wanglab/gogpt-training-data huggingface dataset:
Protein: Multifunctional alkaline phosphatase superfamily protein PehA (Phosphodiesterase) (EC 3.1.4.-) (Phosphonate ester hydrolase) (PEH) (EC 3.1.-.-) (Phosphonate monoester hydrolase) (BcPMH) (EC 3.1.3.-) (Sulfuric ester hydrolase) (EC 3.1.6.-) (Q45087)
Organism: Trinickia caryophylli (Paraburkholderia caryophylli)
Function: Hydrolytic enzyme with a broad substrate specificity acting on phosphate diesters and phosphonate monoesters. Hydrolyzes phosphate mono- and triesters, sulfate monoesters and sulfonate monoesters. Hydrolyzes glyphosate monoesters. Does not hydrolyze DNA or cGMP. Hydrolyzes glyceryl glyphosate, but this substrate has a much lower affinity than the glyphosate monoesters.
Interaction partners:
Sequence:
MTRKNVLLIVVDQWRADFIPHLMRAEGREPFLKTPNLDRLCREGLTFRNHVTTCVPCGPARASLLTGLYLMNHRAVQNTVPLDQRHLNLGKALRAIGYDPALIGYTTTTPDPRTTSARDPRFTVLGDIMDGFRSVGAFEPNMEGYFGWVAQNGFELPENREDIWLPEGEHSVPGATDKPSRIPKEFSDSTFFTERALTYLKGRDGKPFFLHLGYYRPHPPFVASAPYHAMYKAEDMPAPIRAENPDAEAAQHPLMKHYIDHIRRGSFFHGAEGSGATLDEGEIRQMRATYCGLITEIDDCLGRVFAYLDETGQWDDTLIIFTSDHGEQLGDHHLLGKIGYNAESFRIPLVIKDAGQNRHAGQIEEGFSESIDVMPTILEWLGGETPRACDGRSLLPFLAEGKPSDWRTELHYEFDFRDVFYDQPQNSVQLSQDDCSLCVIEDENYKYVHFAALPPLFFDLKADPHEFSNLAGDPAYAALVRDYAQKALSWRLSHADRTLTHYRSSPQGLTTRNH
Protein: Uncharacterized protein (Q57VT0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transmembrane protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Letm1 RBD domain-containing protein
- ATP synthase delta chain
- ATP synthase, epsilon chain, putative
Sequence:
MLRRSSAALIRRTPVRHSGGELFVRPKLEEIPPADQCRGFFGPLNDSLKFLRLLDIKWMMNRAVAMRREYLIATPTLFTFIWMFTWKGAVIYFWGDRAPPRRMDWNTEETGRLPLGFKPTPAPL
Protein: Myocyte-specific enhancer factor 2C (Myocyte enhancer factor 2C) (Q8CFN5)
Organism: Mus musculus (Mouse)
Function: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. May also be involved in neurogenesis and in the development of cortical architecture. Isoforms that lack the repressor domain are more active than isoform 1 (By similarity). Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:11554755}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}.
Interaction partners:
- Homeobox protein Nkx-2.5
- Mitogen-activated protein kinase 14
- Transcription factor GATA-4
- Focal adhesion kinase 1
- Mitogen-activated protein kinase 11
- Myocyte-specific enhancer factor 2D
- Histone deacetylase 5
- Nuclear factor of activated T-cells, cytoplasmic 4
- Mitogen-activated protein kinase 12
- Histone deacetylase 4
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPSFEMPVTIPVSSHNSLVYSNPVSTLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLSIKSEPVSPPRDRTTTPSRYPQHTTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
Protein: Fgr34p (A0A1D8PU48)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MNSNFKRFRVLLESNLPNLQNEKSMIEINDRTTVKQLKQLIIAKNDEGSVTRTFIEQIKLSYEGNIIPTSFQEEEASVYELLGLNQELLEQNNSVIKLKLTKHEHVNGTGGLLSREFWKDFQSNDRFRFLPATNDSLQQPNLASSNSVPLESTSDLSAARSTTNPTATSSSSEQGIDSDISTSPTSANPVPSPSNYETSVPSQQDSIPFVNNPSESSTPNIDPIKPASIQVRGGSTWEMEGTSYDTMVEQHSGKKILVKQDDLSNVEYELTLKVDNIVKKVSLGTAQCIVVDNGLHDPYLLLGPMGAAKVHKVFKSASGEPLIQKVLVMMYDIGSDSESESNEQAVPGDANNIDVEDAEIDDLMDRLYTNGRSLLITMVKLTFVLYLMGFRLNQHMMNYWFHYAVLLVLLFHAYVLLCTGANRVIRFGGNVNDVSIMMDRVVRTCVRRTSELELVQSRDPAWLKTVKLNFENIWKDSLLFGLCIFPSMQARVFHQLSLAEEDVSIYEELVEPNEVVDSVEI
Protein: Caffeoyl-CoA O-methyltransferase 2 (PhCCoAOMT2) (EC 2.1.1.104) (5-hydroxyferuloyl-CoA O-methyltransferase 1) (EC 2.1.1.-) (A0A0S2UWT1)
Organism: Petunia hybrida (Petunia)
Function: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A0S2UWC9}.
Interaction partners:
Sequence:
MANNGENGRHQEVGHKSLLQSDALYQYILDTSVYPREPEPMKELREITAKHPWNIMTTSADEGQFLSMLIKLINAKNTMEIGVFTGYSSLATAMALPDDGKILAMDINRENYEIGLPVIEKAGLAHKIEFKEGPALPVLDQMIEDGKYHGSYDFIFVDADKDNYLNYHKRLIDLVKVGGLIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICQLPVGDGITLCRRIS
Protein: Xylan alpha-(1->2)-glucuronosidase (EC 3.2.1.131) (Alpha-glucuronidase) (P96105)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of alpha-(1->2)-glycosidic bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4-O-methylglucuronic acid from xylan.
Interaction partners:
- Endo-1,4-beta-xylanase A
- Endo-1,4-beta-xylanase B
Sequence:
MDYRMCWLEYRGLPADVAGKLKDWFSSVSILEPGSSVLKDEIRRFSERSIGITPRFYSRPLKKEKYIMVGRLESLPIKLDVNLGEEGFMLRTIEWNGSKILLVTGETKKALVYGIFDLMKRIRLGEDIEKMNVLAKPKAKFRMLNHWDNLDGTIERGYAGNSIFFKDNRIIINQRTKDYARLLASIGINGVVINNVNVKKREVYLIDSIYLKKLKKLADIFREYGIKIYLSINFASPVYLGGLDTADPLDERVARWWREKARGIYDYIPDFGGFLVKADSEFNPGPHMFGRTHAEGANMLARALAPFGGVVIWRAFVYNCLQDWRDYKTDRAKAAYDNFKPLDGQFDDNVIIQIKYGPMDFQVREPVNPLFGGMEKTNQILELQITQEYTGQQIHLCFLGTLWKEILEFDTFAKGEGSYVKRIVDGTLFDRENNGFAGVSNVGDSVNWTGHDLAQANLYAFGRLAWNPDEEIERIVEEWIKLTFGDDEKVLENVSYMLMKSHRTYEKYTTPFGLGWMVNPGHHYGPNPEGYEYSKWGTYHRANWEAIGVDRTSRGTGYTLQYHSPWKEIYDDINTCPEDLLLFFHRVRYDHRLKSGKTLLQTMYDLHFEGVEEVEEFIKKWEELKDRVSPDIFERVKERLHMQLEHAKEWRDVINTYFYRRTGIPDEKGRKIYP
Protein: Putative BPES syndrome breakpoint region protein (BPES candidate 1) (Q9GZL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGRDQITNLGSEGETHPWGYSSPPYPLHTFFIPFLPSGFGGSGLGIPSDNEKHDLQDCVEVSRPEGPAPELPSSLCGWNKISSLCGLGFPSRDPKTWDLAMLLSPWVDFFELQLL
Protein: Small ribosomal subunit protein uS13 (30S ribosomal protein S13) (P0A7S9)
Organism: Escherichia coli (strain K12)
Function: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.
Interaction partners:
- Large ribosomal subunit protein uL4
- Elongation factor Tu 1
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL14
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein bL33
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
Sequence:
MARIAGINIPDHKHAVIALTSIYGVGKTRSKAILAAAGIAEDVKISELSEGQIDTLRDEVAKFVVEGDLRREISMSIKRLMDLGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK
Protein: Multidrug resistance protein 4 (SD11716p) (Q9VGM1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MQSMKADELPENPRERSSPLSSLMFCFALPVLFKGRKKTLEQKDLYRALKEHKSDSLGDRLCAAWDEQVAKNETPRLGRALTKVFGFHLFITGVFLLAQEFLTKVTQPICLIGVMAYFAGNDPDRSKAQLWAAGLIAGSVFSVCIGHPYMLGLLHLGMKMRIALSSLIYRKALRLSRTALGDTTVGQVVNLLSNDVGRFDLVLINVHYLWIAPLELIAVTYLMYLEIGISSMFGVAIMLLFLPFQSYLGKRTSVLRLRTALRTDERVRMMNEIISGIQVIKMYAWEKPFGKVVEMTRFNEMLCIKQVNYIRGILISFAMFLSRIFTSSSLIAFVLLGNILNAEKAFFVTAYYNILRRSVTMFFPQGISEFAELLVSVRRLEAFMHRPETKVRDKSKVKNANQKAESPNGDSPKGNGIPENLIEFSQFQARWESHSLEPTLEDINLQLGRRKLVAVIGPVGAGKSSLIQAILGELPGESGTLRINGSYSYAAQEPWLFTGTVRQNILFGLDWDKHRYRTVVKKCALERDFELLPFGDKTIVGERGASLSGGQKARISLARAVYRRADIYLLDDPLSAVDTHVGRHLFDQCMRGYLRSELVILVTHQLQFLEQADLIVIMDKGRISAMGTYSSMKRSGLDFAQLLTAPNKDAEDLDEIDGAGGDGLDLLNVPSLSRRGSKNSKPSTRNNSFTSLSSMAESMAQEASLQMQETRVEGKIGLGLYKEYLTSGSSWFMIFFMVFLCLATQILCSAADYFLSYWVDKNVDGQTDINTDPQDMYYFAALNVAVVVFTIVRTMLFYKMAMRSSTQLHNAMYQGITRAAMYFFNTNPSGRILNRFSKDLGQLDEVLPSVMLDVVQLFLTLLGIIVVICITNPYYLILTLALAIIFYYIREFYLKTSRDVKRLEAVARSPIYSHLSATITGLPTIRALGAQKELIAEFDNLQDLHSSGYYTFLATNRAFGYYLDCFCTLYIVIIILNYFINPPQSPGEVGLAITQAMGMTGMVQWAMRQSAELENTMTAVERVVEYDEIEPEGEFDSREGKKPSPSWPEKGEIIAEDLCLRYFPDPQAKYVLKALNFRIRPCEKVGIVGRTGAGKSSLINALFRLSYNEGIITIDERDTADMGLFDLRSKISIIPQEPVLFSGSMRYNLDPFEEYNDAKLWDALEEVKLKPLISELPNGLQSKISEGGSNFSVGQRQLVCLARAILRENRVLVMDEATANVDPQTDALIQATIRSKFRDCTVLTIAHRLNTIMDSDRVLVMDAGHLVEFGSPYELLTSSESKIFHGMVMETGQNTFDSLLKVAEKAHLESMKPKSE
Protein: Diacylglycerol kinase 6 (AtDGK6) (DAG kinase 6) (EC 2.7.1.107) (Diglyceride kinase 6) (DGK 6) (F4JKI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phosphorylates the second messenger diacylglycerol (DAG) to generate phosphatidic acid (PA), another important signaling molecule. PA is required for plant development and responses to abiotic stress and pathogen attack. May be involved in the accumulation of PA during cold stress.
Interaction partners:
- Sulfoquinovosyl transferase SQD2
- Choline/ethanolaminephosphotransferase 1
- Choline/ethanolaminephosphotransferase 2
- Putative phospholipid:diacylglycerol acyltransferase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Triacylglycerol lipase SDP1L
- Triacylglycerol lipase SDP1
- Phosphoinositide phospholipase C 1
- Phosphoinositide phospholipase C 5
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
Sequence:
MVQSETSMEKYKNLSDFLKKFFIPSYVLSPEDEPEAQISCTTAPENPILVFINSKSGGQLGAELILTYRTLLNDKQVFDLEVETPDKVLQRIYLNLERLKDDSLASKIRDKLKIIVAGGDGTAGWLLGVVSDLNLSNPPPIATVPLGTGNNLPFAFGWGKKNPGTDRSSVESFLGKVINAKEMKIDNWKILMRMKHPKEGSCDITLKLPHSLPRIFPSDQENMEGYHTYRGGFWNYFSLGMDAQVSYAFHSQRKLHPERFKNQLVNQSTYLKLSCTQGWFFASLFHPSSQNIAKLAKIQICDRNGQWNDLHIPQSIRSIVCLNLPSFSGGLNPWGTPNPKKQRDRSLTAPFVDDGLIEIVGFRNAWHGLILLSPNGHGTRLAQANRVRLEFKKGAAKHAYMRIDGEPWKQPLPSNDETVMVEISHHGQVNMLATQNCRSKSMYESSSIIRFSNDEDDSSVVENEEF
Protein: Receptor homology region, transmembrane domain- and RING domain-containing protein 1 (AtRMR1) (ReMembR-H2 protein JR700) (Q9M622)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the trafficking of vacuolar proteins. Functions probably as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) by binding the C-terminal vacuolar sorting determinant (VSD) of vacuolar-sorted proteins.
Subcellular location: Prevacuolar compartment membrane. Protein storage vacuole membrane. Golgi apparatus membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes mainly to the prevacuolar compartment of the protein storage vacuole, but a minor portion also localizes to the Golgi complex.
Interaction partners:
- Vacuolar-sorting receptor 1
- Vacuolar-sorting receptor 4
- Vacuolar-sorting receptor 3
- Syntaxin-51
- Vacuolar-sorting receptor 5
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Vacuolar-sorting receptor 2
- Phosphorylase superfamily protein
- At4g24340
- Fanconi anemia group I-like protein
Sequence:
MRLVVSSCLLVAAPFLSSLLRVSLATVVLNSISASFADLPAKFDGSVTKNGICGALYVADPLDGCSPLLHAAASNWTQHRTTKFALIIRGECSFEDKLLNAQNSGFQAVIVYDNIDNEDLIVMKVNPQDITVDAVFVSNVAGEILRKYARGRDGECCLNPPDRGSAWTVLAISFFSLLLIVTFLLIAFFAPRHWTQWRGRHTRTIRLDAKLVHTLPCFTFTDSAHHKAGETCAICLEDYRFGESLRLLPCQHAFHLNCIDSWLTKWGTSCPVCKHDIRTETMSSEVHKRESPRTDTSTSRFAFAQSSQSR
Protein: Ankyrin 2 (A0A5F9ZHQ5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGRASPCLERDNSSFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Phospholipase B1, membrane-associated (Phospholipase B) (Lysophospholipase) (EC 3.1.1.5) (Phospholipase A2) (EC 3.1.1.4) (Phospholipase AdRab-B) (Phospholipase B/lipase) (PLB/LIP) (Triacylglycerol lipase) (EC 3.1.1.3) (Q05017)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate (Probable). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. {ECO:0000250|UniProtKB:O54728}.
Interaction partners:
Sequence:
MALWPSVFLLGLLPLLGRGADQIQTSSGKNTLEGQLWPESLKTFPFPCDPKTLAESVPSESVHSLRPSDIKFVAAIGNVETAPDSGADDLEEQDGTEKRPEQACMGVVTVLSDIIGRFSPSALMPLCPETRLVPRGGAEDLWMQATELVRSMRENPQLDFEHDWKLINVFFSNTSQCFPCPSAQQKGLVLGGMDKLTRTLDYLQQEVPKAFVNLVDLSELAAFSRWRQGAQLSPAAEPCRCLRETSQLTKVLTQWSYLEAWDSLLASSKYNTQESFAVVFQPFFYESSLSALLAEPPLQDPTTLALSLWNRMMEPIGRKEEPFSEKERKPLRCPTQESPYLFTYRNSGQLTRVSQPQGKLEVREGTEIRCPDKDPSDSVPTSVHRLKPADIKVIGAMGDSLTAGNGAGSQPGNILDVLTQYRGLSWSVGGDQNISTVTTLANILREFNPSLQGFSVGTGRETTSQAFFNQAVAGARADGLIPQAQRLVALMKNDTRINFQEDWKIITVFIGGNDLCDFCNDPVRYSPQNFTDNIGTALDILHAEIPRAFVNLVKVLEISKLRELYQETKVSCPRMILRSLCPCVLKFDDNSTEIASLIETIKEYQERTQQLIDSGRYDTRDDFTVVLQPFFEKVNMPKTQDGLPDNSFFAPDCFHFSSKAHAHAASALWNNMLEPVGQKTTHNDFEGAVNITCPNQVWPFLSTYKNSVQGFGTWLPCRDRSPSASPPTSVHALRPADIQVVAALGDSLTAGIGIGSKPNDLSDGTTQYRGLSYSSGGDGSLDNVTTLPNILRQFNSNLMGFAVGTGDASGTNAFFNQAVPGAKARDLMSQVQTLVQRMKDDHRVNFQEDWKVITVQIGASDLCDYCTDSNLYSAANFYDHLRDALDALHREVPRALVNLVDFMNPSVTRQVFLGNPDKCPVQQASALCNCVLSPRENSYELARLEALAQAYQSSLRELVESGRYDTREDFSVVLQPFFHSIQLPVLQDGRLDTSFFAPDCVHPNQKFHSQLSRALWRNMLEPLGGKTDALDLTAAITLTCPTQNEPFLRTFRNSDYTYPSRPAVENWGSDFLCTAWNASRGVPNSVHELQPGDIKVVAALGDSLTLAMGARPSNSSDPPMFWRGLSWSIGGDGALETHTTLPNILKKFNPSILGFSTGTLEGTMGLNVAVQGARAQDMPAQARDLVERMRNSPEIDLEKDWKLVTLFVGGNDLCHFCENPEGSSEGEYVQHIQQALDVLYEELPRTFVNVVEVMELAGLHQDQGGRCATLLAAQSHCTCFKYSQSSVEMQELKKVNWNLQSGLSRLSYSHQYVQREDFAVVVQPFFQNTLVPLNGRGDTDLTFFSDDCFHFSERGHAEMAIALWNNMLEPVGHKTTSNNFTYSRTKLKCPSPDSPYLYTLRNSRLLPDQAEADPTVLYWAVPVAAGAGLLIGILAMVAGRGMRCRPREDPPLSLSTGL
Protein: Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17) (Q9GZT4)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
Interaction partners:
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Phosphoserine phosphatase
- Cystathionine beta-synthase-like protein
- L-serine dehydratase/L-threonine deaminase
- Alanine--glyoxylate aminotransferase
- Serine dehydratase-like
- PRKCA-binding protein
- D-amino-acid oxidase
- Disrupted in schizophrenia 1 protein
Sequence:
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
Protein: SSD domain-containing protein (D2N109)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MRFDCIEKRFAHAFGAYSGVVVRHPFPFFIIPILITAGLSTGLLRHEQAFMKDELELYTPTDAQARKELSQLDHLFHINDSDPFYATRRYDIRRAGYIIVTNQEEDGDILNPLVMHSAMQLWSIVQSLTVEDEDDRRINYPSICVKFPIPPEFSKALHSLFAPNMTTPEEICVSNPLVEIFKLLLVSDRSFLNRSIDEMTLSQISDAIQFDSGGMTHLLGGVTLDDDKRIAGAKAMLLPYALRHSSDDEDWVAEKWEVRLADFLLQYDSPIIRASWWTYETLAAESARDRLQLIHMLLPCFVCVSIFTIACCCVFSWRRSRPWLAIGGVISAAMAIASAVGILLLAGYGMTSVAYSMPFIVFSVGVDNVFILLSAWRSTSSTETLEHRMKETFADAAVSITVTSLTDLISFGVGCATPFPSVQMFCAYAVAAVIFTYIYQLTFFAAVMVYTNRREINNRHCIFFHKLKKDTLPEKIAAQGDRSFEKNTILAQFFRTTYSDFLLNPLVRIVILVTFCVYLGVASYGCTKVKLGLEPNDLLPENSYGKRTLMMAEKYFSDYGSSLHVWMYNLSEVDVAPRKIWNVLEKEVELYEHTEFTASSDSWLRTFLAFVKQAGLLITPENFVYILKNVFLSQPQFAKYNRDVVLTEDGEHLEASRIPVQLRHVGSANQSRAMRFVTYSSLSMKLRKPN
Protein: Ras-related protein Rab-9B (EC 3.6.5.2) (Rab-9-like protein) (Rab-9L) (Q9NP90)
Organism: Homo sapiens (Human)
Function: Involved in the transport of proteins between the endosomes and the trans Golgi network.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing S.aureus or M.tuberculosis.
Interaction partners:
- GRIP and coiled-coil domain-containing protein 2
- Ras-related protein Rab-9A
- Pleckstrin homology domain-containing family M member 2
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Geranylgeranyl transferase type-2 subunit alpha
- Rho-related BTB domain-containing protein 3
- Vacuolar protein sorting-associated protein 33A
Sequence:
MSGKSLLLKVILLGDGGVGKSSLMNRYVTNKFDSQAFHTIGVEFLNRDLEVDGRFVTLQIWDTAGQERFKSLRTPFYRGADCCLLTFSVDDRQSFENLGNWQKEFIYYADVKDPEHFPFVVLGNKVDKEDRQVTTEEAQTWCMENGDYPYLETSAKDDTNVTVAFEEAVRQVLAVEEQLEHCMLGHTIDLNSGSKAGSSCC
Protein: Hairy and enhancer of split-related protein HELT (HES/HEY-like transcription factor) (Protein Hes-like) (Protein megane) (Q7TS99)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGCG-3'. Required for the development of GABAergic neurons.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14764602, ECO:0000269|PubMed:16644143}.
Interaction partners:
- Sodium-dependent proline transporter
Sequence:
MSDRLKERKRTPVSHKVIEKRRRDRINRCLNELGKTVPMALAKQSSGKLEKAEILEMTVQYLRALHSADFPRGREKELLAEFANYFHYGYHECMKNLVHYLTTVERMETKDTKYARILAFLQSKARLGAEPTFPPLSLPEPDFSYQLHAASPEFPGHSPGEATMFPQGATPGSFPWPPGAARSPALPYLSSATVPLPSPAQQHSPFLAPMQGLDRHYLNLIGHGHPNGLNLHTPQHPPVL
Protein: Ubiquitin-like domain-containing protein (Q1NZ18)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVRSSASRRTSDASEQSSPGFVPNYVRNPPFPYAMKNSFDNFSTPPASSVSNGSGSPGPLNSPTYSYGRRDSFNKTRFLLVRTSVEKGKETYKRVTLPGGSDVERLKTTIEKACKGKKVDMIFTLPENDLVESIDQIHRFKDCQKIDVIFKENDRESTPMVTGDAVNMSEEREVSPKDLVVEKNYGQEDIDIPKNDDHEEQEEPRAPTPAEDLSHYVKEPSPPVSLAATDLDSNNGADEGNGEGHDEPKLIPLTTRQSLDSDPGDFEKVDKEEAAKLADTSPAVAGIAAAIPIISAQVEEEQNDPTVLESEHEPSFVPPASAHQAPSTKATVVEESKQVPEGREPSDLATWIHNNPDVVRNVAAAAAVAGVAGLGYYVYVKKFK
Protein: Testis development-related protein (Protein INM01) (Q86YL5)
Organism: Homo sapiens (Human)
Function: Contributes to normal sperm motility, but not essential for male fertility.
Subcellular location: Nucleus {ECO:0000269|PubMed:20170638, ECO:0000269|PubMed:27069551}. Cytoplasm {ECO:0000269|PubMed:20170638, ECO:0000269|PubMed:27069551}. Note=Mainly nuclear. Also detected in cytoplasm near the midpiece of the flagellum. {ECO:0000269|PubMed:27069551}.
Interaction partners:
- F-box only protein 25
Sequence:
MWKLGRGRVLLDEPPEEEDGLRGGPPPAAAAAAQAQVQGASFRGWKEVTSLFNKDDEQHLLERCKSPKSKGTNLRLKEELKAEKKSGFWDNLVLKQNIQSKKPDEIEGWEPPKLALEDISADPEDTVGGHPSWSGWEDDAKGSTKYTSLASSANSSRWSLRAAGRLVSIRRQSKGHLTDSPEEAE
Protein: At5g58530 (Emb|CAB72177.1) (Glutaredoxin family protein) (Q9FGG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein disulfide isomerase-like 1-6
- Thioredoxin-like 1-3, chloroplastic
- MLO-like protein 9
- TPR repeat-containing thioredoxin TTL1
- Probable disease resistance protein At5g66910
- Glutaredoxin-C5, chloroplastic
Sequence:
MWRPWRKSSVKIHDTYSPTTASFKDIHHLCSDDSPSFPSSPSPSPKTASRVFHRVRAANLILKSWPTRQSNHLLRADSEPINLSRNQNPESDSKQSKTKTEPDVRISIPGAEKSIVVYFTSLRVVRPTFEACKSVTSILHSFPVRIDERDLSMDASFSTELQRIFGKDQNQNQNQAKTPKLPRVFIGGRYIGGAEEVKQLHEIGELKKLVQELPKIEPGVCEMCGGHRFVPCKDCHGSHKVHTEKLGFRTCLTCNENGLVRCSSCSFPQSPPP
Protein: TEPSIN adaptor related protein complex 4 accessory protein (A0A1B0GV70)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MAAAPPLRDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTGSAGEAFLSTIQKAAEVVASAMRPGPESPSTRRLLPRGDTYQPAMMPSASHGPPTLGNLLPGAIPGPRAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPGDLAERVEVVALSDCQQELSLVRTVTRGPRAFLSREEAQHFIKACGLLNCEAVLQLLTCHLRGTSECTQLRALCAIASLGSSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA