wanglab/gogpt-training-data huggingface dataset:
Protein: Solute carrier family 26 member 9 (Anion transporter/exchanger protein 9) (Q8BU91)
Organism: Mus musculus (Mouse)
Function: DIDS- and thiosulfate- sensitive anion exchanger mediating chloride, sulfate and oxalate transport. Mediates chloride/bicarbonate exchange or chloride-independent bicarbonate extrusion thus assuring bicarbonate secretion. May prefer chloride anions and mediate uncoupled chloride anion transport in an alternate-access mechanism where a saturable binding site is alternately exposed to either one or the other side of the membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31339488}; Multi-pass membrane protein {ECO:0000269|PubMed:31339488}. Endomembrane system {ECO:0000250|UniProtKB:Q7LBE3}; Multi-pass membrane protein {ECO:0000269|PubMed:31339488}. Note=Localization to the cell membrane is inhibited by WNK kinases (WNK1, WNK2, WNK3 or WNK4) in a kinase-independent mechanism. {ECO:0000250|UniProtKB:Q7LBE3}.
Interaction partners:
- Cystic fibrosis transmembrane conductance regulator
Sequence:
MNQPRPRYVVDRAAYSLSLFDDEFEKKDRAYPVGEKLRNTFRCSSAKFKAFVFGLLPVLSWLPKYKIKDYIIPDLLGGLSGGCIQVPQGMAFALLANLPAVNGLYSSFFPLLTYFFLGGIHQMVPGTFAVISILVGNICLQLAPESKFQIFNNVTNETYVDTAAMEAERLHVSATLACLTAVIQMALGFMQFGFVAIYLSESFIRGFMTAAGLQILISVLKYIFGLTIPSYTGPGSIVFTFIDICKNLPHTNIASLIFALVSGVFLVLVKELNARYMHKIHFPIPTEMIVVVVATAISGSCKMPKKYHMQIVGEIRQGFPTPVAPMVSQWKGMVGTAFSLAIVGYVINLAMGRTLASKHGYDVDSNQEMIALGCSNFFGSFFKIHVICCALSVTLAVDGAGGKSQVASLCVSLVVMITMLVLGSYLYPLPKAVLGALIAVNLKNSLKQLTDPYYLWRKSKLDCCVWVVSFLSSFFLSLPYGVAVGVAFSILVVIFQTQFRNGSTLAQVMDTDIYVNPKTYNRAQEIAGVKIVTYCSPLYLANSEIFRQKVIAKTGMDPQKVLLAKQKYLRKQEKRTAIPTQQRKSLFMKTKTVSLQELQQDFESAPSTDPNNNQAPAAEAHISYITFSPDASTAAACELPASTRSPQEASDTLASVPPFVTFHTLILDMSGVSFVDLMGIKALAKLSSTYEKIGVQIFLVNIHAQVYNDISHGGVFEDGCVQRSHVFPSIHDAVLFAQANAREAPDRNFHGAPGDTEFSLYDSEEEGPSYWDLEQEMFGTMFHTETLTAL
Protein: Protein Smaug homolog 2 (Smaug 2) (hSmaug2) (Sterile alpha motif domain-containing protein 4B) (SAM domain-containing protein 4B) (Q5PRF9)
Organism: Homo sapiens (Human)
Function: Has transcriptional repressor activity. Overexpression inhibits the transcriptional activities of AP-1, p53/TP53 and CDKN1A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20510020}. Nucleus {ECO:0000269|PubMed:20510020}.
Interaction partners:
- 14-3-3 protein epsilon
- Nanos homolog 1
- Protein Smaug homolog 1
Sequence:
MMFRDQVGILAGWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSNANTGLPCQIHPSPLKRSMSLIPTSPQVPGEWPSPEELGARAAFTTPDHAPLSPQSSVASSGSEQTEEQGSSRNTFQEDGSGMKDVPSWLKSLRLHKYAALFSQMSYEEMMTLTEQHLESQNVTKGARHKIALSIQKLRERQSVLKSLEKDVLEGGNLRNALQELQQIIITPIKAYSVLQATVAAATTTPTAKDGAPGEPPLPGAEPPLAHPGTDKGTEAKDPPAVENYPPPPAPAPTDGSEPAPAPVADGDIPSQFTRVMGKVCTQLLVSRPDEENITSYLQLIEKCLTHEAFTETQKKRLLSWKQQVLKLLRTFPRKAALEMQNYRQQKGWAFGSNSLPIAGSVGMGVARRTQRQFPMPPRALPPGRMGLLSPSGIGGVSPRHALTSPSLGGQGRQNLWFANPGGSNSMPSQSRSSVQRTHSLPVHSSPQAILMFPPDCPVPGPDLEINPTLESLCLSMTEHALGDGTDKTSTI
Protein: Nucleoporin NSP1-like C-terminal domain-containing protein (Q381M9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
- Nuclear pore protein
- Nucleoporin
- Nucleoporin
- Nuclear pore complex protein
- Uncharacterized protein
- Telomerase-associated protein, putative
- Long-chain-fatty-acid-coA ligase protein,putative
- Protein transport protein Sec13, putative
- Protein transport protein sec13, putative
- Poly
Sequence:
MKGFAVRGRAPSGGGFGQPAVDTNATAAAPVLGFGSFGQSNTESVAGVTNPFGQTANQSGGSAPAAGMGGFGSGPSTGGFAVGAQSTSSATQPAPVLGQTVLGFGATPGKGEGGNSVVPTGVGAAAAPSTSAAPTSGFSGFGSGAKTTLNPFGAGFGQTSTTGTTATAPSTGGFGAATSAVGQTPASGATPANTTFDGSASNPGNTGTNPTAGTATAVPAATTMVTNPPSGDTVKAGAPAAFGGFGATPPASGSNPSAAPTPFAGFGAGATAPTNPASTNATAGAATTGGGPFSSITKPSETGGNAPPATAGAGGAGLGPSLGAGVTGGNQSAGATGTVGAGDPTAISGKQASLELRGKMLSTILAQFDKAFSKDYRDFSELSQLMMLRDRQIIERGNEILSHSSHLEEAIANADVTRQTLIELKNKQAAIGTMLQRFEDAVQPIFAQVRPTFNSVDEAREETYTAVINLFDEVETLKLRLQQCVRQHNGSVRHLRQSDDLAKFVGLIDCQLSAMEVCAAQASELEREVDLLLGKSTIA
Protein: N-alpha-acetyltransferase 25, NatB auxiliary subunit (Liver regeneration-related protein LRRGT00164) (Mitochondrial distribution and morphology protein 20) (N-terminal acetyltransferase B complex subunit MDM20) (NatB complex subunit MDM20) (N-terminal acetyltransferase B complex subunit NAA25) (Q6QI44)
Organism: Rattus norvegicus (Rat)
Function: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. May play a role in normal cell-cycle progression.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14CX7}.
Interaction partners:
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 30
- N
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 50
- N
- N-terminal amino-acid N
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 40
Sequence:
MATRGHVQDPNDRRLRPIYDYLDNGNNKMAIQQADKLLKKHRDLHCAKVLKAIGLQRTGRQEEAFTLAQEVAALEPTDDNSLQALTILYREMHRPELVTKLYEAAVKKVPNSEEYHSHLFMAYARVGEYKKMQQAGMALYKIVPKNPYYFWSVMSLIMQSISARDENLSKTMFLPLAERMVEKMVKEDKIEAEAEVELYYMILERLGKYQEALDVIRGKLGEKLTSEIQSRENKCMAMYKKLSKWPECNALSRRLLLKNSDDWQFYLTYFDSVFRLIEEAWTPPAEGEHSLEGEVHCSAEDAVKFIEDRITEASQSSRHVRGPHLAKLELIRRLRSQGCNDEFRLGDPEELMFQYFKKFGDKPCCFTDLKVFVDLLPAAQCTQFINQLLGVVPLSTPTEDKLALPADIRGLQQHLCVVQLTRLLGLYHSMDKNQKLDVVRELMLRYQHGLEFGRSCLKTELQFSDYYCLLAVHVLIDIWREAGEETAVWQALTLLEEGLTHSPSNAQFKLLLVRIYCVLGAFEPVVDLYSSLDAKHIQHDTIGYLLTRYAASLGQYAAASQSCNFALRFFHSNQKDTSEYIIQAYKYGAFEKIPEFIAFRNRLNNSLHFAQVRTERMLLDLLLEANISTSLAESIKSMNLRPEEDDVPWEDLRDNRDLDVFFSWDPKDRNVSEEHKKLSLEEETMWLRIRSLTLRLISALPSLTHPVEPRNSEKTSENGVSSRVDVLRLLLQQLEVAVETGKRFIEKEIQYPFLGPVPTRMGRFFSSGCCQCQVHSFHLVSDVYELDTSGLEGTVDIQERIENSLASLLELLKGVFSTCKGDLLEVKDGNVKTQPAVLENLVFFVETISIVLWVSSYCESVLRPYKLNIQKKKKKKKETSIVMPPIFTSFQDYVTGLQTVISNAVDHIKGLEAHLIALKLEELTLEDTSISPVNLSNCHVLSVRRRDPGSYWKLGAVEPMCADVCPSVQI
Protein: rRNA methyltransferase 1, mitochondrial (EC 2.1.1.-) (21S rRNA (guanosine-2'-O)-methyltransferase) (Mitochondrial large ribosomal RNA ribose methylase) (O94631)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of the 2'-O-methylguanosine corresponding to position 2270 in S.cerevisiae 21S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P25270}.
Interaction partners:
- rRNA methyltransferase 2, mitochondrial
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein bL17m
- Pseudouridylate synthase C18B11.02c
- Putative acyl carrier protein, mitochondrial
- Large ribosomal subunit protein mL43
- tRNA modification GTPase mss1
- AdoMet-dependent rRNA methyltransferase spb1
- Multisubstrate pseudouridine synthase 7
- Large ribosomal subunit protein uL24
Sequence:
MIRSRVNLAREVPKKAKAHLSKERRLIKEDSEFVFGTHSVKNALATRKRECRALYVQNADIHSEFEEFLNKLQYKIPIKSVNKEHLNQITACRPHNGVVLEASSLNVPTISDLLFPAGEEYNNKNGQDSPHNDLNEGKSSSSDNYPPLYVYVDGITDPQNMGAVIRSAYILGAKGILLSKKHNTFLSPVVSKASAGALEVFNISHVKNPMVFLRNSVLKGWKVIGTKPALPDNKDQIYTPHKIKTELMNEPKILVLGSEKGLRTNILTQCSHYVSIPGGDKYVDSLNVSVAAGILLYSLVN
Protein: Target of rapamycin complex subunit LST8 (TORC subunit LST8) (G protein beta subunit-like) (Gable) (Protein GbetaL) (Mammalian lethal with SEC13 protein 8) (mLST8) (Q9BVC4)
Organism: Homo sapiens (Human)
Function: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:31601764}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z2K5}. Note=Targeting to lysosomal membrane depends on amino acid availability: mTORC1 is recruited to lysosome membranes via interaction with GTP-bound form of RagA/RRAGA (or RagB/RRAGB) in complex with the GDP-bound form of RagC/RRAGC (or RagD/RRAGD), promoting its mTORC1 recruitment to the lysosomes. {ECO:0000269|PubMed:31601764}.
Interaction partners:
- Proline-rich protein 5
- Rapamycin-insensitive companion of mTOR
- TELO2-interacting protein 1 homolog
- DEP domain-containing mTOR-interacting protein
- Proline-rich protein 5-like
- Serine/threonine-protein kinase mTOR
- GTP-binding protein Rheb
- Regulatory-associated protein of mTOR
- Proline-rich AKT1 substrate 1
- Target of rapamycin complex 2 subunit MAPKAP1
Sequence:
MNTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEVTPDRSMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRWMYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSGNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLG
Protein: Protein EAR1 (Endosomal adapter of RSP5) (Q03212)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane (By similarity).
Subcellular location: Endosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Vacuole membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- GID complex subunit 8
- Uncharacterized protein TRE1
- Metal homeostatis protein BSD2
- Transcriptional regulatory protein SAP30
- GID complex subunit 7
Sequence:
MSFKFLIESLLLGSISGQIRCGRSSVIPRGDVSYGGDDTDELNMDIMLFAFGTLIVVYIVICIVYFFTKQIATRLITAYYNEHGPGQRISLFSDYDENNAHVHSRRLMENMSLRWPNNLDDADEVRDKLAQLSPEEQFYYKQGEEYIKQNPPFLLNQGLLQQSEDSNPDTTREDPIMNEQTRQYIQEEGAYAWEFSPNPDMPNHTVIVENKTEVSFLNYNYDASISTNLPIPCINKVYYCEFKIFETDGPLNSDENVSKGVISFGLSTQPYPYFRLPGRHHHSIAYDSNGARRFNDSFKLNEQLRTLFPQCEKGDIVGIGYRSRSGTVFFTRNGKKLNEKSVGGHIRGWKFQYLYPIIGSNVPCQIHVNFGTYGFVYIEANVKKWGYAKSNGIKLPPPSYEDYGKDTLLESGGEDNDFDEDFSDGDSDNIAAGSTTNLNDDIIIRNGEILPPPPGFEFTMSPPTGKKIINEEINLDSLPMLPPSYSDDEHHSKNDKSAISGRIIGTSRNLITDEASFDSVDNDNEDENDHERDPEQFSEFDDYESRMHGI
Protein: Regulatory protein RsaL (G3XD78)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Acyl-homoserine-lactone synthase
- Transcriptional activator protein LasR
- HTH-type quorum-sensing regulator RhlR
- Quorum-sensing control repressor
- Acyl-homoserine-lactone synthase
- ATP-dependent RNA helicase RhlB
- HTH-type transcriptional regulator VqsM
- Multiple virulence factor regulator MvfR
- Elastase
- cAMP-activated global transcriptional regulator Vfr
Sequence:
MASHERTQPQNMAFRAKATRTARRESQETFWSRFGISQSCGSRFENGENLPFPIYLLLHFYIEGQITDRQLADLRGKIRE
Protein: NADP-dependent mannitol dehydrogenase (MtDH) (EC 1.1.1.138) (Mannitol 2-dehydrogenase [NADP(+)]) (allergen Cla h 8) (P0C0Y5)
Organism: Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum)
Function: Interconverts D-mannitol and D-fructose. Not active with fructose 6-phosphate or NADH.
Interaction partners:
Sequence:
MPGQQATKHESLLDQLSLKGKVVVVTGASGPKGMGIEAARGCAEMGAAVAITYASRAQGAEENVKELEKTYGIKAKAYKCQVDSYESCEKLVKDVVADFGQIDAFIANAGATADSGILDGSVEAWNHVVQVDLNGTFHCAKAVGHHFKERGTGSLVITASMSGHIANFPQEQTSYNVAKAGCIHMARSLANEWRDFARVNSISPGYIDTGLSDFVPKETQQLWHSMIPMGRDGLAKELKGAYVYFASDASTYTTGADLLIDGGYTTR
Protein: FI04408p (Rox8, isoform D) (Rox8, isoform E) (Rox8, isoform G) (Rox8, isoform H) (Q8IMX4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trivet, isoform I
- SD23764p
- Pre-mRNA-processing factor 39
- U1 small nuclear ribonucleoprotein C
- Polyadenylate-binding protein
- TAR DNA-binding protein 43
- Probable small nuclear ribonucleoprotein Sm D2
- RH42690p
- Putative RNA-binding protein Alsin2
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MDESQPKTLYVGNLDSSVSEDLLIALFSTMGPVKSCKIIREPGNDPYAFIEYSNYQAATTALTAMNKRLFLEKEIKVNWATSPGNQPKTDISSHHHIFVGDLSPEIETETLREAFAPFGEISNCRIVRDPHTMKSKGYAFVSFVKKAEAENAIQAMNGQWIGSRSIRTNWSTRKLPPPREPSKGGGQGGGMGGGPGNGSGVKGSQRHTFEEVYNQSSPTNTTVYCGGFPPNVISDDLMHKHFVQFGPIQDVRVFKDKGFSFIKFVTKEAAAHAIEHTHNSEVHGNLVKCFWGKENGGDNSANNLNAAAAAAAASANVAAVAAANAAVAAGAGMPGQMMTQQQIAAATGAAIPGQMMTPQQIAAQYPYAYQQMGYWYPPATYPTTQMQTQYMQQGYYPYAYPTSAQQAGGVPCIQFSAAGYRMVPPNVAWGVPGTVVPGVTAAAASAAAAANGSLAPQMMYSAAMPQYQTQ
Protein: ALK and LTK ligand 2 (Augmentor alpha) (AUG-alpha) (Q6UX46)
Organism: Homo sapiens (Human)
Function: Cytokine that acts as a physiological ligand for receptor tyrosine kinases LTK and ALK, leading to their activation. Cytokine-binding is sufficient to activate LTK. In contrast, ALKAL2-driven activation of ALK is coupled with heparin-binding to ALK. Stimulation of ALK signaling is involved in neural development and regulation of energy expenditure.
Subcellular location: Secreted {ECO:0000269|PubMed:30061385}. Cell membrane {ECO:0000269|PubMed:34819673}. Note=Following interaction with receptor tyrosine kinase ALK, associates with the cell membrane, membrane-binding is required to activate ALK. {ECO:0000269|PubMed:34819673}.
Interaction partners:
- ALK tyrosine kinase receptor
- Leukocyte tyrosine kinase receptor
Sequence:
MRGPGHPLLLGLLLVLGAAGRGRGGAEPREPADGQALLRLVVELVQELRKHHSAEHKGLQLLGRDCALGRAEAAGLGPSPEQRVEIVPRDLRMKDKFLKHLTGPLYFSPKCSKHFHRLYHNTRDCTIPAYYKRCARLLTRLAVSPVCMEDKQ
Protein: Probable phosphatidylglycerophosphatase, mitochondrial (EC 3.1.3.27) (PGP phosphatase) (Q9Y7U3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphatidylglycerophosphatase involved in the biosynthesis of cardiolipin (CL), a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes and which has important functions for cellular energy metabolism, mitochondrial dynamics and the initiation of apoptotic pathways.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Matrix side {ECO:0000269|PubMed:16823372}.
Interaction partners:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Lysophospholipid acyltransferase
- Phosphatidylglycerol phospholipase C
Sequence:
MLINIEGIQAFCQTIRNPRRIIPHATFPTFSQIPCNINYFLEQKFQVPVDIRALVLDKDNCITLPNETTIAEAELKKIREFQNIYGEKNVILLSNSIGTRKLDPTGELAAHFQQKWNIPVVRHSKLKPLCTEELYTYLSNNSHVSSASQILFIGDRLLTDITLANIMGSWGVWLTRGVGNTTNMMMEVESWLYKRIHTQNPYIPTNRKS
Protein: Boron transporter 4 (Q9XI23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Efflux-type boron transporter polarly localized in roots. Boron is essential for maintaining the integrity of plants cell walls.
Subcellular location: Membrane {ECO:0000269|PubMed:18048682}; Multi-pass membrane protein {ECO:0000269|PubMed:18048682}.
Interaction partners:
- Probable aquaporin NIP5-1
- Aquaporin NIP6-1
- Probable aquaporin NIP7-1
- Katanin p60 ATPase-containing subunit A1
- peptidylprolyl isomerase
- E3 ubiquitin-protein ligase ORTHRUS 2
- Ribosome assembly factor mrt4
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Probable aquaporin TIP5-1
Sequence:
MEEERVDSSKRLFRGIVADLRGRALCYKEDWVAGLRSGFGILAPTTYIFFASALPVIAFGEQLSRDTEGALSTVETLASTALCGVIHSILGGQPLLILGVAEPTVLMYVYLYNFAIGRPELGKQLYLAWAAWVCVWTALLLFVMAILNTADIINRFTRVAGELFGMLISVLFIQQAIKGMVSEFGMPKDEDSKLEKYKFEWLYTNGLLGLIFTFGLLYTALKSRKARSWRYGTGWYRSFIADYGVPLMVVVWTALSFSTPSKLPSGVPRRLFSPLPWDSPSLSHWTVIKDMGKVSPGYIFAAFIPALMIAGLYFFDHSVASQLAQQKEFNLKKPSAYHYDILLLGFMTLICGLLGLPPSNGVLPQSPMHTKSLAVLKRQLIRRKMVKTAKESIRKRETSSQVYENMQEVFIEMDKSPLAQTDPSVIIELQDLKEAVMKSNDEEREGDEESGFDPEKHLDAYLPVRVNEQRVSNLLQSLLVAGAVLAMPAIKLIPTSILWGYFAYMAIDSLPGNQFFERLTLLFVPTSRRFKVLEGAHASFVEKVPYKSMAAFTLLQIFYFGLCYGVTWIPVAGIMFPVPFFLLIAIRQYILPKLFNPAHLRELDAAEYEEIPGTPRNPLELSFRSNDSKRGVQEGDAEILDELTTSRGELKVRTLNLNEDKGNQIYPKEKVKAGDGDMSTTRE
Protein: Mas-related G-protein coupled receptor member E (Q7TN40)
Organism: Rattus norvegicus (Rat)
Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSLRVHTHSPSTQGDMAFNLTILSLTELLSLGGLLGNGVALWLLNQNVYRNPFSIYLLDVACADLIFLCCHMVAIIPELLQDQLNFPEFVHISLIMLRFFCYIVGLSLLVAISTEQCLATLFPSGYLCRRPRYLTTCVCAFIWVLCLLLDLLLSGACTQFFGAPSYHLCGMLWLVVAVLLAALCCTMCVTSLLLLLRVERGPERHQPRGFPTLVLLVILLFLFCGLPFGIFWLSKNLSWHTPLYFYHFSFFMASVHSAAKPAIYFFLGSTPGQRFQEPLRLVLQRALGDEAELGAVREASQGGLVDMTV
Protein: Alpha-dioxygenase 2 (Alpha DOX2) (EC 1.14.99.-) (Fatty acid dioxygenase AlphaDOX2) (Q9C9U3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Alpha-dioxygenase that catalyzes the primary oxygenation of fatty acids into oxylipins. May be involved in the senescence process.
Interaction partners:
- Lipoxygenase 2, chloroplastic
- Lipoxygenase 3, chloroplastic
- Lipoxygenase 6, chloroplastic
- Lipoxygenase 4, chloroplastic
- Triacylglycerol lipase SDP1
- Alpha-dioxygenase 1
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase A
- Triacylglycerol lipase SDP1L
- Phospholipase A2-alpha
Sequence:
MGFSPSSSWFLHPQLHHVVSKMSYFDAFLFYIVHLVDKLGLWHRFPVLLGVAYLGLRRHLHQRYNLVHVGPINGQGYDTDEFCYRTADGKCNHPSDNTIGSQGSFIGRNMPPSTSQYGILDPHPSVVATKLLARKRFIDNGDQFNVIACSWIQFMIHDWVDHLEDTHQIELEAPEEVASGCPLKSFKFLRTKKVPTDDHHKSGAVNTRTPWWDGSVIYGNDETGMRRVRVFKDGKLKISGDGLLERDERGVPISGDIRNSWSGFSLLQALFVKEHNSVCDMLKERYPDFDDEKLYRTARLVTAAVIAKVHTIDWTIELLKTDTLTAGMRINWYGFFGKKVKDMVGARFGPLFSGLVGLKKPNDHGVPYSLTEEFVSVYRMHCLLPETLILRDMNSENVDKENPAIEREIPMTELIGKKAGEKASKLGFEQLLVSMGHQSCGALTLWNYPNWMRNLVAQDIDGEDRPHLIDMAALEIYRDRERGVPRYNEFRKNLLMSPISKWEELTDDEEAIKVLREVYEDDIEKLDLNVGLHAEKKIKGFAISETAFFIFLLVASRRLEADRFFTTNFNEKTYTKEGLEWVNTTETLKDVIDRHFPRLTDQWMRCSSAFSVWGSDPNPKNWVPLYLRSAP
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g53420 (EC 2.7.11.1) (C0LGG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- AT4g00280 protein
- Kinase-like protein
- Interleukin-1 receptor-associated kinase 4 protein
Sequence:
MSLNRFLFTSFSFFLFFIVHFASSATLPTQEGEAFKVVLTTLKKTNIDLNVDPCEVSSTGNEWSTISRNLKRENLQGSLPKELVGLPLLQEIDLSRNYLNGSIPPEWGVLPLVNIWLLGNRLTGPIPKEFGNITTLTSLVLEANQLSGELPLELGNLPNIQQMILSSNNFNGEIPSTFAKLTTLRDFRVSDNQLSGTIPDFIQKWTKLERLFIQASGLVGPIPIAIASLVELKDLRISDLNGPESPFPQLRNIKKMETLILRNCNLTGDLPDYLGKITSFKFLDLSFNKLSGAIPNTYINLRDGGYIYFTGNMLNGSVPDWMVNKGYKIDLSYNNFSVDPTNAVCKYNNVLSCMRNYQCPKTFNALHINCGGDEMSINGTIYESDKYDRLESWYESRNGWFSNNVGVFVDDKHVPERVTIESNSSELNVVDFGLYTQARISAISLTYYALCLENGNYNVNLHFAEIMFNGNNNYQSLGRRFFDIYIQRKLEVKDFNIAKEAKDVGNVVIKTFPVEIKDGKLEIRLYWAGRGTTVIPKERVYGPLISAISVDSSVNPSPRNGMSTGTLHTLVVILSIFIVFLVFGTLWKKGYLRSKSQMEKDFKSLELMIASFSLRQIKIATNNFDSANRIGEGGFGPVYKGKLFDGTIIAVKQLSTGSKQGNREFLNEIGMISALHHPNLVKLYGCCVEGGQLLLVYEFVENNSLARALFGPQETQLRLDWPTRRKICIGVARGLAYLHEESRLKIVHRDIKATNVLLDKQLNPKISDFGLAKLDEEDSTHISTRIAGTFGYMAPEYAMRGHLTDKADVYSFGIVALEIVHGRSNKIERSKNNTFYLIDWVEVLREKNNLLELVDPRLGSEYNREEAMTMIQIAIMCTSSEPCERPSMSEVVKMLEGKKMVEVEKLEEASVHRETKRLENMNTMKKYYEMIGQEISTSMSMIMSDRSESSADH
Protein: Zinc transporter ZIP4 (Activated in W/Wv mouse stomach 2) (mAWMS2) (Solute carrier family 39 member 4) (Zrt- and Irt-like protein 4) (ZIP-4) (Q78IQ7)
Organism: Mus musculus (Mouse)
Function: Plays an important role in cellular zinc homeostasis as a zinc transporter. Regulated in response to zinc availability.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14612438, ECO:0000269|PubMed:14709598, ECO:0000269|PubMed:18020946, ECO:0000269|PubMed:30593504}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Recycling endosome membrane {ECO:0000269|PubMed:14612438}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Apical cell membrane {ECO:0000269|PubMed:12801924, ECO:0000269|PubMed:18020946, ECO:0000269|PubMed:18936158}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Note=Colocalized with TFRC in the recycling endosomes. Cycles between endosomal compartments and the plasma membrane in response to Zn(2+) availability. Zn(2+) deficiency promotes accumulation of SLC39A4 on the surface membrane, whereas high extracellular Zn(2+) levels induce internalization of SLC39A4, but also trigger drastic removal of cellular SLC39A4 via proteasomal and lysosomal degradation pathways (PubMed:14612438, PubMed:18020946, PubMed:30593504). Translocates to the apical membrane during zinc deficiency (PubMed:12801924, PubMed:18020946). Expressed on the apical surface of the intestinal wall (PubMed:18936158). {ECO:0000269|PubMed:12801924, ECO:0000269|PubMed:14612438, ECO:0000269|PubMed:18020946, ECO:0000269|PubMed:18936158, ECO:0000269|PubMed:30593504}.
Interaction partners:
- Zinc transporter ZIP3
- Zinc transporter ZIP1
- Zinc transporter ZIP2
- Probable proton-coupled zinc antiporter SLC30A4
- Proton-coupled zinc antiporter SLC30A2
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A1
- Zinc transporter ZIP11
- Zinc transporter 6
- Proton-coupled zinc antiporter SLC30A5
Sequence:
MLPKSVTQGLVLALLVGTVAVARPRNLLSLLALGQGALDRLELDGLLNTLVARVHCTDGPCEKCLSVENVLALGKPDKPQPAPESVLESRHIIYLSAAAALYLNNPEKTCKDIQAGLLASHVDDYLATLESPEAMTLGLSQLLQKIEAHAASQPTGEKTCVDLPQLLEEAEAAGVSKSAGLVLTALLDHVINGSCFQGLPSPQYFVDFVFRLHSSDPPNITLHELENLMHHLGVGGEDHSDHDDHGDHADHSHPDRKASHQDSELHTPHNSNSSVWDTLCLSAKDIMAVYGLSEEAGVSPQAWAQLTPALVQQQLSGACSPYPTIRIQDQLSQTERYLYGSLATLLICLCAVFGLLLLTCAKCSTATHYIMQTFLSLAVGALTGDALLHLIPKVLGLHTHGGEGHTHEEEVGVGGQATWRLLAVLGGFYIFFLFESFFNLLLPRDQDSEKDGPCSHGGHSHGISLQLAPSNLRQSKQTHESSRSDLVAEETPELLNPETRRLRAELRLLPYLITLGDAVHNFADGLAVGAAFSSSWKTGLATSLAVFCHELPHELGDFAALLHAGLSVKRALLLNLASALTAFAGLYVALAVGVGEEGEAWILAVATGLFLYVALCDMLPAMMNVRDQRPWLLFLLHNVGLLGGWTVLLLLSLYEDNITF