wanglab/gogpt-training-data huggingface dataset:
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic (EC 1.1.1.44) (Q9SH69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:26941195}. Cytoplasm, cytosol {ECO:0000269|PubMed:26941195}.
Interaction partners:
- Probable 6-phosphogluconolactonase 2
- Probable 6-phosphogluconolactonase 1
- 6-phosphogluconolactonase 3, chloroplastic
- Probable 6-phosphogluconolactonase 5
- Probable 6-phosphogluconolactonase 4
- Ribulose-5-phosphate-3-epimerase, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Ribulose-phosphate 3-epimerase
- Ribulose-phosphate 3-epimerase
- Probable ribose-5-phosphate isomerase 4, chloroplastic
Sequence:
MESAALSRIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETLDRAAVEGNLPVSGQYSPRDFVLSIQRPRSLIILVKAGAPVDQTIDAFSEYMEPGDCIIDGGNEWYQNTERRISEAEQKGLLYLGMGVSGGEEGARNGPSLMPGGSFQAYDNIKDILEKVAAQVEDGPCVTYIGEGGSGNFVKMVHNGIEYGDMQLISEAYDVLKNVGGLSNEELAEIFTEWNSGELESFLVEITSDIFRVKDEFGDGELVDKILDKTGMKGTGKWTVQQAAELSVAAPTIAASLDCRYLSGLKDERENAAKVLREAGLKEEIGSASSGIDKKRLVDDVRQALYASKICSYAQGMNLLRAKSLEKSWNLNFGELARIWKGGCIIRAVFLDRIKKAYQRNPDLASLVVDPEFAKEMVQRQAAWRRVVGLAVSAGISTPGMCASLAYFDTYRRARLPANLVQAQRDLFGAHTYERTDRPGAYHTEWTKLARKNH
Protein: Bacteriocin-type signal sequence-containing protein (A3DCU2)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Interaction partners:
- ABC-type bacteriocin transporter
Sequence:
MSEAKKLNIGRELTDEELMEMTGGSTFSIQCQKDYTYKPSLPVVKYGVVIDEPEVVIKYGVGPIVGIKYGVEPIGPIQPMYGIKPVETLK
Protein: Zinc finger protein 750 (Q32MQ0)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in epidermis differentiation. Required for terminal epidermal differentiation: acts downstream of p63/TP63 and activates expression of late epidermal differentiation genes. Specifically binds to the promoter of KLF4 and promotes its expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:22364861}.
Interaction partners:
- Krueppel-like factor 4
- Grainyhead-like protein 3 homolog
- C-terminal-binding protein 1
Sequence:
MSLLKERKPKKPHYIPRPPGKPFKYKCFQCPFTCNEKSHLFNHMKYGLCKNSITLVSEQDRVPKCPKSNSLDPKQTNQPDATAKPASSKSVANGLSAFDSKLQHSSAREDIKENLELQARGTHRCLGQKPALHRASPCKSPAPEAALGAQPALEGAARPSAFVPVGEHRLKGPDNAEAPETLALHNPTAKAVSFHTKSAFHTPGYPWKAGSPFLPPEFPHKISSTKGLGAISPYMHPTIPEYPPHFYTEHGLATIYSPYLLAGSSPECDAPLLSVYGTQDPRHFLPHPGPIPKHLAPSPATYDHYRFFQQYPSNLPIPYGFYRPESAFSSYGLRLPPVTGLTRDQSSHLLEEATLVYPASSPSRLNPSDPNRKHVEFESPIPEAKDSSKAGQRDTEGSKMSPRAGSAATGSPGRPSPTDFMQTSQTCEGLYDLSNKAASSALGRLYPPEQSLTAFRPVKKSTECLPAQAAETTAESPVSLNVVNGDPPAPTGSASLVSEAAPSSPDDSSGMGPLNLSKKSEINLAATHEPTYQGSPQAETASFSELQDLPLNLSVKDPCNTQAPRPAFPGRPRAAEPAAAVPQKTGTEGSEDGPSHPETKPGSLDGDGAPPTGPGEEAPDACAVDSSEEQKQTAAVALCQLAAYSPRNIRVGDGDAAAPEPACRQDTPTLSSMESQEAQCDLRPKGQKRTSLRDAGKSQQGAKKAKLQDTARVFTLRRRARVS
Protein: Functional amyloid transporter FapF (Q9I2F3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Secreted {ECO:0000269|PubMed:15687295}. Cell surface {ECO:0000269|PubMed:15687295}. Cell outer membrane {ECO:0000305|PubMed:23504942}.
Interaction partners:
- Probable functional amyloid protease FapD
- Functional amyloid subunit FapC
- Functional amyloid subunit FapB
- Peptidase C39 domain-containing protein
Sequence:
MTQTLSLRAVLCATTLVSPFLAQAATESEVEALKKELLELRQRYEAQQNALMVLEQRVRQVEAQPQAPQPQRLVKSIQPPAQARNDANAVAGTYGASLKDDGAPAPSVENIYQDASGFFGGGTFSLETGLTYSHYDTRQLFLNGFLALDSIFLGNIGVDQIDADIWTLDLTGRYNWNQRWQVDINAPVVYRESTYQSAGAGGSTSQITEKSVTGDPRLGDVSFGVAYKFLDESESTPDAVVSLRVKAPTGKDPYGIKLKQVPGNNNLNVPDDLPTGNGVWSITPGISLVKTVDPAVLFGSLSYTYNFEESFDDINPQQGVKTGGKVKLGNWFQLGVGVAFALNEKMSMSFSFSELISQKSKVKQDGQSWQTVSGSDANAGYFGLGMTYAVSNRFSIVPSLSIGITPDAPDFTFGVKFPYYF
Protein: REF/SRPP-like protein At2g47780 (O82246)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- WD repeat-containing protein GTS1
Sequence:
MAEDEIVVEEEQSQPQEITPVPPSSSSSPSLVVEDDDEMKLKHLEFIQVAAVYFAACFSTLYELAKDNAGPLKLGVENIEDCVRTVLAPLYEKFHDVPFKLLLFVDRKVDDVFFDVETYVPSLVKQASSQALTVATEVQRTGVVDTTKSIARSVRDKYEPAAEYYAATLWRLLNQLPLFPEVAHLVIPTAFYWSEKYNDAVRYVGDRDYFGAEYLPMIPIEKISDILEQDQCRAD
Protein: UDP-glycosyltransferase 71B1 (EC 2.4.1.-) (Flavonol 3-O-glucosyltransferase UGT71B1) (EC 2.4.1.91) (Q9LSY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses quercetin 3-O-glucosyltransferase activity in vitro. Also active in vitro on benzoates and benzoate derivatives.
Interaction partners:
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
Sequence:
MKVELVFIPSPGVGHIRATTALAKLLVASDNRLSVTLIVIPSRVSDDASSSVYTNSEDRLRYILLPARDQTTDLVSYIDSQKPQVRAVVSKVAGDVSTRSDSRLAGIVVDMFCTSMIDIADEFNLSAYIFYTSNASYLGLQFHVQSLYDEKELDVSEFKDTEMKFDVPTLTQPFPAKCLPSVMLNKKWFPYVLGRARSFRATKGILVNSVADMEPQALSFFSGGNGNTNIPPVYAVGPIMDLESSGDEEKRKEILHWLKEQPTKSVVFLCFGSMGGFSEEQAREIAVALERSGHRFLWSLRRASPVGNKSNPPPGEFTNLEEILPKGFLDRTVEIGKIISWAPQVDVLNSPAIGAFVTHCGWNSILESLWFGVPMAAWPIYAEQQFNAFHMVDELGLAAEVKKEYRRDFLVEEPEIVTADEIERGIKCAMEQDSKMRKRVMEMKDKLHVALVDGGSSNCALKKFVQDVVDNVP
Protein: Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase) (O35331)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00764}.
Interaction partners:
- Pyridoxine-5'-phosphate oxidase
- Chronophin
- Aldehyde oxidase 1
- Aldehyde oxidase 3
- Aldehyde oxidase 2
- Aldehyde oxidase 4
- Pyridoxal phosphate phosphatase PHOSPHO2
- Pyridoxal phosphate homeostasis protein
Sequence:
MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLTSQELHALYEGLKANNVNKYDYVLTGYTRDKSFLGMVVDIVQELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYREKVVPMADIITPNQFEAELLSGRKIHSQEEAFAVMDVLHRMGPDTVVITSSDLPSPKGSDYLMALGSQRMRKPDGSTVTQRIRMEMRKVDPVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSRKDIEDPEIVVQATVL
Protein: Protein NRT1/ PTR FAMILY 7.3 (AtNPF7.3) (Nitrate transporter 1.5) (Q9LQL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity proton-dependent bidirectional nitrate transporter. Involved in nitrate loading into xylem and not in nitrate uptake. Not involved in histidine or dipeptides transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18780802}; Multi-pass membrane protein {ECO:0000269|PubMed:18780802}.
Interaction partners:
- High-affinity nitrate transporter 2.1
- High affinity nitrate transporter 2.4
- High affinity nitrate transporter 2.7
- High-affinity nitrate transporter 2.2
- High affinity nitrate transporter 2.5
- High-affinity nitrate transporter 3.1
- Chloride channel protein CLC-a
- Potassium channel SKOR
- High affinity nitrate transporter
- CBL-interacting serine/threonine-protein kinase 23
Sequence:
MSCLEIYNKDTMKKKEGEEETRDGTVDYYGRPSIRSNSGQWVAGIVILLNQGLATLAFFGVGVNLVLFLTRVLQQNNADAANNVSKWTGTVYIFSLVGAFLSDSYWGRYKTCAIFQVIFVIGLSSLSLSSYMFLIRPRGCGDEVTPCGSHSMMEITMFYFSIYLIALGYGGYQPNIATLGADQFDEEHPKEGYSKIAFFSYFYLALNLGSLFSNTILGYFEDEGMWALGFWASTGSAIIGLILFLVGTPRYRYFKPTGNPLSRFCQVLVAATKKSSVEAPLRGREEMYDGDSEGKNASVNTGRRIVHTDEFKFLDKAAYITARDLDDKKQDSVNPWRLCPVTQVEEVKCILRLMPIWLCTIIYSVVFTQMASLFVEQGAAMNTSVSDFKIPPASMSSFDILSVALFIFLYRRVLEPVANRFKKNGSKGITELHRMGIGLVIAVIAMIAAGIVECYRLKYADKSCTHCDGSSSLSIFWQAPQYSLIGASEVFMYVGQLEFFNAQTPDGLKSFGSALCMMSMSMGNFVSSLLVTMVVKISTEDHMPGWIPRNLNKGHLDRFYFLLAALTSIDLVVYIACAKWYKPIQLEGKDEMQDMSDDDYDTESEEEREKDSKV
Protein: Glucan 1,3-beta-glucosidase D (EC 3.2.1.58) (Exo-1,3-beta-glucanase D) (Q5AVZ7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Rhamnogalacturonase A/B/Epimerase-like pectate lyase domain-containing protein
- Probable glucan endo-1,3-beta-glucosidase eglC
- Probable glucan 1,3-beta-glucosidase A
- glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase
- Glycosyl hydrolases family 32 superfamily
- Probable beta-glucosidase E
Sequence:
MPSQSRSRDRYGRDSDRDRSRVQPRRRYHVSEDDDDDDDFDDNPRDRRYRRDGYRRAPVDSRAYDSHDDYEVVDVEEEPRRYRSDTERRRERARASPGTSPRKRERTRDSGGGHRRRRTEESDGSQAPQAHRDRRSRTRRDRGLDDEDLEDAARRLRRRERERERERRAETSKHKSTDSSNSSAGLLNANALAKLRAQHEELDRQEQRRAEKEAKAERKRRRKRPAVEGQMRTLDPFPDEVPRGQSKGRIVSGAYLEEGRAPDMEVRLRGGGRGPPRERRWEKDSDGSAPLTPFWKRKKWWWIGAIVLVIVVIIIVVAVVVSNNKKSDSDSDSDSNSGSSDSWGGDKSSLNGLDHDSIPKSAQGTVLDPWTWYETTDFNVTYTDETVGGLSVMGLNSTWDDSVAPNENVPPLNKPFPYGSQPIRGVNIGGLLSLEPFITPSLFEGYSSDVVDEYTLTTKLGDNAARKLEEHYATFITEQDFADMAEAGIDHVRIPFSYWAVNPREDEPYVAKISWRYLLRVIEYCRKYGLRVNLDPHGMPGSQNGMNHSGRQGSIRWLNGDDGDTYAQRSLEFHEKISKFFAQDRYKNIITIYGLINEPYMLSLDVEKVLNWTVTAAELVQKNGITAKIAFHDGFLNLSKWKTMLKNGPSNLLLDTHQYTIYNVAQIVLNHTAKVNFVCNDWVGMIGEINSTSEGWGPTICGEFTQADTDCAKNLNNVGRGTRWEGTYSEGDSTMYCPTAEQRTCSCTEANADPSEYSDDYKLFLKTYAEAQMYAFEQAQGWFYWTWHTESAPQWSYKTGWKNGFMPAKAYNPDYKCGDDIPSFGNLPEYY
Protein: H/ACA ribonucleoprotein complex subunit 1 (Nucleolar protein family A member 1) (snoRNP protein GAR1) (Q6AYA1)
Organism: Rattus norvegicus (Rat)
Function: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 3
- H/ACA ribonucleoprotein complex subunit DKC1
- Ribonucloprotein
- Nucleolar protein 56
- Nucleolar protein 58
- rRNA 2'-O-methyltransferase fibrillarin
- Telomerase Cajal body protein 1
- Nucleolar and coiled-body phosphoprotein 1
- Fibrillarin-like 1
- Ribonucloprotein
Sequence:
MSFRGGGRGGFNRGGGGGGFNRGGGSNNHFRGGGGGGGGGGNFRGGGRGGFGRGGGRGGFNKFQDQGPPERVVLLGEFMHPCEDDIVCKCTTEENKVPYFNAPVYLENKEQIGKVDEIFGQLRDFYFSVKLSENMKASSFKKLQKFYIDPYKLLPLQRFLPRPPGEKGPPRGGGGGGGGGRGGRGGGRGGGGRGGGRGGGFRGGRGGGGGFRGGRGGGGGFRGRGH
Protein: ETS variant transcription factor 5 (A0A8I6AQT3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MDGFCDQQVPFMVPGKSRSEDCRGRPVIDRKRKFVDTDLAHDSEELFQDLSQLQEAWLAEAQVPDDEQFVPDFQSDNCSLTEEAGPHQLARAGIEVVLHAPPPTKIKRELHSPSSELSSCSHEQALGAKYGEKCLYNYCAYDRKPPSGFKPLTPPATPLSPTHQNSLFPPPQATLPTSALAPGAGPVQGVGPAPTPHSLPEPGSQQQTFAVPRPPHQPLQMPKMMPESQYPSEQRFQRQLSEPCRPFPPQSGVPGDTRPSYQRQMSEPVVPAAPPPLQGFKQEYHDPLYEHGVPGMPGPPAHGFQSPMGIKQEPRDYCADSEVPNCQSPYMRGRYFSSNHEGFTYEKDPRLYFDDTCVVPERLEGKVKQEPTMYREGPPYQRRGSLQLWQFLVTLLDDPANAHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPDALFSMAFPDNQRPFLKAESDCPLNEEDTLPLTHFEDSPAYLLDMDRCSGLPYAEGFAY
Protein: Potassium channel subfamily K member 10 (Outward rectifying potassium channel protein TREK-2) (TREK-2 K(+) channel subunit) (Q9JIS4)
Organism: Rattus norvegicus (Rat)
Function: Outward rectifying potassium channel. Produces rapidly activating and non-inactivating outward rectifier K(+) currents. Activated by arachidonic acid and other naturally occurring unsaturated free fatty acids.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BUW1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium channel subfamily K member 2
- Potassium channel subfamily K member 9 channel 3)
- Potassium channel subfamily K member 18
- Potassium channel subfamily K member 3 channel 1)
- Potassium channel subfamily K member 1
Sequence:
MKFPIETPRKQVNWDPKVAVPAAAPPVCQPKSATNGHHPVPRLSISSRATVVARMEGASQGGLQTVMKWKTVVAIFVVVVVYLVTGGLVFRALEQPFESSQKNTIALEKAEFLRDHICVSPQELETLIQHALDADNAGVSPVGNSSNSSSHWDLGSAFFFAGTVITTIGYGNIAPSTEGGKIFCILYAIFGIPLFGFLLAGIGDQLGTIFGKSIARVEKVFRKKQVSQTKIRVISTILFILAGCIVFVTIPAVIFKYIEGWTALESIYFVVVTLTTVGFGDFVAGGNAGINYREWYKPLVWFWILVGLAYFAAVLSMIGDWLRVLSKKTKEEVGEIKAHAAEWKANVTAEFRETRRRLSVEIHDKLQRAATIRSMERRRLGLDQRAHSLDMLSPEKRSVFAALDTGRFKASSQESINNRPNNLRLKGPEQLNKHGQGASEDNIINKFGSTSKLTKRKNKDLKKTLPEDVQKIYKTFRNYSLDEEKKEDETEKMCNSDNSSTAMLTECIQQQAEMENGMVPMDTKDQGLENNSLLEDRN
Protein: Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase (GpgP) (MpgP) (EC 3.1.3.70) (EC 3.1.3.85) (C0QRP9)
Organism: Persephonella marina (strain DSM 14350 / EX-H1)
Function: Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively.
Interaction partners:
- Glucosyl-3-phosphoglycerate synthase
- Putative hydroxypyruvate reductase
- Glycosyl transferase, group 2 family
- Phosphate-specific transport system accessory protein PhoU
- histidine kinase
- Phosphate transport system permease protein
- Phosphate transport system permease protein PstA
- Phosphate ABC transporter, ATP-binding protein
Sequence:
MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC
Protein: Protein disulfide-isomerase (EC 5.3.4.1) (Q6FX95)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome H complete sequence
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 70 homolog LHS1
- Tryptophan synthase
- Tubulin beta chain
- Candida glabrata strain CBS138 chromosome D complete sequence
- Dihydrolipoyl dehydrogenase
Sequence:
MLFNKGLLALAATAALGVSAQDAVAPADSAVVKLEQDNFQDFLKENSLVMAEFFAPWCGHCKKLAPEYVKAAEELKSKNVSLVQIDCDDNRDLCMQLQIPGFPSIKLIKDGDIAHAKDYNGARTAEAIVKFMIKQTQPAVQVVEDKAALDALVANSTVPVVVDFGVNDFNATFYQFAHALSDDYVFISLPSKENKISVFLPVEGSSAEEIVFKGDHKTLAKDRSVFEEWLKVESLPFFGEINGEVFNAYLESGLPLAYFFFNEPSEVEENRKFFTDLAKKYRGKMAFVSLDAKQFGRHAENLNMKQQFPLFAIHNMTSNQKFGLPQMAEEEFAKLNKAIKLKTKDITKLVENVLSGKAEAIVKSEEVPSVQESNVFKIVGKTHDKIVADPKKDVLVKYYAPWCGHCKKMAPTYEELADTYASDSSSKDKVVIAEVDATANDIFNVEIAGYPTILLYPAGKNAEPVVYEGDRSLDSFLTFIKENGANGIDGSSLHKKFLETKKAAEQAEIEDDNEDEDGFDDEL
Protein: U2 small nuclear ribonucleoprotein B'' (U2 snRNP B'') (Q9CQI7)
Organism: Mus musculus (Mouse)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P08579}.
Interaction partners:
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein E
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 3
- PHD finger-like domain-containing protein 5A
Sequence:
MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTMEQAAAAANKKPGQGTPNAANTQGTAAPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK
Protein: Beta-galactosidase (EC 3.2.1.23) (A0A8I6G4Z3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
HTAQWMESQLLDVSRLQILGNVSQRTFELDYKRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLKMKMAGLDAIQTYVPWNFHEPQPGQYDFSGDRDVEHFIQLAHQLGLLVILRPGPYICAEWDMGGLPAWLLEKESIVLRSSDPDYLAAVDKWLAVLLPKMKRLLYQNGGPIITVQVENEYGSYFACDYNYLRFLEHRFRYHLGNDIILFTTDGAAEKLLKCGTLQDLYATVDFGTTGNITRAFLIQRNFEPKGPLINSEFYTGWLDHWGQPHSKVNTKKLVASLYNLLAYGASVNLYMFIGGTNFAYWNGANMPYAPQPTSYDYDAPLSEAGDLTEKYFAVRDVIRKFKEVPEGPIPPSTPKFAYGKVALRKFKTVTEALGILCPNGPVKSLYPLTFTQVKQYFGYVLYRTTLPQDCSNPKPIFSSPINGVRDRAYVSVDGVPQGILDRNRMNVLNIRGKAGATLDILVENMGRVNYGNSIKDFKGLISNMTLNFTVLTNWTMFPLDTEALARSHLGNWEAADEGHLDGHSTLRSSNFTLPTFYVGNFSIPSGIPDLPQDTFIQFPGWAKGQVWINGFNLGRYWPTKGPQMTLFVPRNILTTSAPNNITVLELESSPCSNGTLELCTVEFVDTPVIG
Protein: Lens fiber major intrinsic protein (Aquaporin-0) (AQP0) (MIP26) (MP26) (P28238)
Organism: Gallus gallus (Chicken)
Function: Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30301}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6J8I9}. Cell junction {ECO:0000250|UniProtKB:Q6J8I9}. Note=Localizes to thin cell-cell junctions in lens fiber cells. {ECO:0000250|UniProtKB:Q6J8I9}.
Interaction partners:
- Aquaporin 11
- Aquaporin
- Gap junction alpha-8 protein
- Filensin
- Gap junction alpha-3 protein
- Uncharacterized protein
- Beta-crystallin B1
- Aquaporin 3
- Aquaporin 9
- Beaded filament structural protein 2
Sequence:
MRELRSSSFWRAILAEFLGSLLYTLLGLGASLRWAPGPHGVLGSALAFGLAQATLVQALGHVSGGHINPAITLAFLLASQLSLPRALGYLLAQLLGALAGAGVLYGVTPAAVRGTLGLSALHPSVGPGQGTVVELLLTAQFILCVFASFDDRHDGRPGSAALPVGFSLALGHLFGIPFTGAGMNPARSFAPAVITRNFTNHWVFWAGPLLGAALAALLYELALCPRARSMAERLAVLRGEPPAAAPPPEPPAEPLELKTQGL
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (Q9JKA7)
Organism: Rattus norvegicus (Rat)
Function: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. May contribute to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih) (By similarity). May mediate responses to sour stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11675786}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y3Q4}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Sodium channel protein type 2 subunit alpha
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Sodium channel protein type 5 subunit alpha
- Homeobox protein Nkx-2.5
- PEX5-related protein
- Short stature homeobox protein 2
- Inward rectifier potassium channel 2
- T-box transcription factor 18
- Ryanodine receptor 2
Sequence:
MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDGEEEGAGGLQDPSRRSIRLRPLPSPSPSVAAGCSESRGAALGAADSEGPGRSAGKSSTNGDCRRFRGSLASLGSRGGGSGGAGGGSSLGHLHDSAEERRLIAAEGDASPGEDRTPPGLATEPERPGAAAQPAASPPPQQPPQPASASCEQPSADTAIKVEGGAAASDQILPEAEVRLGQSGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFVVDFISSIPVDYIFLIVETRIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPHDCWVSINGMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETKLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVALDRLDRIGKKNSILLHKVQHDLNSGVFNYQENEIIQQIVRHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGPGLGNLGAGQTPRHPRRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPPGLSPLLPSSSSSPPPGACSSPPAPTPSTSTAATTTGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPPPPLPGARGGLGLLEHFLPPPPSSRSPSSSPGQLGQPPGELSPGLAAGPPSTPETPPRPERPSFMAGASGGASPVAFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESMAAFSLYPRAGGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARAASSGGPPLTAAPQREPGARSEPVRSKLPSNL
Protein: Junctional adhesion molecule-like (Dendritic cell-specific protein CREA7) (mCrea7) (Q80UL9)
Organism: Mus musculus (Mouse)
Function: Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20813954}; Single-pass type I membrane protein {ECO:0000269|PubMed:20813954}. Cell junction {ECO:0000250|UniProtKB:Q86YT9}. Note=Localized at the plasma membrane and enriched in areas of cell-cell contacts. {ECO:0000250|UniProtKB:Q86YT9}.
Interaction partners:
- Coxsackievirus and adenovirus receptor homolog
- Plexin-B2
- Immunoglobulin superfamily member 5
- Predicted gene, 49948
Sequence:
MLCLLKLIVIPVILAPVGYPQGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTFHNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPKDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSGSHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEFQRTISPTPPTDKGQQGILNGNQLVIIVGIVCATFLLLPVLILIVKKAKWNKSSVSSMASVKSLENKEKINPEKHIYSSITTWETTERGISGESEGTYMTMNPVWPSSPKASSLVRSSVRSK
Protein: Mitochondrial uncoupling protein 2 (AtPUMP2) (Q9ZWG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PUMPS are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. This leads to a decrease in the efficiency of oxidative phosphorylation and an increase in heat production. May be involved in protecting plant cells against oxidative stress damage (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- At1g72820/F3N23_2
- AT5g26200/T19G15_50
Sequence:
MADFKPRIEISFLETFICSAFAACFAELCTIPLDTAKVRLQLQRKIPTGDGENLPKYRGSIGTLATIAREEGISGLWKGVIAGLHRQCIYGGLRIGLYEPVKTLLVGSDFIGDIPLYQKILAALLTGAIAIIVANPTDLVKVRLQSEGKLPAGVPRRYAGAVDAYFTIVKLEGVSALWTGLGPNIARNAIVNAAELASYDQIKETIMKIPFFRDSVLTHLLAGLAAGFFAVCIGSPIDVVKSRMMGDSTYRNTVDCFIKTMKTEGIMAFYKGFLPNFTRLGTWNAIMFLTLEQVKKVFLREVLYD
Protein: Nociceptin receptor (Kappa-type 3 opioid receptor) (Orphanin FQ receptor) (A0A0R4IZH2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}.
Interaction partners:
Sequence:
MEFPNDSIGFTDPRHFHLYNESLFQNNFSTFNESDSFFPKGFKITIAVVYMIVCVVGLVGNCLVMYVIIRYTKMKTATNIYIFNLALADALVLATLPFQGTDVFLGFWPFGNALCKVVVSIDYYNMFTSVFTLTVMSMDRYVAVCHPVKALDMRTPHKAKVVNICVWVLASAIGVPAMVLGDVEQDNGIECILVLPDPRSYWDPVFGTCVFLLSFLIPVAIISVCYSLMVKRLRSVRILSGSKEKDRNLRRITRMVLVVVAAFVVCWTPIQIMALAQSLGFNLASVQTVVFMHFCIALGYVNSSLNPVLYAFLDENFKRCFREFCHPSRFGIDAQQSGRMRHITREVAFNCKTTDGNSNPA