wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear transcription factor Y subunit A-8 (AtNF-YA-8) (Q9LNP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit B-1
- Nuclear transcription factor Y subunit C-4
- Nuclear transcription factor Y subunit B-7
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit B-6
- Nuclear transcription factor Y subunit C-10
Sequence:
MDKKVSFTSSVAHSTPPYLSTSISWGLPTKSNGVTESLSLKVVDARPERLINTKNISFQDQDSSSTLSSAQSSNDVTSSGDDNPSRQISFLAHSDVCKGFEETQRKRFAIKSGSSTAGIADIHSSPSKANFSFHYADPHFGGLMPAAYLPQATIWNPQMTRVPLPFDLIENEPVFVNAKQFHAIMRRRQQRAKLEAQNKLIKARKPYLHESRHVHALKRPRGSGGRFLNTKKLQESTDPKQDMPIQQQHATGNMSRFVLYQLQNSNDCDCSTTSRSDITSASDSVNLFGHSEFLISDCPSQTNPTMYVHGQSNDMHGGRNTHHFSVHI
Protein: Flo11 domain-containing protein (G8BIT3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Nucleoporin NSP1-like C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- mRNA export factor GLE1
- Histone chaperone
Sequence:
MKLSTASLVSLAALVGSSEATWALFEDLFKDCAPKHVKPICKIKDIFCDTDDSNESSVSARDGGSVNFKAAFVVSGAERNDDGTYNVVANYEADQSDQLHQYFGGDIDSLSLTGTGCDDVHLYGKSASDSVENAFKWSTKFQCKPKIKNGKCCLPDGFSVGYDFSESGSSWDALKSVFGSKSCSYGINTQWSFVKSFDPYALLNKELSLFKRDEVVEGVDGSTTFDKRTLGFLLDLLGKCTTKKKIIKQFCWDCECPSTSSSSTVPPSTSSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTPPTESSTTPTESSGKPSESSTTPTESSGKPSESSTTPTESSVKPSESSTTPTESSGKPSESSTTPTESSVKPSESSGKTTTESSTESSGKPSESSTESSGKPSESSTPSGPTDTVTTHSTTVVTITSCSEDKCETSTATTGVTVITEGTTIYTTYCPLTEEETTSTVPTSKQTPIPETTSTTAETTVPTKGGESETENVPSTLTTTTAAPSSSAPTGEGEASKSEGESQTTAAPPASEGEAPKSEGESQTTVAPTGEAPKSEGESQTTAAPTGEAPKSEGESQTTAAPTGEAPKSEGESQTIAAPSSAAPEGEAPKPEGESQTTAAPTGEAPKSEGESQTTAAPTGEAPKSEGESQTVAAESSSVPEVSQVPSESANETTAAVSTYEGAGARNSVGLLLVGAAALLL
Protein: Hydroxyethylthiazole kinase (EC 2.7.1.50) (4-methyl-5-beta-hydroxyethylthiazole kinase) (TH kinase) (Thz kinase) (K7VCB9)
Organism: Zea mays (Maize)
Function: Thiazole kinase involved in thiamine salvage pathway.
Interaction partners:
- Bifunctional TENA2 protein
- 40S ribosomal protein S27a
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein eS31 domain-containing protein
- thiamine phosphate synthase
- Thiamine synthesis3
- Thiamine thiazole synthase, chloroplastic
Sequence:
MDVGAKEEEMGQVWWGHRAWSLLSAVRARAPLVQCITNLVSMDIAANVLLAAGASPAMVHSLREVPDFTPRCDAVYVNVGTLSEDWLPSMRAAASAGRPWVLDPVAAAASGFRMKACLELLSLCPAVVRGNASEILALASRSTAASSNFKGVDSSHCSVDAIEAAKALALSSSAVVAVSGAVDFVTDGKQVISVSNGVPMMQKITATGCAVTALIAAFVAMEPSDAIVAAACALAIFGLVGEIGMESAKGPASLRMHLIDALYCLNEETVTSRVRISLRP
Protein: Tropomyosin 3 isoform 1 (A0A0S2Z4G4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAGITTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLNEM
Protein: Tocopherol O-methyltransferase, chloroplastic (EC 2.1.1.95) (Gamma-tocopherol methyltransferase) (Vitamin E pathway gene 4 protein) (AtVTE4) (Q9ZSK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of tocopherol (vitamin E). Methylates gamma- and delta-tocopherol to form beta- and alpha-tocopherol, respectively.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Tocopherol cyclase, chloroplastic
- 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, chloroplastic
- Phytol kinase 1, chloroplastic
- Protein VTE6, chloroplastic
- Phytoene synthase 1, chloroplastic
- Homogentisate solanesyltransferase, chloroplastic
- Homogentisate phytyltransferase 1, chloroplastic
- 4-hydroxyphenylpyruvate dioxygenase
- Monosaccharide-sensing protein 3
- GPI ethanolamine phosphate transferase 2
Sequence:
MKATLAAPSSLTSLPYRTNSSFGSKSSLLFRSPSSSSSVSMTTTRGNVAVAAAATSTEALRKGIAEFYNETSGLWEEIWGDHMHHGFYDPDSSVQLSDSGHKEAQIRMIEESLRFAGVTDEEEEKKIKKVVDVGCGIGGSSRYLASKFGAECIGITLSPVQAKRANDLAAAQSLAHKASFQVADALDQPFEDGKFDLVWSMESGEHMPDKAKFVKELVRVAAPGGRIIIVTWCHRNLSAGEEALQPWEQNILDKICKTFYLPAWCSTDDYVNLLQSHSLQDIKCADWSENVAPFWPAVIRTALTWKGLVSLLRSGMKSIKGALTMPLMIEGYKKGVIKFGIITCQKPL
Protein: KH-type splicing regulatory protein (M0QXW7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQ
Protein: AN1-type zinc finger protein 5 (Zinc finger A20 domain-containing protein 2) (Zinc finger protein 216) (O76080)
Organism: Homo sapiens (Human)
Function: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Paired box protein Pax-6
- NF-kappa-B essential modulator
Sequence:
MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI
Protein: Protein kinase, putative (Q388H2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSMEELHATPPPQRFNDASESDPNDDDDDNSSTSTAGPPGSTRTGRYRRFVAESSVISNKSPNTPPPRGYRRSGAAKRNGSYRVAFSSKQHSRNGRSLSNTSTVASLMGSVQEWSCSFCMFSPGRAAAPPQRSFLFSQRMSLGGGYVPLPNGGAHSSLSVSPRPCIESPRLDGWRHSIPFSPSHGASISGPAGTGDAGGVNASNSHVTGRASPSSASPSPLPGMYWFGLPSMAASGGTPPRSVAYYAMGGSPRLVNRGGSGCFTSAARKELSGLVRSLASHIALTGTPIGNGNTTHPVDIHKGPLIGVGGFAKVYAGVDCVTGSLVAIKEINMAEVNDQEGFRAISKEFGVLKSLKHPNIVSYIFFEHSVSQKVCRIVMELHTGGSTLSLLERFGPLQETILRRFSRHLLEAIAFIHQKGFLHRDIKPANILVSHDGVVKLCDFGCCKRVNELNKSTNCVIGTPLYMAPEFIKGEGTHKSDIWSMGCSLFELATGKLPWYHTGVRDHIPLMFYITTTSESPLVLPPNEEEFDFSPEFIHFLEQCFIRNVSQRPEAVELLKHPWITGRRLHPDSLFTGAGVSVSQNWQSTYGVADEEQLCQNELEEVSARISVEMCNVWIAGGIKGVPATPLRVSQQTELQHKSDDITNTLSAGERRPLELQATMGNSRSESPAASCFSGAGGASTSPTICLDAALHDTFSYTVPRGASAGNFVFPQSTSFSTSLTSPQYLRITDDGNLEFATVADDDQVEVSADIDDAFLNVPRVRTDGKHNFTLDACSKTPVYPGSINGPGANVLSNSPCNTPQVDPASNDNSNVSLTSTVRSSTCRNSRFVPLAHNQSMSLLSSSSFGSRVVSPSRYSQQALNISPTTSQCLQPLTRVTPSSPKPTSPSTAQSSEDVPREGASHLLPSSIRSRLPENVKRDVNGRLCMCFPVPTGDPEKCLRIPLNIDPEDVQCKVIERSPSLVVTFSDNIKAQITAKMNELSATGTTDNVESGLEGHSTVSRVGNSFFRGTVRASPNVRHSLGSTSRPRNLASITKSVVAVSDPHPHNYQGRRSGSSLCASLTYSSSTDGRTPTHSGDV
Protein: Uncharacterized protein (Q586S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKGGGGIVCFSQECLYFPSPLTDASIENIIELSSLLVRTEDPCENVVAFKVLSAVRNRYGVQPSVGLIFAGECVRVKFMLDIRRLRRLAARRGGVEEGAVELPDAGTRDEVFVDICVVPREVMAPYESVSGFFGGDCSSKGPSGPDVAAAFWKQRGRVQARERNAVRCALRCIYGELGVPDSLVMKRSHGKVEGLVEGCETAAVEKAPAAQPQLGSAVRNAGGEVSPPSTALRSRHSPKGAGDQTAASASPLVYSPVNCASGTVPSGRCSNGYEAAVGEASRMTNVIAPDSGREMYSLLSVFLLYKVPFPVCCILLFLSFLCGIIE
Protein: Oxidative stress-induced growth inhibitor 1 (Bone marrow stromal cell-derived growth inhibitor) (BMSC-derived growth inhibitor) (Ovary, kidney and liver protein 38) (huOKL38) (Pregnancy-induced growth inhibitor OKL38) (Q9UJX0)
Organism: Homo sapiens (Human)
Function: Regulates the differentiation and proliferation through the regulation of cell death.
Interaction partners:
Sequence:
MSSSRKDHLGASSSEPLPVIIVGNGPSGICLSYLLSGYTPYTKPDAIHPHPLLQRKLTEAPGVSILDQDLDYLSEGLEGRSQSPVALLFDALLRPDTDFGGNMKSVLTWKHRKEHAIPHVVLGRNLPGGAWHSIEGSMVILSQGQWMGLPDLEVKDWMQKKRRGLRNSRATAGDIAHYYRDYVVKKGLGHNFVSGAVVTAVEWGTPDPSSCGAQDSSPLFQVSGFLTRNQAQQPFSLWARNVVLATGTFDSPARLGIPGEALPFIHHELSALEAATRVGAVTPASDPVLIIGAGLSAADAVLYARHYNIPVIHAFRRAVDDPGLVFNQLPKMLYPEYHKVHQMMREQSILSPSPYEGYRSLPRHQLLCFKEDCQAVFQDLEGVEKVFGVSLVLVLIGSHPDLSFLPGAGADFAVDPDQPLSAKRNPIDVDPFTYQSTRQEGLYAMGPLAGDNFVRFVQGGALAVASSLLRKETRKPP
Protein: Pleckstrin homology and RhoGEF domain containing G6 (F5H731)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKAFGPPHEGPLQGLVASRIETYGGRHRASAQSTAGRLYPRGYPVLDPSRRRLQQYVPFARGSGQARGLSPMRLRDPEPEKRHGGHVGAGLLHSPKLKELTKAHELEVRLHTFSMFGMPRLPPEDRRHWEIGEGGDSGLTIEKSWRELVPGHKEMSQELCHQQEALWELLTTELIYVRKLKIMTDLLAAGLLNLQRVGLLMEVSAETLFGNVPSLIRTHRSFWDEVLGPTLEETRASGQPLDPIGLQSGFLTFGQRFHPYVQYCLRVKQTMAYAREQQETNPLFHAFVQWCEKHKRSGRQMLCDLLIKPHQRITKYPLLLHAVLKRSPEARAQEALNAMIEAVESFLRHINGQVRQGEEQESLAAAAQRIGPYEVLEPPSDEVEKNLRPFSTLDLTSPMLGVASEHTRQLLLEGPVRVKEGREGKLDVYLFLFSDVLLVTKPQRKADKAKVIRPPLMLEKLVCQPLRDPSTSFLQGVFSSPSSQRGEGGAGTEIK
Protein: 2-iminobutanoate/2-iminopropanoate deaminase (EC 3.5.99.10) (Enamine/imine deaminase) (P0AF93)
Organism: Escherichia coli (strain K12)
Function: Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Aspartate carbamoyltransferase regulatory chain
- Aspartate carbamoyltransferase catalytic subunit
- L-threonine dehydratase biosynthetic IlvA
- Thiamine import ATP-binding protein ThiQ
- RutC family protein YjgH
Sequence:
MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVRR
Protein: Pterin-4-alpha-carbinolamine dehydratase (PHS) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Dimerization cofactor of hepatocyte nuclear factor 1-alpha) (DCoH) (Dimerization cofactor of HNF1) (Phenylalanine hydroxylase-stimulating protein) (Pterin carbinolamine dehydratase) (PCD) (P61457)
Organism: Homo sapiens (Human)
Function: Involved in tetrahydrobiopterin biosynthesis (By similarity). Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription (By similarity). Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also acts as a coactivator for HNF1B-dependent transcription.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24204001}. Nucleus {ECO:0000269|PubMed:24204001}. Note=Recruited to the nucleus through the interaction with HNF1B. {ECO:0000269|PubMed:24204001}.
Interaction partners:
- Dihydropteridine reductase
- Hepatocyte nuclear factor 1-alpha
- Phenylalanine-4-hydroxylase
- Tryptophan 5-hydroxylase 1
- Tyrosine 3-monooxygenase
- Tryptophan 5-hydroxylase 2
- Pterin-4-alpha-carbinolamine dehydratase 2
- Hepatocyte nuclear factor 1-beta
- Sepiapterin reductase
- GTP cyclohydrolase 1
Sequence:
MAGKAHRLSAEERDQLLPNLRAVGWNELEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
Protein: Uncharacterized protein, isoform B (A0A0B4LG18)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- GH14707p
- FI19907p1
- Putative inner dynein arm light chain, axonemal
- GH13165p
- Male fertility factor kl3
- Dynein axonemal heavy chain 7
- Dynein axonemal light chain 1
- Dynein heavy chain at 93AB, isoform C
- Dynein, axonemal, intermediate chain 2, isoform C
- Dynein axonemal intermediate chain 4
Sequence:
MATKPGKGDGKQVKGKLRTSKNKTDGPGGGGGDADDFDAWMKSRQLLKPDDQLDLTEAELGEEITKVLTPTNTNIVRNLVVYSFKEGEFVPAPLPGNTVTLIAFAGNSLHVDSDEGRRQIEESDEIGYPLPMPNYTVVEQRETDNVDGEEGEGEEDDDGATAKDAAVEDEDVEEEDDEEAKGTEGDEGEGEGEGEGAAARQEDDEPAHQAAAVSSKKRKLINQFNYCERGALTYTNPKRNVDTQTIPPPRSQFGANVLQWVIYDSYMENFAESQKDGTKKEERKRGKREKKFRDKSAIAEQLNKKYLKCWQILERMINQNIYDDIAHDYRYWEDPADEFREGEGNLLPLWKFQYDKTKKMNVTDILFNPSYYDLFAVCFGSHDFMKQTNEGYLCLFTVKNPSFPDYIIQTDCGVMCCDIHPTYPFLAVIGLYDGNVAVYNLREDCKEPLYVSRGVNCKHGECVWQIKWGLDMADGEVNFFSVSSDGRVFNWILMQNKLWVTTIITLYRENGLVDGPDGTKVTLKSGGSCMVFHPVDNKIFLVGTECGYIYKCSTAFSSKYLMTYYAHNMSVYRIDFNRFNSNIFVSCGADWMVKVWEDMRPDPLFIFDLGAAVGDVKWAPYSSTVFAAVTTEGKVHVFDLNVNKYKAICIQAVVPKRKNKLTRLSFNEKLAFIVVGDEKGVTTSLKLSPNLRMMVKPPKKQLYLDQNTLQIGKLEKLLSLVRELPEGSTAVPDAATTVRS
Protein: Altered inheritance of mitochondria protein 46, mitochondrial (Found in mitochondrial proteome protein 34) (P38885)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosomes element 1
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
Sequence:
MRLISKVLVKTNCLEVGMRRAPQWYSHYSTTAGNARVNKKGSKVVPVLTGLALASIFAKKWYDDSQIKKADATSVAVDASISAFPKKMGPPQWPFSTQYELIGKGVRCVSSITFKAYGLGIYVAAEDKHLVSEVLDSKFLSQAFIDTAAPPSPENSHQDNLRAALNDPAKAPILINNLLDSGIRLMSKNTPIKAGSFKLLMDGTKKSVLKNPDSQSQDKDRLEAGFQELHDCFRSVKGLVARDDDFFIELNKDCSMNLSYYARKKDEFVILGTVKEPLIGKLLFAHYLAAVDPPSPEARKEVIDALVSLS
Protein: Rho1 guanine nucleotide exchange factor 2 (Q9UTR5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stimulates the exchange of Rho1 and Rho5 GDP-bound form into GTP-bound form. Controls septum formation, cell wall synthesis and localization of F-actin patches.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16291723, ECO:0000269|PubMed:16324155, ECO:0000269|PubMed:16823372}. Note=Septum. Localizes to cell tips during interphase and the septum in mitotic cells.
Interaction partners:
- GTP-binding protein rho1
- GTP-binding protein rho5
- Cell wall integrity and stress response component 1
- Rho1 guanine nucleotide exchange factor 1
- Protein kinase C-like 1
- Rho-type GTPase-activating protein 1
- Arrestin family protein 1
- Uncharacterized serine-rich protein C11G7.01
- Protein kinase C-like 2
- Rho-GTPase-activating protein 5
Sequence:
MLRNGAQNGNINSESHESFGKAAKGFRIFSSFSSSQKLFQRRSSGSITHSPTALSSTTSLNENDGNHFRPASSLSFSPSSLSRKDSGPGDGLEVNKKNNFYRRSSSTDDFGISHARSRKEIQSLGRPHTRQSFSVSDVSNGSSYPNIRKNSVHVNAPMPSFPEGSTAVLLKHHSGSKSASAISNIAPSHSNSTSSRRPYIHPAFLSQVAVEFRKRLNIGDRVKDGLLYKDAFLGSEAVDVLMHIVRTTDRNLALLLGRALDSQKMFHDVTYSHRLRDSLKEVYQYRRIISPPPGLSSMDSNGSSIENNFLYTKRRANTSDSFDSVLSDSSTTPTISSSVQVNSLAFITSSLSAITKEPEAPETEYNPHGVFTLLTECYSSTCSRNRLCYSISCPRRLEQQARLHLKVQPVLSGGSTSITDKQEEDHRLWSENVPKQVVDQIDVREWKRQEIIFEVIYTERDFVRDLEYIRDFWIKPLSTSNVIPENNRQQFIRCVFHNIMQIHAVNSRLSNALNRTQTLQPVVNTIGDLFLDYVPKFEPFIKYGANQAIAKFEFEREKSTNRNFANYVHEVERLRESRKLELNGYLTKPTTRLARYPLLLSGVLKYTDKDNPDTENIPRVIEMIREFLTKLNYETGKTENRLSLLQLNEQLSCSPADRAKLTLFDPSRLLIFKGVVKLKASSYSNGDTENDIHMFLLDNFLLLCKIKIQMKRRVHKLHLRPLPLELLSISYIEDSPSRGSLPRRPSSALLTNPISITKSNPPPVKAYGLQLVFIGARGFSISLYLNTLIARDQWKQHIEKQQDIIRKRHLVFESRGICCQSWFTGNKLLCAVAYDAGRKLLFGTYKGLYISSRKSNNGSCLEPIFKLQLPNISQLDVIEEHNVLLLLAEKILYELPLDALDSVEQINSKSLRRVTGHVSFVKTGFCMQRILVCAVKSTVLNTTLRIYEADRALKNKKTQSLKKPFGNQATLKIFTEVQMPMEALSVHFLKTKLCVGSFKGFDIISLENAVFQSLLNPADTSFRFLEKREDIRPIAMFRLRGEFLLCYSDFAFFVNTNGWKSRQSWMINWEGQPQGCALCYPYILAFEPDFIEIRNAETAELVQIIMGQNIKLLTDGRGLISEGGEILYSTEPIPFSSGENPIVHSLILPPANAAGPAL
Protein: LD25575p (P58IPK) (Q9VHA8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- DnaJ homolog shv
- GH07340p
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase A6 homolog
- Heat shock protein 83
- Endoplasmic reticulum chaperone BiP
- X-box-binding protein 1
- RE14391p
- Heat shock 70 kDa protein cognate 5
- Nucleotide exchange factor Sil1
Sequence:
MALPLSDLLMIGGGEKKLAACLVLLLLELFLEGAESTASPADIENHLELGKEFLARGQLSDALTHYHAAVEGDANNYLTLFKRGTVYLALGKTRFAVQDFSRVLELKPDFMAARIQRGVVHMKSGEYEQAIQDFDQVLQEEPNNGLVLEHYSRLAPAQEQWVLVQQLIQYSDHQNAIPMITQLLEISPWAVPFRQARSDAYIAINDPLLAIADLRQVNRLTQDSTEGHYKIAQLLYTIGHATNALKEIRECLKFDPEHKLCFPFYKKLRKVEKQLVNAEQAREEKHFAECIAAGEAVLRNEPEETMIRYEGHKVLCTCYTGDEQFGKALQQCKEALDIMKDAQVYCDRADALLGTEMYDDAIHSFQAALDLEESNTRAKEGIQRAKKLQKQSERRDYYKILGVKRSASKQEIVKAYRKAAQKWHPDNFRDEEKKVAEKKFIDIAAAKEVLTDPEKRRQFDNGEDPLDPESNQRGGFHGEHPFGHFQHGSPFQFKFHFN
Protein: Head peptide (Aea-HP) (AeaHP) [Cleaved into: Decapeptide 1 (Decapeptide I); Decapeptide 2 (Decapeptide II); Decapeptide 3 (Decapeptide III)] (Q9GQV7)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Has a role in inhibiting host-seeking behavior during a reproductive cycle.
Subcellular location: Secreted {ECO:0000269|PubMed:11931033}.
Interaction partners:
Sequence:
MWKFASIVVLVVCLAWAVYCEDQRPPSLKTRFGRSADEPESDNYVSNDIMEKRSAQRPPSLKTRFGRSEGAEVMEKRSAQRPPSLKTRFGRSVANPESDGYMRKRSAESEPFVTRIRHGRANKKRAAN
Protein: Complement C8 gamma chain (A0A8I5ZKU8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTSGLCFLWHWTVDSDLEQCTPPPPCPITYCHRTAMLSPGAVLFFTLILMASSLGQRTRKPYGSTSPISTIQAQANFNAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHIAPQGAAMAASTFRKLDGICWQVRQLYGITGVPGRFLLQAPRARGPVHVVVAETDYQSFAILYLEQARRLSVKLYTRTLPVSDSALNAFEERVRGANLTEDQIFFFPKYGFCETADQFHILNDNTYKREHRPLLHSFITLFKLRDNRASIAALGPIP
Protein: Large ribosomal subunit protein uL24B (60S ribosomal protein L26-B) (L33) (YL33) (P53221)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL22B
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL29A
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL3
Sequence:
MAKQSLDVSSDRRKARKAYFTAPSSERRVLLSAPLSKELRAQYGIKALPIRRDDEVLVVRGSKKGQEGKISSVYRLKFAVQVDKVTKEKVNGASVPINLHPSKLVITKLHLDKDRKALIQRKGGKLE
Protein: Ercc1 (Q7KMG7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair endonuclease XPF
- DNA repair protein complementing XP-A cells homolog
- Crossover junction endonuclease MUS81
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit SLX1 homolog
- E3 ubiquitin-protein ligase Fancl
- General transcription and DNA repair factor IIH helicase subunit XPD
- DNA mismatch repair protein spellchecker 1
- Probable DNA mismatch repair protein Msh6
- FI23547p1
Sequence:
MEDFDDDSFNDVLGAMEMPTAAKQPKVDAPAATAVNPAPSNSTEPSGSGRPAPGKPASNPHCVLVHSKQRGNPILKSILNVPLEFRDDIVPDYVVGRTSCVLYLSLKYHNLNPDYICQRLKALGKMYELRVLLVQVDTPEPNNALKSLTRISLLADLTMMLAWNAEEAGKIIETYKQFEKRPPDLIMERVESNPHQKLLAALTNIKPVNKTDAAALLHTFGNLGNIINASEERLSQVMGLGPRKAKKLYKTLQEPFLSK
Protein: Type IV methyl-directed restriction enzyme EcoKMrr (EcoKMrr) (Mrr restriction system protein) (P24202)
Organism: Escherichia coli (strain K12)
Function: Involved in the acceptance of foreign DNA which is modified. Restricts both adenine- and cytosine-methylated DNA.
Interaction partners:
- Type IV methyl-directed restriction enzyme EcoKMcrBC
- Galactokinase
- Small ribosomal subunit protein uS12
- UTP--glucose-1-phosphate uridylyltransferase
- Type I restriction enzyme EcoKI endonuclease subunit
- Type IV methyl-directed restriction enzyme EcoKMcrA
- Type I restriction enzyme EcoKI specificity subunit
- Type IV methyl-directed restriction enzyme EcoKMcrB subunit
- Type I restriction enzyme EcoKI methylase subunit
- Protease 7
Sequence:
MTVPTYDKFIEPVLRYLATKPEGAAARDVHEAAADALGLDDSQRAKVITSGQLVYKNRAGWAHDRLKRAGLSQSLSRGKWCLTPAGFDWVASHPQPMTEQETNHLAFAFVNVKLKSRPDAVDLDPKADSPDHEELAKSSPDDRLDQALKELRDAVADEVLENLLQVSPSRFEVIVLDVLHRLGYGGHRDDLQRVGGTGDGGIDGVISLDKLGLEKVYVQAKRWQNTVGRPELQAFYGALAGQKAKRGVFITTSGFTSQARDFAQSVEGMVLVDGERLVHLMIENEVGVSSRLLKVPKLDMDYFE
Protein: Large ribosomal subunit protein eL21x/eL21w (60S ribosomal protein L21-2) (Q9FDZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein eL28y
- Large ribosomal subunit protein uL5z
- Large ribosomal subunit protein eL28z
- Large ribosomal subunit protein uL5y/uL5x/uL5w
- Large ribosomal subunit protein eL32z
Sequence:
MPAGHGVRARTRDLFARPFRKKGYIPLSTYLRTFKVGDYVDVKVNGAIHKGMPHKFYHGRTGRIWNVTKRAVGVEVNKQIGNRIIRKRIHVRVEHVQQSRCAEEFKLRKKQNDVLKADAKARGETISTKRQPKGPKPGFMVEGMTLETVTPIPYDVVNDLKGGY
Protein: LIM domain-binding protein 3 (Protein cypher) (Z-band alternatively spliced PDZ-motif protein) (O75112)
Organism: Homo sapiens (Human)
Function: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
Interaction partners:
- Alpha-actinin-2
- Myotilin
- Filamin-C
- Myozenin-2
- Myozenin-1
- Telethonin
- Troponin T, cardiac muscle
- Myozenin-3
- Myosin-7
- BAG family molecular chaperone regulator 3
Sequence:
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASDPGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPASAQPPAAASPSAASPPLATAAAHTAIASASTTAPASSPADSPRPQASSYSPAVAASSAPATHTSYSEGPAAPAPKPRVVTTASIRPSVYQPVPASTYSPSPGANYSPTPYTPSPAPAYTPSPAPAYTPSPVPTYTPSPAPAYTPSPAPNYNPAPSVAYSGGPAEPASRPPWVTDDSFSQKFAPGKSTTSISKQTLPRGGPAYTPAGPQVPPLARGTVQRAERFPASSRTPLCGHCNNVIRGPFLVAMGRSWHPEEFTCAYCKTSLADVCFVEEQNNVYCERCYEQFFAPLCAKCNTKIMGEVMHALRQTWHTTCFVCAACKKPFGNSLFHMEDGEPYCEKDYINLFSTKCHGCDFPVEAGDKFIEALGHTWHDTCFICAVCHVNLEGQPFYSKKDRPLCKKHAHTINL