wanglab/gogpt-training-data huggingface dataset:
Protein: Protein max (Myc-associated factor X) (Myc-binding novel HLH/LZ protein) (Protein myn) (P28574)
Organism: Mus musculus (Mouse)
Function: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the MYC:MAX complex in vivo. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements (By similarity).
Subcellular location: Nucleus. Cell projection, dendrite {ECO:0000250}.
Interaction partners:
- Myc proto-oncogene protein
- Max-interacting protein 1
- MAX gene-associated protein
- N-myc proto-oncogene protein
- Max dimerization protein 1
- Mitogen-activated protein kinase 14
- Transcription factor E2F6
- Protein L-Myc
- Zinc finger and BTB domain-containing protein 17
- Mitogen-activated protein kinase 11
Sequence:
MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGGTISAFDGGSDSSSESEPEEPQSRKKLRMEAS
Protein: Transmembrane protein 243 (MDR1- and mitochondrial taxol resistance-associated protein) (MM-TRAG) (Q9BU79)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEDFATRTYGTSGLDNRPLFGETSAKDRIINLVVGSLTSLLILVTLISAFVFPQLPPKPLNIFFAVCISLSSITACILIYWYRQGDLEPKFRKLIYYIIFSIIMLCICANLYFHDVGR
Protein: Glutathione synthetase (GSH-S) (EC 6.3.2.3) (Q86B44)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutamate--cysteine ligase
- GCS light chain
Sequence:
MSSDANTAVLRNCIRLPLAEDELLEVTAKAKDYAIMHGAAMRSKTAFSPDSLNFAPFVLVPSSFPRKEFEKAVALQPIINRLMHNVAHDEEFITTTLAETIKVDEFTANLFNIYRKVLAHGFTQKTSLGMLRSDLMLESGCPELSPRALRTAAGEDRGQDAGAAVGQIAGANGAAGVGTAAGTGSKEEEHREVQLSRVTKEPERRATGAQSAYCCWKQVEINTIASGFGHLGPASKTIQRFVLSELGHADKLHNMPDNNALAGLCDGMVKAWDIYAKPQAVILFIIEDVSYNICDQRFHEFYIRETYPHIKVLRRTLTEVHREGKLGQSKELLLGSQEVAVIYFRAGYEPGHYHSQADWDARYLMETSLAIKCPSIHYHLAGTKKVQQALAQPAVLERFINDPEEIKAVGKIFTGLYSLDDNEAGNASYEMALRTPERFVLKPQREGGGNNVYGVDIPDALKRMSRVERSAWILMDLIHPPLTKGYMVRPGGDMPPQIVDMVSELGIFGVVIGDAEHIVHNYQAGHMLRTKLSTANEGGVAAGLGALDSPYLIDSDDEDEQK
Protein: Guanine nucleotide-binding protein subunit alpha homolog (Protein concertina) (P25157)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in a signal transduction pathway used during gastrulation. Required specifically for the ventral furrow and posterior midgut invaginations, where it is necessary for coordinating cell shape changes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1899050}.
Interaction partners:
- Rho guanine nucleotide exchange factor 2, isoform D
- Guanine nucleotide-binding protein subunit beta-1
- Ras-like GTP-binding protein Rho1
- G protein beta subunit 5
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma-e
- Chaperone Ric-8
- Guanine nucleotide-binding protein subunit gamma-1
- Guanine nucleotide-binding protein subunit gamma
- G protein alpha s subunit subunit alpha)
Sequence:
MSGITLTKLTQERISIPNNNVITNGVENNIDSDTLSGTLTHLMEEHRTRVGAVTGPEAATTSTDGLISNGAERLRLQGSRLQTSRFACFRCCGNIITYLVRLRSTPEELEQRYKSKEIDKFLEKEKHTFRRQVKLLLLGAGESGKSTFLKQMRIIHGVNFDYELLLEYQSVIYQNVIRGMQVLLDAREKLNIAWGSDGREQDAYDAKLMECNSLDVPKFMEYAPPISRLWQDRGIRRAFERRREFQISDSVSYFLDEIQRLATPDYVPTHKDILHCRKATKGVYEFCVKVQNIPFVFVDVGGQRTQRQKWTRCFDSSVTSIIFLVSSSEFDQVLAEDRKTNRLEESKNIFDTIVNNATFKGISIILFLNKTDLLEQKVCNPETDIRWYYPHFNGNPHSVLDVQNFILQMFMSVRRSSSISRIYHHFTTAIDTRNINVVFNSVKDTILQRNLNALMLQ
Protein: Probable transcriptional regulatory protein At2g25830 (O82314)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Aspartate--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MASHCSMRVILLRFSNGVSSRSILNSTNHRLLSLTMTNTLSSLSSISPHTTTSHFTAASQQSDDQNCFRKLQLRKISISTPLCMGRRSSKIAGRKGAQDSKKAKLYCRIGKEVVSAVKKGGPNPVSNTTLATILDKAKELDVPKDIVERNIKRASEKGQEAFIEKIYEVYGYGGVSMVVEVLTDKINRSVAAIRSVVKDYGGKMADSGSVMFKFKRVRVVNIKVTEADKDQLLIIALDAGAEDVIEPPTYEDDTDEDREERYYKIVTSNENYSTILSKLRDEGVNFEPDNGSELLPLTTVEVDDEAMELNKELMQKLLELDDVDAVYIDQK
Protein: Putative amidase C550.07 (EC 3.5.1.4) (O59805)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Putative amidase C869.01
- Putative amidase PB8B6.03
- Glutamyl-tRNA
Sequence:
MTIDWRQIAAKYCAHRDGSIPEPFKIKTLPKDTVLNVTKIPSECGLLTPKEIELTEKYDATALAEMIKDRKVTSVELVTAFCKRAAIAQQLVNCVNELFYEEALARAAELDEYYAKTGSLVGPLHGVPVSVKEHISIKNHTATASFLAKANIIAEKDSDLVATVRKAGAVFYCRTPQPQAIMHLETSSNLTGVTVNPFNRKLTPGGSSGGEGALLGIKASVLGIGSDIGGSIRSPAANNGLFGLRPSTLRLSRKGCQGAVSGQETILGVVGPLGRSVRDMNLFMKACIDSQPWLDDASLLPMPWRSVAPPKTLKVGIMRSDNVVNPQPPVARAMQMAIDQLSKNPDFDLVDVEPLDHKYSWDLISEMYWLDGGKVYYDLFNKVGEPILPLTEWIMHQPNVKPHDITAVWKLTAARDEYRNRYLKHLQAYGVDVLLTPVGPSPAPKLGEAKYWTYTSVWNLLDLPAVVFPVTTVDPKLDVKDESYIPMNEQDAANYETYSPEDYLDAPVSLQLVGKRWQDEELLAALDKIVSML
Protein: Progranulin (PGRN) (Acrogranin) (Epithelin/granulin precursor) (Glycoprotein of 88 Kda) (GP88) (Glycoprotein 88) (PC cell-derived growth factor) (PCDGF) (Proepithelin) (PEPI) [Cleaved into: Paragranulin; Granulin-1; Granulin-2; Granulin-3; Granulin-4; Granulin-5; Granulin-6; Granulin-7] (P28798)
Organism: Mus musculus (Mouse)
Function: Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation. Regulates protein trafficking to lysosomes and, also the activity of lysosomal enzymes. Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB. In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures. Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases. Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity.
Subcellular location: Secreted {ECO:0000269|PubMed:28073925, ECO:0000269|PubMed:28541286, ECO:0000269|PubMed:8496151}. Lysosome {ECO:0000269|PubMed:27789271, ECO:0000269|PubMed:28073925}. Note=Endocytosed by SORT1 and delivred to lysosomes. Targeted to lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic pathways (By similarity). Co-localized with GBA1 in the intracellular trafficking compartments until to lysosome (PubMed:27789271). {ECO:0000250|UniProtKB:P28799, ECO:0000269|PubMed:27789271}.
Interaction partners:
- Sortilin
- Prosaposin
- TAR DNA-binding protein 43
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Antileukoproteinase
- Guanine nucleotide exchange factor C9orf72 homolog
- Charged multivesicular body protein 2b
- Transmembrane protein 106B
- Cathepsin D
- Microtubule-associated protein
Sequence:
MWVLMSWLAFAAGLVAGTQCPDGQFCPVACCLDQGGANYSCCNPLLDTWPRITSHHLDGSCQTHGHCPAGYSCLLTVSGTSSCCPFSKGVSCGDGYHCCPQGFHCSADGKSCFQMSDNPLGAVQCPGSQFECPDSATCCIMVDGSWGCCPMPQASCCEDRVHCCPHGASCDLVHTRCVSPTGTHTLLKKFPAQKTNRAVSLPFSVVCPDAKTQCPDDSTCCELPTGKYGCCPMPNAICCSDHLHCCPQDTVCDLIQSKCLSKNYTTDLLTKLPGYPVKEVKCDMEVSCPEGYTCCRLNTGAWGCCPFAKAVCCEDHIHCCPAGFQCHTEKGTCEMGILQVPWMKKVIAPLRLPDPQILKSDTPCDDFTRCPTNNTCCKLNSGDWGCCPIPEAVCCSDNQHCCPQGFTCLAQGYCQKGDTMVAGLEKIPARQTTPLQIGDIGCDQHTSCPVGQTCCPSLKGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARTCEKDVDFIQPPVLLTLGPKVGNVECGEGHFCHDNQTCCKDSAGVWACCPYLKGVCCRDGRHCCPGGFHCSARGTKCLRKKIPRWDMFLRDPVPRPLL
Protein: G/T mismatch DNA glycosylase (Thymine DNA glycosylase) (Q9PUA4)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MEAEELGRYYAYLQQAQAFYTFPFHQMMTAPPTMEAMTEQPTLEGIPEPNLAQEPPKEVKKGGRKRKAKATEPKQPKKPAAKKEKATKSKGKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFDLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSNEQLNHMDDHTLPHKYGIGFTNMVERTTPGSKDLSSKEFREGGRILMQKLQKYKPRIAAFNGKCIYEIFSREVFGIRVKNLEFGLQPHKVPETETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIAPNTEVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYCDRAPYESEQCNFSSNGTAPSNPQYCEGSSFGEVPNGQWMTQSFADQIPEFSAGMTQEREGSSA
Protein: Exonuclease mut-7 (EC 3.1.-.-) (Exonuclease 3'-5' domain-containing protein 3 homolog) (P34607)
Organism: Caenorhabditis elegans
Function: Represses the transposition of Tc1, Tc3, Tc4, and Tc5, perhaps by degrading transposon-specific messages. Also affects sperm development, sensitivity to RNAi of mainly germline expressed genes, silencing of some germline transgenes, X chromosome loss, and is required for cosuppression (functional silencing of chromosomal loci induced by transgenes) and for silencing induced by antisense RNA oligomers.
Interaction partners:
- SH2 domain-containing protein
- PAP-associated domain-containing protein
- MUTator
- MUTator
- RNA helicase
- DRBM domain-containing protein
- RNA-directed RNA polymerase
- Piwi domain-containing protein
- Piwi-like protein 1
- RNase NYN domain-containing protein
Sequence:
MEEEPYKRKLTKAEKKAKYRTDYAEPLKSRREVLKAIMNGPESERERKVRAKNREFFNEDYRSGVNIYGMAVDMMKAMPDRGKTSGQSLAVWYLEDFGVWLKESGQETELRQKYLTGTIQINALDVCTIGQKQLLSEIFDITKEKFTEDITQLLDAAIKKQDFSVAADMAIQYNLLRDHHFEHLVLPLMLSGKDQTAYKLISNNERMQQQLVEFFDRMVGISVVAVEEMLKPYKETKIMTIPMEKLTGKTLDKLISTIINKNTHEYNFSRELSKFAKNHSQNGNLKALKFNISERYEKGKSDDNYFQHMVETFTKAEDVREPILFYLWSSNDTEKQIDAICFAIYLGIASSSSYQLPNVMRDFFRQPDSKLREAKELLVRRKTLQVPLNGEQLFVFENERRTQIHMVKTESEMNYLCSEIKSLSDEPAPVYVGFDSEWKPSNLTAVHDSKIAIIQLFFKNCVWLVDCVELEKANMADDWWQKFASRLFGDSPVKVVGFDMRNDLDAMATIPALKSSMKIEDTKNAFDLKRLAENVCDIDMEILELPKKTFKLADLTHYLLGLELDKTEQCSNWQCRPLRKKQIVYAALDAVVVVETFKKILSIVEEKNKDADIEKIVRESNVMAPKKDKGHKSYRKLKTIPWLELYDILRSHRNPTRSPQRPHDIKVIVDTMLIGFGKNLRRVGIDVILPKDVSDFRKYLKEIERVGGEHLRHIITVPSKSYEALKMDYDNYTIAIPELNNMSPVDQLIEFFDLFNVDIRPEDVYPRCTECNSRLQIKFPGPVLHFLHQYCVIHVQNVYRADMSEFPLEEWWNRMLHINPDDYDGVKVEMSRPSPTSKWIVATVPTGCLHITRQTALHTNLPDGIEVRIHKVPDDEFKRRNLSFYVCGECGTVACDGRGNQASESTSQEC
Protein: Peroxisomal membrane protein PEX3 (PMP PEX3) (Peroxin-3) (Peroxisomal membrane protein PAS2) (C4R6F0)
Organism: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10359594, ECO:0000269|PubMed:21576455, ECO:0000269|PubMed:8702562}; Single-pass membrane protein {ECO:0000255}. Note=Traffics to peroxisomes via the endolasmic reticulum (ER), where it accumulates in the absence of PEX19. {ECO:0000269|PubMed:21576455}.
Interaction partners:
- PEX19 peroxisomal biogenesis protein
- Peripheral peroxisomal membrane peroxin
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein
- Peroxisomal membrane protein PEX14
- Mitochondrial fission 1 protein
- Mitochondrial protein involved in sorting of proteins in the mitochondria
- K+/H+ antiporter with a probable role in intracellular cation homeostasis
- Subunit of a heterodimeric peroxisomal ATP-binding cassette transporter complex
Sequence:
MLEYTAGLIRRNKKKFLISSGIIGVGYYVTKTINNKIQEFQNRIREENFAKEQIKRRFHQTQSDCYMTFLSLLPVLCEPIMDDLPVETITKQLQIRRLEKQIGNKDVKNSGSTVLSDDFSTSQEGAISEDTNKPPELKSKNQLWQELKIKAITRFLTLIYCESLLIVFLHLQLNILSRKSYLETAIRLASETQGIDLVDQESNGDFSGNTQDENLSEQAFLSFSWWLLNKGWLEIKNKIEPCVEQHFGGINPRQQLKINEFAELLNKCQNCIDLKVLNLTEDDIHLGVGVIEDQSQPVGRKSTNFITNALLPPKEFEFFLLQQTNDLDFLSRFNNNIVNTESLNMLLDELNNYLNNADINLIVNKLATLGITKVLDEIVLNLLQKNRPNPISDMNIRDIDLNDFPPYKLAALLANITKQSISLTNNSVENPILADLNNLPELNDLSASVYSNFDP
Protein: Antizyme inhibitor 1 (AZI) (Ornithine decarboxylase antizyme inhibitor) (O35484)
Organism: Mus musculus (Mouse)
Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production.
Subcellular location: Nucleus {ECO:0000269|PubMed:19449338}.
Interaction partners:
- Ornithine decarboxylase antizyme 1
- Ornithine decarboxylase antizyme 3
- Ornithine decarboxylase antizyme 2
- Spermidine synthase
- Double-stranded RNA-specific adenosine deaminase
Sequence:
MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQTVVAQIKPFYTVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIFTSPCKQVSQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKFSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYFMMSFSDWYEMQDAGITSDAMMKNFFFAPSCIQLSQEDSFSTEA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8I637)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein phosphatase PPM5, putative
Sequence:
MYILRNMFCIKFMLYFLWLLYLLFLNIEFIKFKTFQSLVSYDRPSKCLSENSKHHVNSDNNKGNKLFGQKQFGNINKCDVKDDELKISKDNTSKKKKICFKKEKRSNEEEYNNLEKESVEGTCNLLNILNVEKTKVFDNYESTYKHGENNDIICMSNLKEDESKENYIYNWNLGKESLVKFLGFSDYFKINGVKYSDFELTSIPIIGENKSKGRVQEMFKTVIPSNDGDPAKEVKLFIKRIPVEWWIKQFNLMEKYDGEYLVKAENYVMEGVALSFLSEHHPGIAPKLLKILYDGKNVNHDIMEEYKFKDIYEFNNMLIERINNNMDGYIVMVSELFGEDLFDFNKRFTKEKSDVRNSDEFKKELLYKCLRLLVRLHSAGLSHLDLTAENVLITDDYDIRLCDFAKSTPLYSDKLRHIDKKKKKKVYLFESCVPTIGKREYTPIECWRIRKKLREKNITDPFEHVKTISMQRFRKEYYFNVSHADYFMLGVLFIWIWNCGHMWKTSFPSESVNFTTFLENNMNLSCYPSTKSWPSDFKFIVKELMNEECRKKLNLKNLMTHPWFNET
Protein: Integrin alpha-IIb (GPalpha IIb) (GPIIb) (Platelet membrane glycoprotein IIb) (CD antigen CD41) [Cleaved into: Integrin alpha-IIb heavy chain; Integrin alpha-IIb light chain] (Q9QUM0)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-3
- von Willebrand factor
- Fibronectin
- Vitronectin
- Talin-1
- Fermitin family homolog 3
- Talin-2
- Platelet glycoprotein Ib alpha chain
- Filamin-A
- Calcium and integrin-binding protein 1
Sequence:
MARASCAWHSLWLLQWTPLFLGPSAVPPVWALNLDSEKFSVYAGPNGSHFGFSVDFHKDKHGSVSIVVGAPRALNASQEETGAVFLCPWKANGGKCNPLLFDLRDETRNLGFQIFQTFKTGQGLGASVVSWNDVIVACAPWQHWNVLEKRDEAEKTPVGGCFLAQLQSGGRAEYSPCRANTMSSVYAESFRGDKRYCEAGFSLAVTQAGELVLGAPGGYFFLGLLARVPIENIISSYRPGTLLWHVSNQRFTYDNSNPVFFDGYRGYSVAVGEFDGDPSTTEYVSGAPTWSWTLGAVEILDSYYQPLHRLHGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPKGPQALSTPTLLLTGTQLYGRFGSAIAPLGDLNRDGYNDIAVAAPYGGPSGQGQVLIFLGQSEGLSPRPSQVLDSPFPTGSGFGFSLRGAVDIDDNGYPDLIVGAYGASKVAVYRAQPVVMATVQLMVQDSLNPTLKNCVLDQTKTPVSCFNIQMCVGATGHNIPQKLHLKAELQLDLQKPRQGRRVLLLASQQASLTLSLDLGGRDKPICHTTGAFLRDEADFRDKLSPIVLSLNVSLPPEETGGAPAVVLHGETHVQEQTRIILDCGEDDLCVPQLRLTATAGDSPLLIGADNVLELKIEAANDGEGAYEAELAVHLPPGAHYMRALSNIEGFERLVCTQKKENESRVALCELGNPMKKDTRIGITMLVSVENLEEAGESVSFQLQVRSKNSQNPNSKVVMLPVAIQAEATVELRGNSFPASLVVAAEEGDREQEDLDRWVSRLEHTYELHNIGPGTVNGLRLLIHIPGQSQPSDLLYILDVQPQGGLLCSTQPSPKVDWKLSTPSPSSIRPVHHQRERRQAFLQGPKPGQQDPVLVSCDGSASCTVVECELREMVRGQRAMVTVQVMLGLSSLRQRPQEQFVLQSHAWFNVSSLPYSVPVVSLPSGQARVQTQLLRALEERAIPVWWVLVGVLGGLLLLTLLVLAMWKAGFFKRNRPPLEEDEEEE
Protein: INO80 complex subunit B (B8ZZ93)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKLWRRGSTSGAMEAPEPGEALELSLAGAHGHGVHKKKHKKHKKKHKKKHHQEEDAGPTQPSPAKPQLKLKIKLGGQVLGTKSVPTFTVIPEGPRSPSPLMVVDNEEEPMEGVPLEQYRAWLDEDSNLSPSPLRDLSGGLGGQEEEEEQRWLDALEKGELDDNGDLKKEINERLLTARQRRCC
Protein: SD03914p (Q8MSR6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEPQIETQMQPQIETRMQHDVLSVQSPQNHQPQVQSHDQSQMQHQIPPQIEPQIEVQNQEQNTLQLVPQAQHQVVPHVQLQSQLVPHVQTQGTTTTVTYEQIYQQHIVQQTVQQSSNKMQVISLPSAGSETTRQWQTQQSQQQQQVQWSSVGGLEAIKSAPVESVAPTTTTYYISASDLYPQQTETYTMLQPASNESYVIEQVNHQQQHCQQQIQMSQQQHQRQHQQQQAQQQQQPIMILIQQPEIQQPVASASNPQQAPLHIYNAATSNDVHQMQHTQRQQIRQQYQHQQYQRLQQPQQTRVVQSHPVLGMPGATSISTKVTPIPVTAARGRPLTLKCRFCHNGPRFSSSLEYSRHIIDLHPAVAPFNCPHCPMAFAGRTKRSQHILSHHVVQQYQCGQCSHVFPAQKALDVHIQRFHMTLKTDPSGAVKVEDVQLQITSERRPRGRPYKPRLQLQQHQLQPQQKLQVQQHQQQQKALQQLPQAQHHQQQQQPQLQQEVLQQVQQLQVQVQPQQHQQHQQVLQVQQPQQQPLMQPQSPHPSTVEMQASPTTPRKILCCPDCEDCTSGHSHANEQFEELQTLQAPPTVLTPPSTIVSVPSPQPMVYSQHITMPSPEQSEPDSTTTLRQYRKRGVIVGPQGPLHLATPVASPSPSSSPSSSTVDHIPPASPATPASPAPPPSPAVASTVQVSELRTSHHCLYCEERFTNEISLKKHHQLAHGALTTMPYVCTICKRGYRMRTALHRHMESHDVEGRPYECNICRVRFPRPSQLTLHKITVHLLSKPHTCDECGKQFGTESALKTHIKFHGAHMKTHLPLGVFRNEDAASKSPSNNNSHASSDKLENPATPIEETPLTPMSSGGHLYHSPDEYPNSVESCAGNSVALESYATTP
Protein: Isoleucine--tRNA ligase, cytoplasmic (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IRS) (IleRS) (Q8BU30)
Organism: Mus musculus (Mouse)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41252}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P41252}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Lysine--tRNA ligase
- Glutamine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Probable leucine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
Sequence:
MVQQVPENISFPAEEEKILEFWSKHNCFQECLKQSKLRPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIKGPEDVAKMGIAEYNKQCRAIVMRYSAEWKSTVTRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACGTPLSNFESNQNYKDVQDPSVFVTFPLEEDENTSLVAWTTTPWTLPSNLALCVNPEIQYVKIKDVARGKLFILTEARLSALYKQESDYEILERFPGASLKGKKYKPLFDYFIKCKENGAFTVLVDHYVKDEEGTGVVHQAPYFGADDHRVCMDFNIIQKDSVPVCPVDASGCFTEEVTHFVGQYVKDADKNIIRMLKEQGRLLAAGTFTHSYPFCWRSDTPLIYKSVPSWFVRVEPMVDQLLKNNDLCYWVPEFVREKRFGNWLKEARDWAISRNRYWGTPIPLWVSEDLEEVVCIGSVAELEELSGTKISDLHRESIDHLTIPSRCGKAPLRRVSEVFDCWFESGSMPYAQVHYPFESKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLILASDGQKMSKRKKNYPDPVSIIDKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFFIQNVFRLHKEEEVKFLYNEHTVRESPNITDRWVLSFMQSLLGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGESGVEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKLLIDPASLRDKDTLSIHYLMLPRVREELIDKKTENAVSRMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALEDIRSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMMAIKRLSNEELERFQKSGSIVVEGHELHEEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYNAKSEGRYLNNVIESHTDFIFATIKAPLKPYPVPTSDNILIQEQTQLKGSELEITLTKGSCVPGPACAYVNLNICANGTEQGGVLLLENPKGDNQLNLVKLKTVVTSVFGVKNAKLSVFHGETEIQNQTDLLSLSGRTLCVTAGASPSPISSPSTLLCQYLNLQLLNAEPQECLTGTVGTLLLENPLGQNGLTHQGLVHEAAKVFGLRSRRLRLFLNETQTQEITEDIPMKTLNMKTVYVSVLPTTADG
Protein: Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (P22791)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:1971108}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Peroxisomal bifunctional enzyme
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- Squalene monooxygenase
Sequence:
MQRLLAPARRVLQVKRVMQESSLSPAHLLPAAQQRFSTIPPAPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRRKIQNQWKQAGNNQPFTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFKGLKLEETYTNKDVDKALLKASLDMFNKKTKASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRLDSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARRPV
Protein: Carboxypeptidase N catalytic chain (CPN) (EC 3.4.17.3) (Carboxypeptidase N polypeptide 1) (Carboxypeptidase N small subunit) (Q9JJN5)
Organism: Mus musculus (Mouse)
Function: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:10878383}.
Interaction partners:
- Carboxypeptidase N subunit 2
- Carboxypeptidase B2
Sequence:
MPDLPSAFLPLLLLSKFVTPVTFRHHRYDDLVRTLYKVHNQCPDITRLYNIGRSVKGRYLYVLEFSDYPGIHEPLEPEVKYVGNMHGNEVLGRELLLQLSEFLCEEFRNRNQRILRLIQDTRIHILPSMNPDGYEVAAAQGPNMSGYLVGRNNANGVDLNRNFPDLNTYFYYNSKNGGPNHHLPLPDNWKSQVEPETRAVIQWIRSLNFVLSANMHGGAVVANYPYDKSLEHRFRGPHRTSNSPTPDDELFQTLAKVYSYAHGWMHQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPRQEELQREWLGNREALIQFLEQVHQGIKGMVLDENSNNLTGAVISVTGINHDVTSGEHGDYFRLLLPGTYSVTAKAPGYDPKTVTVTVGPAGPTVVDFQLKRSSSQVYPVQRAPGRGQGGRAKQPRTSRKKDPATKRHRGPA
Protein: Spermatogenesis-associated protein 46 (Q4FZF2)
Organism: Mus musculus (Mouse)
Function: Plays a role in spermiogenesis and fertilization.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:27488028}. Note=Located throughout the subacrosomal area (PubMed:27488028). {ECO:0000269|PubMed:27488028}.
Interaction partners:
- Serine-rich single-pass membrane protein 1
- Sperm acrosome membrane-associated protein 1
Sequence:
MDNYSLLSTPRPRISSSALSAFPDIMSSLATSLPDLGDTQNGEQLRRNCTIYRPWFSPYSYFVCTDKESHLEAYGFPEVDREEGRGDNCLLEDVAESVCSSSSSQENTYPREANRKSKHGLDSITSQDILMASKWHPAQQNGYKCASCCRMYPTLHSLKSHIKGGFKEGFSCKVYYRKLKTLWGKEQKARTGDRISLGSCQAFK
Protein: Small ubiquitin-related modifier 2 (SUMO-2) (SMT3 homolog 2) (Sentrin-2) (Ubiquitin-like protein SMT3A) (Smt3A) (P61959)
Organism: Rattus norvegicus (Rat)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- SUMO-conjugating enzyme UBC9
- Tyrosyl-DNA phosphodiesterase 2
- E3 SUMO-protein ligase PIAS4
- Ran GTPase-activating protein 1
- Cellular tumor antigen p53
- SUMO-activating enzyme subunit 1
- Small ubiquitin-related modifier 1
- Protein kinase C zeta type
- SUMO specific peptidase 1
Sequence:
MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY