wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c oxidase assembly factor 6 (B8A5J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Complex III subunit 9
- Cytochrome b-c1 complex subunit 6
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MSAPNASQRKACWDARDELWKCLDVNKDLTSACEKHQREFEANCPAQWVKYFSKRRDFLKYKEKIEKEGYEPTEGASKL
Protein: Spindle assembly abnormal protein 6 homolog (Q7ZVT3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21273447}. Note=Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. {ECO:0000250|UniProtKB:Q6NRG6}.
Interaction partners:
- Serine/threonine-protein kinase PLK4
- Centrosomal P4.1-associated protein
- SCL-interrupting locus protein homolog
- Centrosomal protein of 135 kDa
- Centrosomal protein 192.
- WRN RecQ-like helicase.
- Pericentrin
- Helicase ATP-binding domain-containing protein.
- FA complementation group M.
- Centrosomal protein of 63 kDa
Sequence:
MTELLFNKRLQVLVKSKDTDERRSVIRVSIELQLPSSPVHRKDLVVRLTDDTDLYFLYNLIISEEDFQSLKVQQGLLIDFTSFPQKFIDLLEQCICEQDKESPRFLLQLSSSSSAFDHSPSNLNIVETNAFKHLTHLSLKLLPGSDTDIKKYLASCLSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQELESSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVPQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLSRKQETVAMFETPAAALRSAAVPHNMAFPITSTINSKYPLALSCVSSGSRSVLTSSNGPKVQFNPMSVKPSAAEVSPAAFSQPANKENSEPVGLDSKYFERRDDSIPLRGLLPSMHLNREVPKPLNTAAAKATPSAFFPG
Protein: Dihydroorotate dehydrogenase, electron transfer subunit (Q725W0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Dihydroorotate dehydrogenase
- Dihydroorotase
- Orotate phosphoribosyltransferase
- Carbamoyl phosphate synthase large chain
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase small chain
- Orotidine 5'-phosphate decarboxylase
- Pyridine nucleotide-disulfide oxidoreductase
Sequence:
MHTSACTELKVLDLVPFGLTSGEARFYALRLERPDWGTWAPGQFVMLRPAGWALDMLWARPFSICRVSRRDLVIFFQVVGRGTRRLAELHAGDTVHVWGPLGNSFAVEPDTPTLLLAGGIGIAPFIGYVHEHPKPWNVWMDFGHRMPLGCYPFDSISDRIMADTHMEECPEDLQKFIDLLGSRMAEFAEKQGLVLACGPTPFLKTVRDLALHHGVRTQLSLETRMACGVGACLGCVCRTTEKWPDPAKAEGRVQTCTSGPIFWADQITFDEA
Protein: Protein S100 (S100 calcium-binding protein) (A0A060WYU6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- S100 calcium binding protein, beta
- S100 calcium binding protein, beta
- Protein S100
- Protein S100
- Protein S100
- S100 calcium binding protein P
- TIR domain-containing protein
Sequence:
MGSKLESAMEGLIQVFHSYSSKEGDKYKLSKVELKNLLQGELSEFLAACKDPMVVEKIMSDLDDNKDGEVDFQEFVVLVVALTVACNEFFVEGLNE
Protein: G-protein coupled receptor-associated protein LMBRD2 (LMBR1 domain-containing protein 2) (Q68DH5)
Organism: Homo sapiens (Human)
Function: Recruited to ligand-activated beta-2 adrenergic receptor/ADRB2, it negatively regulates the adrenergic receptor signaling pathway. May also regulate other G-protein coupled receptors including type-1 angiotensin II receptor/AGTR1 (Probable).
Subcellular location: Cell membrane {ECO:0000305|PubMed:28388415}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSGAALGLEIVFVFFLALFLLHRYGDFKKQHRLVIIGTLLAWYLCFLIVFILPLDVSTTIYNRCKHAAANSSPPENSNITGLYATANPVPSQHPCFKPWSYIPDGIMPIFWRVVYWTSQFLTWILLPFMQSYARSGGFSITGKIKTALIENAIYYGTYLLIFGAFLIYVAVNPHLHLEWNQLQTIGIAAANTWGLFLLVLLLGYGLVEIPRSYWNGAKRGYLLMKTYFKAAKLMTEKADAEENLEDAMEEVRKVNESIKYNHPLRKCVDTILKKCPTEYQEKMGRNMDDYEDFDEKHSIYPSEKSLVKLHKQVIYSVQRHRRTQVQWQILLEQAFYLEDVAKNETSATHQFVHTFQSPEPENRFIQYFYNPTFEWYWECLLRPWFYKILAVVLSIFSVIVVWSECTFFSTTPVLSLFAVFIQLAEKTYNYIYIEIACFLSIFFLSICVYSTVFRIRVFNYYYLASHHQTDAYSLLFSGMLFCRLTPPLCLNFLGLTHMDSSISHKNTQPTAYTSIMGSMKVLSFIADGFYIYYPMLVVILCIATYFSLGTRCLNLLGFQQFMGDDDMTSDLVNEGKELIRKEKRKRQRQEEGENRRREWKERYGHNREDSTRNRNIHTDPKESNFSDVNTNRSAFKYTRANNRTERDRIELLQDAEPLDFNAETFTDDPLESESGRYQPGGRYLSMSRSDIFNDV
Protein: Protein-arginine deiminase type-1 (EC 3.5.3.15) (Peptidylarginine deiminase I) (Protein-arginine deiminase type I) (Q9Z185)
Organism: Mus musculus (Mouse)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ULC6}.
Interaction partners:
Sequence:
MASPRAVQLSLRKPTHAVCVVGVETLVNVYSDVPKGAKTFGVSGSSEVKIYMVYDPSRVAEPAGWAHWPLDANVDVVVVADTVSKDLYDFKVKVSYFESQEAAALAHSVLYLTAVDVSLDVDTGRTGKVKKGSGDKKTWRWGPGGSGAILLVNCDRDIHGSREDLHANHLKSLEDLQDMSPMVLSCGGPDELFESHKLVLKASLSDSRRLKVFCARGGTSLSNYKQVLGPRHSSYEVERHSGERAIQFYVEGLAFPDASFSGLLSLSVSLVDTRPLSEVSVFTDSVTFRVAPWIMTPNTQPPLELYVCSVTDIHGRNDKFLEDMSHLATKANCKLVVCPRAENRNDRWIQDELEFGYIDAPHKSFPVVFDSPRNRGLRDFALKRILGPDFGYVTREIEFAGASGLDSFGNLDVSPPVRVGNTDYPLGRILIGGSFPKPSGRRMARVVRDFLQAQQVQSPVELYSDWLSVGHVDEFLSFVPTSDQKGFRLLLASPSACLQLFQEKKEEGYGEAEQFDGLKHKAKRSINDILADKHLRRDSAHVQKCIDWNREVLKRELGLSESDIVDIPQLFFLKGAYAEAFFPDMVNMVVLGKYLGIPKPFGPLINGRCCLEEKVRSLLEPLGLRCVFIDDFLFYHQLLGEIHCGTNVRRKPFTFKWWNSVP
Protein: Neutral amino acid transporter B(0) (ATB(0)) (ASC-like Na(+)-dependent neutral amino acid transporter ASCT2) (Insulin-activated amino acid transporter) (Sodium-dependent neutral amino acid transporter type 2) (Solute carrier family 1 member 5) (P51912)
Organism: Mus musculus (Mouse)
Function: Sodium-dependent amino acids transporter that has a broad substrate specificity, with a preference for zwitterionic amino acids. It accepts as substrates all neutral amino acids, including glutamine, asparagine, and branched-chain and aromatic amino acids, and excludes methylated, anionic, and cationic amino acids.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7702599, ECO:0000269|PubMed:8662767}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome {ECO:0000250|UniProtKB:Q15758}.
Interaction partners:
- Large neutral amino acids transporter small subunit 1
- Sodium-coupled neutral amino acid symporter 1
- Amino acid transporter heavy chain SLC3A2
- Sodium-coupled neutral amino acid symporter 2
- Glutaminase kidney isoform, mitochondrial
- Sodium- and chloride-dependent neutral and basic amino acid transporter B
- High affinity cationic amino acid transporter 1
- Sodium-dependent neutral amino acid transporter B
- Glutaminase liver isoform, mitochondrial
- Solute carrier family 2, facilitated glucose transporter member 1
Sequence:
MAVDPPKADPKGVAVDSSRRCPALGSREDQSAKAGGCCGSRDRVRRCIRANLLVLLTVAAVVAGVGLGLGVSAAGGADALGPARLTRFAFPGELLLRLLKMIILPLVVCSLIGGAASLDPSALGRVGAWALLFFLVTTLLASALGVGLALALKPGAAVTAITSINDSVVDPCARSAPTKEALDSFLDLVRNIFPSNLVSAAFRSFATSYEPKDNSCKIPQSCIQREINSTMVQLLCEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPVGILFLVASKIVEMKDVRQLFISLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIMTPLATAFGTSSSSATLPLMMKCVEEKNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLNGVSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVSLPVKDISLILAVDWLVDRSCTVLNVEGDAFGAGLLQSYVDRTKMPSSEPELIQVKNEVSLNPLPLATEEGNPLLKQYQGPTGDSSATFEKESVM
Protein: Transcription factor MTB1 (Basic helix-loop-helix protein 113) (Protein MYC2-TARGETED BHLH 1) (Transcription factor bHLH113) (bHLH transcription factor bHLH113) (A0A3Q7ELQ2)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcription factor that negatively regulates jasmonate (JA) signaling. Negatively regulates JA-dependent response to wounding, JA-induced expression of defense genes, JA-dependent responses against herbivorous insects, and JA-dependent resistance against Botrytis cinerea infection. Plays a positive role in resistance against the bacterial pathogen Pseudomonas syringae pv tomato DC3000.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MVTGNMLWSGEDKAMVASVLGKEAFEYLMSGSVSAECSLMAIGNDQNLQNKLSDLVERPNAANFSWNYAIFWQISRSKSGELVLGWGDGCCREPKEAEEREVKKILNLRLDDEGQQRMRKRVLQKLHMLFGGTDEDNYAFGLDRVTDTEMFFLASMYFSFPRGEGGPGKCFGSGKYLWLSDALTSNLDYCARSFLAKSAGMQTIALIPTDVGVVELGSVRSIPESLELLQNIKSCFSSFLSLVRDKQAAGIAAVPEKNEGNNPRLSNSGAVTERTDGNPKIFGHDLNSGTHFREKLAVRKAEERPWDMYQNGNRMPFVNARNGLNPASWAQFSNVKLGKPVELYAPPTPGHNLMNGGREEFRLNNFQHQKPAARMQIDFTGATSRTIVSPAHNVESEHSDVEASCKEDRAGPVDEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNISKMDKASLLGDAIAYITELQKKLRDMESERELRLGSTSRDAITSEDSPSSEIQIRGPDINIEAANDEVIVRVSCSLETHPLSRIIQIFKEAQINVVESKLSAGNGTVYHTFVIKSSGSEQLTKEKLLAAFSSESNSLRQLSPKLHKVILPSLF
Protein: Delta(9)-fatty-acid desaturase fat-6 (EC 1.14.19.-) (EC 1.14.19.1) (Fatty-acid desaturase 6) (FAT-6) (Stearoyl-CoA desaturase fat-6) (G5EGN2)
Organism: Caenorhabditis elegans
Function: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols. Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases. Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- Nuclear hormone receptor family member nhr-80
- Delta
- Delta
- Nuclear hormone receptor family member nhr-49
- Mediator of RNA polymerase II transcription subunit 15
- Delta
- Acetyl-CoA carboxylase
- Long chain fatty acid elongase 2
- Sterol regulatory element binding protein sbp-1
Sequence:
MTVKTRSNIAKKIEKDGGPETQYLAVDPNEIIQLQEESKKIPYKMEIVWRNVALFAALHFAAAIGLYQLIFEAKWQTVIFTFLLYVFGGFGITAGAHRLWSHKSYKATTPMRIFLMILNNIALQNDVIEWARDHRCHHKWTDTDADPHNTTRGFFFAHMGWLLVRKHPQVKEQGAKLDMSDLLSDPVLVFQRKHYFPLVILCCFILPTIIPVYFWKETAFIAFYTAGTFRYCFTLHATWCINSAAHYFGWKPYDSSITPVENVFTTIAAVGEGGHNFHHTFPQDYRTSEYSLKYNWTRVLIDTAAALGLVYDRKTACDEIIGRQVSNHGCDIQRGKSIM
Protein: Troponin I, cardiac muscle (Cardiac troponin I) (P23693)
Organism: Rattus norvegicus (Rat)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T, cardiac muscle
- Troponin C, slow skeletal and cardiac muscles
- Actin, alpha cardiac muscle 1
- Tropomyosin alpha-1 chain
- Myosin-6
- Troponin T, slow skeletal muscle
- Tropomyosin beta chain
- Tropomyosin alpha-4 chain
- Tropomyosin 3
- Troponin T, fast skeletal muscle
Sequence:
MADESSDAAGEPQPAPAPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQEMEREAEERRGEKGRVLSTRCQPLVLDGLGFEELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLTQKIYDLRGKFKRPTLRRVRISADAMMQALLGTRAKESLDLRAHLKQVKKEDIEKENREVGDWRKNIDALSGMEGRKKKFEG
Protein: CXADR-like membrane protein (Adipocyte adhesion molecule) (Coxsackie- and adenovirus receptor-like membrane protein) (CAR-like membrane protein) (Q9H6B4)
Organism: Homo sapiens (Human)
Function: May be involved in the cell-cell adhesion. May play a role in adipocyte differentiation and development of obesity. Is required for normal small intestine development.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:14573622, ECO:0000269|PubMed:22155368}. Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tissue factor pathway inhibitor
- N-glycosylase/DNA lyase
Sequence:
MSLLLLLLLVSYYVGTLGTHTEIKRVAEEKVTLPCHHQLGLPEKDTLDIEWLLTDNEGNQKVVITYSSRHVYNNLTEEQKGRVAFASNFLAGDASLQIEPLKPSDEGRYTCKVKNSGRYVWSHVILKVLVRPSKPKCELEGELTEGSDLTLQCESSSGTEPIVYYWQRIREKEGEDERLPPKSRIDYNHPGRVLLQNLTMSYSGLYQCTAGNEAGKESCVVRVTVQYVQSIGMVAGAVTGIVAGALLIFLLVWLLIRRKDKERYEEEERPNEIREDAEAPKARLVKPSSSSSGSRSSRSGSSSTRSTANSASRSQRTLSTDAAPQPGLATQAYSLVGPEVRGSEPKKVHHANLTKAETTPSMIPSQSRAFQTV
Protein: Fes1C (Q9LZL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g43860
- Heat shock 70 kDa protein 17
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Heat shock 70 kDa protein 4
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein eL38z/eL38y
Sequence:
MAKDGPNWDGLLKWSLSHSDGTRPTCQLSEEDRKWFAEAMQSQTVDVVKRLKEITQVLQTPQQVLEAHEVTPQDIEGLLDELQEHVESIDMANDLHSVGGLVPLLGYLKNSNANIRAKSADVVSTIVENNPRSQESVMEANGLESLLLRFTSDTDMHSRTQALGAISSLIRNNKPGITGFRIANGYSGLKDALETDSVRFQRKALNLLHYLLQENDSDSDIAIEFGLHHLMMHLVSSFDADVREAALRGLLELVKARKDCSTCGSSIVKGDERLRQILKDRIKAISRVKAMSLFMSQEDLSAAKEERQLLDSLWTTIFNEPSSL
Protein: Ribosome association toxin RatA (Toxin RatA) (P0AGL5)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Binds to 50S ribosomal subunits, preventing them from associating with 30S subunits to form 70S ribosomes and reducing polysomes. It does not cause ribosomes to dissociate however. The antibiotic paromomycin blocks the anti-association activity of RatA. Overexpression results in inhibition of growth in liquid cultures, and in a decrease in protein translation. The other gene of this operon, ratB, is not the cognate antitoxin in this strain; in CFT073 however it does fulfill this function.
Interaction partners:
- UPF0125 protein RatB
- Small toxic protein ShoB
- Small toxic protein TisB
- Ubiquinone biosynthesis O-methyltransferase
Sequence:
MILFVGFLLMEIVMPQISRTALVPYSAEQMYQLVNDVQSYPQFLPGCTGSRILESTPGQMTAAVDVSKAGISKTFTTRNQLTSNQSILMNLVDGPFKKLIGGWKFTPLSQEACRIEFHLDFEFTNKLIELAFGRVFKELAANMVQAFTVRAKEVYSAR
Protein: SS18L1 subunit of BAF chromatin remodeling complex (Q9BR54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQSLSTEARYVPRVPQHRDQISPRSPQHGGQICPRSPLHRGQICPRSPPARRYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALTQSGSSQGLHSQGSLSDAISTGLPPSSLLQGQIGN
Protein: Formyltetrahydrofolate deformylase (EC 3.5.1.10) (Formyl-FH(4) hydrolase) (P37051)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). Provides the major source of formate for the PurT-dependent synthesis of 5'-phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool.
Interaction partners:
- Bifunctional protein FolD
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Serine hydroxymethyltransferase
- Aminomethyltransferase
- Phosphoribosylglycinamide formyltransferase
- Dihydrofolate reductase
- Methionine synthase
- Dihydromonapterin reductase
- Formate dehydrogenase-O major subunit
- Formate dehydrogenase, cytochrome b556
Sequence:
MHSLQRKVLRTICPDQKGLIARITNICYKHELNIVQNNEFVDHRTGRFFMRTELEGIFNDSTLLADLDSALPEGSVRELNPAGRRRIVILVTKEAHCLGDLLMKANYGGLDVEIAAVIGNHDTLRSLVERFDIPFELVSHEGLTRNEHDQKMADAIDAYQPDYVVLAKYMRVLTPEFVARFPNKIINIHHSFLPAFIGARPYHQAYERGVKIIGATAHYVNDNLDEGPIIMQDVIHVDHTYTAEDMMRAGRDVEKNVLSRALYKVLAQRVFVYGNRTIIL
Protein: CD69 (Q5M851)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- T-cell surface glycoprotein CD4
- Sphingosine 1-phosphate receptor 1
- L-selectin
- T-lymphocyte activation antigen CD80
- Interferon gamma
- CD44 antigen
- Granzyme B
- Forkhead box P3
- Receptor-type tyrosine-protein phosphatase C
- Low affinity immunoglobulin gamma Fc region receptor III
Sequence:
MNSEECSITENSSSHLERGQRDHGTSVHFEKHREGSIQVPIPCAVLVVVLITSLIIALFALSVGKYNCPGFYENLESFDHHAASCKNEWFSYNGKCYFFSTTTKTWALAQKSCSEDDATLAVIDSEKDMAFLKRYAGGLKHWIGLRNEASQTWKWANGKEFNSWFNVTGSKKCVSLNHTDVASVDCEANLHWICSKASL
Protein: Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Lysosomal thiol reductase IP30) (Q9ESY9)
Organism: Mus musculus (Mouse)
Function: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds. Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation.
Subcellular location: Secreted {ECO:0000250}. Lysosome {ECO:0000269|PubMed:11701933}.
Interaction partners:
Sequence:
MSWSPILPFLSLLLLLFPLEVPRAATASLSQASSEGTTTCKAHDVCLLGPRPLPPSPPVRVSLYYESLCGACRYFLVRDLFPTWLMVMEIMNITLVPYGNAQERNVSGTWEFTCQHGELECRLNMVEACLLDKLEKEAAFLTIVCMEEMDDMEKKLGPCLQVYAPEVSPESIMECATGKRGTQLMHENAQLTDALHPPHEYVPWVLVNEKPLKDPSELLSIVCQLYQGTEKPDICSSIADSPRKVCYK
Protein: LEM domain-containing protein Bocksbeutel (Q709R6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inner nuclear membrane protein. May have a role in maintaining the structural integrity of the nuclear lamina. During pupal development, plays essential and redundant functions with the other LEM domain proteins; MAN1 and Ote. Also has a redundant but important role with Ote in larval development.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885, ECO:0000269|PubMed:24700158}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15035436, ECO:0000269|PubMed:16439308}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Note=Detected in the nucleus envelope and cytoplasm. In the cytoplasm, it appears to localize to discrete foci. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus, nucleoplasm {ECO:0000269|PubMed:15035436}. Cytoplasm {ECO:0000269|PubMed:15035436}. Note=Predominantly expressed in the nucleoplasm with very low expression levels in the cytoplasm. {ECO:0000269|PubMed:15035436}.; SUBCELLULAR LOCATION: [Isoform B]: Nucleus inner membrane {ECO:0000269|PubMed:15035436}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:15035436}. Note=Appears to be predominantly expressed in the nucleus envelope but expression is not uniform. Outside of the nucleus it is located to discrete foci which may be the endoplasmic reticulum. {ECO:0000269|PubMed:15035436, ECO:0000305|PubMed:15035436}.
Interaction partners:
- Barrier-to-autointegration factor
- Inner nuclear membrane protein Man1
- Otefin
- Cell division cycle 5, isoform A
Sequence:
MSDLSYLDTLGNKELLAKCLEHGLPGVPVTDSTRSVIIRRLKAKITGVPLNKSKSASKKAIPRRETVHGSQVTTPTSEPVRRTPGKSAGRTSSNNNKISEQSRRTIAYGLDNTSISGRSVQTTTTVSDMSSQSEDDDSYMVDSPVPNYSKDQQPRRYVSLAKSGVLTTSYTREVDQPLYEQEDIPRSYTYERPHVPAATLHALPTYEPRIEPSTYRPTDLGFSRPLLTQTNLNSTSYEESSTYNPKLSPISPRNTFSGSARPFGGPAPAPAPIRQRQSVPVSGSNLARGRLLQPTTAVNTLYPQLNEFYDQPNDAGEPMETESESEVEEVPINSHFQKNRFSPLARKPLVRHHDQVSPMAQFRALAVSLDQKYNLKFYLILVVSVMLATMVYVVLTPNA
Protein: Fatty acid synthase, beta subunit (Q5AQM2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Fatty acid synthase subunit alpha
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase alpha subunit pkiB reductase
- Fatty acid synthase alpha subunit stcJ reductase]
- Fatty acid synthase, putative
- Uncharacterized protein
- 3-oxoacyl-[acyl-carrier-protein] synthase
- Fatty acid activator Faa4, putative
- AMP-binding enzyme, putative
- Uncharacterized protein
Sequence:
MYGTSTGPQTGINTPRSSQSLRPLILSHGSLEFSFLVPTSLHFHASQLKDTFTASLPEPTDELAQDDEPSSVAELVARYIGHVAHEVEEGEDDAHGTNQDVLKLALNEFERAFMRGNDVHAVAATLPGITAKKVLVVEAYYAGRAAAGRPTKPYDSALFRAASDEKARIYSVFGGQGNIEEYFDELREVYNTYTSFVDDLISSSAELLQSLSREPDANKLYPKGLNVMQWLREPDTQPDVDYLVSAPVSLPLIGLVQLAHFAVTCRVLGKEPGEILERFSGTTGHSQGIVTAAAIATATTWESFHKAVANALTMLFWIGLRSQQAYPRTSIAPSVLQDSIENGEGTPTPMLSIRDLPRTAVQEHIDMTNQHLPEDRHISISLVNSARNFVVTGPPLSLYGLNLRLRKVKAPTGLDQNRVPFTQRKVRFVNRFLPITAPFHSQYLYSAFDRIMEDLEDVEISPKSLTIPVYGTKTGDDLRAISDANVVPALVRMITHDPVNWEQTTAFPNATHIVDFGPGGISGLGVLTNRNKDGTGVRVILAGSMDGTNAEVGYKPELFDRDEHSVKYAIDWVKEYGPRLVKNATGQTFVDTKMSRLLGIPPIMVAGMTPTTVPWDFVAATMNAGYHIELAGGGYYNAKTMTEAITKIEKAIPPGRGITVNLIYVNPRAMGWQIPLIGKLRADGVPIEGLTIGAGVPSIEVANEYIETLGIKHIAFKPGSVDAIQQVINIAKANPKFPVILQWTGGRGGGHHSFEDFHQPILQMYSRIRRHENIILVAGSGFGGAEDTYPYLSGNWSSRFGYPPMPFDGCLFGSRMMTAKEAHTSKNAKQAIVDAPGLDDQDWEKTYKGAAGGVVTVLSEMGEPIHKLATRGVLFWHEMDQKIFKLDKAKRVPELKKQRDYIIKKLNDDFQKVWFGRNSAGETVDLEDMTYAEVVHRMVDLMYVKHEGRWIDDSLKKLTGDFIRRVEERFTTAEGQASLLQNYSELNVPYPAVDNILAAYPEAATQLINAQDVQHFLLLCQRRGQKPVPFVPSLDENFEYWFKKDSLWQSEDLEAVVGQDVGRTCILQGPMAAKFSTVIDEPVGDILNSIHQGHIKSLIKDMYNGDETTIPITEYFGGRLSEAQEDIEMDGLTISEDANKISYRLSSSAADLPEVNRWCRLLAGRSYSWRHALFSADVFVQGHRFQTNPLKRVLAPSTGMYVEIANPEDAPKTVISVREPYQSGKLVKTVDIKLNEKGQIALTLYEGRTAENGVVPLTFLFTYHPDTGYAPIREVMDSRNDRIKEFYYRIWFGNKDVPFDTPTTATFNGGRETITSQAVADFVHAVGNTGEAFVERPGKEVFAPMDFAIVAGWKAITKPIFPRTIDGDLLKLVHLSNGFKMVPGAQPLKVGDVLDTTAQINSIINEESGKIVEVCGTIRRDGKPIMHVTSQFLYRGAYTDFENTFQRKDEVPMQVHLASSRDVAILRSKEWFRLDMDDVELLGQTLTFRLQSLIRFKNKNVFSQVQTMGQVLLELPTKEVIQVASVDYEAGTSHGNPVIDYLQRNGTSIEQPVYFENPIPLSGKTPLVLRAPASNETYARVSGDYNPIHVSRVFSSYANLPGTITHGMYTSAAVRSLVETWAAENNIGRVRGFHVSLVDMVLPNDLITVRLQHVGMIAGRKIIKVEASNKETEDKVLLGEAEVEQPVTAYVFTGQGSQEQGMGMELYATSPVAKEVWDRADRHFIENYGLSIIDIVKNNPKELTVHFGGPRGKAIRQNYMSMTFETVNADGTIKSEKIFKEIDETTTSYTYRSPTGLLSATQFTQPALTLMEKASFEDMRSKGLVQRDSSFAGHSLGEYSALAALADVMPIESLVSVVFYRGLTMQVAVERDEQGRSNYSMCAVNPSRISKTFNEQALQYVVGNISEQTGWLLEIVNYNVANMQYVAAGDLRALDCLTNLLNYLKAQNIDIPALMQSMSLEDVKAHLVNIIHECVKQTEAKPKPINLERGFATIPLKGIDVPFHSTFLRSGVKPFRSFLLKKINKTTIDPSKLVGKYIPNVTARPFEITKEYFEDVYRLTNSPRIAHILANWEKYEEGTEGGSRHGGTTAASS
Protein: Zinc finger protein X-linked (E9PEP7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDEDGLELQQEPNSFFDATGADGTHMDGDQIVVEVQETVFVSDVVDSDITVHNFVPDDPDSVVIQDVIEDVVIEDVQCPDIMEEADVSETVIIPEQVLDSDVTEEVSLAHCTVPDDVLASDITSASMSMPEHVLTGDSIHVSDVGHVGHVGHVEHVVHDSVVEAEIVTDPLTTDVVSEEVLVADCASEAVIDANGIPVDQQDDDKGNCEDYLMISCGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQPEDEDLNVAEIADEVYMEVIVGEEDAAAAAAAAAVHEQQMDDNEIKTFMPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKRRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYRCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELKKHMRIHTGEKPYQCQYCEYRSADSSNLKTHVKTKHSKEMPFKCDICLLTFSDTKEVQQHALIHQESKTHQCLHCDHKSSNSSDLKRHIISVHTKDYPHKCDMCDKGFHRPSELKKHVAAHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQSELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP
Protein: Uncharacterized amino-acid permease C11D3.08c (Q10087)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized amino-acid permease C965.11c
Sequence:
MSDIDKESLKQNQKQWENEVELGESREANQDDELLMSLGYKPEFTREFSYVSIFGQSFGSMGLCPAMAGSLIFSMNCGGGGMVWSWIIGCICLIPVSISLGELASSMPTSGGLYFWIFTLASPSSRAFLCWVCGYVSVLGYATIYASTVYSASSMVQALAVIGSPSYSPTKYEQYGIYAALLFVISAMTAIPSRVIAKVNIINITFQFLVSIILIIALAAGSDSTTRNSGSFIFGDFTNYSGWSNMGWAFILSFTTPVWVVSGFESSAAVAEESTNAAKAAPFAMISSLGVATILGWCIVITVVATMGHDFNAILGSSLGQPVAQVLVNNVGNKGALGIFSLLVIALCLNCISLLIAASREVFAFCRDGGIPGSRYLRLLTKQKVPLNAILLVLLYSLLVGLLILVNVTAISSVFNLAIIALYIAYSGPLMCRFVYNKFQPGVFYVGKWSKPAALWSLVWMWFMILMLLFPQYQKPNQDEMNWAIVVLGFVMVFCVVYYYLPKIGGKTFFTGPIPTVQQENEYISGVPLNELSLSSLPLPKDFDQKQITE