wanglab/gogpt-training-data huggingface dataset:
Protein: Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (Lysophosphatidylinositol acyltransferase) (LPIAT) (Lyso-PI acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 7) (MBOA-7) (Q19468)
Organism: Caenorhabditis elegans
Function: Acyltransferase which mediates the conversion of lysophosphatidylinositol (1-acyl-sn-glycero-3-phosphatidylinositol or LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) (LPIAT activity). Prefers sn-2-LPI rather than sn-1-LPI as the acyl acceptor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Involved in the selective incorporation of arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA) and (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA (EPA-CoA) into PI. Besides its role in biomembranes, PI is a precursor of PI 3-phosphate (PIP3) and its fatty acid composition has an important role in PI3P signaling.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholipid/glycerol acyltransferase domain-containing protein
- Phospholipid/glycerol acyltransferase domain-containing protein
- Lysophosphatidylinositol acyltransferase 10
- O-acyltransferase
- O-acyltransferase
- Zrt
- Transmembrane 9 superfamily member
- Uncharacterized protein K12H4.5
- Transmembrane 9 superfamily member
- Zinc transporter zipt-7.2
Sequence:
MENILGLMSKDDWIYTGLLLFSFGASCYVRKIGNNILASGALGFAMSLFIIGPKIVYSLGICSIAISIQLLANKKSTPLYVFLTTFTYLMFVRFAHYILPVNEVASHTNVIQLIITLRIIGITFEENDAWVHKSDENPTKRYLTELPTILEKFAYFYHFCGLFTGPYYTYQMLIDSQNPILKSWDPTLEVKSRFVRLLWSVPVFVITNHYFPLDILRSDAIWEVSFFTRLVYAALIFVVFKTRVYSAWAIAESICVILGIGIYPAASNPKIIMGPTDLNAFDKLKTRENIEMSSDAIVNLDIPKVEFSDGFRDGMKAWNRSVQTWLALYVHSRVKVMRVETTMLVSAVWHGTYAGYFMSFGVVAMCAILEDVIFKLVPVDTETGVRPKWFRILYTHTIRCRGFEMLATGFLLKNAYDVHHFWSSIYYWLPLLCIPFYIYSAKISKPKKAQKSE
Protein: Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Fragilis protein 2) (Mouse ifitm-like protein 2) (Mil-2) (Q9D103)
Organism: Mus musculus (Mouse)
Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16326387}; Single-pass membrane protein {ECO:0000269|PubMed:16326387}. Lysosome membrane {ECO:0000250|UniProtKB:P13164}.
Interaction partners:
- CD81 antigen
- B-lymphocyte antigen CD19
- Ubiquitin-like protein ISG15
- Antiviral innate immune response effector IFIT1
- Interferon-induced protein with tetratricopeptide repeats 3
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced 35 kDa protein homolog
Sequence:
MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR
Protein: Small ribosomal subunit protein eS4C (40S ribosomal protein S4-C) (Q9P4W9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein uL3A
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18A
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein uL4B
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL3B
Sequence:
MVRGPKKHLKRVAAPHHWLLDKLSGTYAPKPSPGPHKARECLPLIVFLRNRLKYALNGREVKAILMQRLIKVDGKVRTDSTFPTGFMDVISVDKTGEHFRLVYDIKGRFTVHRITAEEAKYKLCKVKRVQLGAKGVPFLVTHDGRTIRYPDPLIKVNDTIKLNLETNKIESFIKFDTSAQVMVTGGRNMGRVGTIVHREHHLGSFEIIHVKDALDREFATRLSNVFVIGETGKSWISLPKGKGVKLSITEERDRRRALKGLA
Protein: Nucleoporin (A0A1D8PD79)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phm7p
Sequence:
MAEEKKAGGGDSAAAAPAIKFDQDKLLKTVQTLQFGWFVGNVLTLLGFFLFTLSYFGILPDVGFVWYLISLLGALISFGILLVQFIQKNGFKVPLLIKDDNFHYFLLAFFLIAMRAYVWITLVPFVIFSSFHVLNYVNTHLLPIVGLDGNNPISKHITAFVNKNNLASIQIASGIELLTVVWLFLRMITFRKRSLTPFLVFLVFLKKRHEVSPFTRKYFDFFAAQGDSIVSTINNPVINDVWGHVKTAFRTIDSFKLVHDRTKDEDKAK
Protein: Bublin coiled-coil protein (UPF0184 protein C9orf16 homolog) (P58686)
Organism: Mus musculus (Mouse)
Function: Essential for intermediate filament organization in intestinal cells, interacts with intermediate filament and regulates intestinal lumen morphology.
Subcellular location: Cell junction {ECO:0000269|PubMed:33857431}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33857431}. Note=In the intestine, localizes subapically and at cell junctions. Interacts with intermediate filament (IF) proteins and localizes to the IF network in an IF-dependent manner (By similarity) (PubMed:33857431). In dividing cells, localizes to interpolar and kinetochore microtubules (By similarity). {ECO:0000250|UniProtKB:Q9BUW7, ECO:0000269|PubMed:33857431}.
Interaction partners:
- Mitochondrial transcription rescue factor 1
Sequence:
MSGPNGDLGMPVDAGTEGENDSFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPGDASP
Protein: Insulin gene enhancer protein isl-1 (Islet-1) (P53405)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA-binding transcriptional activator. Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. May be involved in subtype specialization of primary motoneurons. May bind to insulin gene enhancer sequences. Essential for heart development (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P61372}.
Interaction partners:
- NK2 homeobox 5.
- Paired box protein Pax-6
- LIM/homeobox protein Lhx3
- GATA-binding protein 4.
- Neurogenic differentiation factor 1
- T-box transcription factor TBX5-A
- Homeobox protein Nkx-2.2a
- Homeobox protein HB9
- POU domain protein
- Myocyte enhancer factor 2ca
Sequence:
MGDMGDPPKKKRLISLCVGCGNQIHDQYILRVSPDLEWHAACLKCAECNQYLDESCTCFVRDGKTYCKRDYIRLYGIKCAKCNIGFSKNDFVMRARSKVYHIECFRCVACSRQLIPGDEFALREDGLFCRADHDVVERATMGAGDPLSPLHPARPLQMAAEPISARQPALRPHVHKQPEKTTRVRTVLNEKQLHTLRTCYNANPRPDALMKEQLVEMTGLSPRVIRVWFQNKRCKDKKRSILMKQLQQQQPNDKTNIQGMTGTPMVATSPERHDGGLQANQVEVQSYQPPWKVLSDFALQSDIDQPAFQQLVNFSEGGPGSNSTGSEVASMSSQLPDTPNSMVASPIEA
Protein: Retinoid X nuclear receptor beta (Retinoid X receptor beta isoform 1) (Retinoid X receptor, beta) (Q5STP9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQTPEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPPPPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVKPPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYSCRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMPVDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYPEQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA
Protein: FMRF-Like Peptide (Q95QP2)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptors family 1 profile domain-containing protein
- FMRF-Like Peptide
- FMRF-Like Peptide
- FMRF-Like Peptide
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 9
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptides 2
- FMRFamide-like neuropeptides 1
Sequence:
MLGYTQSRVVITLLLFSVFLAVCMATPSGYPGQELQNVSDDYPIYEEEGLQLSAEGTDEPHEEKRAVFRMGKRAMMRFGKRAMMRFGKRSVFRLG
Protein: Microtubule-associated protein 70-2 (AtMAP70-2) (70 kDa microtubule-associated protein 2) (Q8L7S4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific protein that interact with microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated to microtubules.
Interaction partners:
Sequence:
MSDVSGDGDLSATVTEHEVTPQPPVSSATYPSLTVSASYKESSGGKSSSKRRPIRPSFDAAADNEFITLLHGSDPVKVELNRLENEVRDKDRELGEANAEIKALRLSERQREKAVEELTEELTKLDEKLKLTESILESKNLEIKKINEEKKASMAAQFAAEATLRRVHAAQKDDDMPPIEAILAPLEAELKLARSEIGKLQEDNRALDRLTKSKEAALLEAERTVEAAMAKAAMVDDLQNKNQELMKQIEICQEENKILDRMHRQKVAEVEKLTQTVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKTLDRELARAKVTANRVATVVANEWKDGNDKVMPVKQWLEERRFLQGEMQQLRDKLAITDRAAKSEAQLKEKFQLRLKVLEETLRGTSSSATRNTPEARSMSNGPSRRQSLGGAENLQKFTSNGALSKKAPASQMRHSLSINSTSVLKNAKGTSKSFDGGTRSVDRGKALLNGPGNYSFNKATDDSKEAESGNGWKENSEEKPQSEDPEAATEDSVPGVLYDLLQKEVVSLRKASNEKDQSLKDKDDAIEMLAKKVETLTKAMEVEAKKMRREVAAMEKEVAAMRVEKDQDARAKRFSNSKSPSNTAQILAGRAAGRSGGLTKSTQ
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q381C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar protein, putative
- NLE domain-containing protein
- Ribosome biogenesis protein BOP1 homolog
- rRNA processing protein, putative
- Pescadillo homolog
- Nucleolar GTP-binding protein 1
- 60S ribosomal protein L24, putative
- CCAAT-binding factor domain-containing protein
- Nucleolar complex protein 2
- RNA-binding protein, putative
Sequence:
MRCCVRALWRSEKRLPRRFREVPEEFTDFRSSDCRPLVFTPRRPEPLRDVSLSDVKIDESALQSTPLQELWQRPVATLDPERMGLPPYLVEYLHRRFEQLREGESPSEVHKCGFEGLTVVQARALQHFYARQDVALCAPTGTGKTFALCLALIARLMRDGPMKLFSVLFLAQNDNLCMQIARWMREMWWYKDDDRLVFTATSDVPPGVVYRRLTRELIRDGAGNVVKAVDRRPYVCVATPEVFWNFFRRHKEALEKRDASRGRKRRSFNRTPALPSLDLIVVDEVDDVLPSTSPNAAGNLLMKELYRFTKYQAPVQLVFTSATLAGSTVNHVRRFLKKNILESRTSRIFESEIQSFSQKVATTGNTSKVSVPANIQHLFYTADTLAEQRECVAVAMKQSNSTCCHSYDEGKILVILPESASRELFVREVLKPAFAGDAVEPEITRDDVPSCSPLRCSGQVNDTESSTRGKTLAPRGRKIIISGSSSVRGLDISGLTHVLMLATPRSSAEYAHWCGRVGRFGEHGVSVVILSRFAVREVSAFCEVLNIPFKVQRRYAAVDVDAERRSFGS
Protein: Diablo IAP-binding mitochondrial protein (Diablo homolog, mitochondrial) (Direct IAP-binding protein with low pI) (Second mitochondria-derived activator of caspases) (SMAC) [Cleaved into: Diablo IAP-binding mitochondrial protein, cleaved form] (Q9NR28)
Organism: Homo sapiens (Human)
Function: Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10972280, ECO:0000269|PubMed:14523016, ECO:0000269|PubMed:28288130}. Cytoplasm, cytosol {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:28288130}. Note=Released into the cytosol in a PARL-dependent manner when cells undergo apoptosis. {ECO:0000269|PubMed:10929711, ECO:0000269|PubMed:28288130}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Baculoviral IAP repeat-containing protein 2
- Baculoviral IAP repeat-containing protein 3
- Cytochrome c
- Apoptotic protease-activating factor 1
- Caspase-9
- Baculoviral IAP repeat-containing protein 7
- Serine protease HTRA2, mitochondrial
- Caspase-7
- Caspase-3
Sequence:
MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED
Protein: Cell adhesion molecule CEACAM19 (Carcinoembryonic antigen-like 1) (Carcinoembryonic antigen-related cell adhesion molecule 19) (CEA cell adhesion molecule 19) (Q7Z692)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cell adhesion molecule CEACAM18
- Cell adhesion molecule CEACAM20
Sequence:
MEIPMGTQGCFSKSLLLSASILVLWMLQGSQAALYIQKIPEQPQKNQDLLLSVQGVPDTFQDFNWYLGEETYGGTRLFTYIPGIQRPQRDGSAMGQRDIVGFPNGSMLLRRAQPTDSGTYQVAITINSEWTMKAKTEVQVAEKNKELPSTHLPTNAGILAATIIGSLAAGALLISCIAYLLVTRNWRGQSHRLPAPRGQGSLSILCSAVSPVPSVTPSTWMATTEKPELGPAHDAGDNNIYEVMPSPVLLVSPISDTRSINPARPLPTPPHLQAEPENHQYQQDLLNPDPAPYCQLVPTS
Protein: Lytic murein transglycosylase (Q9HX28)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Membrane-bound lytic murein transglycosylase F
- Probable glycosylase
- N-acetylmuramoyl-L-alanine amidase
Sequence:
MRNPERSALLKVSGLLGSTVVAMGLGLSSACAQKNPTVEYNQPAAPLQTKAPFSGAGPAASVPAGAPNEAQPGQSFEQWRDAFRQQALAGGIDAQTFDRAFAGVQPDPAVVEADRSQPEFTRPVWKYLEGALDPLRVRQGQARLAQHARILGEVDARYAVDADAVVAIWGMESNYGSHMGNKNVIRSLATLAYEGRRPEFAHAQLLAALKILQHGDVPASFMIGSWAGAMGQTQFIPTTHNQYAVDFDGDGKRDIWGSPGDALASTANYLKASGWIAGQPWGFEVRLPAGFDYSLAELTIRKPLGEWQGMGVQGVNGGPLPSGLSGEQASLLLPAGHRGPAFLVLHNFRAILKYNNSSAYALAVGLLADSFKGGGRIVGAWPLEDVPLSRSQRIELQRQLAARGHDPGAVDGIIGANTRKAIRACQQEFGWPADGYPTPALLDRLRTP
Protein: Homeobox protein SIX6b (SIX homeobox 6b) (Sine oculis-related homeobox 6b) (Q5TYZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Retinal homeobox protein Rx2
Sequence:
MFQLPILNFSPQQVAGVCETLEESGDIERLGRFLWSLPVAPAACEVLNRNESVLRARAIVAFHTGNFRELYHILENHKFTKESHSKLQALWLESHYQEAEKLRGRPLGPVDKYRVRKKFPLPKTIWDGEQKTHCFKERTRHLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQQQVLSNGSVRSLSGEDGAVDRLGNASSPEASLSSKAAASAISITSSDSECDI
Protein: Glutamine synthetase (EC 6.3.1.2) (A8WCU3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ferredoxin--nitrite reductase, chloroplastic
- glutamate synthase
- glutamate synthase
- glutamate synthase
- glutamate dehydrogenase
- Glutamate--glyoxylate aminotransferase 2
- Glutamate dehydrogenase
- glutamine--fructose-6-phosphate transaminase
- glutamine--fructose-6-phosphate transaminase
- glutamine--fructose-6-phosphate transaminase
Sequence:
MSLLTDLVNLNLSDCTDKIIAEYIWIGGSGMDLRSKARTLSGPVSDPSKLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRCNAAKIFSHPDVAAEEPWYGIEQEYTLLQKDVKWPIGWPLGGYPGPQGPYYCGVGVDKAYGRDIVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAGDELWVARYILERITEIAGVVLSFDPKPIQGDWNGAGAHTNYSTKSMRSDGGYEVIKKAIAKLGLRHKEHIAAYGEGNERRLTGRHETADINTFLWGVANRGASIRVGRDTEKAGKGYFEDRRPASNMDPYVVTSMIAETTILWKP
Protein: Uncharacterized protein (Q5AXA3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MLYNEAHPGHRARDELCLGWASRYDGYGNTKSATSQRLRFNWKMPALMLICFIIGLFLAVVHHLYYQLLNNTVIHTKSQQTWANRIGTGLVFLIKTFLAAAVGIVCTQVLWWSLRSRSIEVSTLDSLFDLRNNILSFLNPLVYDIRLIPIIAVFTPSALSVQSSIASTVSPMSIPSILWNAKLFAGWNGRLVNGQPISAWASVKPNITRVVTATAVHGFVLSLSAPAVNSSYTLNFHGPSLQCTNSTSLHHAVVEYYNEYGAEAGDPWSPPDMEQQYFSKLDETSTDSAKIVFAIFASGGPYTFTFTNGIQDLETIPQC
Protein: Rhomboid-type serine protease 2 (EC 3.4.21.105) (Golgi rhomboid protease rbd2) (Rhomboid protein 2) (O74926)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable serine protease.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:27655872}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 48
- Sterol regulatory element-binding protein 1
- Uncharacterized protein C13E7.11
- UBX domain-containing protein 10
- Sterol regulatory element-binding protein cleavage-activating protein
- Putative transcription factor sre2
- Large ribosomal subunit protein uL30C
Sequence:
MIFMILGRSKEFILKLPIWTQIITYIAILVYALSFFGISTGVLSLSWIGLLQKRQLYEIITYVTLHLSMLHIVFNFVSLLPAMSQFEKKQGTLACILVTVIPYTLFPGIMHLIVYHFFLRKDYVSIAGLSGWAFAFISASCVHSPQRLISFFNLFSIPAYCFPIIYLIMTTILVPKASFIGHASGAVMGYCTPFMLGSIPLKSWAQNVDPIFQSWVKNYHSFDQLSHAQLPIAEPLSTFSSFPGKGTRLGG
Protein: No mechanoreceptor potential A, isoform A (No mechanoreceptor potential A, isoform B) (A1Z8J4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRPRKGIHVLLTTLVVSLSLSKINGQTTCKNGLGRVLYERLPNQQLQGYDDDVVRDTAPPFRVLEKCQDLCLRDRSGSNNLVRTCTSFDFQPGSRITSFGGNSEYEESLCYLTSEQAGPEGIGSLMLVPNSVHFNEICLTSSRPERECPSRRYVFERHPRKKLKLPISDIKEITAANRSDCEDKCLNEFSFVCRSANFDSTMRSCTLSRFTRRTHPELMEDDPNSDYLENTCLNAERRCDGLAVFVKEENKRLGGPFEVDIFNNMTLEECQTMCLRAEKYFCRSVEFDDQSKQCILSEEDSISQKDDISISSSPTHHFYDLVCLDNQRANDYPDNSVTSHLFSSGRRPDTAFQRYRNSRLGGEFHSEITGRSLSECLDECLRQTSFQCRSAVYSDRFRTCRLSRYNQKDGMRIIYDADYDYYENLMLNVVGGGADGDGGGHGGSSDGKRPGDQSGSNWRQPNKHDDRYGSGGSSVGGGSHGGTGSGGSRLPPGEGVDYGRPYDRYPDIAGNEYDRNPYGGDRDRDRYPPDRYGSRYPTGGDGIGYNRPYDRFPDDYDRYPAGAGVNGDRDRERDRDRYPVVGDRDRYPGAVDRDRYPGVRDRDRYPEPYPPERYADRYGDRRYPERERDRDRDRLPYRPLPYPGINDNSLPSDLPHTRPYPTDDDAPFRPYGYGGGRYGENRYEGRYPPRFPPSRERDPVGGYTGRDAPDSIFPDRRYRPSSMDSPRYPYLPDSRGPPGRYDDIVHSARRPEPDSAKRYPPAPIAPTGSSSKYASTPNRFPVGNDRYPIDIYKYGNRPGPNDLGRRPGLERPPPPFYDYDYEERYGDRYGPYDREYDGPPGRRPPSGGPYGRYDSPFNRPYGGNGLDDRPLPLPGLGLSHPPTPYGGGGAGHVGVGVGVNSGPPRPPITRCEESDNFKQIAARHKMRRHFVRRALIVPSLIQCERECIESRDFVCRSFNYRDSAASGYEDRDRDRDRDSPNCELSDRDSRELDIHDPGTFDASNYDFYERSIGRSDGECMDVTQTCNEEGMEFTIRTPEGFLGRIYTYGFYDRCFFRGNGGTVNVLRLSGPQGYPDCGTQRYGDTLTNIVVVQFSDNVQTSRDKRYNLTCIFRGPGEAVVSSGYIGAGSGSPIPIEYLPAENTLSSKVRLSILYQGRPTTTIAVGDPLTFRLEAQDGYNHVTDIFATNVVARDPYSGRSIQLIDRFGCPVDPFVFPELDKLRDGDTLEARFNAFKIPESNFLVFEATVRSCREGCQPAYCPGPAGRQEPSFGRRRRSLNTTEIPEPEALALEGSSQLEASTLDEVTVVNSTTVSATLGQVPLNETQLGEKTKETEEPEQVREMIEVFETREEIEKESYPRKLVAPVETVCMTPAEYHGLITAIILLMILLFSITLVAGLGYRRYWKSISKNRLVDRHSPIHSLGHSHSSIRTHERFTEIGHMPNLNGGGGGAAAGTGGGANQSASNRASNAFRTNMSMFGGSLHKTFATGNLARMCQLPVINPMRSTNQSSHQFEDPSEPIYTDPSLFERSRQVADHSVTHPQNEFPTTVRNYRCEV
Protein: U1 SNP1-associating protein 1 (Q03714)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1 and in HRD1 autoubiquitination and degradation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19898607}; Multi-pass membrane protein {ECO:0000269|PubMed:19898607}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Protein OS-9 homolog
- Cell division control protein 48
- UBX domain-containing protein 2
- DER1-like family member protein 1
- Degradation in the endoplasmic reticulum protein 1
- ER-derived vesicles protein ERV41
- Coupling of ubiquitin conjugation to ER degradation protein 1
- ERAD-associated E3 ubiquitin-protein ligase DOA10
Sequence:
MSEYLAQTPCKFTIWSSEIDLIRTNLLVNAHPLSTVGRLLQYIHYQIYKQLRAIYQPEEQCTNSEIPHTPLNSINTYFLSYEGRELSATCLLKDITSSSHPDSNHFIRLQLEKRTSPSGSAFDLEYDMEGEFNSMNIQFEINTLSSQRIFNSMEPNLPIGTTLARLEKLALERIKDFEKSAGNLCGIKEDHSVSDLQGFIIKGKQTPMFLNYGSDSDYYKDLNLVDLIGIDFAPAHNSFFTFLFKMNHEQNSHIANDEERFVLEFISDATLSITQMNVKPDTTVKQVKDFICSVYTHSLNLRRNDIKLIYKGQLLHENNFAGNSSKISEYIKEPHEVKVHVQINQEYTESGPGFWNEVFNNPNIFQFMPPDTRSQSPVSFAPTQGRSPAAIRGEERGIPYVTESGNDIVPTDELYRKCIINGDEVVFIPVSELNPQSSYLSVIKGDYGEIKIPISSNDYRINGDNILLSPSAIEQLESALNFKIERPRDSTLLHPSGEHVRAADNTSSANDNNTVENDESAWNRRVVRPLRNSFPLLLVLIRTFYLIGYNSLVPFFIILEFGSFLPWKYIILLSLLFIFRTVWNTQEVWNLWRDYLHLNEIDEVKFSQIKEFINSNSLTLNFYKKCKDTQSAIDLLMIPNLHEQRLSVYSKYDIEYDTNTPDVGQLNLLFIKVLSGEIPKDALDELFKEFFELYETTRNMNTLYPQDSLNELLLMIWKESQKKDINTLPKYRRWFQTLCSQIAEHNVLDVVLRYIIPDPVNDRVITAVIKNFVLFWVTLLPYVKEKLDDIVAQRARDREQPAPSAQQQENEDEALIIPDEEEPTATGAQPHLYIPDED
Protein: Protein NRT1/ PTR FAMILY 6.3 (AtNPF6.3) (Nitrate transporter 1.1) (AtNRT1) (Nitrate/chlorate transporter) (Protein CHLORINA 1) (Q05085)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dual affinity nitrate transporter. Involved in proton-dependent nitrate uptake and in the regulation of the nitrate transporter NRT2.1. Acts also as a nitrate sensor that trigger a specific signaling pathway stimulating lateral root growth and seed germination. The uptake activity is not required for sensor function. Displays an auxin transport facilitation inhibited by high nitrate concentration. Required to prevent auxin accumulation in preemerged lateral root primordia and young lateral roots when external nitrate concentration is low or null. May be involved in the basipetal transport of auxin out of the lateral root tips. Acts as a bidirectional transporter involved in root-to-shoot nitrate translocation. Recognizes specifically nitrate and chlorate, but not nitrite, alanine, sulfate, phosphate or the di-peptide Ala-Ala.
Subcellular location: Membrane {ECO:0000269|PubMed:20627075}; Multi-pass membrane protein {ECO:0000269|PubMed:20627075}.
Interaction partners:
- High-affinity nitrate transporter 2.1
- CBL-interacting serine/threonine-protein kinase 23
- High affinity nitrate transporter
- Protein NLP7
- High affinity nitrate transporter 2.4
- Ferredoxin--nitrite reductase, chloroplastic
- Nitrate reductase 1
- Nitrate reductase 2
- High-affinity nitrate transporter 3.1
- High-affinity nitrate transporter 2.2
Sequence:
MSLPETKSDDILLDAWDFQGRPADRSKTGGWASAAMILCIEAVERLTTLGIGVNLVTYLTGTMHLGNATAANTVTNFLGTSFMLCLLGGFIADTFLGRYLTIAIFAAIQATGVSILTLSTIIPGLRPPRCNPTTSSHCEQASGIQLTVLYLALYLTALGTGGVKASVSGFGSDQFDETEPKERSKMTYFFNRFFFCINVGSLLAVTVLVYVQDDVGRKWGYGICAFAIVLALSVFLAGTNRYRFKKLIGSPMTQVAAVIVAAWRNRKLELPADPSYLYDVDDIIAAEGSMKGKQKLPHTEQFRSLDKAAIRDQEAGVTSNVFNKWTLSTLTDVEEVKQIVRMLPIWATCILFWTVHAQLTTLSVAQSETLDRSIGSFEIPPASMAVFYVGGLLLTTAVYDRVAIRLCKKLFNYPHGLRPLQRIGLGLFFGSMAMAVAALVELKRLRTAHAHGPTVKTLPLGFYLLIPQYLIVGIGEALIYTGQLDFFLRECPKGMKGMSTGLLLSTLALGFFFSSVLVTIVEKFTGKAHPWIADDLNKGRLYNFYWLVAVLVALNFLIFLVFSKWYVYKEKRLAEVGIELDDEPSIPMGH
Protein: Precursor of secreted transmembrane peptide 7 (Phytocytokine STMP7) (Secreted transmembrane peptide 7) (Q6DBB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of STMP7 accumulates at the plasma membrane and is proteolytically cleaved to release the STMP7 in the apoplasm. {ECO:0000269|PubMed:31001913}.
Interaction partners:
Sequence:
MGSKTSTNMVALLLSLLILIFTLSSQVKVVEATSRKLANGRPIVWTPASRSCGASHASWKKNNGPCKRPPRTAPASYNSP