wanglab/gogpt-training-data huggingface dataset:
Protein: Uricase (EC 1.7.3.3) (Urate oxidase) (Q54LT2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
- Xanthine dehydrogenase
- 5-hydroxyisourate hydrolase
- Allantoicase
Sequence:
MATLIDNRYGKARVRVLRVFKGPNEYHKVFDFDCRVLLRGAEFSETYLTGDNSKVVATDTMKNTVYVIAQKEEFKSLEEYGILLGKHFLATYSWVNGVEVVMRENQWRRIKTSNGKEQAHSFQRDREIHSVTVTSSRDKSPVVVSGIDDLLIMKTTQSGFEGFHRDKYTSLKETKDRVFATVVTANWTYNTLSVDYSKVFEQFKLSVFDIFAQTYSRSVQETLFLIAKDVISKVPQVEQVHLSLPNKHAFGFDFSRLNIENNQTVFQPVEEPSGLIEGTIKRSHSRL
Protein: ATP-dependent DNA helicase YoaA (EC 5.6.2.3) (DNA 5'-3' helicase YoaA) (P76257)
Organism: Escherichia coli (strain K12)
Function: DNA-dependent ATPase and 5'-3' DNA helicase (By similarity). Involved in the repair of replication forks and tolerance of the chain-terminating nucleoside analog 3' azidothymidine (AZT). May unwind potentially damaged 3' nascent ends such as those terminated by AZT, promote repair and AZT excision.
Interaction partners:
- Putative DNA repair helicase RadD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta
- ATP-dependent DNA helicase RecQ
- DNA polymerase III subunit chi
- DNA polymerase III subunit psi
- DNA polymerase I
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- RutC family protein YoaB
Sequence:
MTDDFAPDGQLAKAIPGFKPREPQRQMAVAVTQAIEKGQPLVVEAGTGTGKTYAYLAPALRAKKKVIISTGSKALQDQLYSRDLPTVSKALKYTGNVALLKGRSNYLCLERLEQQALAGGDLPVQILSDVILLRSWSNQTVDGDISTCVSVAEDSQAWPLVTSTNDNCLGSDCPMYKDCFVVKARKKAMDADVVVVNHHLFLADMVVKESGFGELIPEADVMIFDEAHQLPDIASQYFGQSLSSRQLLDLAKDITIAYRTELKDTQQLQKCADRLAQSAQDFRLQLGEPGYRGNLRELLANPQIQRAFLLLDDTLELCYDVAKLSLGRSALLDAAFERATLYRTRLKRLKEINQPGYSYWYECTSRHFTLALTPLSVADKFKELMAQKPGSWIFTSATLSVNDDLHHFTSRLGIEQAESLLLPSPFDYSRQALLCVLRNLPQTNQPGSARQLAAMLRPIIEANNGRCFMLCTSHAMMRDLAEQFRATMTLPVLLQGETSKGQLLQQFVSAGNALLVATSSFWEGVDVRGDTLSLVIIDKLPFTSPDDPLLKARMEDCRLRGGDPFDEVQLPDAVITLKQGVGRLIRDADDRGVLVICDNRLVMRPYGATFLASLPPAPRTRDIARAVRFLAIPSSR
Protein: Fatty-acid and retinol-binding protein 1 (Oo-FAR-1) (Q8WT57)
Organism: Onchocerca ochengi (Filarial nematode worm)
Function: Binds retinol and different fatty acids.
Subcellular location: Secreted {ECO:0000269|PubMed:12106870}.
Interaction partners:
- Crossover junction endonuclease MUS81
- DNA polymerase
- ATP-dependent RNA helicase
- Probable small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
- DNA repair endonuclease XPF
- Probable histone-binding protein lin-53
- DNA_pol_D_N domain-containing protein
- Sm protein F
Sequence:
MYHQLILMALIGVIMANVVPFSMSNIPEEYKEFIPEEVKNFYKNLTQEDRQILRELASKHATFTNEDAALEALKNKSDKLYQKAVELRNFVKAKIDSLKPDAKAFVDEIIAKVRSLRPEDGQKLDMEKLKQAARDIIAKYEALNEETKEELKATFPNTTKIITNEKFKRIANSFLQKN
Protein: ribose-phosphate diphosphokinase (EC 2.7.6.1) (Q57ZX2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transketolase
- Ribose-phosphate pyrophosphokinase, putative
- Ribokinase
- Ribose 5-phosphate isomerase, putative
- Orotidine 5'-phosphate decarboxylase
- NUDIX hydrolase, conserved
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- inorganic diphosphatase
- inorganic diphosphatase
Sequence:
MSKPTVSEEHHADVIRQHLTGIENAYYYNPGNEMAAVHPAEGTVSPRQSQDIQPVCIVAGNGNRPLAEAVALLLGIPTHQTLVAQRASGEVNVRICESVLGADVYIIQSTSGNGLIDVNTAIMELLLLVRKMRLSNARRVTAIIPFFSYSKQDRKRNIRSTISAAAVANMLTTVGVDRVTTLDLHAGQTQGFFGNTPLDNLQMYQEFAQYLHSQVWFNSNNMTIVALSAGSVERARLLADTLNIDQIATVLLRRNASGTVTLQCVGEVKGRICVVVEGICDTGEVLVKTSELLNQLGATKVTACCTHGILTPPCPQLLNECDALSEVVVSDSIPQEEHQRLVPKLKVLTIAPLIATVVFKHTQDASFVPLFEQPKLREGKGSVDSP
Protein: GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Phosphatidylinositol-glycan biosynthesis class B protein) (PIG-B) (Q9JJQ0)
Organism: Mus musculus (Mouse)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- GPI alpha-1,6-mannosyltransferase 2
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI ethanolamine phosphate transferase 1
- GPI alpha-1,4-mannosyltransferase I, stabilizing subunit
- GPI ethanolamine phosphate transferase, stabilizing subunit
- Dolichol-phosphate mannosyltransferase subunit 1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GPI alpha-1,2-mannosyltransferase 4
- GPI ethanolamine phosphate transferase 2
Sequence:
MESQAADYNPASRNLHGSSGEMKLRRRKSRQYVSAQEKRSPRRGLLGENTYLVLFTIALRILNCFLVQTSFVPDEYWQSLEVAHRMVFSYGYLTWEWTERLRGYTYPLIFASIYKVLHLLGKDSVQFLIWIPRLGQALLSAVADIRLYSLLKQLENQEVAQWVFLCQLCSWFTWYCCTRTLTNTMETSLTALALFYYPLEGSRSVNSVKYSLLVALACVVRPTALIPWVPLLFRHFYQEQRKLHLTLHHFLPVGFITFSLSLIIDRIFFGQWTLVQLNFLKFNVLQNLGTFYGSHPWHWYLSQGFPVVLGTHLPFFIHGCFLAPRRLHILLLTVLWTLLVYSMLGHKEFRFIYPVLPFCMVFCGYSLAHLKTWRKAALSFLLLSNVPLAFYTGLVHQRGTLDVMNHIQKVCPRGPDPASASVFIMMPCHSTPYYSHVHCPLSMRFLQCPPDLTGKTQYLDEADMFYLNPLRWLQQEFHSNASLPTHLVTFNVLEKEINTFLTSGNYERAATFFHTHWPERRTGSHIHVYERRLPGRVNTGGN
Protein: Heat shock protein HSP 90-beta (O57521)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Not required for myofibril formation in skeletal muscles.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}.
Interaction partners:
- Prostaglandin E synthase 3
- Stress-induced-phosphoprotein 1
- Protein SGT1 homolog
- Cell division cycle 37 homolog
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
- Receptor
- Receptor-interacting serine-threonine kinase 3.
- Aryl hydrocarbon receptor 1a.
- Receptor-interacting serine-threonine kinase 2.
Sequence:
MPEEMRQEEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELVSNASDALDKIRYESLTDPTKLDSGKDLKIDIIPNVQERTLTLIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVKVDHGEPIGRGTKVILHLKEDQTEYIEEKRVKEVVKKHSQFIGYPITLYVEKERDKEISDDEAEEEKAEKEEKEEEGEDKPKIEDVGSDDEEDTKDKDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDISNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFAELAEDKDNYKKFYDAFSKNLKLGIHEDSQNRKKLSELLRYQSSQSGDEMTSLTEYVSRMKENQKSIYYITGESKDQVAHSAFVERVCKRGFEVLYMTEPIDEYCVQQLKDFDGKSLVSVTKEGLELPEDEDEKKKMEEDKAKFENLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIMETLRQKAEADKNDKAVKDLVILLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDEDEDVPVEEPSSAAAPEDIPPLEGDDDASRMEEVD
Protein: Protein SPT10 (P35208)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for normal transcription at a number of loci in yeast. Affects transcription at Ty1 elements, at PHO5, STE6 and ADH2.
Interaction partners:
- Protein SPT21
- Histone H3
- Histone H2A.1
- Histone H2B.1
- Protein HIR2
- Histone H4
- Histone H2A.2
- Proline utilization trans-activator
- Transcription elongation factor SPT6
- Histone promoter control protein 2
Sequence:
MLNQHTSSVPDDEHLQMAHQNSSSEVRNEAAVPDQLLTPLQPYTILLKDGETIATMYPIPAYPDLLPLGLLNFLLDEFNMEVEKGDSFPYYETLSLEEFKNVWFHNDGHVCIMVLGEIPELDYSMDTEADTNDNFGTEIETTKHTTQYKKRKERRNLNLSMQWEKQCLGIFDLKPAYPGRSAHVVTGTFLVNAGIRGKGIGKTLMETFIEWSKKLGFTSSFFPLIYGTNVGIRRILEGLNFRRIGKLPEAGILKGFDVPVDSFMYGKEFTHITKSIDLLRDPQKSIEIGKYERLKHFLETGKYPLHCDRNEKARLRVLSKTHSVLNGKLMTKGKEIIYDTDQQIQIALEIHLMEHLGINKVTSKIGEKYHWRGIKSTVSEVISRCQKCKMRYKDGTGVIIEQKRAVKQAHMLPTQHIETINNPRKSKKHDNALLGQAINFPQNIISSTLNDVEGEPTPPDTNIVQPTFQNATNSPATTAEANEANKRSEFLSSIQSTPLLDDEQSMNSFNRFVEEENSRKRRKYLDVASNGIVPHLTNNESQDHANPVNRDERDMNHSVPDLDRNDHTIMNDAMLSLEDNVMAALEMVQKEQQQKINHRGEDVTGQQIDLNNSEGNENSVTKIVNNESNTFTEHNSNIYY
Protein: Receptor expression-enhancing protein 3 (Q6NUK4)
Organism: Homo sapiens (Human)
Function: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Probable JmjC domain-containing histone demethylation protein 2C
- Alkaline phosphatase, tissue-nonspecific isozyme
Sequence:
MVSWMISRAVVLVFGMLYPAYYSYKAVKTKNVKEYVRWMMYWIVFALYTVIETVADQTVAWFPLYYELKIAFVIWLLSPYTKGASLIYRKFLHPLLSSKEREIDDYIVQAKERGYETMVNFGRQGLNLAATAAVTAAVKSQGAITERLRSFSMHDLTTIQGDEPVGQRPYQPLPEAKKKSKPAPSESAGYGIPLKDGDEKTDEEAEGPYSDNEMLTHKGLRRSQSMKSVKTTKGRKEVRYGSLKYKVKKRPQVYF
Protein: Cathepsin S (EC 3.4.22.27) (Q02765)
Organism: Rattus norvegicus (Rat)
Function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P25774}.
Interaction partners:
- Myeloperoxidase
- Legumain
- Cathepsin D
- Toll-like receptor 9
- H-2 class II histocompatibility antigen gamma chain
- Cystatin-C
- Matrix metalloproteinase-9
- Complement C1q subcomponent subunit A
- Lysosome-associated membrane glycoprotein 1
- Cathepsin E
Sequence:
MAVLGAPGVLCDNGATAERPTLDHHWDLWKKTRMRRNTDQNEEDVRRLIWEKNLKFIMLHNLEHSMGMHSYSVGMNHMGDMTPEEVIGYMGSLRIPRPWNRSGTLKSSSNQTLPDSVDWREKGCVTNVKYQGSCGSCWAFSAEGALEGQLKLKTGKLVSLSAQNLVDCSTEEKYGNKGCGGGFMTEAFQYIIDTSIDSEASYPYKAMDEKCLYDPKNRAATCSRYIELPFGDEEALKEAVATKGPVSVGIDDASHSSFFLYQSGVYDDPSCTENMNHGVLVVGYGTLDGKDYWLVKNSWGLHFGDQGYIRMARNNKNHCGIASYCSYPEI
Protein: Protein hcp1 (Q9I747)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for assembly of the protein secretion apparatus HSI-I. Actively secreted during chronic infection of cystic fibrosis patients.
Subcellular location: Secreted {ECO:0000269|PubMed:16763151}.
Interaction partners:
- Type VI secretion system spike protein VgrG1a
- AAA+ ATPase ClpV1
- Type VI secretion system sheath protein TssB1
- Type VI secretion system sheath protein TssC1
- Type VI secretion system baseplate subunit TssG
- Type VI secretion system accessory component TagJ
- Type VI secretion system component TssM1
- Type VI secretion system component TssE1
- Type VI secretion system component TssF1
- Type VI secretion system component TssA1
Sequence:
MAVDMFIKIGDVKGESKDKTHAEEIDVLAWSWGMSQSGSMHMGGGGGAGKVNVQDLSFTKYIDKSTPNLMMACSSGKHYPQAKLTIRKAGGENQVEYLIITLKEVLVSSVSTGGSGGEDRLTENVTLNFAQVQVDYQPQKADGAKDGGPVKYGWNIRQNVQA
Protein: Sucrose 1F-fructosyltransferase (EC 2.4.1.99) (O81986)
Organism: Helianthus tuberosus (Jerusalem artichoke) (Helianthus tomentosus)
Interaction partners:
Sequence:
MMASSTTTTPLILHDDPENLPELTGSPTTRRLSIAKVLSGILVSVLVIGALVALINNQTYESPSATTFVTQLPNIDLKRVPGKLDSSAEVEWQRSTYHFQPDKNFISDPDGPMYHMGWYHLFYQYNPQSAIWGNITWGHSVSKDMINWFHLPFAMVPDHWYDIEGVMTGSATVLPNGQIIMLYSGNAYDLSQVQCLAYAVNSSDPLLIEWKKYEGNPVLLPPPGVGYKDFRDPSTLWSGPDGEYRMVMGSKHNETIGCALIYHTTNFTHFELKEEVLHAVPHTGMWECVDLYPVSTVHTNGLDMVDNGPNVKYVLKQSGDEDRHDWYAIGSYDIVNDKWYPDDPENDVGIGLRYDFGKFYASKTFYDQHKKRRVLWGYVGETDPQKYDLSKGWANILNIPRTVVLDLETKTNLIQWPIEETENLRSKKYDEFKDVELRPGALVPLEIGTATQLDIVATFEIDQKMLESTLEADVLFNCTTSEGSVARSVLGPFGVVVLADAQRSEQLPVYFYIAKDIDGTSRTYFCADETRSSKDVSVGKWVYGSSVPVLPGEKYNMRLLVDHSIVEGFAQNGRTVVTSRVYPTKAIYNAAKVFLFNNATGISVKASIKIWKMGEAELNPFPLPGWTFEL
Protein: Cytotoxin 3 (CX3) (Toxin CM-7) (P01446)
Organism: Naja kaouthia (Monocled cobra) (Naja siamensis)
Function: Monomer: shows cytolytic activity. Exhibits concentration-dependent growth inhibitory effects in the lung cell lines A549 (IC(50)=1.22 ug/ml) and NL20 (IC(50)=2.76 ug/ml), in the prostate cell lines PC-3 (IC(50)=4.46 ug/ml) and RWPE-1 (IC(50)=0.65 ug/ml), and in the breast cell lines MCF-7 (IC(50)=12.23 ug/ml) and 184B5 (IC(50)=2.83 ug/ml), with high selectivity for the lung cancer cell line A549 (selectivity index=2.26). Induces primarily necrosis in the A549 cell line, and mainly late apoptosis in the MCF-7 and PC-3 cell lines.
Subcellular location: Secreted {ECO:0000269|PubMed:33263003, ECO:0000269|PubMed:33915327, ECO:0000269|PubMed:7210030}. Target cell membrane {ECO:0000250|UniProtKB:P60301}.
Interaction partners:
Sequence:
LKCNKLIPLAYKTCPAGKNLCYKMFMVSNKTVPVKRGCIDACPKNSLLVKYVCCNTDRCN
Protein: Transcriptional regulator Myc-B (c-Myc-B) (Q7ZVS9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Transcriptional regulator Myc-A
- Protein max
Sequence:
MPLNSSMECKNYDYDYDSYQPYFYFDNEDEDFYNHQHGQPPAPSEDIWKKFELLPTPPLSPSRRPSLSDPFPSTADKLEMVSEFLGDDVVNHSIICDADYSQSFLKSIIIQDCMWSGFSAAAKLEKVVSERLASLQAARKESSRTESADICRSVGFLQDMSTPASQCIDPSVVFPFPLTDSTKPCKPAPTPASTTLPLDTPPNSGSSSSSSDSESDDEDDEDEEEEEEIDVVTVEKRKSVKKSDANATHQSPVVLKRCHVNIHQHNYAAHPSTRNEQPAVKRIKFESHIRVFKQISHNRKCASPRTSDSEDNDKRRTHNVLERQRRNELKLSFFALRDVIPDVANNEKAAKVVILKKATECIASMQEDEQRLISLKEQLRRKCEHLKQRLEQLSCS
Protein: dTDP-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) (Thymidine diphospho-4-keto-rhamnose 3,5-epimerase) (dTDP-4-keto-6-deoxyglucose 3,5-epimerase) (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) (dTDP-L-rhamnose synthase) (P37745)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Interaction partners:
- dTDP-4-dehydrorhamnose reductase
- dTDP-glucose 4,6-dehydratase 1
- Putative O-antigen transporter
- Glucose-1-phosphate thymidylyltransferase 1
- UDP-galactopyranose mutase
- dTDP-glucose 4,6-dehydratase 2
- Glucose-1-phosphate thymidylyltransferase 2
- Putative O-antigen polymerase
- Putative glycosyltransferase WbbK
- Beta-1,6-galactofuranosyltransferase WbbI
Sequence:
MNVIRTEIEDVLILEPRVFGDDRGFFYESFNQSAFEHILGYPVSFVQDNHSRSSKNVLRGLHFQRGEYAQDKLVRCTHGAVFDVAVDIRPNSVSFGKWVGVLLSADNKQQLWIPKGFAHGFLVLSDIAEFQYKTTNYYHPESDCGICWNDERIAIDWPQTSGLILSPKDERLFTLDELIRLKLIA
Protein: Vesicle-associated membrane protein-associated protein A (VAMP-A) (VAMP-associated protein A) (VAP-A) (33 kDa VAMP-associated protein) (VAP-33) (Q9Z270)
Organism: Rattus norvegicus (Rat)
Function: Binds to OSBPL3, which mediates recruitment of VAPA to plasma membrane sites (By similarity). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (By similarity). With OSBPL3, may regulate ER morphology (By similarity). May play a role in vesicle trafficking.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24262037}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9P0L0}. Nucleus membrane {ECO:0000269|PubMed:24262037}. Note=Present in the plasma membrane and in intracellular vesicles, together with SNARE proteins. May also associate with the cytoskeleton. Colocalizes with OCLN at the tight junction in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
Interaction partners:
- Oxysterol-binding protein
- StAR-related lipid transfer protein 3
- Potassium voltage-gated channel subfamily B member 1
- Acyl-CoA-binding domain-containing protein 5
- STARD3 N-terminal like
- Acyl-CoA-binding domain-containing protein 4
- Acyl-CoA-binding domain-containing protein 5
- Protrudin
- Potassium voltage-gated channel subfamily B member 2
- Oxysterol-binding protein-related protein 1
Sequence:
MASASGAMAKHEQILVLDPPSDLKFKGPFTDVVTTNLKLQNPSDRKVCFKVKTTAPRRYCVRPNSGVIDPGSIVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNISDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPLPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSAVSFRDNVTSPLPSLLVVIAAIFIGFFLGKFIL
Protein: Pyruvate carboxylase, mitochondrial (EC 6.4.1.1) (Pyruvic carboxylase) (PCB) (Q05920)
Organism: Mus musculus (Mouse)
Function: Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P11498}.
Interaction partners:
- Citrate synthase
- NADP-dependent malic enzyme
- Citrate synthase, mitochondrial
- Phosphoenolpyruvate carboxykinase, cytosolic
- ATP-citrate synthase
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Pyruvate kinase PKM
- L-lactate dehydrogenase A chain
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Sequence:
MLKFQTVRGGLRLLGVRRSSSAPVASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTFGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVNVSPSPVDPAVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (A0A087WVT9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
Protein: Chromosome transmission fidelity protein 8 (Q65ZA6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Replication factor C (RFC) complex has an essential but redundant activity in sister chromatid cohesion establishment. An RFC-like complex (ctf18-RFC) is formed where ctf18 replaces rfc1 in the RFC complex along with the association of dcc1 and ctf8. This complex is required for efficient establishment of chromosome cohesion during S-phase. Acts as a PCNA loader, loading PCNA onto primed templates.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Sister chromatid cohesion protein dcc1
- Replication factor C subunit 4
- U3 small nucleolar ribonucleoprotein protein imp3
- Replication factor C subunit 5
- Replication factor C subunit 3
- Chromosome transmission fidelity protein 18
- Replication factor C subunit 2
- Decapping nuclease din1
Sequence:
MSEIRLIRAINDELYLVEVQATLERKADSLHIGDLKIIKEKNSEKKKATLTVGNQYMEGVVESLKKPLAVLQKTNADPVDVYSSPSHELKCCSIIRERIRFSSRPLPTK
Protein: Arginase (EC 3.5.3.1) (F1P5B4)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Ornithine aminotransferase
- Ornithine transcarbamylase, mitochondrial
- Ornithine decarboxylase
- Uncharacterized protein
- Argininosuccinate lyase
- Nitric oxide synthase, inducible
- Spermidine synthase
- Glycine amidinotransferase, mitochondrial
- Spermine synthase
- M20_dimer domain-containing protein.
Sequence:
MALRGGFARLFRRRADAGLRLSRRAHSVALVGAPFSRGQKRRGVDHGPATLRAAGLVERLAGLGCQLYDFGDLNFTQVPNDELYNNLIYYPRSVGLASQVLADAVSRAVAAGHSCVTIGGDHSLALGSVSGHARQCPHLGVIWVDAHADINTPLTTQSGNLHGQPLSFLLRELQDKVPQLPGFSWLKPCLSASDIVYIGLRDVDPAEYYILKNYDIQYFSMRDVDRLGIQKVMERTFEQLMGRRQRPIHLSFDIDAFDPSLAPATGTPVLGGLTYREGMYIAEEIHNTGMLSAVDMVEVNPLLGASQEEVNATASLAVDVIATCFGQTREGAHTAFDELPTPSSPDESDSEQQVRI
Protein: Caveolin-2 (Q18879)
Organism: Caenorhabditis elegans
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can regulate their activity. Thought to have a role in the uptake of lipids and proteins in the intestinal cells; operates in the apical uptake of lipid markers and trafficking of yolk proteins. Affects fecundity and egg laying.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Apical cell membrane {ECO:0000269|PubMed:19158391}. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-1
- Tyrosine protein-kinase src-1
- Voltage-dependent calcium channel type A subunit alpha-1
- Voltage-dependent L-type calcium channel subunit alpha
- Voltage-dependent T-type calcium channel subunit alpha
- BTB domain-containing protein
- VWFA domain-containing protein
- CAlcium channel Localization Factor
Sequence:
MTRQNTSESDNTQRPPIPQYDTVDDIDELTDAMDKEDHHHHHHHHEHHHQHQGIAQYDTVEEVETLETVHHRTSLNQEVPTPQRRSHPQYDNLDDIDDQEYITEVEVKSNRGSTLTTRPHVTIKQDEIEDIGERQVTVIEIASQKGSTKRVAPRKDYAPSIPLPEHPAQQSAPPTQQSRPQTTSHKPPNPEMEFDIGVKNIAPVLIHKMNMDDRDPKDSAQYLNTSFFEVFNEPSEQYHSIACVWTLSFKIFEIVRIYSYKILTLIFGLIIAFLGGILFALFAFLNIWIFRPILILTRMAFAQIVLIWPMFLIYIVRPFFYSVGAIFSTARLHTSRGEQVVEVWEKHIHHV