wanglab/gogpt-training-data huggingface dataset:
Protein: oxoglutarate dehydrogenase (succinyl-transferring) (EC 1.2.4.2) (Q383T1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MMRRLSPVNGSVVSPNVVAAVSSVLQRQQRHQSDAPLRRLLYENDSFLSGTSARYIESMYENWKADKSSVNESWNEVFSSRDLQSFERPLLTSPIRVVPASAEDKMEVAQSQDICARLTLMIQAFEDYGHLAARTDPLDAEDDSLHRSPQVKPRERVHLGLESFGFSKEDHDRVVRVGFMDQLGGAMSSSSRAMTIKELHDHLTKCFCGRVGCELGHVDDANVVCFVREVVEGYNTEHNPLRRPLSKEEKLWVWDLVASAVHFEDFFKRKYTTQKRFGCDGAESLIVGLRSLMESASDHGVEKVNFGMAHRGRLNTLYNVIGKSFPVILKEFVGITAPELEPFKVQSDVKYHLGAKSTVKMRNGKLMFTELLANPSHLEAVNPVLQGYTRAAQLKHGDAGQSKVLPVEIHGDAAFAGQGVTFETMCISEVPKFTTGGTIHVVVNNQIGFTTDPRCSRSSPYCSDLGRAFQCPIFHVNGDCPEDVARVFAFAVDLRSRFNKSVVIDLVCYRRYGHNENDDPTITQPLLYKRVHATPDVFARYSEKLVEEGVVTKEQQTAKAKEQKDHYGKYQSEVGNIRYSDYLKSGIPELWRGMKYSDELGEVTLEPTAVARESLQPVIDSLKKVPEGFVVNSKLKAVLEQRVQSLEKGEKIDWGAAEALAFGSLLLEGTHVRVMGQDVERGTFSHRHAVLHDQNKVDTYTPLAHIRKDQAPFIITNSPLNEYGVLGYASGYAIYDPNALVLWEAQFGDFANGAAIIFDQFLSSGETKWNQQQAVVVSLPHGFDGRGAEHSSGRIERFLQAVAEDVDTPAYSPEERAHRVNMEVVFPSTPAQYFHLLRRHVRRNFRKPLMLFFSKQFLRTPNESSMEQITSGGFQPVIGDPSVPPEKARRLVMCTGQIYHILNRYRESNNCGRDVALVRIEELSPFPVAEVQKLLADYSGVELMWAQEEPRNQGAFYHVESRVEYYTGGARELRYAGRAISAAPSTAYKSTHDAEERYICECVFS
Protein: Response regulator CiaR (Q8DU28)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Interaction partners:
- histidine kinase
- histidine kinase
- Serine protease HtrA
- Lipoprotein
- histidine kinase
- histidine kinase
- Response regulator of the competence regulon, ComE response regulator of sakacin A production
Sequence:
MIKLLLVEDDLSLSNSIFDFLDDFADVMQVFDGEEGLYEAESGVYDLILLDLMLPEKNGFQVLKELREKGITTPVLIMTAKEGLDDKGHGFELGADDYLTKPFYLEELKMRIQALLKRSGKFNENNLTYGELTVDTATNTTMVNGKEVELLGKEFDLLVYFLQNQNVILPKSQIFDRIWGFDSDTTISVVEVYVSKIRKKLKDTTFGKNLQTLRSVGYILKDAN
Protein: Mitochondrial glycine transporter (Solute carrier family 25 member 38 homolog) (Q9P6N6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03064}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03064}.
Interaction partners:
Sequence:
MSEIKKTEKLGVKSSKHLAAGALGGFISSTTLQPLDLLKTRCQQSQRDSLPKMVRRIILHEGGVFSLWKGTLPSILRSTTGSSCYFYFLNWLRHFAPQSKNIASSHIQNLWMGGFARAAVGFAFMPVTVIKVRYESNLYSYTTIYSSIRDIWKKEGISGFFRGFGVTALRDAPHAGLYVYFYELSKQNLHKLFDRFSPSSSVQGTVPHRNIVNVMSGLISGATATAITNPFDMLKTRVQLEPHIYKNFLHSAKLVYANEGFRGFLDGFFLRVLRKSISSTITWSVYEWALHRKVIK
Protein: Protein MET1, chloroplastic (PDZ domain, K-box domain, and TPR region containing protein) (Q94BS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in photosystem II supercomplex formation and repair, probably acting as a psbB/psbC chaperone on the stromal side of the membrane.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:25587003}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:25587003}; Peripheral membrane protein {ECO:0000269|PubMed:25587003}; Stromal side {ECO:0000269|PubMed:25587003}. Note=In thylakoids, enriched in stroma lamellae, and also present in grana. {ECO:0000269|PubMed:25587003}.
Interaction partners:
- DUF2996 family protein
- Expressed protein
- Chlorophyll a-b binding protein 6, chloroplastic
- Chlorophyll a-b binding protein 2.2, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 6, chloroplastic
- Chlorophyll a-b binding protein CP29.1, chloroplastic
- Protein CURVATURE THYLAKOID 1B, chloroplastic
- Cysteine-rich receptor-like protein kinase 17
- Chlorophyll a-b binding protein CP29.3, chloroplastic
- Chlorophyll a-b binding protein CP29.2, chloroplastic
Sequence:
MSLAPSSYPSLYSSPSLPRTQQTKQNPSLITQSSFISAKSLFLSSNSASLCNTHVAKRRNLALKASETESSAKAEAGGDGEEEEKYETYEIEVEQPYGLKFRKGRDGGTYIDAILPGGSADKTGKFTVGDRVIATSAVFGTEIWPAAEYGRTMYTIRQRIGPLLMQMEKRNGKAEDTGELTEKEIIRAERNAGYISSRLREIQMQNYLKKKEQKAQREKDLREGLQFSKNGKYEEALERFESVLGSKPTPEEASVASYNVACCYSKLNQVQAGLSALEEALKSGYEDFKRIRSDPDLETLRKSKDFDPLLKQFDESFINESAINAIKSLFGFNKK
Protein: Gadd45b protein (Gadd45b2 protein) (Growth arrest and DNA damage 45 beta) (Growth arrest and DNA-damage-inducible, beta) (Q6PC51)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 4
- Cellular tumor antigen p53
- Cyclin-dependent kinase 1
- Cyclin B1
- Cyclin B2
- Proliferating cell nuclear antigen
- Cyclin B3
- Dual specificity mitogen-activated protein kinase kinase 7
- Cysteine-serine-rich nuclear protein 1b
Sequence:
MTLEEVVGCNITDTKMDTVSQALEELLVAAQRQDCLTVGVYESAKLMNVDPDCVVLCILATDEEDLDDIALQIHFTLLQAFCCDNDINILRVSGLRRLAQVLDEPATVENSEPRDFHCILVTNSQCQPLKCQALKDVGTYCEESRCKNQWIPYLSLQER
Protein: MKL1 protein (A4FUJ8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEAIIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLEARVSEPLLSATSASPTQVVSQLPMGRDSREMLFLAEQPPLPPPPLLPPSLTNGTTIPTAKSTPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDRGAPPMDSSYAKILQQQQLFLQLQILNQQQQQHHNYQAILPAPPKSAGEALGSSGTPPVRSLSTTNSSSSSGAPGPCGLARQNSTSLTGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQISPVPGAPKAPAATSILHKAGEVVVAFPAARLSTGPALVAAGLAPAEVVVATVASSGVVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDTFGEMVTSPLTQLTLQASPLQILVKEEGPRAGSCCLSPGGRAELEGRDKDQMLQEKDKQIEALTRMLRQKQQLVERLKLQLEQEKRAQQPAPAPAPLGTPVKQENSFSSCQLSQQPLGPAHPFNPSLAAPATNHIDPCAVAPGPPSVVVKQEALQPEPEPVPAPQLLLGPQGPGLIKGVAPPTLITDSTGTHLVLTVTNKNADSPGLSSGSPQQPSSQPGSPAPAPSAQMDLEHPLQPLFGTPTSLLKKEPPGYEEAMSQQPKQQENGSSSQQMDDLFDILIQSGGNPRNFSRFQGAAIPAREGEAIPEDSLWVPPGSTAITFC
Protein: Protein cornichon homolog 1 (Q22361)
Organism: Caenorhabditis elegans
Function: Negatively regulates export of glr-1 from the endoplasmic reticulum to synapses.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24094107}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000269|PubMed:24094107}. Cell projection, dendrite {ECO:0000269|PubMed:22213799}.
Interaction partners:
- Glutamate receptor 1
- STarGazin
- Glutamate receptor 2
- STarGazin
- Protein transport protein Sec24C
- Suppressor of lurcher protein 1
- Transmembrane emp24 domain-containing protein bai
- CUB domain-containing protein
- CUB domain-containing protein
- Pre-mRNA-processing factor 19
Sequence:
MAFTFAAFCYLLALIAVGFCIFFAIYTVICVDELRTDYKNPIEQCRNLNQLILPEYIIHGTFTVLFIFSWQLISILANLPLAFYHIYTYAKRPVMSGPGIYDPTTILNRSTLSSTLRISWIKLAFYLVSFFYYLYAMIYTLVTSN
Protein: 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase (DAROPP reductase) (DARP reductase) (EC 1.1.1.302) (2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase) (2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase) (DARIPP synthase) (CglRED) (Q6FU96)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
Interaction partners:
- GTP cyclohydrolase II
- tRNA pseudouridine
- Pseudouridine synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Riboflavin synthase
- Fructose-bisphosphate aldolase
Sequence:
MLRVRDDLPPFLKNYLPDGHRNGRPFVTLTYAQSIDAKIAKQRGVRTTISHIETKEMTHYLRYFHDGILIGSGTVLADDPGLNCKWIGPNNDPDESMEEKSPRPIILDPKLKWKYSGSKMEELCNQGMGKPPIVITTKTPKVKEANVEYMIMEPDANDRISWKSILDTLRRNYDMKSVMIEGGSHVINQLLMCSDLIDSLIVTIGSIYLGSEGVTVSPPDEVKLKDISWWKGTSDVVMCSRLQN
Protein: Effector protein HopM1 (Hrp outer protein M1) (Type III effector HopPtoM) (Q887D0)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Function: Involved in the suppression of basal resistance and promotion of disease symptoms in plants. Mediates the ubiquitination and degradation, via the host proteasome, of a low-abundance immunity-associated protein in Arabidopsis thaliana. May be involved in the inhibition of a host vesicle trafficking pathway.
Subcellular location: Secreted. Host membrane. Note=Secreted via the type III secretion system (T3SS). Localized to the plant endomembrane.
Interaction partners:
- Type III chaperone ShcM
- Type III effector AvrE
- Effector protein HopAB2
- Type III chaperone ShcE
Sequence:
MISSRIGGAGGVELSRVNQQHDTVPAQTAHPNAVTAGMNPPLTPDQSGSHATESSSAGAARLNVAARHTQLLQAFKAEHGTAPVSGAPMISSRAALLIGSLLQAEPLPFEVMAEKLSPERYQLKQFQGSDLQQRLEKFAQPGQIPDKAEVGQLIKGFAQSVADQLEHFQLMHDASPATVGQHAKADKATLAVSQTALGEYAGRASKAIGEGLSNSIASLDEHISALDLTLQDAEQGNKESLHADRQALVDAKTTLVGLHADFVKSPEAKRLASVAAHTQLDNVVSDLVTARNTVGGWKGAGPIVAAAVPQFLSSMTHLGYVRLSTSDKLRDTIPETSSDANMLKASIIGMVAGIAHETVNSVVKPMFQAALQKTGLNERLNMVPMKAVDTNTVIPDPFELKSEHGELVKKTPEEVAQDKAFVKSERALLNQKKVQGSSTHPVGELMAYSAFGGSQAVRQMLNDVHQINGQTLSARALASGFGGAVSASSQTLLQLKSNYVDPQGRKIPVFTPDRAESDLKKDLLKGMDLREPSVRTTFYSKALSGIQSSALTSALPPVTAQAEGASGTLSAGAILRNMALAATGSVSYLSTLYTNQSVTAEAKALKAAGMGGATPMLDRTETALNNIRHPNRESLPHTFQKSTLSGIPRVAENAYHMGRGALQLPTQMAVDTVRVVDEGVLNAVASAREALKQPTKDDDALRALEEGLLDPR
Protein: HTH-type transcriptional regulator SgrR (P33595)
Organism: Escherichia coli (strain K12)
Function: Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions; this repression likely provides one measure of control over sgrR at the level of synthesis. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute-binding domain.
Interaction partners:
- Putative inhibitor of glucose uptake transporter SgrT
- PTS system glucose-specific EIICB component
- Sugar efflux transporter A
- Thiamine-binding periplasmic protein
Sequence:
MPSARLQQQFIRLWQCCEGKSQDTTLNELAALLSCSRRHMRTLLNTMQDRGWLTWEAEVGRGKRSRLTFLYTGLALQQQRAEDLLEQDRIDQLVQLVGDKATVRQMLVSHLGRSFRQGRHILRVLYYRPLRNLLPGSALRRSETHIARQIFSSLTRINEENGELEADIAHHWQQISPLHWRFFLRPGVHFHHGRELEMDDVIASLKRINTLPLYSHIADIVSPTPWTLDIHLTQPDRWLPLLLGQVPAMILPREWETLSNFASHPIGTGPYAVIRNSTNQLKIQAFDDFFGYRALIDEVNVWVLPEIADEPAGGLMLKGPQGEEKEIESRLEEGCYYLLFDSRTHRGANQQVRDWVSYVLSPTNLVYFAEEQYQQLWFPAYGLLPRWHHARTIKSEKPAGLESLTLTFYQDHSEHRVIAGIMQQILASHQVTLKIKEIDYDQWHTGEIESDIWLNSANFTLPLDFSVFAHLCEVPLLQHCIPIDWQADAARWRNGEMNLANWCQQLVASKAMVPLLHHWLIIQGQRSMRGLRMNTLGWFDFKSAWFAPPDP
Protein: Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Q9HYU4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase
- Phospholipid/glycerol acyltransferase domain-containing protein
- Probable non-ribosomal peptide synthetase
- Fatty acid oxidation complex subunit alpha
- 3-methylmercaptopropionyl-CoA dehydrogenase
- Triacylglycerol lipase
- Lipase LipC
- 3-ketoacyl-CoA thiolase
- PvdJ
- PvdL
Sequence:
MIENFWKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIVNFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQK
Protein: Small ribosomal subunit protein uS3m (Ribosomal protein VAR1, mitochondrial) (P02381)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. uS3m is essential for mitochondrial protein synthesis and required for the maturation of small ribosomal subunits.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS46
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS4m
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS47
Sequence:
MKLKLLNMILSMMNKTNNNNNIIINNTLDSLMNKKLLLKNMLLDMNNKKMNNMKRMLNNNNMNPAGANPVVHRIGPAGNINNKLQHLNNMNNWNTQIYNYNKNMEIMNTMNDKLINKLLYKMMTLKLNNMNINKIIMSKTINQHSLNKLNIKFYYYNNDINNNNNNNNNNYYMNMMNKLMNIMNNNMNNNLCNILSYYYKKKVTIEPIKLSYIYLNSDIFSKYISLNDMDKYNNGILTNYQRMLNNIMPKLNDHNISMNYINNINNINNNKYNNMINLLNNNNNINNNNNYNNNNNNYIGNINNIYNNMTIDNIPMDILMYKYLVGWSIKFKGRLSNNNGRTSTTNLLNGTFNNKKYLWSNINNNYKLNYIPSNHNLYNNSNINKNGKYNIKVKLNFI
Protein: Large ribosomal subunit protein mL53 (39S ribosomal protein L53, mitochondrial) (L53mt) (MRP-L53) (Q96EL3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein uL10m
- Large ribosomal subunit protein mL66
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL64
- Large ribosomal subunit protein mL65
- Mitochondrial ribosomal protein L40
- Large ribosomal subunit protein mL45
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL1m
Sequence:
MAAALARLGLRPVKQVRVQFCPFEKNVESTRTFLQTVSSEKVRSTNLNCSVIADVRHDGSEPCVDVLFGDGHRLIMRGAHLTALEMLTAFASHIRARDAAGSGDKPGADTGR
Protein: Sodium/glucose cotransporter 1 (Na(+)/glucose cotransporter 1) (High affinity sodium-glucose cotransporter) (Solute carrier family 5 member 1) (P53790)
Organism: Rattus norvegicus (Rat)
Function: Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (By similarity). Has a primary role in the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception (By similarity). Acts as a water channel enabling passive water transport in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity comparable to aquaporins and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q8C3K6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13866}.
Interaction partners:
- Solute carrier family 2, facilitated glucose transporter member 2
- RGD1563815 protein
- Solute carrier family 2, facilitated glucose transporter member 5
- Taste receptor type 1 member 3
- Receptor protein-tyrosine kinase
- Solute carrier family 15 member 1
- Sodium/hydrogen exchanger 3
- Sodium-dependent glucose transporter 1
- Insulin-2
- Pro-glucagon
Sequence:
MDSSTLSPAVTATDAPIQSYERIRNAADISVIVIYFVVVMAVGLWAMFSTNRGTVGGFFLAGRSMVWWPIGASLFASNIGSGHFVGLAGTGAAAGIAMGGFEWNALVFVVVLGWLFVPIYIKAGVVTMPEYLRKRFGGKRIQIYLSVLSLLLYIFTKISADIFSGAIFINLALGLDIYLAIFILLAITALYTITGGLAAVIYTDTLQTAIMLVGSFILTGFAFREVGGYEAFMDKYMKAIPTLVSDGNITVKEECYTPRADSFHIFRDPITGDMPWPGLIFGLSILALWYWCTDQVIVQRCLSAKNMSHVKAGCTLCGYLKLLPMFLMVMPGMISRILYTDKIACVLPSECKKYCGTPVGCTNIAYPTLVVELMPNGLRGLMLSVMMASLMSSLTSIFNSASTLFTMDIYTKIRKGASEKELMIAGRLFILVLIGISIAWVPIVQSAQSGQLFDYIQSITSYLGPPIAAVFLLAIFCKRVNEPGAFWGLILGFLIGISRMITEFAYGTGSCMEPSNCPKIICGVHYLYFAIILFAISVVTVLVISLLTKPIPDVHLYRLCWSLRNSTEERIDLDAGEEEPVEEDPKDTIEIDAEAPQKEKGCFRKAYDLFCGLDQDKGPKMTKEEEEAMKLKMTDTSEKPLWRTVVNINGIILLAVAVFCHAYFA
Protein: Cyclin-B1-3 (Cyc2-At) (G2/mitotic-specific cyclin-B1-3) (CycB1;3) (Q39069)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B1-2
- Wee1-like protein kinase
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinases regulatory subunit 2
- Cyclin-dependent kinase A-1
- Mitotic spindle checkpoint protein MAD2
- Cyclin-D5-1
- Cyclin-H1-1
Sequence:
MATGPVVHPQPVRGDPIDLKNAAAKNRRALGDIGNVDSLIGVEGGKLNRPITRNFRAQLLENAQVAAAANKKAPILDGVTKKQEVVRAVQKKARGDKREPSKPIEVIVISPDTNEVAKAKENKKKVTYSSVLDARSKAASKTLDIDYVDKENDLAAVEYVEDMYIFYKEVVNESKPQMYMHTQPEIDEKMRSILIDWLVEVHVKFDLSPETLYLTVNIIDRFLSLKTVPRRELQLVGVSALLIASKYEEIWPPQVNDLVYVTDNSYNSRQILVMEKTILGNLEWYLTVPTQYVFLVRFIKASGSDQKLENLVHFLAELGLMHHDSLMFCPSMLAASAVYTARCCLNKTPTWTDTLKFHTGYSESQLMDCSKLLAFIHSKAGESKLRGVLKKYSKLGRGAVALISPAKSLMSSAP
Protein: Beta-adaptin-like protein A (At-bA-Ad) (At-betaA-Ad) (AP complex subunit beta-A) (Adaptor protein complex AP subunit beta-A) (Beta-adaptin A) (Clathrin assembly protein complex beta large chain A) (Q9LDK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Associated with the trans-Golgi network. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). {ECO:0000250}.
Interaction partners:
- AP-4 complex subunit epsilon
- AP-1 complex subunit gamma-1
- AP-1 complex subunit gamma-2
- AP-2 complex subunit sigma
- Clathrin heavy chain 2
- AP-2 complex subunit mu
- Clathrin heavy chain 1
- Pentatricopeptide repeat-containing protein At1g76280
- AP-2 complex subunit alpha-1
- AP-2 complex subunit alpha-2
Sequence:
MAPPAASQRYPSPSQPSGKSEVSDLKTQLRQLAGSRAPGVDDSKRDLYKKVISYMTIGIDVSSVFGEMVMCSATSDIVLKKMCYLYVGNYAKGNPDLSLLTINFLQRDCKDEDPMIRGLALRSLCSLRVPNLVEYLVGPLGSGLKDNNSYVRTIAVTGVLKLYHISPSTCIDADFPATLKSLMLHDSDAQVVANCLSALQEIWSLEASHSEEACREKESLLSKPVIYYFLNRIKEFNEWAQCLILELAVKYVPSDSNDIFDIMNLLEDRLQHANGAVVLATVKVFLQLTLSMTDVHQQVYERIKSPLLTLVSSGSPEQSYAILSHLHLLVVRAPFIFAADYKHFYCQYNEPSYVKKLKLEMLTAVANESNTYEIVTELCEYAANVDIAIARESIRAVGKIALQQYDVNAIVDRLLQFLEMEKDYVTAETLVLVKDLLRKYPQWSHDCISVVGGISSKNIQEPKAKAALIWMLGEYAQDMSDAPYVLENLIENWEEEHSAEVRLHLLTAAMKCFFKRAPETQKALGTALAAGIADFHQDVHDRALFYYRVLQYDVHVAERVVSPPKQAVSVFADTQSSEIKDRVFDEFNSLSVIYQKPSYMFTDKEHRGPFEFSDEVGNISITPEASSDIVPAQQYEANDKDLLLGIDEKDENKGVSNNNGSAYTAPSLESSSNITSQMQELAISGPATSATTPQSFGFDDLFGLGLSTAPAPTPSPPLLKLNARAALDPGAFQQKWRQLPISLTQECSVNPQGIAALTVPQSLIKHMQSHSIHCIASGGQSPNFKFFFFAQKESEPSNYLTECIINTSSAKAQIKVKADEQSTCQAFTTVFETALSKFGMP
Protein: Terminal nucleotidyltransferase 5A (EC 2.7.7.19) (D3Z5S8)
Organism: Mus musculus (Mouse)
Function: Cytoplasmic non-canonical poly(A) RNA polymerase that catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and participates in the cytoplasmic polyadenylation. Polyadenylates mRNA encoding extracellular matrix constituents and other genes crucial for bone mineralization and during osteoblast mineralization, mainly focuses on ER-targeted mRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:33882302}.
Interaction partners:
Sequence:
MHQRYFWTDQGQVAFGGHYMAEGEGYFAMAEDELTGGPYIPLGGDFGGGGSSFGDRCSDYCESPTAHCNVLNWEQVQRLDGILSETIPIHGRGNFPTLELQPSLIVKVVRRRLEEKGIGVRDVRLNGSAASHVLHQDSGLGYKDLDLIFCADLRGEEEFQTVKDVVLDCLLDFLPEGVNKEKITPLTLKEAYVQKMVKVCNDSDRWSLISLSNNSGKNVELKFVDSLRRQFEFSVDSFQIKLDSLLLFYECSENPMTETFHPTIIGESVYGDFHEAFDHLCNKIIATRNPEEIRGGGLLKYCNLLVRGFRPASEEIKTLQRYMCSRFFIDFSDIGEQQRKLESYLQNHFVGLEDRKYDYLMTLHGVVNESTVCLMGHERRQTLNLITMLAIRVLADQNVIPNVANVTCYYQPAPYVADANFSNYYIAQVQPVFTCQQQTYSTWLPCN
Protein: LD27667p (Q95RJ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRILGETSEFFGRANQGPPQSSLRMQRLQPGDECLECQSEGRNHKLRYFYINLEEQLLKCESRSCLWPHNDEVSSDEDLNSEAALPITAPQSELFESPAATLPSHPAALTSKPPPNDDEFILELLQQLTSATETPLKTNVSSSSMPNLHSPSEEKPCPQLELPDLSFLEENSTVCKEPPQALKSELGVPSTVVLPDRLISPPKAKAVQTEDTKAKEHVAHLKGATSQSWQGKAEIPLLPACVKASVRMSPSIKSKGSPFSSPPKKATTQPQGADVVHTGHDALQPWLHHQLVVAQPCGDPLCHHAGALRHRAVLVQP
Protein: Growth hormone secretagogue receptor type 1 (GH-releasing peptide receptor) (Ghrelin receptor) (E7EZL2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Appetite-regulating hormone isoform X1
- Membrane-bound ghrelin O-acyltransferase mboat4
- Growth hormone secretagogue receptor type 1
- Agouti-related neuropeptide.
- Fibronectin type III domain-containing 3Bb.
Sequence:
MTNWTNVSICPLSITLCAENIMDSNATSEDEYPVHLFPVPILTGITVTCSFLFLVGIAGNLLTILVVTKYKDMRTTTNLYLCSMALSDLLIFLCMPLDLYRVWRYRPWNFGDELCKLFQFVSESCTYSTILNITALSVERYFAICFPLRAKVIVTRGRVKGVILLLWTVALCSAGPIFILVGVEHENGTNAWETNECKATEYAIRSGLLTMMVWVSSVFFFLPVLCLTVLYSLIGRRLWRRKENPVGPISSRDKSNKQTVKMLAVVVLAFVLCWLPFHVGRYLVSKSSEANSPVISQISEYCNLVSFVLFYLSAAINPILYNIMSKKFRSAACKLFRVKRAPGRSLQSIVNAESVSVWNEYSWST
Protein: GH19816p (Q8MR52)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLEPPHCSGHSAPTDAMRFETRTDPGQMQNSMSQSQHCKRLSQSSYTNLSNCLVLTPTAQHKLCLETSFTNGSTPHQSGVQPNPRLTSAASSLLSSATTPYDISSALDDSLATVALRQSPSLISAETTATVIVNPEPDAEEIAIPQRLKAVAFDMALTPPPTLPERSMLGRQHSEKKPRSLPLAQVQALRRASDAGAVPGVDLLHDDWYGLAPLASPETLSEISSVSSRTSVPISLANSIERYLQHMGVGVGGPKVPLEDIFESQLHTPKVMRRAPKFSENLAGCAEDTRNLDQYKRLGRVFITFPRIFPDQSPAAHSLDSSDDSFESASAHSLRRLQLPHGANAVQSSKSADPLDGDPDATRQTQPAKKLTFSDSDILTDADCLRLCPHCPCDRDVQRGCCTRSEHGKCGTEISGGCGGAAMGLGSTDTSFYSASSSLEQFATPARQNGGTGASGNHLEEILIRPGVLESHFPVLGGGSAIETPALVAPASPSPLSNGKRPDVVGGRVRKRLSSEEFVFSRSEDLPSLVQIGDRCTGSPAGRRRAKGCVYPAGNSLRLDAAAAVASASASPTSISKFTRTRVAAGGLAAKQAAGNNESNV