wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidate cytidylyltransferase 2 (EC 2.7.7.41) (CDP-DAG synthase 2) (CDP-DG synthase 2) (CDP-diacylglycerol synthase 2) (CDS 2) (CDP-diglyceride pyrophosphorylase 2) (CDP-diglyceride synthase 2) (CTP:phosphatidate cytidylyltransferase 2) (Q99L43)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (By similarity). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By similarity). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16023307}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Cardiolipin synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- Phosphatidate phosphatase LPIN3
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysocardiolipin acyltransferase 1
- Phospholipid phosphatase 2
- Phospholipase D1
- Phosphatidate phosphatase LPIN2
- Phosphatidate cytidylyltransferase 1
Sequence:
MTELRQRVVREDAPPEDKESESEAKLDGETASDSESRAETAPLPTSVDDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFALYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSAIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLKSHLTDKGILTSALEDE
Protein: Serine protease 21 (M0R778)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSARGKTLVPLLVVVVAVEVTLQSTSSHVKPVDPEKPELQEANLLSGPCGHRTIPSRIVGGEEAELGRWPWQGSLRVWGNHLCGATLLNRRWVLTAAHCFQKDNDPFDWTVQFGELTSRPSLWNLQAYSNRYQIEDIFLSPKYTEQFPHDIALLKLSSPVTYSNFIQPICLLNSTYKFANRTDCWVTGWGAIGEDESLPLPNNLQEVQVAIINNTMCNHLFKKPDFRINIWGDMVCAGSPEGGKDACFAKLTYAAPQGDSGGPLVCNQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWIRLTMIRNGMLRPDPAPLLLFLTLAWASSSLLRPA
Protein: Ubiquitin carboxyl-terminal hydrolase 40 (Ubiquitin-specific peptidase 40) (F1Q7D2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- GMP synthase
- Glucocorticoid modulatory element-binding protein 2
- Ubiquitin-ribosomal protein eL40 fusion protein
- Glucocorticoid modulatory element-binding protein 1
- Anaphase-promoting complex subunit 11
- DNA
- E3 ubiquitin-protein ligase TRIP12
- Cellular tumor antigen p53
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-specific peptidase 24.
Sequence:
MFGDLFEEDGDGFSSAPGSGVKGRECEPPPPRGKIKLCGIKNQGGTCYLNSLIQTLLFTPEFREELFHLGPDELGCLADKDKPEAKVRVIPLELQRLFSHLLLVDEQTASTTDLTDSFGWTNNEEMGQQDVQELNRILFSALESSLVDTSGSSLIHRLYHGTLVNQITCKECSYISERQEDFLDLTVSVSGVSGLEEALWNMFVEEEMFEGNNLYRCSGCGQLVRAAKSAKLRKLPPFLTISLLRFNFDFTKCERYKETGSYVFPLTFNLRPFCEQSNWPDSEYSYELFSVIIHKGGCYGGHYHVYIKDIDQLGHWEAPEEEKNVKMKVKTQKQENKTEERKTESENSLETEDPLSVLTGILAQEESKCVLVDQLGQKLLNKIGTPWSKKYKKQYGSISKFLQSHPEVFMLISNGTRVALKAGVPTEASPPELVNSTAADSCPENTEPETATAGENEDPDQCHWFDLNDSTVTAITVKDIEKQFQGKESAYMLFYRKTTLKRPPEAIGNPAYKVPPHLLEMVEEENAGLQHKRAEFDASSNSIEVRLHLAPHYHWQNGALHPSAPGEDSIITVTFDRRKTVGDLRLAIYQMQDLWEGDMALTLAKNVPAGLHLYDTLTDDQMSLYSAGVRNGSDLFVWNGREVSGVVVQTGVEWEPVLLTVLRPSVEELGCSEVSDTDGSGLVRFMKGFAGGATLGTVLEALGPQDALLCQEQSRPGASGGGASGWRVFPPQDMQRTLRELFLKDGDALLLLQPEELDSSIFSLSGDVVTVTTPSDCRWLQVEFCPQSGLKEEQEEEEEEQGKKRSKVSASGNMLLAVVKQKAIEELCLQDELGGVECCLRQMDRTGKLLPPVHEHLSVRDAGIRLMTSLYLCPGPVPTATQLFLYFSVGLVPSVGQELEIIVEESLTVKECLKKMLEMTRLEGESWHLRRVDWCEEIGEPLMDENASLKEAKVIYGDTLVLIEGRLPPKGFLKLSVRMYMDMIDSCPELNHSKPQNAEGLATECSGSEMRFMGYVEISEEASLDDFKTQVMTLPALQDVCVPSPAFMRVWLLEGKKLARILRGNQMTLRKLKLGNGAEVCIQRLMKEEDLGLKDLLLRVQMGVPGEKAYYPSEEFLWDAGRDGSPKGLYAALAAHYGLAPDNLLLAKHLPDKHSWMPISNWTQQVSKRKKKRKAESLQAAPFYLKDGDIIGVKNLLIDNNKEFTTLEDEIGQLRLREEVANQNTRGSTVTGESSLDTGSKKTGSAKNRKPEVALSINVGMFR
Protein: Reticulon-4-interacting protein 1, mitochondrial (EC 1.-.-.-) (Q4W4Z2)
Organism: Caenorhabditis elegans
Function: Plays a role in oxygen metabolism in the mitochondria by regulating the levels of reactive oxygen species (ROS) thereby conferring resistance to oxidative stress. Involved in resistance to P.aeruginosa PA14 infection. Regulates lifespan.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21895890}.
Interaction partners:
- Fatty acid synthase
- Probable cytosolic Fe-S cluster assembly factor oxy-4
- Bifunctional glyoxylate cycle protein
- Succinate dehydrogenase cytochrome b560 subunit
- Protein phosphatase 1 regulatory subunit 21 N-terminal domain-containing protein
Sequence:
MIEKMILRRFFSTKSSTMRAWVSENGSGVELKEVPLPVINKPGQVLLKVKAASVNPIDVDMSQGYGREFLGTWKKIESCDAAASRFPLIPGRDCTAVVESVGGDVHNLAPGDEVMAVVPVILPGTHAEFVVTDSKYCSKKPSNLSFVSAAALPYVASTAYSAFTIARVSQRNAKQQRVLIHGGAGGVGSMAIQLLKAWGCEKIVATCAKGSFDIVKQLGAIPVDYTSDQATQELIEHAPFEVILDTVDSQLAKWSDNVMGVWRNCVHVSIVSPLMREMDKNGVPLGLVTTAMKHFERSFQSHLRGRWFSYAFFRPSSDLMSQLSRFAEDGKIVPVVEQVMGFEELEKAYEKVSQLNGRGKTVIKYD
Protein: Lectin alpha chain [Cleaved into: Lectin beta chain; Lectin gamma-1 chain; Lectin gamma-2 chain] (P81637)
Organism: Dioclea guianensis
Function: D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from rat. Induces lymphocyte proliferation and IFNG production.
Interaction partners:
Sequence:
ADTIVAVELDSYPNTDIGDPSYPHIGIDIKSIRSKSTARWNMQTGKVGTAHISYNSVAKRLSAVVSYTGSSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNSIADANSLHFSFNQFSQNPKDLILQSDATTDSDGNLELTKVSSSGDPQGSSVGRALFYAPVHIWEKSAVVAGFDATFTFLIKSPDRDPADGITFFIANTDTSIPSGSGGRLLGLFPDAN
Protein: TATA box-binding protein-like 1 (TBP-like 1) (21 kDa TBP-like protein) (Second TBP of unique DNA protein) (STUD) (TATA box-binding protein-related factor 2) (TBP-related factor 2) (TBP-like factor) (TBP-related protein) (P62380)
Organism: Homo sapiens (Human)
Function: Part of a specialized transcription system that mediates the transcription of most ribosomal proteins through the 5'-TCT-3' motif which is a core promoter element at these genes. Seems to also mediate the transcription of NF1. Does not bind the TATA box.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor IIB
- Transcription initiation factor IIA subunit 1
- Transcription initiation factor IIA subunit 2
- TATA-box-binding protein
- TATA box-binding protein-like 2
- Nuclear transcription factor Y subunit alpha
- X-box-binding protein 1
- Recombining binding protein suppressor of hairless
- Transcription factor Sp1
- Myoblast determination protein 1
Sequence:
MDADSDVALDILITNVVCVFRTRCHLNLRKIALEGANVIYKRDVGKVLMKLRKPRITATIWSSGKIICTGATSEEEAKFGARRLARSLQKLGFQVIFTDFKVVNVLAVCNMPFEIRLPEFTKNNRPHASYEPELHPAVCYRIKSLRATLQIFSTGSITVTGPNVKAVATAVEQIYPFVFESRKEIL
Protein: DNA primase (EC 2.7.7.-) (Late expression factor 1) (P41417)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays an essential role in viral DNA replication. May generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Interaction partners:
Sequence:
MLVCNYTQKRVDMMWDAIAYNDSRKYAFMTVNARWIHADRYFDTSAQLYSYIVQNKVSDVHVKPLDDGGGREWVVDADYKNYVDEHDLMLKIYIGATAFLLFYTEENVSRVMYTGNRGFHLWLKFTDKFKITSAQNVRVHRYKAFEKPAKLDSDYIQPGSFAHCVREAVRLYVPHMQDSNLDALTLQYWPDVDRDIFCNVNKQIRAPYSYNYKGTKFSRCITKELLDKLKQCYPGYGTGGCGPVTTTTTPSPPKIGSMQTTTKSTT
Protein: Arginyl-tRNA--protein transferase 1 (Arginyltransferase 1) (R-transferase 1) (EC 2.3.2.8) (Arginine-tRNA--protein transferase 1) (Q9Z2A5)
Organism: Mus musculus (Mouse)
Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues.
Subcellular location: Nucleus {ECO:0000269|PubMed:16002466}. Cytoplasm {ECO:0000269|PubMed:16002466}.; SUBCELLULAR LOCATION: [Isoform ATE1-1]: Nucleus {ECO:0000269|PubMed:9858543}. Cytoplasm {ECO:0000269|PubMed:33443146, ECO:0000269|PubMed:9858543}.; SUBCELLULAR LOCATION: [Isoform ATE1-2]: Cytoplasm {ECO:0000269|PubMed:9858543}.
Interaction partners:
- E3 ubiquitin-protein ligase UBR1
- E3 ubiquitin-protein ligase UBR2
- Protein N-terminal glutamine amidohydrolase
- Protein N-terminal asparagine amidohydrolase
- E3 ubiquitin-protein ligase UBR4
Sequence:
MASWSAPSPSLVEYFEGQTSFQCGYCKNKLGSRSYGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMDQTCCPQYTIRCHPLQFQPSKSHKKVLKKMLKFLAKGEISKGNCEDEPMDSTVEDAVDGDFALINKLDIKCDLKTLSDLKGSIESEEKEKEKSIKKEGSKEFIHPQSIEEKLGSGEPSHPIKVHIGPKPGKGADLSKPPCRKAREMRKERQRLKRMQQASAAASEAQGQPVCLLPKAKSNQPKSLEDLIFQSLPENASHKLEVRVVRSSPPSPQFRATFQESYQVYKRYQMVVHKDPPDKPTVSQFTRFLCSSPLEAEHPADGPECGYGSFHQQYWLDGKIIAVGVLDILPYCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLHEKTSQLSYYYMGFYIHSCPKMRYKGQYRPSDLLCPETYVWVPIEQCLPSLDNSKYCRFNQDPEAEDEGRSKELDRLRVFHRRSAMPYGVYKNHQEDPSEEAGVLEYANLVGQKCSERMLLFRH
Protein: Temperature shock-inducible protein 1 (EC 3.1.1.-) (P27654)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to have esterase activity. Prefers ester of fatty acids from 4 to 16 carbon atoms.
Subcellular location: Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP) found only in mother cells.
Interaction partners:
Sequence:
MSVSKIAFVLSAIASLAVADTSAAETAELQAIIGDINSHLSDYLGLETGNSGFQIPSDVLSVYQQVMTYTDDAYTTLFSELDFDAITKTIVKLPWYTTRLSSEIAAALASVSPASSEAASSSEAASSSKAASSSEATSSAAPSSSAAPSSSAAPSSSAESSSKAVSSSVAPTTSSVSTSTVETASNAGQRVNAGAASFGAVVAGAAALLL
Protein: Solute carrier family 25 member 19 (J3QLV3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVGYDPKPDGRNNTKFQVAVAGSVSGLVTRALISPFDVIKIRFQLQHERLSRSDPSAKYHGILQASRQILQEEGPTAFWKGHVPAQILSIGYGAVQFLSFEMLTELVHRGSVYDAREFSVHFVCGGLAACMATLTVHPVDVLRTRFAAQGEPK
Protein: N-acetylmuramoyl-L-alanine amidase isoform X1 (Peptidoglycan recognition protein 2) (Peptidoglycan recognition protein long) (A5GZR3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTPGALWIMVMAGICMQSSAVHLRNMEHFITAVAHLEHLNPQLSSLALVSNLCQIADQTHNVTHGFMRSSNNETETHPKIKERLNINLNLSHFFSQALHHFITAAYEEKGVVLTPDGTTVALAPLLLGLESGLRAENVSSQPNGFYLHPLARTLGLSFLNSTPTVRLGAEGCWDSVSAPMVFTLSNFPSLVTDAVVHGGMDGAILGKHLSVVNCSKMNVSTLLRSYYLRTVEELDDVLDPHLKGRNRRQNFQKITSSSLLQEKVAGVLPSQGDAELESLIAKGIKEFVLRYMAIPSKPCLNLQTCSQNMRAMQRFHQKDWGWYDIGYSFVVGSDGYIYEGRGWMSQGAHTKGRNNVGYGVAFIGDYSGRLPSTHDMELVRHHLVKCGVNNGFLQEDFTILGHRQVVVTTSCPGNALYSEITTWMHYKDKDPLK
Protein: Mid1-interacting protein 1 (Gastrulation-specific G12-like protein) (Mid1-interacting G12-like protein) (Protein STRAIT11499 homolog) (Spot 14-related protein) (S14R) (Spot 14-R) (Q6P7D5)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the regulation of lipogenesis in liver. Up-regulates ACACA enzyme activity. Required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol and phospholipid. Involved in stabilization of microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm {ECO:0000250|UniProtKB:Q9CQ20}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQ20}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q9CQ20}.
Interaction partners:
- Thyroid hormone-inducible hepatic protein
Sequence:
MMQICDTYNQKHSLFNAMNRFIGAVNNMDQTVMVPSLLRDVPLSEPDLDNEVSVEVGGSGSCLEERTTPAPSPGSANGSFFAPSRDMYSHYVLLKSIRNDIEWGVLHQPSSPPAGSEEGTWKPKDILVGLSHLESTDAGEEDLEQQFHYHLRGLHTVLSKLTRKANILTNRYKQEIGFSNWGH
Protein: Receptor-type tyrosine-protein phosphatase epsilon (Protein-tyrosine phosphatase epsilon) (R-PTP-epsilon) (EC 3.1.3.48) (P23469)
Organism: Homo sapiens (Human)
Function: Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
- Growth factor receptor-bound protein 2
- Receptor-type tyrosine-protein phosphatase alpha
- WD repeat-containing protein 5
Sequence:
MEPLCPLLLVGFSLPLARALRGNETTADSNETTTTSGPPDPGASQPLLAWLLLPLLLLLLVLLLAAYFFRFRKQRKAVVSTSDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRIRSADDCKQFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCHQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPVHAGPIVVHCSAGVGRTGTFIVIDAMMAMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYTFIYQALLEYYLYGDTELDVSSLEKHLQTMHGTTTHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEYTDYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMIWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGEITIEIKNDTLSEAISIRDFLVTLNQPQARQEEQVRVVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK
Protein: Centrosomal protein of 97 kDa (Cep97) (Leucine-rich repeat and IQ domain-containing protein 2) (Q9CZ62)
Organism: Mus musculus (Mouse)
Function: Acts as a key negative regulator of ciliogenesis in collaboration with CCP110 by capping the mother centriole thereby preventing cilia formation. Required for recruitment of CCP110 to the centrosome (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IW35}. Note=Recruited at the distal end of the mother centriole by MPHOSPH9. {ECO:0000250|UniProtKB:Q8IW35}.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Kinesin-like protein KIF24
- Centrosomal protein of 290 kDa
- Centrosomal protein of 164 kDa
- Centrosomal protein of 104 kDa
- Neuralized-like protein 4
- Centrosomal protein of 83 kDa
- Tau-tubulin kinase 2
Sequence:
MAVARVDGALAPGEGSVVNWSGQGLQKLGANLPCEADVHTLILDKNQIIKLENLEKCKQLIQLSVANNRLVRMMGVAKLTQLRVLNLPHNSIGCVEGLKDLVHLEWLNLAGNNLKTMEQVNSCTALQHLDLSDNNIPQIGDVSKLISLKTLLLHGNIITSLRMAPAYLPRNLSILSLAENEIRDLNEISFLASLSELEQLSIMNNPCVMATPSIPGFDYRPFIVSWCLNLRVLDGYVISQKESLKAEWLYSQGKGRSYRPGQHIQLVQYLATVCPLTSALGLQTAEDAKLEKILSKQRFHQRQLMSQSQDEELSPLAAVETRVHRTPECSSPGQDFQESEPVLQINSWVGISSNDDQLYAVKNNFPAAAHAARYSRNDLHLEDIQTDEDKLNCSLLSSESTFMPVASGLSPVSPTVELRLQGINLGLEDDDGADEFTKGLENQDEDKDKEKSLWDMSESCVEMLKRKISTEVSEAAGLLPCPKSVIISAALKEDTHSLTSLPESAGHSASRTEANSEEAMSPATSEKFPCRILTQRPAALGQDKVTLQKLNAAATKLQACWRGFYTRNYNQQAKGVRYEIRLRRMQEHIVCLTDEVRRLRKERDEERVKTFVQEEAVRFLWNEVRSVQAWQQTVEQRLASWPPDVPPISSTLASPKPPLFPHHQDPSSDQSSDWLVAEDEAAQGRSAPDFPDSGFHSSLTEQVPCLQDSLDFEKSSVESSENSVLGNSADTVKCVKDRDSEATAEEHSDCSRESSASEQDNTLLQQYLTSVQQLDDAAEAADSDDVAGDGKRHLACSPERFDASSDSETHRVASTSQDEISQTPENCQLNEEAQGQPPECDPAFQGLHVGVTVQPV
Protein: Uncharacterized protein (Q38A53)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRTSIIVRWVPKYFKRSIQAPQRQRRGGPTIEATCGRDNKSYPSADARRETVSGHAKKQKARDATVMASKQRVPHPKAFSPHRTPEVRALAEKATTILRCFDQQKLEGQVFSRGIGPDCHSSGLSPSALTKDHCEDAQLRRSKGSLCFMGKTEVLAVLKAVLPPPPLNNAASLSHGDCQRLSEPCGSTRSLLVAIPDDEAANVHGYLRRIRGKAEDKEGDITSIDSAAGGTTLAASMSLRDVTIFLQLYEAVESEDGALLLQLMGVLRRIVFSGHGCEFNEGSPKDTVGVVSQLLVVLSSLGLAEEHVLQRLVSSTGPFLTTPLILNSKESNLIQLLVALHRFGFHHEKCYTACVRALQTAAHRDPLNSFIRHALLKRGSKEPAQLSKGGIRIPRCLNGLTVSDLLEALSGMALSLHRQKVVVDLLLATIVAIVLNEELAMTNKPHLRNPENIVTTADEHAFMQDWISARALQVQRAAKVSEQMELPHPVIPQLFERLAVRYRGLIVDGGDGDISPENVGFYDAVTADLIKVSRSK
Protein: Sodium-dependent organic anion transporter (Soat) (Solute carrier family 10 member 6) (SLC10A6) (Q70EX6)
Organism: Rattus norvegicus (Rat)
Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similarity). May play an important role by delivering sulfoconjugated steroids to specific target cells in reproductive organs (By similarity). May play a role transporting the estriol precursor 16alpha-hydroxydehydroepiandrosterone 3-sulfate (16a-OH-DHEAS) at the fetal blood vessel endothelium (By similarity). Can also transport other sulfoconjugated molecules such as taurolithocholic acid-3-sulfate and sulfoconjugated pyrenes (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/bile acid cotransporter 7
Sequence:
MSADCEGNSTCPANSTEEDPPVGMEGQGSLKLVFTVLSAVMVGLVMFSFGCSVESRKLWLHLRRPWGIAVGLLCQFGLMPLTAYLLAIGFGLKPFQAIAVLIMGSCPGGTVSNVLTFWVDGDMDLSISMTTCSTVAALGMMPLCLYVYTRSWTLPQSLTIPYQSIGITLVSLVVPVASGIYVNYRWPKQATFILKVGAAVGGMLLLVVAVTGVVLAKGWNIDVTLLVISCIFPLVGHVMGFLLAFLTHQSWQRCRTISIETGAQNIQLCIAMMQLSFSAEYLVQLLNFALAYGLFQVLHGLLIVAAYQAYKRRQKSQYRRQHPECQDISSEKQPRETSAFLDKGAEAAVTLGLEQHHRTAELTSHVPSCE
Protein: Polyphosphoinositide phosphatase (EC 3.1.3.-) (Phosphatidylinositol 3,5-bisphosphate 5-phosphatase) (Q7Z9H9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Protein VAC14 homolog
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Phosphoinositide 3-phosphatase
- Phosphatidylinositol 3-kinase pik3
- Autophagy-related protein 18
- Presequence translocated-associated motor subunit pam17
- Probable inositol polyphosphate 5-phosphatase C9G1.10c
- Vacuolar protein sorting-associated protein 38
- Serine/threonine-protein kinase vps15
- Vacuolar protein sorting-associated protein atg6
Sequence:
MPATNSDEPLVKFELYQLKKCYYIVSENATATIFRILKITQSEDELSISIEEAAKILFRQKLQLYLEKLENESADGKLILVTKAYAILGLFRFTAGYYLYLCTERKVVAVIGGHNVYHVDKTQFIELNPSRRHNTSVERKCMSSIEKVDLARTFYFSYSYDLSQTIQYGFTHPIPQHQVRDMFVWNWNMLRPILDSVGIDSPWCIPLIHGFVDQAKLSVYGKPIIVTLIARRSRHFAGARFLRRGIRDDGYVANEVETEQIVFDGSASSFPISSTTPGIPCYTSYVQHRGSIPLRWSQEFSNITPKPPIGIDFHDPFYASTALHFDRLFGHYGIPCIVLNLVKSSEKVKRESLLLDEFESAIQYLNQFLKDSQKIQYIAWDMSAASKKKVPVTKTLEQMASDIVKKTGFFCTADRFFPGTFQTGVVRTNCVDCLDRTNAAQFVIGKCVLAAQLRALGVLDSPQLDYESDAVRLLAEMYHGHGDAIALQYGGSLLVNTLDTYRKNNQWSSTSRDLIESVKRFYSNSFVDFQRQEAISLFLGNFTVHGKIVVFGEKRLQALTEKFKNGQLVRRDYRYWWTPVYVNQELRCKNAYCDSIQRKGIKFPANYFDNVYTPNSISSFSEVLLPNLISTLNFAPLSLIPLLRKSFLPLSYNGFGIEAPSLNPFIPRRNQPRDMFKTSAEEENEDEDEDDDKFRRVSLYKWLFNNEERPVHKFIRKRLHQIPVSNKVQPRDQKQPDFKIPNTDINVYKIHFQYNNISGLADNYTLLSKHDRAMYNNYADYSPDKIKEIKEKELNTYNDYFNSAISENPTLKSDRSEKVAFYSAWITDYKST
Protein: Protein SMALL AUXIN UP-REGULATED RNA 12 (Q9SIG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provide a mechanistic link between auxin and plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), and triggers PM H(+)-ATPases activity by promoting phosphorylation of their C-terminal autoinhibitory domain as a result of PP2C-D subfamily of type 2C phosphatases inhibition, thus leading to the acidification of the apoplast and the facilitation of solutes and water uptake to drive cell expansion (By similarity). Triggers plant growth probably by promoting cell elongation (By similarity). Regulates branch angles and bending (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- Probable magnesium transporter NIPA7
- Uncharacterized protein T32G9.25
- Probable magnesium transporter NIPA6
- At3g12955
Sequence:
MAVKRSSKLTQTAMLKQILKRCSSLAKNQCYDEDGLPVDVPKGHFPVYVGEKRSRYIVPISFLTHPKFKSLLQQAEEEFGFNHDMGLTIPCEEVVFRSLTSMIG
Protein: Fructokinase-2 (EC 2.7.1.4) (ZmFRK2) (Q6XZ78)
Organism: Zea mays (Maize)
Function: May play an important role in maintaining the flux of carbon towards starch formation. May also be involved in a sugar-sensing pathway.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase
- Glucose-6-phosphate isomerase
- Sorbitol dehydrogenase
- fructose-bisphosphatase
- Fructose-1,6-bisphosphatase, chloroplastic
- Glycosyl hydrolase family 31 protein
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha
- Beta-fructofuranosidase, cell wall isozyme
- Mannose-6-phosphate isomerase 1
Sequence:
MAPLGDGGAAAAAASNNLVVSFGEMLIDFVPDVAGLSLAESGGFVKAPGGAPANVACAIAKLGGSSAFVGKFGDDEFGHMLVNILKQNNVNAEGCLFDKHARTALAFVTLKHDGEREFMFYRNPSADMLLTEAELDLGLVRRARVFHYGSISLISEPCRSAHMAAMRAAKAAGVLCSYDPNVRLPLWPSPDAAREGILSIWKEADFIKVSDDEVAFLTRGDANDEKNVLSLWFDGLKLLVVTDGDKGCRYFTKDFKGSVPGFKVDTVDTTGAGDAFVGSLLVNVAKDDSIFHNEEKLREALKFSNACGAICTTKKGAIPALPTVATAQDLIAKAN
Protein: Myeloid leukemia factor 2 (Myelodysplasia-myeloid leukemia factor 2) (Q15773)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- DnaJ homolog subfamily B member 6
- ADP-ribosylation factor GTPase-activating protein 2
- Secretagogin
- Rootletin
Sequence:
MFRFMRDVEPEDPMFLMDPFAIHRQHMSRMLSGGFGYSPFLSITDGNMPGTRPASRRMQQAGAVSPFGMLGMSGGFMDMFGMMNDMIGNMEHMTAGGNCQTFSSSTVISYSNTGDGAPKVYQETSEMRSAPGGIRETRRTVRDSDSGLEQMSIGHHIRDRAHILQRSRNHRTGDQEERQDYINLDESEAAAFDDEWRRETSRFRQQRPLEFRRLESSGAGGRRAEGPPRLAIQGPEDSPSRQSRRYDW
Protein: p53-regulated apoptosis-inducing protein 1 (p53AIP1) (Q9HCN2)
Organism: Homo sapiens (Human)
Function: May play an important role in mediating p53/TP53-dependent apoptosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11030628}.
Interaction partners:
- Cellular tumor antigen p53
- Zinc finger protein 420
Sequence:
MGSSSEASFRSAQASCSGARRQGLGRGDQNLSVMPPNGRAQTHTPGWVSDPLVLGAQVHGGCRGIEALSVSSGSWSSATVWILTGLGLGLSRPFLPGATVLRDRPLGSAFELSYDQKKAPLRLQ
Protein: Low-density lipoprotein receptor-related protein (A0A8I6G721)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
FQISPDLSFPPPPLNFPLLLPPLERRASPLLLFANRRDVRLVDAGGVKLESTIVASGLEDAAAVDFQFSKGAVYWTDVSEEAIKQTYLNQTGAAAQNIVISGLVSPDGLACDWVGKKLYWTDSETNRIEVANLNGTSRKVLFWQDLDQPRAIALDPAHGYMYWTDWGEAPRIERAGMDGSTRKIIVDSDIYWPNGLTIDLEEQKLYWADAKLSFIHRANLDGSFRQKVVEGSLTHPFALTLSGDTLYWTDWQTRSIHACNKWTGEKRKEILSALYSPMDIQVLSQERQPHFHTPCEEGNGGCSHLCLLSPREPFYSCACPTGVQLQDNGKTCKAGAEEVLLLARRTDLRRISLDTPDFTDIVLQVGDIRHAIAIDYDPLEGYVYWTDDEVRAIRRAYLDGSGAQTLVNTEINDPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRKILVSEDLDEPRAIVLHPVMGLMYWTDWGENPKIECANLDGRDRHVLVNTSLGWPNGLALDLQEGKLYWGDAKTDKIEVINIDGTKRQTLLEDKLPHIFGFTLLGDFIYWTDWQRRSIERVHKVKASRDVIIDQLPDLMGLKAVNVAKVVGTNPCADGNGGCSHLCFFTPHATKCGCPIGLELLSDMKTCIIPEAFLVFTSRATIHRISLETNNNDVAIPLTGVKEASALDFDVSNNHIYWTDVSLKTISRAFMNGSSVEHVIEFGLDYPEGMAVDWMGKNLYWADTGTNRIEVARLDGQFRQVLVWRDLDNPRSLALDPTKGYIYWTEWGGKPRIVRAFMDGTNCMTLVDKVGRANDLTIDYADQRLYWTDLDTNMIESSNMLGQERMVIADDLPYPFGLTQYSDYIYWTDWNLHSIERADKTSGRNRTLIQGHLDFVMDILVFHSSRQDGLNDCVHSNGQCGQLCLAIPGGHRCGCASHYTLDPSSRNCSPPSTFLLFSQKFAISRMIPDDQLSPDLILPLHGLRNVKAINYDPLDKFIYWVDGRQNIKRAKDDGTQPSMLTSPSQSLSPDRQPHDLSIDIYSRTLFWTCEATNTINVHRLDGDAMGVVLRGDRDRPRAIAVNAERGYMYFTNMQDHAAKIERASLDGTEREVLFTTGLIRPVALVVDNALGKLFWVDADLKRIESCDLSGANRLTLEDANIVQPVGLTVLGRHLYWIDRQQQMIERVEKTTGDKRTRVQGRVTHLTGIHAVEEVSLEEFSAHPCARDNGGCSHICIAKGDGTPRCSCPVHLVLLQNLLTCGEPPTCSPDQFACATGEIDCIPGAWRCDGFPECADQSDEEGCPVCSASQFPCARGQCVDLRLRCDGEADCQDGSDEANCDEINKPPSDDVPAHSSAIGPVIGIILSLFVMGGVYFVCQRVMCQRYTGASGPFPHEYVGGTPHVPLNFIAPGGSQHGPFPGIPCSNVPLYDRNHVTGASSSSSSSTKATLYPPILNPPPSPATDPSLYNMDMFYSSNIPSTARPYRPYIIRGMAPPTTPCSTDVCDSDYSTSRWKTSKYYLDLNSDSDPYPPPPTPHSQYLSAEDSCPPSPVTERSYCHLFPPPPSPCTDSS