wanglab/gogpt-training-data huggingface dataset:
Protein: PDZ and LIM domain protein 5 (Enigma homolog) (Enigma-like PDZ and LIM domains protein) (Q62920)
Organism: Rattus norvegicus (Rat)
Function: May play an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May be required to restrain postsynaptic growth of excitatory synapses. Isoform 1, but not isoform 2, expression favors spine thinning and elongation.
Subcellular location: [Isoform 1]: Postsynaptic density {ECO:0000269|PubMed:19900557}. Presynapse {ECO:0000269|PubMed:19900557}. Postsynapse {ECO:0000269|PubMed:19900557}. Cytoplasm, cytosol {ECO:0000269|PubMed:19900557}. Note=Detected both at presynaptic and postsynaptic sites, exclusively at excitatory synapses, but not inhibitory synapses, in hippocampal neurons. {ECO:0000269|PubMed:19900557}.; SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density {ECO:0000269|PubMed:19900557}. Presynapse {ECO:0000269|PubMed:19900557}. Postsynapse {ECO:0000269|PubMed:19900557}. Cytoplasm, cytosol {ECO:0000269|PubMed:19900557}. Note=Detected both at presynaptic and postsynaptic sites, exclusively at excitatory synapses, but not inhibitory synapses, in hippocampal neurons. {ECO:0000269|PubMed:19900557}.
Interaction partners:
- Sorbin and SH3 domain-containing protein 2
- Guanylate-binding protein 2
- PDZ and LIM domain protein 1
Sequence:
MSNYNVSLVGPAPWGFRLQGGKDFNMPLTISSLKDGGKASQAHVRIGDVVLSIDGISAQGMTHLEAQNKIKACTGSLNMTLQRASAAAKSEPVAVQKGEPKEVVKPVPITSPAVSKVTSTTNMAYNKVPRPFGSVSSPKVTSIPSPSSAFTPAHAATSSHASPPPVAAVTPPPLSASGLHASANPSAAQCSSPPNTGKPAVHVPRQPTVTSVCSESAQELAEGQRRGSQGDIKQQNGPPRKHIVERNTEFYHIPTHSDASKKRLIEDTEDWRPRTGTTQSRSFRILAQITGTEHLKESENDNAKKANSTPEPSQQSASPLSAAESLESPGSNRPVVAGLRSAAAFKPVGSTSVKSPSWQRPNQAAPSTGRISNSASSSGTGAPMKPAVGPPQPSDQDTLVQRAEHIPAGKRTPMCAHCNQAIRGPFLVALGKSWHPEEFNCAHCKNTMAYIGFVEEKGALYCELCYEKFFAPECGRCQRKILGEVINALKQTWHVSCFVCVACGKPIRNNVFHLEDGEPYCETDYYALFGTICRGCEFPIEAGDMFLEALGSTWHDTCFVCSVCCESLEGQTFFSKKDKPLCKKHAHSVNF
Protein: Protein BPS1, chloroplastic (Protein BYPASS 1) (Q9LMM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal root and shoot development. Prevents constitutive production of a root mobile carotenoid-derived signaling compound that is capable of arresting shoot and leaf development.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- Cell division cycle 45
- Origin of replication complex subunit 2
- DNA polymerase epsilon subunit B
- Minichromosome maintenance 10
- Origin of replication complex subunit 5
- Probable DNA helicase MCM8
Sequence:
MARPQDPPRGFFPFGNPFKNLSSKNSVLSSKLLPLLNNFETNLASSISKLVPKEKSDILTVSWMKQAMESLCETHNGIKTLITDLELPVSDWEDKWVDVYLDISVKLLDLCNAFSSELTRLNQGHLLLQFALHNLEANSPQNLSKAQSSLDSWKQHIVSKNPRIENCRAILSSLVQTLNLPKVKNSAKGKVLMRALYGVKVKTLYISGVFAAAFSGSSQNLMYLTVSNELPWAQSFMEVQNTMNAEIKNIFLSDGLTVLKELEAVASGVKKLYPAIQQGSIDPISLQPLKDSVTELSNGIDLVSKEVDCFFKILLSGRDTLLENLRSMGASTLQATSPKKAAGKNYRGF
Protein: Glycosyltransferase-like KOBITO 1 (EC 2.4.1.-) (Protein ABA INSENSITIVE 8) (Protein ELONGATION DEFECTIVE 1) (Q9C9Z9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the coordination between cell elongation and cellulose synthesis by promoting the expression of genes involved in cell elongation and cellulose synthesis. Acts as a regulator of plasmodesmatal permeability. Mediates abscisic acid (ABA) and sugar responses essential for growth (e.g. seed germination, stomatal regulation and ABA-regulated gene expression). Required for normal organogenesis by promoting cell elongation, regulating cell differentiation in vascular tissues and maintaining root meristem identity. Regulates crystalline cellulose microfibrils deposition and parallel organization during the elongation phase of the cell. Maybe a glycosyltransferase. Negative factor in light inhibition of hypocotyl elongation through modulating cellulose biosynthesis.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:15010620}. Cytoplasm {ECO:0000269|PubMed:14742875}. Cell membrane {ECO:0000269|PubMed:12215501}. Note=The cell membrane subcellular localization first observed (PubMed:12215501) and the punctate pattern within the cytoplasm (PubMed:14742875) could not be confirmed (PubMed:15010620).
Interaction partners:
Sequence:
MKSTHHHRAPLISASSSSSSSSQNHSFVSRLLLLLTLLPVSLACLAFILQWRGGGLADPASASVRSSTSVPGGSDLNHEVFPGMETVSSVSPKSHQSSSDCSNLARSSSPSFPYYADWKFGVDTSLKPKICITTSTSAGLDQILPWMFYHKVLGVSTFFLFVEGKAATPSISKVLESIPGVKVIYRTKELEEKQAKSRIWNETWLSSFFYKPCNYELFVKQSLNMEMAIVMARDAGMDWILHLDTDELIYPAGAREYSLRRLLLDVPPNVDMVIFPNYESSVERDDIKDPFTEVSMFKKNYDHLPKDTYFGMYKEATRNNPNYFLTYGNGKSVARVQDHLRPNGAHRWHNYMKTPNEIKLEEAAVLHYTYSKFSDLTSRRDRCGCKPTKEDVKRCFMLDFDRSAFIIASTATDEEMLSWYREHVVWGDKDVKTKLLRKGILTRIYSPMVVIQALKESGVFSSVVSSASTNLSKKKFLSSIHKSNSSRSTASESLPSKESKSEGISARHLLEAESAIPPLSPPGMEQARFFTED
Protein: HTH-type transcriptional activator AaeR (P67662)
Organism: Escherichia coli (strain K12)
Function: Activates transcription of the aaeXAB operon.
Interaction partners:
- HTH-type transcriptional regulator YjiE
- Elongation factor Tu 2
- DNA topoisomerase 4 subunit A
- DNA helicase IV
- Uncharacterized protein YaeQ
- Elongation factor Tu 1
- Cold shock-like protein CspC
- Uncharacterized protein YciQ
- Cell division topological specificity factor
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
Sequence:
MERLKRMSVFAKVVEFGSFTAAARQLQMSVSSISQTVSKLEDELQVKLLNRSTRSIGLTEAGRIYYQGCRRMLHEVQDVHEQLYAFNNTPIGTLRIGCSSTMAQNVLAGLTAKMLKEYPGLSVNLVTGIPAPDLIADGLDVVIRVGALQDSSLFSRRLGAMPMVVCAAKSYLTQYGIPEKPADLSSHSWLEYSVRPDNEFELIAPEGISTRLIPQGRFVTNDPMTLVRWLTAGAGIAYVPLMWVINEINRGELEILLPRYQSDPRPVYALYTEKDKLPLKVQVVINSLTDYFVEVGKLFQEMHGRGKEK
Protein: Uncharacterized protein (Q385H8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
METSGPKTVPGTDLCHRVLYAAVVGDNAKGCLPGSVKKMTPDGVVIVDHVMRCARYYVPGLCLSGSLPTSKCESLLDFSDQVPPLSAEPQKQELIDRILYYSSELESRTQQLELRKQEVQSLQNKLRIVNKELKRRGIVIADTPERGYTKGSDFKKVYSPDDSYIGNNFPAPPNSRDIGSDDPTRPPLPPLRIDGDLRSYTSRPPPPYSAEPLVPPFISCALPPKSLIADQPGVTALPSGRRVQQAFAKMVQNSRRHDNPAAAGCQPVSNRDGLVGTIPQAEGVESINGVERFGNDGADNNSRREEEGNSDVAAKKSHSYK
Protein: LYN proto-oncogene, Src family tyrosine kinase (E5RJ37)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSA
Protein: Zinc finger protein 697 (Q5TEC3)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MKQEDNQGVCAHQDSEDKGMGSDFEDSEDREGDPEEREMGSNPHDTNKREGHPEPEMGSNPQDSRHREAVPDICTEGQLSEEEGVSVRGEEDDQSGVADMAMFPGLSESDSISRSLREDDDESAGENRLEEEEEQPAPPVLPWRRHLSLGSRHRGDKPAHRRFHRLHHPMAVDLGELDSLVASIMDAPTICPDCGESFSPGAAFLQHQRIHRLAEAAAAASLEPFGLAGECDAMVGMMGVGVAGGFGAGPPLARPPREKPFRCGECGKGFSRNTYLTNHLRLHTGERPNLCADCGKSFSWRADLLKHRRLHTGEKPYPCPECGEAFSLSSHLLSHRRAHAAASGAGAAALRPFACGECGKGFVRRSHLANHQRIHTGEKPHGCGECGKRFSWRSDLVKHQRVHTGEKPYMCSECGETFSVSSHLFTHKRTHSGERPYVCRECGKGFGRNSHLVNHLRVHTGEKPFRCGQCEKRFSDFSTLTQHQRTHTGEKPYTCIECGKSFIQSSHLIRHRRIHTGNKPHKCAGCGKGFRYKTHLAQHQKLHLC
Protein: Myosin-G heavy chain-like protein (Q8RXT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MALNFFSTSLHPISNPSSSSRSKQSHHLLLQLSSPPATRVRSERSEIGVTDDNNNNNDTSSSSFSGSSSSSSVRTQLDLLEQLTSTSDGYLSDGGGSRGLTIRDQLAGLVGDRDDDFSIPLGKNLKKVSPKFLTISQKRNIKRQSYLNEVSQRNDSVFFATIGAFVILPPLVILAIAILTGYVQLFP
Protein: Protein-arginine deiminase type-1 (EC 3.5.3.15) (PAD-R11) (Peptidylarginine deiminase I) (Protein-arginine deiminase type I) (O88806)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the deimination of arginine residues of proteins.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ULC6}.
Interaction partners:
Sequence:
MASQRAVQLSLRKPAHAVCVIGVGTLVDVYSDVPKGAKTFEVSGSSEVKIYMVYDPSRVAEPAGPAHWPLDANVDVVVVADTVSKNLHDLKVKVSYFKSQDTAALAHSLLYLTAVDVSLDVDTGRTGKVKKGSGDKKNWRWGSGGSGAILLVNCDRDVHGSREDLHDSHLRSLEDLQDMSPMVLSCDGPDDLFKSHKPVLKASLPDSRRLGVFCARGGTSLSNYKQVLGPRHNSYEVERHPGERDIQFYVEGLAFPDASFSGLLSLSVSLVDTRPLSEVLVFTDSVTFRVAPWIMTPNTQPPLELYVCSVTDMHGSNDKFLEDMSHLATKANCKLVVCPRLENRNDRWIQDEMEFGYIDAPHKSFPVVFDSPRNRGLRDFALKKILGPDFGYVTREIQFAGASGLDSFGNLDVSPPVRVGNTEYPLGRILIGGNFPKSSGRRMARVVRDFLHAQQVQAPVELYSDWLSVGHVDEFLSFVPTSDQKGFRLLLASPSACLQLFQEKKEEGYGEAKQFDGLKHKTKRSINDILADRHLRRDSAHVQKCIDWNREVLKQELGLSESDIVDIPQLFFLKGAYAEAFFPDMVNMVVLGKYLGIPKPFGPIINGRCCLEEKVRSLLEPLGLRCVFIDDFLFYHQLLGEIHCGTNVRRKPFAFRWWNSVP
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase) (Q9UT09)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pentafunctional AROM polypeptide
- Chorismate synthase
- Chorismate mutase
- Putative phospho-2-dehydro-3-deoxyheptonate aldolase
- Anthranilate phosphoribosyltransferase
- Probable acetolactate synthase small subunit
- Putative prephenate dehydratase
- Glutamine synthetase
- Tryptophan synthase
- Aromatic amino acid aminotransferase C569.07
Sequence:
MSPVFLPSGETYDQEHLDDNRVLGYNPLVPAALVQQEIPVSETSRKVITDSRKEIQAILNKQDDRIIVVVGPCSIHDPKLAMDYAKLLKPKADELQDALCVVMRCYLEKPRTTIGWKGLVNDPNLDGSFAINKGIRMARQMYCDVTNFGIPLASEMLDNISPQFFADLLSFGAIGARTTESQLHRELASALSFPVGFKNGTDGTVGVAIDAIGATAHPHTMLGVTKQGLAAITMTRGNKDTFIILRGGKKGPNYDAEHVAAVRKDLEKANLPPRIMIDCSHGNSSKNHLNQPKVSKSIAEQIRNGDSSIVGVMIESHINEGRQDAPIRPGVKDTLKYGVSITDACVSWEQTAPMLDDLAEAVRARRQNQKSN
Protein: Stretch-inhibitable nonselective channel (SIC) (Q9Z182)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGAVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKSEIYQYYGFSHTMGRLRRDRWSSVVPRVVELNKNSDTDEVVVPLDNLGNPNCDGHQQGYAPKWRAEDAPL
Protein: Odorant-binding protein 2b (Odorant-binding protein IIb) (OBPIIb) (Q9NPH6)
Organism: Homo sapiens (Human)
Function: Probably binds and transports small hydrophobic volatile molecules.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Kinesin-like protein KIF22
- Apolipoprotein D
- Odorant binding protein 2A
Sequence:
MKTLFLGVTLGLAAALSFTLEEEDITGTWYVKAMVVDKDFPEDRRPRKVSPVKVTALGGGKLEATFTFMREDRCIQKKILMRKTEEPGKYSAYGGRKLMYLQELPRRDHYIFYCKDQHHGGLLHMGKLVGRNSDTNREALEEFKKLVQRKGLSEEDIFTPLQTGSCVPEH
Protein: Killer cell lectin-like receptor subfamily G member 1 (C-type lectin domain family 15 member A) (ITIM-containing receptor MAFA-L) (MAFA-like receptor) (Mast cell function-associated antigen) (Q96E93)
Organism: Homo sapiens (Human)
Function: Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19604491}; Single-pass type II membrane protein {ECO:0000269|PubMed:19604491}.
Interaction partners:
- Cadherin-1
- Cadherin-2
- Cadherin-17
- Interleukin-7 receptor subunit alpha
- T-cell surface glycoprotein CD8 alpha chain
- Eomesodermin homolog
- CD160 antigen
- T-box transcription factor TBX21
- CD27 antigen
- Integrin alpha-E
Sequence:
MTDSVIYSMLELPTATQAQNDYGPQQKSSSSRPSCSCLVAIALGLLTAVLLSVLLYQWILCQGSNYSTCASCPSCPDRWMKYGNHCYYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLRNNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKKCPFADQALF
Protein: Histone-lysine N-methyltransferase NSD3 (EC 2.1.1.370) (EC 2.1.1.371) (Nuclear SET domain-containing protein 3) (Wolf-Hirschhorn syndrome candidate 1-like protein 1 homolog) (WHSC1-like protein 1) (Q6P2L6)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase. Preferentially dimethylates 'Lys-4' and 'Lys-27' of histone H3 forming H3K2me2 and H3K27me2. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Bromodomain-containing protein 4
- Bromodomain-containing protein 3
- Histone H3.2
- Histone H3.1
- Lysine-specific histone demethylase 1B
- Bromodomain-containing protein 2
- Histone H3.3
- Actin-histidine N-methyltransferase
- NUT family member 1
- Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
Sequence:
MDFSFSFMQGIMGNTIQQPPQLIDSANIRQEDAFDNHSDIVEDGGPTPFEATLQQGFQYPPTTEDLPPLTNGYPPSISLYETQTKYPPYNQYPNGSANGFGAVRNFSPTDYYHSEIPNTRPHEILEKPSPPQPPPPPSVPQTVIPKKTGSPEIKLKITKTIQNGRELFESSLCGDLLNEVQASEHTKSKHESRKEKRKKSNRHESSRSEERRSHKIPKLEPEGQNRPNERVDTAPEKPREEPVLKEAIPVQPILSSVPTTETSTGVKFQVGDLVWSKVGTYPWWPCMVSSDPQLEVHSKINTRGAREYHVQFFSNQPERAWVHEKRVREYKGHEQYEELLAEAAKQASNHSEKQKIRKPRPQRERAQWDIGIAHAEKALKMTREERVEQYTFIYIDKQPEEASSQAKKNVTSKTEVKKPRRPRSVLNSQPEQTNAGEVASSQSSTDLRRQSQRRHTSLEEEEPPPVKIAWKTAAARKSLPASITMHKGSLDLQKCNMSPVVKIEQVFALQNATGDGKFIDQFVYSTKGIGNKTEISVRGQDRLIISSPSQRSEKPAQSASSPEATSGSAGPVEKKQQRRSIRTRSESEKSAEVVPKKKIKKEQVETAPQASLKTGLQKGASEISDSCKPLKKRSRASTDVETASCTYRDTSDSDSRGLSDGQVGFGKQVDSPSATADADASDAQSVDSSLSRRGVGTSKKDTVCQVCEKAGDCLVACEGECCRHFHVECLGLTAVPEGHFTCEECETGQHPCFSCKVSGKDVKRCSVSVCGKFYHEACVRKFPTAIFESKGFRCPQHCCSSCSMEKDIHKASKGRMMRCLRCPVAYHVGDACVAAGSVSVSSHILICSNHSKRSSQSAAINVGFCFVCARGLIVQDHSDPMFSSYAYKSHYLLSESNRAELMKLPMIPSSSASKKRCEKGGRLLCCESCPASFHPECLSIDMPEGCWNCNDCKAGKKLHYKQIVWVKLGNYRQVLWWPAEICSPRSVPLNIQGLKHDLGDFPVFFFGSHDYYWVHQGRVFPYVEGDKHFAEGQTSINKTFKKALEEAAKRFQELKAQRESKEALEMERTSRKPPPYKHIKANKVIGKVQVQVADLSEIPRCNCKPGDENPCGLESQCLNRMSQYECHPQVCPAGDRCQNQCFTKRLYPDAEVIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFYMLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFNYNLDCLGNGRTVCHCGADNCSGFLGVRPKSACTSAVDEKTKNAKLKKRRKVKAEAKPIHEDYCFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPHGKWECPWHRCDECGSVAVSFCEFCPHSFCKAHGKGALVPSALEGRLCCSSHDPASPVSPEYWSKIRCKWESQDSGEEVKE
Protein: HDC12388 (Kinetochore Mis12-Ndc80 network component 2, isoform A) (Q6IKI1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CG1558-RA protein
- Nnf1b
- Kinetochore protein Spc25
- Nnf1a
- Nuf2
- Mis12
- Kinetochore protein NDC80
Sequence:
MENFSLQQLIELQNIQKELNSNKDTYLKTYRQVLKKKFRSELNNLVRADFNIVKTELKVPQLPPLPPEDEKTTATVQFSDMAKDYEFTKDCLSLL
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 4B (Mast cell surface glycoprotein Gp49A) (Q61450)
Organism: Mus musculus (Mouse)
Function: Plays a role in mast cell activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10630292, ECO:0000269|PubMed:10982834, ECO:0000269|PubMed:11046024}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIAMLTVLLYLALILEPRTAVQAGHLPKPIIWAEPGSVIAAYTSVIIWCWGSWEAQYYYLDKEKSVNPWDTEVPLENRNKTKFKIRFMTASYAGIYNCYYKSAAGFSEHSDAMELVMTGAYENPSLSVYPSSNVTSGVSISFKCSSSTLFGRFILIQEGKHGLSWTLDSQHQANQPTHATFVLDAVAPNHNGTFRCYGFFRNEPQVWSKPSNSLDLMISETKEQSCTPTEDGLETYQKILIGVLVSFLLLFFLLLFLILIGYQCRHKNKANASVKNTQSEDNAELNSWNPQNEDPPRELCTPR
Protein: Formyltetrahydrofolate deformylase 2, mitochondrial (EC 3.5.1.10) (F4JP46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Deformylase involved in photorespiration. Prevents excessive accumulation of 5-formyl tetrahydrofolate (THF), a potent inhibitor of the Gly decarboxylase/Ser hydroxymethyltransferase complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18628352}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Serine hydroxymethyltransferase 1, mitochondrial
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Serine hydroxymethyltransferase 5
- Serine hydroxymethyltransferase 3, chloroplastic
- Serine hydroxymethyltransferase 6
- Serine hydroxymethyltransferase 4
- Serine hydroxymethyltransferase 7
- Serine hydroxymethyltransferase 2, mitochondrial
Sequence:
MIRRVSTTSCLSATAFRSFTKWSFKSSQFHGESLDSSVSPLLIPGFHVFHCPDVVGIVAKLSDCIAAKGGNILGYDVFVPENKNVFYSRSEFIFDPVKWPRRQMDEDFQTIAQKFSALSSVVRVPSLDPKYKIALLLSKQDHCLVEMLHKWQDGKLPVDITCVISNHERAPNTHVMRFLQRHGISYHYLPTTDQNKIEEEILELVKGTDFLVLARYMQLLSGNFLKGYGKDVINIHHGLLPSFKGRNPVKQAFDAGVKLIGATTHFVTEELDSGPIIEQMVERVSHRDNLRSFVQKSEDLEKKCLMKAIKSYCELRVLPYGTQRTVVF
Protein: F-box/WD repeat-containing protein pof10 (Skp1-binding protein 2) (Q9P7W4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11820777, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cullin-1
- RING-box protein pip1
- F-box/WD repeat-containing protein pof1
- F-box protein pof15
Sequence:
MKSEPTSLDFTSSNLRRMNRDHSSNNTNRTVLNLPKEILIIIFSFLDPRSLLSAQCTCKYWKKLLSDDLSWRTAFFHHFAGDQSQIFSPLGNGTWRQEYLLRSTITRAYEKGKGQTVQYDCRVGQLTNLYYDFSSGRLYSGNWLTGTISVSDPTTGKVERSLLHASTDGSFTHGLSTMTLGKQIFGFGFMDGRVGVILMSRQAETPRKFRYCLDSHADSVTCIDALTGDLPPTGEIGMVTGSDDGSVHCWDVKTGVSLQSFQFRSSQILSLCFRPKYKMLLVDTFNYELNSYQLYLIPGYARSRKNEQPILLSSRKCVLTDEEEPPCLMTADCCAGVAFLSRGAPKNCICRVSFKEFLEKNDNVGVQTSSIPLNGKPTSISLDTNDRVLSKSTPGRGARLLAVGDENGLVYVVNTRTEDPNKAILRTITAYSNFPITDIYLNEVAMVVGSASGYCGVYDTVTGNFLKKIASARNAARREPINCILLDSNPLSLKGVITMSKHVKSWSYTIPKPFVNKRSKVLPLRPSVTHDNLSKSSDYSKNEVEREIMLGLDQIAQERREKMEARQKFEQHFGEGLVGLSEEEIIAYVTMLSQEEEAKRMVQLSMDVDKIEEDFKENDEQATSSLNALSSNHEPPQEQANVAELNEQEQIELAMRLSLMEM
Protein: Stomoxyn (Q8T9R8)
Organism: Stomoxys calcitrans (Stable fly) (Conops calcitrans)
Function: Has antimicrobial activity against most Gram-positive and Gram-negative bacteria, filamentous fungi and yeasts tested. Has trypanolytic effect on T.b.rhodesiense and limited hemolytic activity against bovine red blood cells.
Subcellular location: Secreted {ECO:0000269|PubMed:12372834}.
Interaction partners:
Sequence:
MNFYKYLVVLVVLVLCLSATQTEARGFRKHFNKLVKKVKHTISETAHVAKDTAVIAGSGAAVVAATG
Protein: UDP-glucuronic acid decarboxylase 1 (EC 4.1.1.35) (UDP-glucuronate decarboxylase 1) (UGD) (UXS-1) (Q5PQX0)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11877387}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Ubiquitin-like protein FUBI
- UDP-glucose 4-epimerase
Sequence:
MVSKGLLRLVSSVNRRKMKLLLGIALFAYAASVWGNFVNMRSIQENGELKIESKIEEIIEPLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARVKKGRTRHS
Protein: Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein) (Q2EEZ0)
Organism: Bovine coronavirus
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004402, ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}; Single-pass type I membrane protein {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface. {ECO:0000256|HAMAP-Rule:MF_04207, ECO:0000256|RuleBase:RU361278}.
Interaction partners:
Sequence:
MFLLPRFVLVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVTTNPRNYSYMDLNPALCGSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYDSPCFSQQGVFRYDNVSSVWPLYPYGRCPTAADINTPDVPICVYDPLPIILLGILLGVAVIIIVVLLLYFMVDNGTRLHDA
Protein: Uncharacterized lipoprotein YpdI (O32528)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Protein YfdX
Sequence:
MKVNLILFSLFLLVSIMACNVFAFSISGGGSERSYKETEKTSAMTTTHSTKLQPSQAILFKMREDAPPLNLTEEMPPPFPTKANYLIHPVR
Protein: Uncharacterized protein ycf70 (P0C307)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MVYGYGKSNMPHPNRKRKGTDTQYDYWEELLVMVSGLYALFCVFLVLFIFFDSFKQESNKLELSGKEEKKKLNGENRLSRDIQNLLYIK
Protein: COP1-interacting protein 7 (O80386)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits transcriptional activation activity. Positive regulator of light-regulated genes, probably being a direct downstream target of COP1 for mediating light control of gene expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:9668129}.
Interaction partners:
- E3 ubiquitin-protein ligase COP1
- E3 ubiquitin-protein ligase CIP8
- Protein COP1 SUPPRESSOR 2
- TRF-like 10
Sequence:
MDPRTRLDYALFQLTPTRTRCDLVIFSGGENEKLASGIFQPFVTHLKSVSDQISKGGYSVTLRPSSVGVPWFTKVTLQRFVRFVTTPEVLERSVTLEKEIEQIEDSIQANAAAIAGEAEGNELGGTWTSQKSTALSKTKGETDGDTVEENSKVGLQRVLENRKAALCKEQAMAYARALVVGFELDYMDDLFSFADAFGASRLREACVNFVDLCKRKNEDRMWVDQITAMQAFPRPELTFMGDSGIVLAGEENDLLNATNVKHGNSMDASSQGSFETGQEGRAQMAMPWPNQFPQYMQNFQGHGYPPPYMFPGMQGQSPYFHGNMQWPVNMGDVESNEKSSKKKKKKKKNKKKSKQDESAEPSDNSSTETESEDGNEGKKQSRKVVIRNINYITSKRNGAKESDSDESGEEEGFVDGDSIKQQVEEAIGSVERRHKSTSHRQRKHKSHNGDDDSSNKETKGNDNWDAFQNLLLKDNDSEPEELLRISSTALNMASEVVRKREPPSDDSFLVAIGNEDWGRETSIEKFNAGENVRIIRKGNNYDEEMLNPGRSDESRSYSQAEMSVHDGKLRTRNEAEEDWFIRNQAGPETDPSLVKTFVGDHFHLNKSSERDVLTDDSFMIHSRVENQVEDSRLRTEIMDLDVYGTTQQENSAPENTPHEPDDLYMVLGREQDVKPTLLPWTPEIDFETNTLAQRTSRIDLITATKASAGEQTLDGKEKKSRGISKGKDAKSRASSRPDPASKAKRPAWGSRAAVSKSKSEMEEERKKRMEELLIQRQKRIAEKSSGGSVSSSLASKKTPTVTKSVKSSIKNEKTPEAAQSKAKPVLRSSTIERLAVARTAPKEPQQKPVIKRTSKPSGYKTEKAQEKKSSKIGQSDAKSVELSRDPSLEIKETVVEDSHSYLSEKQVDALPAVASVDDFKDIKELHSLPSEETARVKNRPNEIIAEKVQDQTKIDDQETVKNTSVSEDKQITTKHYSEDVGEVQASQEKPVSPKKSVTFSETNMEEKYYFSPAVSEIDISTPPATEADHSRKKWNSEETSPKATAKVFRKLLMFGRKK