wanglab/gogpt-training-data huggingface dataset:
Protein: Ceramide synthase 5 (CerS5) (LAG1 longevity assurance homolog 5) (Sphingoid base N-palmitoyltransferase CERS5) (EC 2.3.1.291) (Sphingosine N-acyltransferase CERS5) (EC 2.3.1.24) (Q8N5B7)
Organism: Homo sapiens (Human)
Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA). Can use other acyl donors, but with less efficiency (By similarity). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Plays a role in de novo ceramide synthesis and surfactant homeostasis in pulmonary epithelia (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D6K9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingolipid delta
- 3-ketodihydrosphingosine reductase
- Sphingolipid delta
- Sphingomyelin phosphodiesterase 2
- Ceramide glucosyltransferase
- Sphingomyelin phosphodiesterase
- Acid ceramidase
- Sphingosine kinase 1
- Ceramide kinase
- Neutral ceramidase
Sequence:
MATAAQGPLSLLWGWLWSERFWLPENVSWADLEGPADGYGYPRGRHILSVFPLAAGIFFVRLLFERFIAKPCALCIGIEDSGPYQAQPNAILEKVFISITKYPDKKRLEGLSKQLDWNVRKIQCWFRHRRNQDKPPTLTKFCESMWRFTFYLCIFCYGIRFLWSSPWFWDIRQCWHNYPFQPLSSGLYHYYIMELAFYWSLMFSQFTDIKRKDFLIMFVHHLVTIGLISFSYINNMVRVGTLIMCLHDVSDFLLEAAKLANYAKYQRLCDTLFVIFSAVFMVTRLGIYPFWILNTTLFESWEIIGPYASWWLLNGLLLTLQLLHVIWSYLIARIALKALIRGKVSKDDRSDVESSSEEEDVTTCTKSPCDSSSSNGANRVNGHMGGSYWAEE
Protein: Solute carrier family 12 member 2 (Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 2) (BSC2) (Na-K-Cl cotransporter 1) (NKCC1) (A0A0G2KTI4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cation-chloride cotransporter which mediates the electroneutral transport of chloride, potassium and/or sodium ions across the membrane. Plays a vital role in the regulation of ionic balance and cell volume. Important for maintenance of endolymph volume in the otic vesicle, probably by regulating ion homeostasis. Also plays a role in normal development of the swim bladder.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:19633174, ECO:0000305|PubMed:31367042}; Multi-pass membrane protein {ECO:0000305|PubMed:31367042}.
Interaction partners:
- Cortexin 3
Sequence:
MSASPPISAGDYLSAPEPDALKPAGPTPSQSRFQVDLVTESAGDGETTVGFDSSPPEYVAEPPPDGLRDSVSGGEEAKGRFRVVNFAASSPDAAPAETAQNGDTVMSEGSLHSSTGGQQHHHYDTHTNTYYLRTFGHNTIDAVPKIDFYRQTAAPLGEKLIRPTLSELHDELDKEPFEDGFANGEELTPAEESAAKDVSESKGVVKFGWIKGVLVRCMLNIWGVMLFIRMTWIVGQAGIAYSCIIVIMATVVTTITGCSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVELLMDSGLLMIDQTNDIRVIGTITVILLLGISVAGMEWEAKAQIFLLVILITAIFNYFIGSFIAVDSKKKFGFFSYDAGILAENFGPDFRGQTFFSVFSIFFPAATGILAGANISGDLADPQMAIPKGTLLAILITGLVYVGVAISAGACIVRDATGIESNFTLISNCTDAACKYGYDFSSCRPTVEGEVSSCKFGLHNDFQVMSVVSGFSPLISAGIFSATLSSALASLVSAPKVFQALCKDNIYPGIAIFGKGYGKNNEPLRGYFLTFGIALAFILIAELNVIAPIISNFFLASYALINFSVFHASLANSPGWRPSFKYYNMWASLAGAILCCVVMFIINWWAALLTNVIVLSLYIYVSYKKPDVNWGSSTQALTYHQALTHSLQLCGVADHIKTFRPQCLVMTGAPNSRPAILHLVHAFTKNVGLMLCGHVRISSRRPNFKELNSDMLRYQRWLLNNNSKAFYTCVVAEDLRQGTQYMLQAAGLGRLRPNTLVIGFKNDWRTGDIKEVETYINLIHDAFDFQYGVVILRLREGLDISHIQGQDDSSGMKDVVVSVDISKDSDGDSSKPSSKATSVQNSPAVQKDEDDDGKAHTQPLLKKDKKSPTVPLNVADQRLLDASQQFQQKQGKGTVDVWWLFDDGGLTLLIPYLIANKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDITVLGDINTKPKSEGLTEFAEMIEPYKLREDDMEQEAAEKLKSEEPWRITDNELELYKAKGNRQIRLNELLKEHSSTANLIVMSMPLARKGAVSSALYMAWLDTLSKDLPPILLVRGNHQSVLTFYS
Protein: Microneme associated antigen (O77394)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Rhoptry associated adhesin
Sequence:
MHDFFLKSKFNILSSPLFNNFYKRNNEDEYFKKDRNNNDDLGVMHNYADDSEWREHNKKDRMTSLKNELNEQLIYTYYNNFNNNYEYYNKSTEKLKEKNNEDEYNEEQEYEPTANLLQDKNKINDMNNFYNNFNKNSLFNYQNFQNADKNFLYLLNKKNKNNSTNENILVDEFKKLKNHVLFLQMMNVNLQKQLLTNHLINTPKIMPHHIIINNKTEVSSNAVSEIQNNKDKKKNGTMYILLKKILSSRFNQMIFVSSIFISFYLINKHWQRALKISQLQKKINSNFLLKSVRLFEESLGIRKNKYI
Protein: Helix-loop-helix 34 (P90953)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Involved in specifying AVH neuron identity, acting in concert with unc-42. Involved in serotonin-mediated feeding behavior, probably acting by modulating expression of genes involved in glutamate signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator homolog
- PAS domain-containing protein cky-1
- xanthine dehydrogenase
Sequence:
METNLSEEKQKPSKSQAQQRRQMENYEFSQLANELPLARAISGQHIDKTTMVRLATAYIKLHNIFGQSQRAYSSADYYYGSDSLWTNNHLDLLDGFFVILDRRGDVLYISETISIYLGLSQVEMTGNAMVDYIHEQDINCFNSALNYCDLNWPQMCNVRVKSSLTKRANKDAVRASPGYKVLRLEITMGPNTNTRMIACYPMPTPVLSTVTIPSNSFVIITSIDLHITFADEKAHQLLNNPFYPDSNIKGMSLYSLIDISDSEVISKMHFDIFNLGAYKTPYYRMILNQTSETFYVESNIFRHTSISSKQFNDSITFVSSIL
Protein: Leptin receptor overlapping transcript-like 1 (Endospanin-2) (Q6PDU4)
Organism: Rattus norvegicus (Rat)
Function: Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tmem50a protein
- Transmembrane protein 50B, isoform CRA_b.
Sequence:
MAGIKALISLSFGGAIGLMFLMLGCALPIYNQYWPLFVLFFYILSPIPYCIARRLVDDTDAMSNACKELAIFLTTGVVVSAFGLPVVFARAHLIEWGACALVLTGNTVIFATILGFFLVFGSNDDFSWQQW
Protein: Nodal modulator 3 (A1Z843)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
- Nicalin
Sequence:
MRFFSGVFVILLIKLFQNANAGEVEVVGCGGFIKSHAEIDFSRVEIKLLTKQGSLKDKTDCSPSNGYYFLPIYDKGDYLLSISPPPGWSFEPEQVELNFDGKTDVCSQGRDVNFVFKGFGITGQVALAAGGGARGVDVELRSEQGEVRRTKSDANGVFSFTPIIPGNYVVKASHARWHFSKAEHKVVVVSGNTELPANSLVVSGFDVVGRFDSSSPLPGNLGVALYKKKGQSLVPKCETSSPAPPNSVNSAYESASSCFSQLDKSGEYIFKNVPSGKYLLQAINLDSKLKLHLSPELLELEVGKDTLQIKDEFKITGFTVSGRVLTSAGGEPLKSAVIKVNGKKVAETDAQGSYTLENLKAGTVNIEVESSQLQFSPLQVKAQINTASLPTIVPSAYEVCGKVVSPKSHNVGLTKIGSTFHSSASTNAETGNWCAFLPVGKYTIEVLTTDADKAAGVQFFPVQQQTEVRDAPVNGITFSQLRAKIRGELQCLPDATATCTSAEVTLQALDATGQPTENKWKARAHRGKYVFKDMLPGPYELTIPQGNLCYESTRVFLNVASAEEDAPPFVHKGYEVSIISSHRALMKYTHVTGPSEPKAPTESLKIASGVNTFCVKKYGSYDFKLEGCHTYDESLPSKFITPEPDQLQTLIINAVAHKTGVRVLSTEPTADSIKLVLESESLGQEVITPVAESHKVDGKFAYRYDTYLKPEQVLRITPVSDVLLFAPQQHEIVGSSDCVDIAFNFVATRGLILRGKVVPAIKDAKITLSFPDQPELESLEVLTSVTGEFKFGPIEESLAFDLKAEKESYVFSDYNRQTASFSAHKLCEISVVVKDEAGQTLGGVLLSLSGGESYRKNLVTGDNGAINFHSLSPSQYYLRPMMKEYKFEPNSKMIDIKDGETVSVTLVGKRFAYSIFGTVSSLNGDPFAGVNVQATADNSCPQQPEEATSEANGQYRIRGLQPGCSYSVRVVPDKEIVERSIPAQHTVKVANEDVRDINLVAISPLKIVDITARVTATLNEHYKTLRIVMYRKGNSDSPVFSQRVGTPVNPKARLNPGITVFFPRIPLDGKSYVVELQSTLSDKTYTYKLPSTTFVADRGSVFVELEFKPEVRAAEADLNQNSISALVLIALVAIAFFKQDLATSFLSFVWSKLNDVAADLAQRQKSKTQVRKNEPINQREIEQMADQINAIKKKKTKKI
Protein: Sclerostin (Q99P67)
Organism: Rattus norvegicus (Rat)
Function: Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- LDL receptor related protein 5
- Tumor necrosis factor ligand superfamily member 11
- Dickkopf homolog 1
- Low-density lipoprotein receptor-related protein 4
- Bone morphogenetic protein 2
- Parathyroid hormone
- Protein Wnt
- Osteocalcin
- Bone morphogenetic protein 4
Sequence:
MQLSLAPCLACLLVHAAFVAVESQGWQAFKNDATEIIPGLREYPEPPQELENNQTMNRAENGGRPPHHPYDTKDVSEYSCRELHYTRFVTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRVKWWRPNGPDFRCIPDRYRAQRVQLLCPGGAAPRSRKVRLVASCKCKRLTRFHNQSELKDFGPETARPQKGRKPRPRARGAKANQAELENAY
Protein: Synaptotagmin-like protein 4 (Exophilin-2) (Granuphilin) (Q96C24)
Organism: Homo sapiens (Human)
Function: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles (By similarity). {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-27A
- Syntaxin-binding protein 1
- Ras-related protein Rab-3A
- Ras-related protein Rab-8A
- Ras-related protein Rab-27B
- One cut domain family member 2
- Syntaxin-1A
- Syntaxin-3
- Insulin
- Unconventional myosin-Va
Sequence:
MSELLDLSFLSEEEKDLILSVLQRDEEVRKADEKRIRRLKNELLEIKRKGAKRGSQHYSDRTCARCQESLGRLSPKTNTCRGCNHLVCRDCRIQESNGTWRCKVCAKEIELKKATGDWFYDQKVNRFAYRTGSEIIRMSLRHKPAVSKRETVGQSLLHQTQMGDIWPGRKIIQERQKEPSVLFEVPKLKSGKSALEAESESLDSFTADSDSTSRRDSLDKSGLFPEWKKMSAPKSQVEKETQPGGQNVVFVDEGEMIFKKNTRKILRPSEYTKSVIDLRPEDVVHESGSLGDRSKSVPGLNVDMEEEEEEEDIDHLVKLHRQKLARSSMQSGSSMSTIGSMMSIYSEAGDFGNIFVTGRIAFSLKYEQQTQSLVVHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTINPLYDETLRYEIPESLLAQRTLQFSVWHHGRFGRNTFLGEAEIQMDSWKLDKKLDHCLPLHGKISAESPTGLPSHKGELVVSLKYIPASKTPVGGDRKKSKGGEGGELQVWIKEAKNLTAAKAGGTSDSFVKGYLLPMRNKASKRKTPVMKKTLNPHYNHTFVYNGVRLEDLQHMCLELTVWDREPLASNDFLGGVRLGVGTGISNGEVVDWMDSTGEEVSLWQKMRQYPGSWAEGTLQLRSSMAKQKLGL
Protein: Uridylate kinase PUMPKIN, chloroplastic (EC 2.7.4.22) (Plastid UMP kinase) (Protein DEFECT IN PSAA/B TRANSCRIPT ACCUMULATION 1) (Uridine monophosphate kinase) (UMP kinase) (UMPK) (Q9LSA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible phosphorylation of UMP to UDP. Required for specific post-transcriptional processes of many plastid transcripts (e.g. PSI (PsaA, PsaF), PSII (D1, CP43, CP47), Cytochrome b(6)f (Cytb(6)), ATP synthase (AtpC), LHCs (LHCa3, LHCb2), and NDH (NdhH)), thus being essential for retaining photosynthetic activity in chloroplasts. Associates with group II introns of the plastid transcripts trnG-UCC, trnV-UAC, petB, petD and ndhA to stabilize corresponding precursor RNAs.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19037728, ECO:0000269|PubMed:30409856}.
Interaction partners:
Sequence:
MAIPLPLTSCSPISTSSSISRTSFVPLTLRNRTFFSNQNYSRRVLISCSSSLSSDNGSSPDSMNGNGNGNGSSLNGQSSFPRLPSFDGTSKPPLKWRRVLLKVSGEALAGDEEQNIDPKVTMAIAREVAAVTRLGIEVAIVVGGGNIFRGSTWAGCSGLDRSSADYIGMLATVMNAIFLQATMESIGIPTRVQTAFRMSEVAEPYIRRRAIRHLEKGRVVIFAAGTGNPFFTTDTAAALRCAEINAEVVLKATNVDGVFDDDPKRNPNARLLDSLTYQEVTSKDLSVMDMTAITLCQENNIPVVVFNLSEPGNIAKAIKGERVGTLIGGTWNSIVTTTS
Protein: F-box/LRR-repeat protein 10 (Q9SDA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATTTVVCGGGGDVEGCDGERSLDLLPAALLETIMTKLDVASLCSLASTCKTLKSCVTRVLTFTPNFHIFNVSLSMETVRPLLFPNQQLSSLKLDCGRLGNSAIDILVRPSLREISLHNCRDFSGDLISEIGRKCKDLRLLCLGSVAEKVGRSISRCALEDLLNGCSHLEVLALMFDLSLYLRPGDGRIFGLVSDRLTHLELGHITSRMMTQLLTSTEISGQDSNRVTTSTVLQNVQRLRLSVDCITDAVVKAISKSLPSLIDLDIRDAPLEDPRQVSDLTDFGLHEINQNGKLKHLSLIRSQEFHPTYFRRVSDQGMLFLADKCLGMETICLGGFCRVTDAGFKTILHSCASLSKFSIYHGPKLTDLVFHDILATTLSLSHVSLRRCHLLTDHAIQKLASSLKLENLDLRGCRNLRDETLTAVSHLPKLKVLLLDGADISDTGLSYLKEGVLDSLVSLSVRGCRNLTDKFMSTLFDGSSKLALRELDLSNLPNLTDAAIFALAKSGAPITKLQLRECRLIGDASVMALASTRVYEDECPGSSLCLLDLYDCGGITQLSFKWLKKPFFPRLKWLGITGSVNRDIVDALARRRPHLQVSCRGEELGNDGEDDWDSADIHQHIEAQEDELEQWILGDEGDVEMEDAEDESEEDASEED
Protein: Lysozyme-like protein 4 (Lysozyme-4) (Q9D925)
Organism: Mus musculus (Mouse)
Function: May be involved in fertilization. Has no detectable bacteriolytic in vitro. Has no lysozyme activity in vitro (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:21444326}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:21444326}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:21444326}. Note=Found in the principal piece of sperm tail (PubMed:21444326). {ECO:0000269|PubMed:21444326}.
Interaction partners:
Sequence:
MQLYLVLLLISYLLTPIGASILGRCTVAKMLYDGGLNYFEGYSLENWVCLAYFESKFNPSAVYEDPQDGSTGFGLFQIRDNEWCGHGKNLCSVSCTALLNPNLKDTIQCAKKIVKGKHGMGAWPIWSKNCQLSDVLDRWLDGCDL
Protein: Coatomer subunit beta-2 (Beta-coat protein 2) (Beta-COP 2) (Q9SV20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit alpha-2
- Coatomer subunit alpha-1
- Coatomer subunit beta'-1
- Coatomer subunit beta'-3
- Coatomer subunit beta'-2
- Coatomer subunit gamma
- Coatomer subunit epsilon-2
- Coatomer subunit epsilon-1
- Structural molecule
Sequence:
MDKSSTMLVHYDKGTPAVANEIKEALEGNDVEAKVDAMKKAIMLLLNGETIPQLFITIIRYVLPSEDHTIQKLLLLYLELIEKTDSKGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRMKETEIVEPLTPSVLQNLEHRHPFVRRNAILAIMSIYKLPHGDQLFVDAPEMIEKVLSTEQDPSAKRNAFLMLFTCAEERAVNYLLSNVDKVSDWNESLQMVVLELIRSVCKTKPAEKGKYIKIIISLLSATSSAVIYECAGTLVSLSSAPTAIRAAANTYCQLLLSQSDNNVKLILLDRLYELKTLHRDIMVELIIDVLRALSSPNLDIRRKTLDIALDLITHHNINEVVQMLKKEVVKTQSGELEKNGEYRQMLIQAIHACAVKFPEVASTVVHLLMDFLGDSNVASALDVVVFVREIIETNPKLRVSIITRLLDTFYQIRAGKVCPCALWIIGEYCLSLSEVESGISTITQCLGELPFYSVSEESEPTETSKKIQPTSSAMVSSRKPVILADGTYATQSAASETTFSSPTVVQGSLTSGNLRALLLTGDFFLGAVVACTLTKLVLRLEEVQSSKTEVNKTVSQALLIMVSILQLGQSPVSPHPIDNDSYERIMLCIKLLCHRNVEMKKIWLESCRQSFVKMISEKQLREMEELKAKTQTTHAQPDDLIDFFHLKSRKGMSQLELEDQVQDDLKRATGEFTKDENDANKLNRILQLTGFSDPVYAEAYVTVHHYDIALEVTVINRTKETLQNLCLELATMGDLKLVERPQNYSLAPERSMQIKANIKVSSTETGVIFGNIVYETSNVMERNVVVLNDIHIDIMDYISPAVCSEVAFRTMWAEFEWENKVAVNTTIQNEREFLDHIIKSTNMKCLTAPSAIAGECGFLAANLYAKSVFGEDALVNLSIEKQTDGTLSGYIRIRSKTQGIALSLGDKITLKQKGGS
Protein: Probable inactive serine protease 37 (Probable inactive trypsin-X2) (Q9DAA4)
Organism: Mus musculus (Mouse)
Function: Plays a role in male fertility. May have a role in sperm migration or binding to zona-intact eggs. Involved in the activation of the proacrosin/acrosin system (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:A4D1T9}. Secreted {ECO:0000305}.
Interaction partners:
- Inactive serine protease 54
- A disintegrin and metallopeptidase domain 3
- Serine protease 44
Sequence:
MKLIIYLTILAGTALVTHSSVQKEDHAPYLAYLKSNFNPCVGVLIKASWVLAPSHCYLPNLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLMLIKLAKPATFNHKVQVLPIATTNVRPGTVCTLSGLDWSQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSSHRNSLCVRFVKVFSRIFGEVAVATVICKNKLQGIEVGHFMGGDVGIYTNIYSYVPWIEKTTKEKMT
Protein: Snurportin-1 (RNA U transporter 1) (Q68FP5)
Organism: Rattus norvegicus (Rat)
Function: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95149}. Cytoplasm {ECO:0000250|UniProtKB:O95149}. Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta. It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway. {ECO:0000250|UniProtKB:O95149}.
Interaction partners:
- Exportin-1
- GTP-binding nuclear protein Ran
- Importin subunit beta-1
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Exportin-5
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup214
- Importin-13
- Importin subunit alpha
Sequence:
MEELSQALASSFSVSQELNSTAAPHPRLSQYKSKYSSLEQSERRRQLLELQKSKRLDYVNHARRLAEDDWTGMESGEEEKKKDEEEMDLDPVKKLPKRYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTTAKDYTILDCIYSEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMNSKLPEEEGLGEKTKINPFKFVGLKNFPCTPESLCKVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDILGVAVPAGPLTTKPEYAGHQLQQIIEHKRSQEDTKEKLTHKASENGHYELEHLSTPKLRSPPHSSESLMDS
Protein: Protein AMEIOTIC 1 (C0RWW9)
Organism: Zea mays (Maize)
Function: Plays a fundamental role in building the proper chromosome structure at the beginning of meiosis in male meiocytes. Required for the transition from leptotene to zygotene in meiocytes. Required for homologous chromosome pairing, and initiation and progression of meiotic recombination. Regulates meiocyte cytoskeleton organization.
Subcellular location: Nucleus {ECO:0000269|PubMed:19204280}. Chromosome {ECO:0000269|PubMed:19204280}. Note=Diffuse localization in the nucleus during the initiation of meiosis. Binds to chromatin in early meiotic prophase I. {ECO:0000269|PubMed:19204280}.
Interaction partners:
- 26S protease regulatory subunit 7 homolog A
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- Proteasome subunit alpha type
- 26S proteasome regulatory subunit RPN7
- 26S protease regulatory subunit 8
Sequence:
MDVETVQAGPALAAHLQLQASPKPQVKKYYFKKKTSSSHSRNGKDDVNHDSTIQPRSPLSRQSLTFDAIPTYHAGAFYEIDHDKLPPKSPIHLKSIRVVKVSECTNLDITVKFPSLQALRSFFSSYPAPGTGPELDERFVMSSNHAARILRRRVTEEELEGEVQQDSFWLIKPRLYDFAAPQQVPSRTLCLPPPPAPPAATLGLTADSCLLTTLKCDGAGWGMRRRVRYIGRHRDEAPKEASVDGYDTESSVREVQQPPATQEVKRSERNCKRKREAEASSKDNNGDEGKKNNKVQGASKKISKKAKKRTVESKDGDPRHGKDRWSAERYAAAEKSLLNIMRSRDARFGAPVMRQVLREEARKHIGDTGLLDHLLKHMAGRVPEGSVHRFRRRHNADGAMEYWLEPAELAEVRKQAGVSDPYWVPPPGWKPGDDVSLVAGDILVKRQVEELTEEVNGVKRQMEQLLCKDDGDFGAERDYSSLKEKYQRAVRANEKLEKQVLCLKDMCENVVQMNGELKKEVSAFKEKYEHIADKNDKLEEQVTYLSSSFLSFKDQLVVALKLELAPSEAVPRTALFVASGEQMTGTVIQGGQDRAERKSSFRVCKPQGKFLLPSMASGMTIGRGASSTCPAAATPGPGIPRSTSFPSMPGLPRSSRGPVEVVAAASGLDEHVMFGAHFSTPPSASSTNDAAKLQLSLPSPRSPLQPQKLFDTVTAAASGFSPQKLMHFSGLTRRDVDTSSSSSGACGSGLLEGKRVLFDADAGGISAVGTELALATPSYC
Protein: Large ribosomal subunit protein uL6c (50S ribosomal protein L6, chloroplastic) (Protein EMBRYO DEFECTIVE 2394) (O23049)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein binds directly to 23S ribosomal RNA and is located at the aminoacyl-tRNA binding site of the peptidyltransferase center.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL3c
- Large ribosomal subunit protein bL27c
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL2cz/uL2cy
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL4c
- Large ribosomal subunit protein uL16c
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS14m
Sequence:
MASSLVSSFQPRSAFLGDRNVFKVSSTPFAQVGYSSKTIECKESRIGKQPIAVPSNVTIALEGQDLKVKGPLGELALTYPREVELTKEESGFLRVKKTVETRRANQMHGLFRTLTDNMVVGVSKGFEKKLILVGVGYRATVDGKELVLNLGFSHPVKMQIPDSLKVKVEENTRITVSGYDKSEIGQFAATVRKWRPPEPYKGKGVKYSDEIVRRKEGKAGKKK
Protein: RE65433p (Q9VRT2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- Zinc carboxypeptidase A 1
- Uncharacterized protein
- Venom allergen-1
- trypsin
- Peptidase S1 domain-containing protein
- GH20109p
- Retinoid-inducible serine carboxypeptidase
- FI02848p
- Serine protease K12H4.7
Sequence:
MKFACATVLLLATILGAQAVDWNSVKNLNIETPMPKVHGETLPSGRITGGQIAEPNQFPYQVGLLLYITGGAAWCGGTIISDRWIITAAHCTDSLTTGVDVYLGAHDRTNAKEEGQQIIFVETKNVIVHEDWIAETITNDISLIKLPVPIEFNKYIQPAKLPVKSDSYSTYGGENAIASGWGKISDSATGATDILQYATVPIMNNSGCSPWYFGLVAASNICIKTTGGISTCNGDSGGPLVLDDGSNTLIGATSFGIALGCEVGWPGVFTRITYYLDWIEEKSGVVNNGD
Protein: Fluoroquinolones export permease protein Rv2687c (P9WJB1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c involved in fluoroquinolones export. Confers resistance to ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and sparfloxacin. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Fluoroquinolones export permease protein Rv2686c
- Fluoroquinolones export ATP-binding protein Rv2688c
- Conserved protein
- Transmembrane protein
- Anti-sigma-M factor RsmA
- Uncharacterized protein Rv0955
Sequence:
MTRLVPALRLELTLQVRQKFLHAAVFSGLIWLAVLLPMPVSLRPVAEPYVLVGDIAIIGFFFVGGTVFFEKQERTIGAIVSTPLRFWEYLAAKLTVLLAISLFVAVVVATIVHGLGYHLLPLVAGIVLGTLLMLLVGFSSSLPFASVTDWFLAAVIPLAIMLAPPVVHYSGLWPNPVLYLIPTQGPLLLLGAAFDQVSLAPWQVGYAVVYPIVCAAGLCRAAKALFGRYVVQRSGVL
Protein: Uncharacterized protein (Q581Q0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
Sequence:
MLSSTALLLRGQYKTRLKKRMVGFIPKVIPRKIKNNMVALRSEANTGHMEGYLKTETERLDATGRKVQKVLWDPVLQRHCLFKETKIKGPFMTKSAIAKKVDFPIGGAEKMLKK
Protein: Calreticulin-3 (Calreticulin-2) (Calsperin) (Q9D9Q6)
Organism: Mus musculus (Mouse)
Function: CALR3 capacity for calcium-binding may be absent or much lower than that of CALR (By similarity). During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A3
- Protein disulfide-isomerase-like protein of the testis
- Protein disulfide-isomerase A4
- Hypoxia up-regulated protein 1
- A disintegrin and metallopeptidase domain 3
- Tapasin
- Calnexin
- Protein disulfide-isomerase
Sequence:
MVSARALLWAICVLRVALATVYFQEEFLDGERWRNRWVQSTNDSQFGHFRVSSGKFYGHKEKDKGLQTTQNSRFYAISASFKPFSNKGKTLVIQYTVKHEQKMDCGGGYIKVFPSDLDQKKMNGKSQYYIMFGPDICGFDIKKVHVILYFKNQYHENKKPIRCKVDGFTHLYTLILRPDLSYEVKVDGQSIESGSIEYDWNLTSLRKTEKTSLDSRDWDQVEGSKVQDWEKHFLDAGASKPSDWNSELDGDWLQKPPYEDGLKAEGIDKDVWLHQKMRPAGYLTQYDLSEFENIGAIGLELWQVRSGTIFDNFLITDDEEYAEKFGKATWGETKGPEKEMDAIQAKEEVKKAREEDEEDLLMGKFHRHNHFSRFHRQGEL