHLNHLLKSPFCVHPGTSRVCVPIDIERMDSFNPLKVPTVNDLLQELDKNSQNDNGHGPTMETNTTENQKDNARGQSNKGHGFSTSLNPYTLYFKSFSSQLFKETVGNKRKHENLEF
Protein: Reproductive homeobox 3A (V9GXY5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
RASRSVNGCETKMDSTQGTKVLPAEEGKNEEDGGQVESALGATAARGRGKEALNGESPAAAGTAGLVEEDRNKEDGGTKGGEKNEQEVREQIPEHVEGESDQAEAPRQVPRRRLHHRFTQWQLDELERIFRMNYFLSLEARDGFRRGENNTGGIRGYKVSEVLLLLLRTSFLKTVEEPCSATIAKAT
Protein: 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) (E3NZ06)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKIAVIGQSLFGQEVYKELKNEGHMIVGVFTIPDKDGKVDPLAIEAEKDGVPVFKFPRWRLKGKAITEVVDQYKAVGAELNVLPFCSQFIPMEVIDHPKHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTVFWADDGLDTGPILLQRECDVEPNDNVNSIYKRFLFPEGVKGMVEAVRLIATGKAPRIKQPEEGATYECIQKKENSKIDWNQPAEAIHNWIRGNDRVPGAWAEIDGKSVSFYGSTLLENDHFSSNGQPLEIPGASRAALVTKNGLVLFGNDGKMLLVKNLQFEDGKMIPGSQYFKAGVTSTVELSEDENRFAEQMRVVWKSILTNVEKIEDTTDFFKSGAASMDVVRLVEEVKLRAAQLQLQNEDVYMATSFQEFIQMCVRKLRGEDEEEEFNVDYVEKKLNNMTIHIPHQLFINGEFVDAEGGKTYKSINPTDGQAICDVSLAQISDVEKAVAAAKEAFEEGEWGKMNPRDRGKLLYKLADLMEQHQEELATIESIDSGAVYTLALKTHIGMSIQTFRYFAGWCDKIQGCTIPINQARPNRNLTFTKKEPIGVCGIVIPWNYPLMMLAWKTAACLAAGNTVVLKPAQVTPLTALKFAELTALAKFPKGVVNILPGSGSLVGQRLSDHPDVRKLGFTGSTEIGKHIMKSCAVSNVKKVSLELGGKSPLIIFNDCDLDKAVRMGMSSVFFNKGENCIAAGRLFIEESIHDIFLERVVSEIRKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCEKGVKEGAKLVCGGKQVERPGFFFEPTVFTDVQDHMYIAVEESFGPVMIISKFSNGEVDKVLQRANATEFGLASGVFTRDISKALYVSEKLQAGTVFINTYNKTDVAAPFGGFKQSGFGKDLGQEALNEYLKTKCVTVEY
Protein: Protein SEC13 homolog (GATOR complex protein SEC13) (Secretory protein 13) (Q9V3J4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat (By similarity). At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles (By similarity). Recruited to transcriptionally active chromatin at the time of transcription initiation by RNA polymerase II. Required for proper expression of ecdysone-responsive genes such as Eip74EF and Eip75B during larval development. Required for reactivation of transcription after heat shock. Required for nuclear import of phosphorylated Mad via importin msk. Has no role in classical nuclear localization signal (cNLS)-dependent nuclear import via importin-beta.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20144761}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:20144761}. Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:P55735}. Lysosome membrane {ECO:0000305|PubMed:27166823}. Note=Localizes to chromatin, specifically to areas undergoing transcriptional activation. Chromatin localization is independent of the nuclear pore complex (PubMed:20144761).
Interaction partners:
- GATOR2 complex protein Wdr24
- Nucleoporin seh1
- Nuclear pore complex protein Nup107
- Secretory 16, isoform I
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup75
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin 43kD
- GATOR complex protein Iml1
- GATOR2 complex protein Mio
Sequence:
MVSLLQEIDTEHEDMVHHAALDFYGLLLATCSSDGSVRIFHSRKNNKALAELKGHQGPVWQVAWAHPKFGNILASCSYDRKVIVWKSTTPRDWTKLYEYSNHDSSVNSVDFAPSEYGLVLACASSDGSVSVLTCNTEYGVWDAKKIPNAHTIGVNAISWCPAQAPDPAFDQRVTSRSAAVKRLVSGGCDNLVKIWREDNDRWVEEHRLEAHSDWVRDVAWAPSIGLPRSQIATASQDRHVIVWSSNADLSEWTSTVLHTFDDAVWSISWSTTGNILAVTGGDNNVTLWKENTEGQWIRINYESGTAIQSKQPSHLPHSHSQQQQALQQHQQQAPSHPGPSSDSEHSSNLSNSQLSN
Protein: Large ribosomal subunit protein mL48 (39S ribosomal protein L48, mitochondrial) (L48mt) (MRP-L48) (Q8JZS9)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96GC5}.
Interaction partners:
- 39S ribosomal protein L40
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL30m
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS22
- Large ribosomal subunit protein mL62
Sequence:
MSGTLGKVLGVWTNTVSKQGFSLLRFRSLGENPIFSAGGILWTSRHYKTKPTHGIGRYRHLVKVQEPKKKKAKVELRAINVGTDYEYGVLNIHLTAYDMSLAESYAQYVHRLCNRLSIKVEESYAMPTKTMEVMRLPDQGNKMVLDSVLTTHERVVQISGLSATFAEIFLEVLQSNLPEGVRLSVREHTEEDFKGRFKARPELEELLAKLN
Protein: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I) (GNT-I) (GlcNAc-T I) (P26572)
Organism: Homo sapiens (Human)
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with BRI3 isoform 1 at the perinuclear region. {ECO:0000269|PubMed:30983867}.
Interaction partners:
- Alpha-mannosidase 2
- Alpha-mannosidase 2x
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
- Adhesion G protein-coupled receptor L2
- Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- Diacylglycerol O-acyltransferase 1
Sequence:
MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALSSQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVTHIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSAWNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN