wanglab/gogpt-training-data huggingface dataset:
Protein: Centromere/microtubule binding protein cbf5, putative (Q38CM1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar protein 10
- 50S ribosomal protein L7Ae, putative
- Uncharacterized protein
- Nucleolar RNA binding protein, putative
- Nucleolar protein 56
- Gar1/Naf1 RNA binding region
- H/ACA ribonucleoprotein complex subunit
- H/ACA ribonucleoprotein complex subunit 2
- Integral membrane bound transporter domain-containing protein
- Guanine nucleotide-binding protein subunit beta-like protein
Sequence:
MVSKKLGEAQRKEDFCIPLEGQHTDCALSPEEWPLLLKNYDRLNVRSSHFTVLDCGWSPLRRPLSQYVKYGMINLDKPSNPSSHEVVSWIKRILKCEKTGHAGTLDPKVTGALIICIDRATRLVKSQQNAGKTYIGVLRLHDTVSEKKVVASLQRLTGPCFQRPPLIAAVKRQLRIRNIYSNQLIEYDKHRHLAVFETHCEAGTYIRTLCVHLGLILGVGGHMEELRRIRTGVISEDDHISTMHDVLDAQWLYDNEKDETYLRRVILPCEYLLTNYKRVVVKDSAVNAVCYGAKLMIPGLARFDNGIERDDVIVLMTTKGEAIALAYAEMSTSQMASVDHGIVARSKRVIMDRDTYPRRWGLGPVAVKKRTMMKDGLLDKYGRPQANTPSDWFYVDYGGVSTNAEGVQYGEAPRKNGKRPRSEADDT
Protein: Cathepsin Lb (F1R7B3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Napsin A aspartic peptidase
- Cathepsin D
- BH3-interacting domain death agonist
- Apoptosis regulator Bcl-2
- Baculoviral IAP repeat-containing 5b.
Sequence:
MELQSVRFACESPPGRMMFALLVTLYISAVFAAPSIDIQLDDHWNSWKSQHGKSYHEDVEVGRRMIWEENLRKIEQHNFEYSYGNHTFKMGMNQFGDMTNEEFRQAMNGYTHDPNQTSQGPLFMEPSFFAAPQQVDWRQRGYVTPVKDQKQCGSCWSFSSTGALEGQLFRKTGKLISMSEQNLVDCSRPQGNQGCNGGLMDQAFQYVKENKGLDSEQSYPYLARDDLPCRYDPRFNVAKITGFVDIPSGNELALMNAVAAVGPVSVAIDASHQSLQFYQSGIYYERACSSSRLDHAVLVVGYGYQGADVAGNRYWIVKNSWSDKWGDKGYIYMAKDKNNHCGVATKASYPLM
Protein: Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1) (Transcription elongation factor TFIIS.o) (P10711)
Organism: Mus musculus (Mouse)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB1
- General transcription factor IIF subunit 1
- General transcription factor IIE subunit 1
- TATA-box-binding protein
- Transcription initiation factor IIA subunit 2
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB9
- General transcription and DNA repair factor IIH helicase subunit XPD
Sequence:
MEDEVVRIAKKMDKMVQKKNAAGALDLLKELKNIPMTLELLQSTRIGMSVNALRKQSTDEEVTSLAKSLIKSWKKLLDGPSTDKDPEEKKKEPAISSQNSPEAREESSSSSNVSSRKDETNARDTYVSSFPRAPSTSDSVRLKCREMLAAALRTGDDYVAIGADEEELGSQIEEAIYQEIRNTDMKYKNRVRSRISNLKDAKNPNLRKNVLCGNIPPDLFARMTAEEMASDELKEMRKNLTKEAIREHQMAKTGGTQTDLFTCGKCKKKNCTYTQVQTRSADEPMTTFVVCNECGNRWKFC
Protein: Trimethylguanosine synthase (DUF707) (Q56Y17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 2-like protein
- H/ACA ribonucleoprotein complex subunit 3-like protein
- H/ACA ribonucleoprotein complex subunit 1-like protein 2
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
- Nucleolar protein 56
- Nucleolar protein 56
- O-fucosyltransferase 27
- Probable ribosome-binding factor A
- At4g12700
- O-fucosyltransferase 15
Sequence:
MGTMHRSGAPRRTNENAKVIITTILGIVFGTFIGITLPSLSFKINLPSRLISSLDVAISGDKSPEDFGSRKFPEIYVPTNPRGAELLPPGIVVAKTDFYLRRLWGEPNEDLKKKPKYLVTFTVGFEQRNHINGVVKKFSEDFQILLFHYDGRTTEWDQFEWSKSAIHISTRKQTKWWYAKRFLHPDVVSAYEYIFIWDEDLGVEHFNADKYIELVKKHGLEISQPGLEPNNGLTWEMTKRRGDREVHKDTKEKPGWCKDPHLPPCAAFVEIMAPVFSREAWRCVWHMIQNDLVHGWGLDFALRRCVEPAHEKIGVVDSQWIIHKVIPSLGSQGKSENGKAPWQGVRDRCKMEWTMFQNRLADADKEYLGKMVKD
Protein: Trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (P19813)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1697585}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1697585}.
Interaction partners:
- Catalase
- Protein YIPF
- Aldose 1-epimerase
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- Glucose-6-phosphate isomerase
- 1,4-alpha-glucan-branching enzyme
- hexokinase
- Hexokinase-3
- hexokinase
- Phosphoacetylglucosamine mutase
Sequence:
MPGSTWELHLLLLLGLGLGSEQALPPPCESQIYCHGELLHQVQMARLYPDDKQFVDMPLSTAPDQVLQSFAELAATYNNTVPREQLEKFVQEHFQAVGQELESWTPGDWKESPQFLQKISDPKLRAWAEQLHLLWKKLGKKIKPEVLSQPERFSLIYSQHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMAETVKGMLQNFLDLVTAYGHIPNGGRVYYLQRSQPPLLTLMMDRYVAHTGDLAFLRENIETLALELDFWAENRTISVSSGGNSHTLNRYHVPYGGPRPESYSKDTELAHTLPEGSWETLWAELKAGAESGWDFSSRWLVGSPNPDSLGSIRTSKLVPVDLNAFLCQAEELLSGFYSRLGNESQATKYRNLRAQRIAALTALLWDEDKGAWFDYDLENQKKNHEFYPSNLTPLWAGCFSDPAIADKALQYLQDSQILNHRHGIPTSLQNTGQQWDFPNAWAPLQDLVIRGLAKSPSARTQEVAFQLAQNWIRTNFDVYSQRSAMYEKYDISNAQPGGGGEYEVQEGFGWTNGVALMLLDRYGDRLSSGTQLALLEPHCLAAALLLSFLTR
Protein: Annexin A4 (35-beta calcimedin) (Annexin IV) (Annexin-4) (Carbohydrate-binding protein p33/p41) (Chromobindin-4) (Endonexin I) (Lipocortin IV) (P32.5) (PP4-X) (Placental anticoagulant protein II) (PAP-II) (Protein II) (P09525)
Organism: Homo sapiens (Human)
Function: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
Subcellular location: Zymogen granule membrane {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein {ECO:0000250|UniProtKB:P50994}.
Interaction partners:
- Protein S100-A10
- C-C chemokine receptor type 5
Sequence:
MATKGGTVKAASGFNAMEDAQTLRKAMKGLGTDEDAIISVLAYRNTAQRQEIRTAYKSTIGRDLIDDLKSELSGNFEQVIVGMMTPTVLYDVQELRRAMKGAGTDEGCLIEILASRTPEEIRRISQTYQQQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDEGNYLDDALVRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRISQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAEKLYKSMKGLGTDDNTLIRVMVSRAEIDMLDIRAHFKRLYGKSLYSFIKGDTSGDYRKVLLVLCGGDD
Protein: SD02625p (Q8T4G2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGQVTAQPMTPVEVWPLLVIGSRSEQSSNGLNEAQYHRDQTDYRMGMPHSLLQLHPDEYVSGHRKRPGGDHEEAMPGEPLILAAALAAHPRLLEVARKDDAQRGGSNPCGNHEGTVELDEQSARTTQVLHLRQIDRLRRGQASNVVVAHAVLLKAAAGCHQQMVLAIAKIKSASLHIGHCIPLHTAVDHSIHNGGVQQAGRVLVLERVVSIKR
Protein: Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (G3MU80)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQCSPDPEDLLIVPTHDIPSYDESLDPFGPEGHLSLDIDCFSKFMSRSDNRIMSKPIIVRGIPWRILAICRNQQGSRHSMNSRVNRSNFNFGFFLQCNNDELLQKRGMWRCYGTAVLEVLNADGPSIQKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDGYVVNDTIKLRCRFTADVPTGANYMWDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESNIVLAMQRVFYELQMASEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYCGVEQKINERFSFPEKMNLASCCELGPMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHESAVDPTSSAKWCKFDDDVVSRTTTDDAIVSNFGGEKTMNSSAYMLVYVRDNAIDQFLAPIPDSQIPQSVSRTFEMERLHRNREKKKLEEEQLCMGIVLVTPDIVASNHSFDLVDQSIVHDSIPHETVWKHMFTAELYQFVHDRLFEKSAMQKIDMFDSDDEARQARRDNLRRIKSKKFNFRLWRMTDSYSLERTTQKLTSRLRPSEFIDCKTDTRLDTLLSQDFETIYVEFSNNIERPLCEYDTARDLLFFVKYYDTMTDKFTIIGHTMFDCHKRFNLYRSMLCEMIGLPADTELKYYMEHAASYLELVDLTQNYSIGRLVEEQDGGILVVEKVETSTSTQNAKQKMNELFLDVEVEFVQSFYNKKPEEEPFEQFVKRICLDDKLFTVAEEIGARLNVDPKKVLIWTRVSGSRFEPFFDDYMLNTCKGLMTRPVHDPRAYKRYRVQYAIMPFDIDEISKHRIQTKLFWQLPNGHVEELTLFPLKEGTVIDIINEAKRYYPFVEGGSGKFRLLQIGAPPLSNQRVYQIYGENTLISDLDQRTMYKLVSSALHCRLEEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRLRRKLNDVSDADFAKYKFALLSRDKLCRTIEFNNGEKVNLADMANQTTGVPQVYIGLDHKSPIQHSSEAAIRILN
Protein: SCAN domain-containing protein 1 (P57086)
Organism: Homo sapiens (Human)
Function: May regulate transcriptional activity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger protein 24
- PiggyBac transposable element-derived protein 1
- Zinc finger protein 397
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein 396
- Zinc finger and SCAN domain-containing protein 22
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger protein 394
- Myeloid zinc finger 1
Sequence:
MAATEPILAATGSPAAVPPEKLEGAGSSSAPERNCVGSSLPEASPPAPEPSSPNAAVPEAIPTPRAAASAALELPLGPAPVSVAPQAEAEARSTPGPAGSRLGPETFRQRFRQFRYQDAAGPREAFRQLRELSRQWLRPDIRTKEQIVEMLVQEQLLAILPEAARARRIRRRTDVRITG
Protein: E3 ubiquitin-protein ligase SIAH1A (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1A) (Seven in absentia homolog 1a) (Siah-1a) (Siah1a) (mSiah-1a) (P61092)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation. It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling. Has some overlapping function with SIAH2 (By similarity). Required for completion of meiosis I in males. Induces apoptosis in cooperation with PEG3. Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4. Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Partially nuclear.
Interaction partners:
- Calcyclin-binding protein
- Catenin beta-1
- Axin-1
- E3 ubiquitin-protein ligase SIAH1B
- Adenomatous polyposis coli protein
- Ubiquitin carboxyl-terminal hydrolase 19
- Glycogen synthase kinase-3 beta
- Beta-catenin-interacting protein 1
- Dapper homolog 1
Sequence:
MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKAEHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC
Protein: Major capsid protein (Gene product 34) (gp34) (Gene product T) (gpT) (Major head protein) (Q9T1W1)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Capsid protein that self-assembles to form an icosahedral capsid, about 54 nm in diameter.
Subcellular location: Virion {ECO:0000269|PubMed:8599204}. Host cytoplasm {ECO:0000305|PubMed:8599204}. Note=Capsid.
Interaction partners:
Sequence:
MIVTPASIKALMTSWRKDFQGGLEDAPSQYNKIAMVVNSSTRSNTYGWLGKFPTLKEWVGKRTIQQMEAHGYSIANKTFEGTVGISRDDFEDDNLGIYAPIFQEMGRSAAVQPDELIFKLLKDGFTQPCYDGQNFFDKEHPVYPNVDGTGSAVNTSNIVEQDSFSGLPFYLLDCSRAVKPLIFQERRKPELVARTRIDDDHVFMDNEFLFGASTRRAAGYGFWQMAVAVKGDLTLDNLWKGWQLMRSFEGDGGKKLGLKPTHIVVPVGLEKAAEQLLNRELFADGNTTVSNEMKGKLQLVVADYL
Protein: Ragulator complex protein LAMTOR4 homolog (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 4) (Q9VZL6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of the TOR pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. As part of the Ragulator complex, may activate the TOR signaling cascade in response to amino acids.
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- Ragulator complex protein LAMTOR3 homolog
- Ragulator complex protein LAMTOR1
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- Ragulator complex protein LAMTOR2 homolog
- GH04846p
- GH16429p
- Raptor, isoform B
- Serine/threonine-protein kinase mTor
- Folliculin
- RE13835p
Sequence:
MLKMDREKLIVPNQIGYLILKEDGAVLESGGDLKNDERSANVIMGLLNLTETIDESFMPSSSCERITIDYEHHYYSICMSNRRIYIIKISKSQNGVTTTTSSSSSNSVYNDASDSGAVLA
Protein: Ferredoxin (P83520)
Organism: Brugmansia arborea (Angel's trumpet tree) (Datura arborea)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:7765623}.
Interaction partners:
Sequence:
ATYKVKLVTPDGPVEFDCPDDVYILDQAEEEGHELPYSCRAGSCSSCAGKVTAGTVDQSDGNFLDDDQMADGFVLTCVAYPQSDVTIETHKEEELTG
Protein: Thrombospondin-type laminin G domain and EAR repeat-containing protein (TSP-EAR) (Q8WU66)
Organism: Homo sapiens (Human)
Function: Plays a critical role in tooth and hair follicle morphogenesis through regulation of the Notch signaling pathway. May play a role in development or function of the auditory system.
Subcellular location: Secreted {ECO:0000250|UniProtKB:J3S6Y1}. Cell surface {ECO:0000250|UniProtKB:J3S6Y1}. Cell projection, stereocilium {ECO:0000250|UniProtKB:J3S6Y1}. Note=Secreted protein which may bind to the cell surface via a membrane receptor. {ECO:0000250|UniProtKB:J3S6Y1}.
Interaction partners:
Sequence:
MSALLSLCFVLPLAAPGHGTQGWEPCTDLRPLDILAEVVPSDGATSGIRIVQVHGARGLQLSVAAPRTMSFPASRIFSQCDLFPEEFSIVVTLRVPNLPPKRNEYLLTVVAEESDLLLLGLRLSPAQLHFLFLREDTAGAWQTRVSFRSPALVDGRWHTLVLAVSAGVFSLTTDCGLPVDIMADVPFPATLSVKGARFFVGSRRRAKGLFMGLVRQLVLLPGSDATPRLCPSRNAPLAVLSIPRVLQALTGKPEDNEVLKYPYETNIRVTLGPQPPCTEVEDAQFWFDASRKGLYLCVGNEWVSVLAAKERLDYVEEHQNLSTNSETLGIEVFRIPQVGLFVATANRKATSAVYKWTEEKFVSYQNIPTHQAQAWRHFTIGKKIFLAVANFEPDEKGQEFSVIYKWSHRKLKFTPYQSIATHSARDWEAFEVDGEHFLAVANHREGDNHNIDSVIYKWNPATRLFEANQTIATSGAYDWEFFSVGPYSFLVVANTFNGTSTKVHSHLYIRLLGSFQLFQSFPTFGAADWEVFQIGERIFLAVANSHSYDVEMQVQNDSYVINSVIYELNVTAQAFVKFQDILTCSALDWEFFSVGEDYFLVVANSFDGRTFSVNSIIYRWQGYEGFVAVHSLPTVGCRDWEAFSTTAGAYLIYSSAKEPLSRVLRLRTR
Protein: UPF0053 protein YegH (P76389)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEWIADPSIWAGLITLIVIELVLGIDNLVFIAILAEKLPPKQRDRARVTGLLLAMLMRLLLLASISWLVTLTQPLFSFRSFTFSARDLIMLFGGFFLLFKATMELNERLEGKDSNNPTQRKGAKFWGVVTQIVVLDAIFSLDSVITAVGMVDHLLVMMAAVVIAISLMLMASKPLTQFVNSHPTIVILCLSFLLMIGFSLVAEGFGFVIPKGYLYAAIGFSVMIEALNQLAIFNRRRFLSANQTLRQRTTEAVMRLLSGQKEDAELDAETASMLVDHGNQQIFNPQERRMIERVLNLNQRTVSSIMTSRHDIEHIDLNAPEEEIRQLLERNQHTRLVVTDGDDAEDLLGVVHVIDLLQQSLRGEPLNLRVLIRQPLVFPETLPLLPALEQFRNARTHFAFVVDEFGSVEGIVTLSDVTETIAGNLPNEVEEIDARHDIQKNADGSWTANGHMPLEDLVQYVPLPLDEKREYHTIAGLLMEYLQRIPKPGEEVQVGDYLLKTLQVESHRVQKVQIIPLRKDGEMEYEV
Protein: Translation initiation factor eIF2B subunit delta (eIF2B GDP-GTP exchange factor subunit delta) (Q09924)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 2 subunit gamma
- Probable eukaryotic translation initiation factor 2 subunit beta
- Probable U3 small nucleolar RNA-associated protein 18
- Serine--tRNA ligase, cytoplasmic
Sequence:
MGFSAEQAKKDGKDQSPVSESSSVGGTSPATASSVVSPNEPKLSGKEAKALKKARKQASRRAKAEAAAANNPPGVSEEKKVAIPNKNSNQQKKASKQNPQNSPETDANLQEKKIFEEKQVSIFSHLDWRRRRTTENIPKDIHPAVIRLGLKLANYKIFGSNQRCIDLLKTFKIVIQDYQTPYGTTLSRHLTTHINSQIAYLVSTRPLSISMGNAIRFLKLEISVLDIDLTDDEGKELLLEKIDSYIRDRIIIAGQVIVQAATEKIQDGDVILTYLHSSTVNDVLIHAKNVGKKFRVVVVDSRPEFEGRVCLKLLTEHGIECTYVMISALSYIMQEVTKIFLGGHAMLSNGALYSRAGTSLISLLGHESNVPVIACCESYKFTERIQLDSLVYNELAPGDQLVNMGVDDFEEKPGVLANWKSVKNLKLLSLKYDVTPPRLITVCVCEMGLLPSTSVPAIINEFKQVYA
Protein: Nucleoprotein (Nucleocapsid protein) (Q9QK88)
Organism: Rift valley fever virus (RVFV)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
EQWVREFAYQGFDARRVIELLKQYGGADWEKDAKKMIVLALTRGNKP
Protein: Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (Linoleate hydratase) (Myosin cross-reactive antigen) (MCRA) (B5XK69)
Organism: Streptococcus pyogenes serotype M49 (strain NZ131)
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate, and of linoleate at its cis-9- and cis-12-double bond to yield 10-hydroxy-12-octadecenoate and 10,13-dihydroxyoctadecanoate. Is not active on trans-double bonds and esterified fatty acids as substrate; is only active on cis-9- and/or cis-12-double bond of C16 and C18 fatty acids without any trans-configurations, producing 10-hydroxy and 10,13-dihydroxy derivatives. Appears to play a role in oleic acid detoxification and bacterial virulence.
Interaction partners:
Sequence:
MYYTSGNYEAFATPRKPEGVDQKSAYIVGTGLAGLAAAVFLIRDGHMAGERIHLFEELPLAGGSLDGIEKPHLGFVTRGGREMENHFECMWDMYRSIPSLEIPGASYLDEFYWLDKDDPNSSNCRLIHKRGNRVDDDGQYTLGKQSKELIHLIMKTEESLGDQTIEEFFSEDFFKSNFWVYWATMFAFEKWHSAVEMRRYAMRFIHHIDGLPDFTSLKFNKYNQYDSMVKPIIAYLESHDVDIQFDTKVTDIQVEQTAGKKVAKTIHMTVSGEAKAIELTPDDLVFVTNGSITESSTYGSHHEVAKPTKALGGSWNLWENLAAQSDDFGHPKVFYQDLPAESWFVSATATIKHPAIEPYIERLTHRDLHDGKVNTGGIITITDSNWMMSFAIHRQPHFKEQKENETTVWIYGLYSNSEGNYVHKKIEECTGQEITEEWLYHLGVPVDKIKDLASQEYINTVPVYMPYITSYFMPRVKGDRPKVIPDGSVNLAFIGNFAESPSRDTVFTTEYSIRTAMEAVYSFLNGERGIPQGFNSAYDIRELLKAFYYLNDKKAIKDMDLPIPALIEKIGHKKIKDTFIEELLKDANLM
Protein: Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase) (MASA homolog) (Q9UHY7)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.
Interaction partners:
- Methylthioribulose-1-phosphate dehydratase
- Acireductone dioxygenase-requiring))
- Methylthioribose-1-phosphate isomerase
- Cleavage stimulation factor subunit 3
- E3 ubiquitin-protein ligase NRDP1
- Gamma-adducin
- Beta-adducin
- Alpha-adducin
- Acyl-coenzyme A thioesterase THEM4
Sequence:
MVVLSVPAEVTVILLDIEGTTTPIAFVKDILFPYIEENVKEYLQTHWEEEECQQDVSLLRKQAEEDAHLDGAVPIPAASGNGVDDLQQMIQAVVDNVCWQMSLDRKTTALKQLQGHMWRAAFTAGRMKAEFFADVVPAVRKWREAGMKVYIYSSGSVEAQKLLFGHSTEGDILELVDGHFDTKIGHKVESESYRKIADSIGCSTNNILFLTDVTREASAAEEADVHVAVVVRPGNAGLTDDEKTYYSLITSFSELYLPSST
Protein: Beta-glucosidase 45 (F4HVG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKNLTSFVIVILLQSLLFHVYGRHQSSSKNILVDSSPFPSDFLFGTASSAYQYEGAFLTDGKSLNNWDVFTHKNPGKILDKNNADRAVDQYNRFLEDIQLMSFLGVNSYRFSISWCRILPRGRFGEINYLGIKYYNIFIDALISRGIKPFVTLNHVDYPQELEDRFQSWLNPEMQKEFGYLADICFKHFGNRVKYWTTLNEPNQQLILGYLTGKFPPSRCSSPYGNCSQGNSETEPFIAAHNMILAHAKAVNIYKTKYQKEQKGSIGIVVQTSWFEPISDSNADKEAAERAQSFYSNWILDPVIYGKYPKEMVDILGPALPQFSSNEVKNLEKSRADFVGINHYTSYFIQDCLTSACNTGHGAFKAEGYALKLDRKGNVTIGELTDVNWQHIDPTGFHKMLNYLKDRYPNMPMFITENGFGDLQKPETTDKELLNDTKRIQYMSGYLEALQAAMRDGANVKGYFVWSLLDNFEWLFGYKVRFGLFHVDLTTLKRSKLRYETSDDSYEARSSHVTNHILSRRNTNPFTKWVNVLRRTSTSCTKP
Protein: Pre-mRNA-splicing factor CWC21 (Complexed with CEF1 protein 21) (Q03375)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome, together with ISY1. May do so by stabilizing the catalytic center or the position of the RNA substrate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
- Pre-mRNA-splicing factor BUD31
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SNT309
- Pre-mRNA-splicing factor CWC2
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-splicing factor SNU114
Sequence:
MSYNGIGLKSAKGSSTSGHVQRSLASNNRRRPQGSQQQRQQRQNAIKKASHDKASRPLAVQKQIETHMEKREIEVQVSELRDRLEEEETLSEEQIDKKCEALRAKLTNEWQEQQRMSSLYTPRKARLTEEQHRHE
Protein: Elongation factor 1-delta (E9PRY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEAPLGSILSPCPGRAATGRAGTGRVGTGLRPPAVLQLCPLLAFYRCVRKMRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWVNKSSFDQAERAFVEWSQALLLAPDGSRRQGTPNTGQQVAVPDLAHQPSPPVNGQPPLGSLQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRLQERAGLAEGARRGRRDRRGRNILGNKRAGLRRADGEAPSALPYCYFLQKDAEAPWLSKPAYDSAECRHHAAEALRVAWCLEAASLSHRPGPRSGLSVSSLRPNRKMATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVAGASRQENGASVILRDIARARENIQKSLAGSSGPGASSGTSGDHGELVVRIASLEVENQSLRGVVQELQQAISKLEARLNVLEKSSPGHRATAPQTQHVSPMRQVEPPAKKPATPAEDDEDDDIDLFGSDNEEEDKEAAQLREERLRQYAEKKAKKPALVAKSSILLDVKPWDDETDMAQLEACVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNKI
Protein: Retinoblastoma-like protein 1 (107 kDa retinoblastoma-associated protein) (p107) (pRb1) (P28749)
Organism: Homo sapiens (Human)
Function: Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation (By similarity). Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression (By similarity). Controls histone H4 'Lys-20' trimethylation (By similarity). Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters (By similarity). Potent inhibitor of E2F-mediated trans-activation. May act as a tumor suppressor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor E2F5
- Transcription factor E2F4
- Transcription factor Dp-1
- Cyclin-dependent kinase 2
- Transcription factor E2F1
- Transcription factor E2F3
- Transcription factor E2F2
- Transcription factor Dp-2
- Retinoblastoma-like protein 2
- G1/S-specific cyclin-E1
Sequence:
MFEDKPHAEGAAVVAAAGEALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVTHWLACSLYVACRKSIIPTVGKGIMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKYEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRQDLLNPSFKGLPSDFHTADFTASEEPPCIIAVLCELHDGLLVEAKGIKEHYFKPYISKLFDRKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTRDTPLGKLTAQANVEYNLQQHFEKKRSFAPSTPLTGRRYLREKEAVITPVASATQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTDEQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLEIVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWSHDSALWEALQVSANKVPTCEEVIFPNNFETGNGGNVQGHLPLMPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSSSITAENVSILPGQTLLTMATAPVTGTTGHKVTIPLHGVANDAGEITLIPLSMNTNQESKVKSPVSLTAHSLIGASPKQTNLTKAQEVHSTGINRPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPREVVAYNKNINDDFEMIDCDLEDATKTPDCSSGPVKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAPPLSPFPHIKQQPGSPRRISQQHSIYISPHKNGSGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH