wanglab/gogpt-training-data huggingface dataset:
Protein: Homeotic protein deformed (P07548)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Homeotic protein controlling Drosophila head development. Transcriptional activator of the apoptotic activator protein rpr in cells at the maxillary/mandibular boundary.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein extradenticle
- Homeobox protein abdominal-A
- Homeotic protein Sex combs reduced
- Homeobox protein abdominal-B
- Homeobox protein homothorax
- Deformed epidermal autoregulatory factor 1
- Segmentation protein fushi tarazu
- Segmentation protein cap'n'collar
- Heme oxygenase
- Homeotic protein antennapedia
Sequence:
MSSFLMGYPHAPHHVQSPMSMGNGLDPKFPPLADDYHHYNGHYSMTASTGHMSGAVGGGAGVGSVGGGGAGGMTGHPHSMHPADMVSDYMAHHHNPHSHSHSHTHSLPHHHSNSAISGHHQASAGGYSSNYANATPPSHPHSHPHAHPHQSLGYYVHHAPEFISAGAVHSDPTNGYGPAANVPNTSNGGGGGGSGAVLGGGAVGGSANGYYGGYGGGYGTANGSVGSTHSQGHSPHSQMMDLPLQCSSTEPPTNTALGLQELGLKLEKRIEEAVPAGQQLQELGMRLRCDDMGSENDDMSEEDRLMLDRSPDELGSNDNDDDLGDSDSDEDLMAETTDGERIIYPWMKKIHVAGVANGSYQPGMEPKRQRTAYTRHQILELEKEFHYNRYLTRRRRIEIAHTLVLSERQIKIWFQNRRMKWKKDNKLPNTKNVRKKTVDANGNPTPVAKKPTKRAASKKQQQAQQQQQSQQQQTQQTPVMNECIRSDSLESIGDVSSSLGNPPYIPAAPETTSSYPGSQQHLSNNNNNGSGNNNNNNNNNNSNLNNNNNNNQMGHTNLHGHLQQQQSDLMTNLQLHIKQDYDLTAL
Protein: CARD domain-containing protein E10 (Q66677)
Organism: Equine herpesvirus 2 (strain 86/87) (EHV-2)
Function: Activates host NF-kappa-B and JNK pathways. Induces hyperphosphorylation and redistribution of host bcl-10 from the cytoplasm to the plasma membrane. The inhibitory effect of cellular bcl-10 on NF-kappa-B pathway is then overcome allowing NF-kappa-B activation.
Subcellular location: Host cell membrane {ECO:0000269|PubMed:11238466}. Note=E10 does not contain a putative transmembrane and must therefore be targeted to the plasma membrane in a different manner. The two cysteines located on the C-terminal region are essential for the protein localization and constitute a consensus site for geranylgeranylation.
Interaction partners:
Sequence:
MAEKYPLQAGDPCVTLTEEDIWDVERLCLEELRVLLVSHLKSHKHLDHLRAKKILSREDAEEVSSRATSRSRAGLLVDMCQDHPRGFQCLKESCKNEVGQEHLVDLLERAFEKHCGDKLTQKWWESGADGRNPRRPPGSEDNSGYTALLPTNPSGGGPSIGSGHSRPRGRDDSGGIGGGVYPFSHGGARVVGGGWGGWGESGGAGRGGSLLSGGHGGHPPHGGPGGGGRDYYGGGGSGYYESIPEPANFPNSGGGGRGGGVRYDAGGDGRLGGLPPDPQEVDDPSLSVQGRGGPAPDPPSPPLRTRRFFCC
Protein: Metallothionein-1X (MT-1X) (Metallothionein-IX) (MT-IX) (P80297)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. May be involved in FAM168A anti-apoptotic signaling.
Interaction partners:
- Metallothionein-1F
- Metallothionein-2
- Metallothionein-1M
- Metallothionein 1H-like protein 1
- Metallothionein-1H
- Metallothionein
- Metallothionein-1G
Sequence:
MDPNCSCSPVGSCACAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGTSDKCSCCA
Protein: Uncharacterized protein (Q380Y5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNLNEVASGYFGDIPYCLPLECSAFFDALTSSRLHRIPQSMMSRIDSEAYYTDKNTRFHNLLSGERGTINRRGNPSTGDPIGIMDLIPYLHCASPADRIACNDCTGGCYIAIELNESSQEVGRDRTEEASRISHCIFVTLDLKGIDHMWQSLLIFLLGGTDNDDVVYVLTDVDIYFHMGAPYGSFMFSIWALAISSLLHHFASFPNDRIQERLSHVKVILKFSKDCVRSTTVDDIYLFIESKLKVCVVNKLDTSTGSTNNMENCFTDSFATANQEAWLEKMTEIVTNCHEELCDTGVECVNSNPSCILLIIPEEDSLVSMLEQCLHDSYTSSPMSIAASLDHFPELLAARANGVPLTVFCSKKKIEREFLRPHHECCFGYMDIKFLVFGESNRGEDLDIIRALFHRLPHTIYVPYPGHCSSENNFVDTERVSNDCLQDAMNVVLWLFRRFRFESRKEDTGPVLRIPESFFATMDASLFFDEVMSAMCSFGLLSQLRNSDGLPSYQLSVIGRALSYRFRLPYDSSFPELSPFDVKCIFWCHALRQPKAVAEKLICNSHKFTSWVRDAINRFCSRYQIVFTENLSMGDETLVRALSSIPKYYDSVSRVELFLCCTTGKRTTLSRQSTRMISTSCRGWFDQASPGTDMCGPQKSPVNIYCYPSHHELCEIHFGGKVLQCPLDVSYPLIASHVILHTALWNNAVFLECAQEIGKTPLLSIPLALLESPLFKRMTRGSGDARTGMWLDNCIGDNPSPSDAMELGSLMGRTVSFLGLCNCGRSLRKREESGCSLKRPRREALESLKVPSDAEVETIKEFVNLAKRLGRENAEKRFKTVKGFAFLNDSHENHPYYLHLMKTSSS
Protein: Adenylate cyclase, putative (O06362)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDAEAFVGFRQVPAARYGGLMATTAALPRRIHAFVRWVVRTPWPLFSLSMLQSDIIGALFVLGFLRYGLPPQDNIQLQDLPPVNLLIFVSTVIILFLAGAVVNLKLLMPVFRWQRRDNLLTEPDPAATELARSRALRMPLYRTLISLAVWATGGGVFILASWSVAKHAAPVVAVATALGATATAIIGYLQSERVLRPVAVAALRSGVPENVNAPGVILRLMLAWIPSTGVPLLAIVLAVAADKIALLHATPEALFNPILMMALAALGIGSVSTLLVAMSIADPLRQLRWALSEVQRGNYNAHMQIYDASELGLLQAGFNDMVRELSERQRLRDLFGRYVGEDVARRALERGTELGGQERDVAVLFVDLVGSTQLAATRPPAEVVQLLNEFFRVVVETVARHGGFVNKFQGDAALAIFGAPIEHPDGAGAALSAARELHDELIPVLGSAEFGIGVSAGRAIAGHIGAQARFEYTVIGDPVNEAARLTELAKLEDGHVLASAIAVSGALDAEALCWDVGEVVELRGRAAPTQLARPMNLAAPEEVSSEVRG
Protein: Clavesin-1 (Cellular retinaldehyde-binding protein-like) (Retinaldehyde-binding protein 1-like 1) (clathrin vesicle-associated Sec14 protein 1) (Q8IUQ0)
Organism: Homo sapiens (Human)
Function: Required for normal morphology of late endosomes and/or lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Early endosome membrane {ECO:0000269|PubMed:19651769}; Peripheral membrane protein {ECO:0000269|PubMed:19651769}.
Interaction partners:
Sequence:
MGPVSLLPKYQKLNTWNGDLAKMTHLQAGLSPETIEKARLELNENPDVLHQDIQQVRDMIITRPDIGFLRTDDAFILRFLRARKFHQADAFRLLAQYFQYRQLNLDMFKNFKADDPGIKRALIDGFPGVLENRDHYGRKILLLFAANWDQSRNSFTDILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLIKPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGTLPPYDMGTWARTLLGPDYSDENDYTHTSYNAMHVKHTSSNLERECSPKLMKRSQSVVEAGTLKHEEKGENENTQPLLALD
Protein: Small ribosomal subunit protein bS21m (37S ribosomal protein mrp21, mitochondrial) (Q8WZK1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS8m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS19m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS11m
Sequence:
MNSSYFPGVLGVRWVHTNRKLQKRKEEHGAFQDSLHFMIPAAETKDLGASVTVGNSLTRAFRQVDRICQRNNVPRLFRSQRFYEKPSEKRSRVRSERHRARFRAGIVRLVNLAKNMRRWGY
Protein: AT01712p (Q6NMT8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- FI04011p
Sequence:
MSNTSVRPIPTLKGIFSVPRVTQSRNFLKENKVSLRSLEKSTSQKLAAKEPTRPKWMPPLRRSSSVMGDSKAEKPAAKGKTIKQNSLQNGRSTSRSQHQLAVAVPAEGERFDGLEERNPILYDPSENLESENLQEPSSDTDIDRCQSCGTNRSSTSIAIQTEDITDELYLTNALKKCNFDARSILEESGAKYGENYKPMQYENEEDLEQLPLSARSNSSKQSRFNMSEMEAMPMTEAEPANYGASDDEAPLSARSRFTTASNVTTISSKSKRREHKLGSRDEVRLPRYLEKQKREKAVAKQLAESLDPDCPRGHVLLSDQDRLTHLTNAKKRYEQLVNELNHMPMTAQTLRVRNRKAEIDKELTTVEEDIRIYSKAKVFVLASKSRQL
Protein: ATP-dependent Clp protease ATP-binding subunit ClpX (P0CAU2)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Function: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit
- CpdR
- ATP-dependent zinc metalloprotease FtsH
- Lon protease
- Cell division protein FtsZ
- Regulator of CtrA degradation
- Cell cycle transcriptional regulator CtrA
- ATP synthase subunit beta
- ATP-dependent protease subunit HslV
- RNA-binding protein Hfq
Sequence:
MTKAASGDTKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREEHKIAFVKSKDGVPTPREICEVLDDYVIGQGHAKKVLAVAVHNHYKRLNHASKNNDVELAKSNILLVGPTGTGKTLLAQTLARIIDVPFTMADATTLTEAGYVGEDVENIVLKLLQAADYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLEKIISARGAAKSIGFGAKVTDPEERRTGEILRNVEPDDLQRFGLIPEFIGRLPVVATLEDLDEAALVKILTEPKNAFVKQYQRLFEMENIGLTFTEDALHQVAKKAIARKTGARGLRSIMEGILLETMFELPTYEGVEEVVVNAEVVEGRAQPLLIYAEKKGGAASA
Protein: Type-1 angiotensin II receptor (Angiotensin II type-1 receptor) (AT1 receptor) (P43240)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30556}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
Interaction partners:
- Angiotensinogen
- Angiotensin II receptor type 2
- Serpin family E member 1
- Guanine nucleotide-binding protein G
- Uncharacterized protein.
- G protein subunit alpha 12.
- G protein subunit alpha 13.
- Angiotensin-converting enzyme.
- Angiotensin-converting enzyme.
- Lysophosphatidic acid receptor 1
Sequence:
MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYVAIVHPMKSPVRRTMLMAKVTCIIIWLLAGLASLPTIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKTLKRAYEIQKNKPRNDDIFKIIMAIVLFFFFSWVPHQIFTFLDVLIQLGIIHDCKIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKKYFLQLLKYIPPKAKSHSSLSTKMSTLSYRPSDHGNASTKKSASCVEVE
Protein: Protein atp11, mitochondrial (P87127)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for the assembly of the mitochondrial F1-F0 complex. May interact with the alpha and/or beta subunits of F1-ATPase (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Protein atp12
- Cytochrome B pre-mRNA-processing protein 6
- Mitochondrial zinc maintenance protein 1
- ATP synthase subunit beta, mitochondrial
Sequence:
MLPIWKLPVNHLLCHSFKSIPRTSAYAVRFAHHTSNNDDLEVKKNTVYERYERKLKSKAEELHMPVTNLLKKGQTKEREHVIPKKSFSAKKSLVGQNAKKSDLSGLNRYIDVEKIKELPTSTIEKLWRARNIGDDILSACIPKEIYEKMLSRARMYPYFVLPLPRGDKGIESHFLQWNFPNKNEAHLLVTSLLEYKLKGSYAAPHTIMLHFADLLNLKGITLMRCQFEPKKLSANDVQLLVLAIQKFYNASENTPLGKERLALLAAFSKGADFDLHKVATHMDMLE
Protein: Reverse rubrerythrin-1 (revRbr 1) (NADH peroxidase) (NPXase) (Npx) (EC 1.11.1.1) (Rubperoxin 1) (Rpr 1) (Q97D82)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries from NADH to revRbr 1. Plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Also exhibits NADH oxidase (NADH:O(2) oxidoreductase) activity in vitro, which is 100-fold lesser than that of FprA1/2 using the same electron transfer components. Therefore, its predominant function is most likely as a scavenger of its preferred substrate, H(2)O(2).
Interaction partners:
- Reverse rubrerythrin-2
- Rubredoxin
- Transcriptional regulator PerR
- Desulfoferrodoxin
- NADH-rubredoxin oxidoreductase
- Flavo-diiron protein FprA2
- Flavo-diiron protein FprA1
Sequence:
MKKFKCVVCGYIYTGEDAPEKCPVCGAGKDKFVEVKDEGEGWADEHKIGVAKGVDKEVLEGLRANFTGECTEVGMYLAMARQADREGYPEVAEAYKRIAFEEAEHASKFAELLGEVVVADTKTNLQMRVDAEKGACEGKKELATLAKKLNYDAIHDTVHEMCKDEARHGSAFRGLLNRYFK
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (H0YMI4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMQLVYCVFFFLLVCRSNKSPWVCLTCSSVHCGRYVNGHAKKHYEDAQVPLTNHKKSEKQDKVQHTVCMDCSSYSTYCYRCDDFVVNDTKLGLVQKVREHLQNLENSAFTADRHKKRKLLENSTLNSKLLKVNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCCINGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEGRWFHFNDSTVTLTDEETVVKAKAYILFYVEHQAKAGSDKL
Protein: Homeobox protein Hox-D1 (Homeobox protein Hox-GG) (Q9GZZ0)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-B1
- Homeobox protein Hox-A1
- Endoplasmic reticulum junction formation protein lunapark
Sequence:
MSSYLEYVSCSSSGGVGGDVLSLAPKFCRSDARPVALQPAFPLGNGDGAFVSCLPLAAARPSPSPPAAPARPSVPPPAAPQYAQCTLEGAYEPGAAPAAAAGGADYGFLGSGPAYDFPGVLGRAADDGGSHVHYATSAVFSGGGSFLLSGQVDYAAFGEPGPFPACLKASADGHPGAFQTASPAPGTYPKSVSPASGLPAAFSTFEWMKVKRNASKKGKLAEYGAASPSSAIRTNFSTKQLTELEKEFHFNKYLTRARRIEIANCLHLNDTQVKIWFQNRRMKQKKREREGLLATAIPVAPLQLPLSGTTPTKFIKNPGSPSQSQEPS
Protein: GH13495p (Q9VBT7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LP23833p
Sequence:
MVEQGKEDATEFHPAPEWLDETYLERLLRDLKNDPGLRITDLVIKPATAKGDNYASVMTRVRILFLKSGAKSPETEYYIVKTTYENDAFASGIFSQYQVSTTEMRMYEKILPQLSSLIEKTRQPEKVFAKTLHVDYEHEAIIFEDLAVTKYVLADRLVGFDLEHTRLGLRKLAKMHAAAAVLNERQPGLLTKFDHGIFNRHTQAFAPFFVNTVGVAADFARECPELGERYATKLKKLQERVMEYSTRVYDPQPGDFNTLVHGDYWVNNVMLRYGENKEPLDMTLIDFQFCSWSSPAVDLHYFFNTSVQVDIRYEQQDALFQYYHTVLVETLKDLNFGGYIPTLRQFVLQLERGRFFAVTVALVCQAILTNDQNADADFNALMKDDERGRNFRKVLYTNKRLQDNLKRELPRFDRSGLLDVID
Protein: ATP-dependent helicase FUN30 (EC 3.6.4.12) (P31380)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs, facilitating single-stranded DNA (ssDNA) production by the EXO1 and SGS1 machinery. Promotes gene silencing at heterochromatin by regulating the chromatin structure within or around silent loci. Also required for heterochromatin organization at centromeres.
Subcellular location: Nucleus. Chromosome. Note=Recruited to double-strand breaks (DSBs) sites of DNA damage.
Interaction partners:
- Exodeoxyribonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- ATP-dependent helicase SGS1
- DNA repair protein RAD9
- DNA mismatch repair protein MSH2
- Histone H3
- DNA replication regulator DPB11
- C-1-tetrahydrofolate synthase, mitochondrial
- ISWI chromatin-remodeling complex ATPase ISW1
Sequence:
MSGSHSNDEDDVVQVPETSSPTKVASSSPLKPTSPTVPDASVASLRSRFTFKPSDPSEGAHTSKPLPSGSPEVALVNLAREFPDFSQTLVQAVFKSNSFNLQSARERLTRLRQQRQNWTWNKNASPKKSETPPPVKKSLPLANTGRLSSIHGNINNKSSKITVAKQKTSIFDRYSNVINQKQYTFELPTNLNIDSEALSKLPVNYNKKRRLVRADQHPIGKSYESSATQLGSAREKLLANRKYGRHANDNDEEEEESMMTDDDDASGDDYTESTPQINLDEQVLQFINDSDIVDLSDLSDTTMHKAQLIASHRPYSSLNAFVNTNFNDKDTEENASNKRKRRAAASANESERLLDKITQSIRGYNAIESVIKKCSSYGDLVTSQMKKWGVQVEGDNSELDLMNLGEDDDDDNDDGNNDNNNSNNNNTAGADATSKEKEDTKAVVEGFDETSAEPTPAPAPAPVERETKRIRNTTKPKVVEDEDDDVDLEAIDDELPQSEHEDDDYEEEDEDYNDEEEDVEYDDGDDDDDDDDEFVATRKNTHVISTTSRNGRKPIVKFFKGKPRLLSPEISLKDYQQTGINWLNLLYQNKMSCILADDMGLGKTCQVISFFAYLKQINEPGPHLVVVPSSTLENWLREFQKFAPALKIEPYYGSLQEREELRDILERNAGKYDVIVTTYNLAAGNKYDVSFLKNRNFNVVVYDEGHMLKNSTSERFAKLMKIRANFRLLLTGTPLQNNLKELMSLLEFIMPNLFISKKESFDAIFKQRAKTTDDNKNHNPLLAQEAITRAKTMMKPFILRRRKDQVLKHLPPKHTHIQYCELNAIQKKIYDKEIQIVLEHKRMIKDGELPKDAKEKSKLQSSSSKNLIMALRKASLHPLLFRNIYNDKIITKMSDAILDEPAYAENGNKEYIKEDMSYMTDFELHKLCCNFPNTLSKYQLHNDEWMQSGKIDALKKLLKTIIVDKQEKVLIFSLFTQVLDILEMVLSTLDYKFLRLDGSTQVNDRQLLIDKFYEDKDIPIFILSTKAGGFGINLVCANNVIIFDQSFNPHDDRQAADRAHRVGQTKEVNITTLITKDSIEEKIHQLAKNKLALDSYISEDKKSQDVLESKVSDMLEDIIYDENSKPKGTKE
Protein: SWI/SNF chromatin-remodeling complex subunit snf5 (SWI/SNF complex subunit snf5) (Q09699)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF chromatin-remodeling complex subunit sol1
- SWI/SNF and RSC complexes subunit arp9
- SWI/SNF chromatin-remodeling complex subunit snf22
- SWI/SNF and RSC complexes subunit arp42
- SWI/SNF global transcription activator complex subunit snf59
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF and RSC complexes subunit ssr1
- Transcription initiation factor TFIID subunit 14
- SWI/SNF chromatin-remodeling complex subunit snf30
Sequence:
MDKDIGSAVAELQVCSTHYAMTIVSCGFHSPQSLMNADLQHCLLADQNYLLNNSNKNKGSIIEENTRKPFQSARNLQTSLKTHPESAITRYGLGYAGFGNGWTALKPKILFPSQKRRVKGRFTFPFSRRSNLAQSKLPVDLVPIRLEIDADRYKLRDSFTWNLYDKCISLDQFAEQICIDYDIPLHNVHIVQNISKSIQAQINDYEPRKAQSNLSFVSDVSSSTSETVYAHEPSDSLAKASKQQIPTVQNDLRILIKLDITIGRLNLIDQFEWNLFAPESSAEEFATVMCLDLGLSGEFCTAVAHSIREQCQMYIKYLSLIGYLFDGSEIEDEEVRSYILPPLKNTLRFSDMESSSFAPMIYELNDAEMERQDRGYDREARRMRRRQGRAKHGIMLPDLRDIPKIHRSLFPSSSVPSDDDFMHALSLSTNSDGETLNEINTNNPEREHLIVRLKVDSQKLKIIVEQSQTLTLNNFQQRKLTPLPNSMSFDSLNEFESERNTPSTYGQNISPLPQFSSPSLSSDAFLTNSNSSESALVHMQKLNLPDFTPSWVKRCVIETFAKFPNDRFNVIVKPALNPAERMTVRICCHDCINEYFTAGPGFTFGNFHIHLLSSSHQQKKEVRMNTVLDRNT
Protein: Large ribosomal subunit protein mL39 (39S ribosomal protein L39, mitochondrial) (L39mt) (MRP-L39) (39S ribosomal protein L5, mitochondrial) (L5mt) (MRP-L5) (Q9NYK5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein mL45
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL44
- Large ribosomal subunit protein uL1m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL13m
Sequence:
MEALAMGSRALRLWLVAPGGGIKWRFIATSSASQLSPTELTEMRNDLFNKEKARQLSLTPRTEKIEVKHVGKTDPGTVFVMNKNISTPYSCAMHLSEWYCRKSILALVDGQPWDMYKPLTKSCEIKFLTFKDCDPGEVNKAYWRSCAMMMGCVIERAFKDEYMVNLVRAPEVPVISGAFCYDVVLDSKLDEWMPTKENLRSFTKDAHALIYKDLPFETLEVEAKVALEIFQHSKYKVDFIEEKASQNPERIVKLHRIGDFIDVSEGPLIPRTSICFQYEVSAVHNLQPTQPSLIRRFQGVSLPVHLRAHFTIWDKLLERSRKMVTEDQSKATEECTST
Protein: Falcilysin (EC 3.4.24.-) (Q76NL8)
Organism: Plasmodium falciparum (isolate 3D7)
Function: In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains. In the apicoplast, degrades apicoplast transit peptides after their cleavage. Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17074076, ECO:0000269|PubMed:23471987}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A0L7KF24}. Plastid, apicoplast {ECO:0000269|PubMed:17074076}. Vesicle {ECO:0000250|UniProtKB:A0A0L7KF24}. Note=Localizes to the food (or digestive) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:17074076, PubMed:23471987). During the trophozoite and early to mid-schizont stages, localizes to the apicoplast (PubMed:17074076). {ECO:0000269|PubMed:17074076, ECO:0000269|PubMed:23471987}.
Interaction partners:
- Dipeptidyl aminopeptidase 1
- M1-family alanyl aminopeptidase.
- Mitochondrial intermediate peptidase, putative
- Aminopeptidase P
- Pyruvate dehydrogenase E1 component subunit alpha
Sequence:
MNLTKLMKVIGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQYLGQLDYSKYRDDAVESVEYQTYKKGPFYIKKKYGDHSEEKENLVSVAWLLNPKVDKTNNHNNNHSNNQSSENNGYSNGSHSSDLSLENPTDYFVLLIINNLLIHTPESVLYKALTDCGLGNNVIDRGLNDSLVQYIFSIGLKGIKRNNEKIKNFDKVHYEVEDVIMNALKKVVKEGFNKSAVEASINNIEFILKEANLKTSKSIDFVFEMTSKLNYNRDPLLIFEFEKYLNIVKNKIKNEPMYLEKFVEKHFINNAHRSVILLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIKNFEELSKYKNAEESPEHLNKFPIISISDLNKKTLEVPVNVYFTNINENNNIMETYNKLKTNEHMLKDNMDVFLKKYVLKNDKHNTNNNNNNNNNMDYSFTETKYEGNVPILVYEMPTTGIVYLQFVFSLDHLTVDELAYLNLFKTLILENKTNKRSSEDFVILREKNIGSMSANVALYSKDDHLNVTDKYNAQALFNLEMHVLSHKCNDALNIALEAVKESDFSNKKKVIDILKRKINGMKTTFSEKGYAILMKYVKAHLNSKHYAHNIIYGYENYLKLQEQLELAENDFKTLENILVRIRNKIFNKKNLMVSVTSDYGALKHLFVNSNESLKNLVSYFEENDKYINDMQNKVNDPTVMGWNEEIKSKKLFDEEKVKKEFFVLPTFVNSVSMSGILFKPGEYLDPSFTVIVAALKNSYLWDTVRGLNGAYGVFADIEYDGSVVFLSARDPNLEKTLATFRESAKGLRKMADTMTENDLLRYIINTIGTIDKPRRGIELSKLSFLRLISNESEQDRVEFRKRIMNTKKEDFYKFADLLESKVNEFEKNIVIITTKEKANEYIANVDGEFKKVLIE
Protein: Outer capsid protein P8 (Structural protein P8) [Cleaved into: Outer capsid protein P8'; Small peptide 1 (Sp1)] (Q85449)
Organism: Rice dwarf virus (isolate Akita) (RDV)
Function: Capsid protein which self-assembles to form the outer icosahedral capsid with a T=13 symmetry, about 70 nm in diameter and consisting of 780 molecules capsid proteins.
Subcellular location: [Outer capsid protein P8]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250}. Note=Found in the peripheral regions of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000250}.
Interaction partners:
Sequence:
MSRQMWLDTSALLEAISEYVVRCNGDTFSGLTTGDFNALSNMFTQLSVSSAGYVSDPRVPLQTMSNMFVSFITSTDRCGYMLRKTWFNSDTKPTVSDDFITTYIRPRLQVPMSDTVRQLNNLSLQPSAKPKLYERQNAIMKGLDIPYSEPIEPCKLFRSVAGQTGNIPMMGILATPPAAQQQPFFVAERRRILFGIRSNAAIPAGAYQFVVPAWASVLSVTGAYVYFTNSFFGTTIAGVTATATAADAATTFTVPTDANNLPVQTDSRLSFSLGGGNINLELGVAKTGFCVAIEGEFTILANRSQAYYTLNSITQTPTSIDDFDVSDFLTTFLSQLRACGQYEIFSDAMDQLTNSLITNYMDPPALPAGLAFTSPWFRFSERARTILALQNVDLNIRKLIVRHLWVITSLIAVFGRYYRPN