wanglab/gogpt-training-data huggingface dataset:
Protein: Rho-related GTP-binding protein RhoG (P84095)
Organism: Homo sapiens (Human)
Function: Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Dedicator of cytokinesis protein 1
- Engulfment and cell motility protein 2
- Engulfment and cell motility protein 1
- Rho GDP-dissociation inhibitor 1
- Rho guanine nucleotide exchange factor 26
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Engulfment and cell motility protein 3
- Kalirin
- Rho GDP-dissociation inhibitor 3
- Kinectin
Sequence:
MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQSAVDGRTVNLNLWDTAGQEEYDRLRTLSYPQTNVFVICFSIASPPSYENVRHKWHPEVCHHCPDVPILLVGTKKDLRAQPDTLRRLKEQGQAPITPQQGQALAKQIHAVRYLECSALQQDGVKEVFAEAVRAVLNPTPIKRGRSCILL
Protein: Synaptosomal-associated protein 47 (SNAP-47) (Synaptosomal-associated 47 kDa protein) (Q6P6S0)
Organism: Rattus norvegicus (Rat)
Function: May play a role in intracellular membrane fusion.
Subcellular location: Endomembrane system {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Appears to be exclusively membrane-bound. {ECO:0000250}.
Interaction partners:
- Syntaxin-3
- Vesicle-associated membrane protein 2
- Syntaxin-4
- Syntaxin-1A
- Syntaxin-12
- Synaptosomal-associated protein 29
- Vesicle-associated membrane protein 7
- Vesicle-associated membrane protein 4
- Vesicle-associated membrane protein 1
- Syntaxin-7
Sequence:
MSSDVRVHTWPCSYYLDLEKQWLPGKLTLTPRSLKFSVDKAEEVLVGLPLSSITEIRKETSLFIFSAITVLEKGQAKHWFSSLRPSRNVVFNIIEHFWRELLLSQPGTAANPTSPMTRGQELMGLMASSQRRMEDTAKVLHHQGEQLDSVMRGLEKMESDLDVADRLLTELETPSWWPFSAKFWKTPVEAKPRDSVSVAPCEPFGKEGVVIRVPAVVSQRTESHSKPGKLTVLVSGLEIHDSSSLLLHRFEKEDVDDIKVHSPYEVSIRQRFIGKPDVAYRLISAKMPEVIPILEVQFSKKIELLEDALVLRSRGRASPAEGGCSIRHAASRLMGCTTHQELPTGGQEGQQSQLQKDWPLLSEGEAQELTQILSKLKGLALDTEAELERQDAALDGITVAVDRATLTVDKHNRRMRKLL
Protein: Activator of lactoyl-CoA dehydratase (Lactoyl-CoA dehydratase component E I) (G3KIM5)
Organism: Anaerotignum propionicum (Clostridium propionicum)
Function: Required for the activation of lactoyl-CoA dehydratase. This protein is extremely sensitive towards oxygen.
Interaction partners:
Sequence:
MYTLGIDVGSASSKAVILKDGKDIVAAEVVQVGTGSSGPQRALDKAFEVSGLKKEDISYTVATGYGRFNFSDADKQISEISCHAKGIYFLVPTARTIIDIGGQDAKAIRLDDKGGIKQFFMNDKCAAGTGRFLEVMARVLETTLDEMAELDEQATDTAPISSTCTVFAESEVISQLSNGVSRNNIIKGVHLSVASRACGLAYRGGLEKDVVMTGGVAKNAGVVRAVAGVLKTDVIVAPNPQTTGALGAALYAYEAAQKK
Protein: FAD:protein FMN transferase (EC 2.7.1.180) (Flavin transferase) (B5XP00)
Organism: Klebsiella pneumoniae (strain 342)
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P41780, ECO:0000269|PubMed:24361839}.
Interaction partners:
Sequence:
MDMTFFRAALLGACVLLSGCDSATTPASPASTATVLDGKTMGTFWRVSVIGVDEAKAEALRAKVQAQLDADDRLLSTWKNDSALMRFNHAADTRPWPVSEAMVDIVTLSLRIGAKTHGAMDITVGPLVNLWGFGPDKQPVTTPDAQAIAAAKARTGLQHLQVINQSGRQFLQKDIPDLFVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALVSRGMNGEGKPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRISHVIDPQTGQPITHKLVSVTVIAPTALEADGWDTGLMVLGPEKAQQVVREQGLAVYMIVKEGEGFKTWMSPQFRTFLVGEKN
Protein: Neutrophil elastase (EC 3.4.21.37) (Elastase-2) (Leukocyte elastase) (Q3UP87)
Organism: Mus musculus (Mouse)
Function: Medullasin modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (By similarity). Capable of killing E.coli; probably digests outer membrane protein A (ompA) in E.coli.
Interaction partners:
- Myeloperoxidase
- Cathepsin G
- Lactotransferrin
- Myeloblastin
- Alpha-1-antitrypsin 1-1
- Alpha-1-antitrypsin 1-2
- Alpha-1-antitrypsin 1-5
- Alpha-1-antitrypsin 1-3
- Alpha-1-antitrypsin 1-4
- Antileukoproteinase
Sequence:
MALGRLSSRTLAAMLLALFLGGPALASEIVGGRPARPHAWPFMASLQRRGGHFCGATLIARNFVMSAAHCVNGLNFRSVQVVLGAHDLRRQERTRQTFSVQRIFENGFDPSQLLNDIVIIQLNGSATINANVQVAQLPAQGQGVGDRTPCLAMGWGRLGTNRPSPSVLQELNVTVVTNMCRRRVNVCTLVPRRQAGICFGDSGGPLVCNNLVQGIDSFIRGGCGSGLYPDAFAPVAEFADWINSIIRSHNDHLLTHPKDREGRTN
Protein: Splicing factor 45 (45 kDa-splicing factor) (RNA-binding motif protein 17) (Q8JZX4)
Organism: Mus musculus (Mouse)
Function: Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- ATP-dependent RNA helicase DHX15
- U2 snRNP-associated SURP motif-containing protein
- Calcium homeostasis endoplasmic reticulum protein
- Splicing factor 3B subunit 1
- SURP and G-patch domain-containing protein 1
- U2 small nuclear ribonucleoprotein A'
- Ataxin-1
- Splicing factor 3A subunit 3
- Probable ATP-dependent RNA helicase DDX46
- Splicing factor 3A subunit 2
Sequence:
MSLYDDLGVETSDSKTEGWSKNFKLLQSQLQVKKAALTQAKSQRTKQSTVLAPVIDLKRGGSSDDRQIADTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFSRRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEPDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSKRGGKIIVGDATEKGEAQDASKKSDSNPLTEILKCPTKVVLLRNMVGAGEVDEDLEVETKEECEKYGKVGKCVIFEIPGAPDDEAVRIFLEFERVESAIKAVVDLNGRYFGGRVVKACFYNLDKFRVLDLAEQV
Protein: UDP-glucose 4-epimerase (EC 5.1.3.2) (Q8T8E9)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MRVLVCGGAGYIGSHFVRALLRDTNHSVVIVDSLVGTHGKSDHVETRENVARKLQQSDGPKPPWADRYAALEVGDVRNEDFLNGVFTRHGPIDAVVHMCAFLAVGESVRDPLKYYDNNVVGILRLLQAMLLHKCDKIIFSSSAAIFGNPTMGSVSTNAEPIDINAKKSPESPYGESKLIAERMIRDCAEAYGIKGICLRYFNACGAHEDGDIGEHYQGSTHLIPIILGRVMSDIAPDQRLTIHEDASTDKRMPIFGTDYPTPDGTCVRDYVHVCDLASAHILALDYVEKLGPNDKSKYFSVFNLGTSRGYSVREVIEVARKTTGHPIPVRECGRREGDPAYLVAASDKAREVLGWKPKYDTLEAIMETSWKFQRTHPNGYASQENGTPGGRTTKL
Protein: Syntaxin, putative (Q580R8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vesicle transport v-SNARE N-terminal domain-containing protein
- Gamma-soluble NSF attachment protein
- Syntaxin, putative
- Soluble N-ethylmaleimide sensitive factor
- Soluble N-ethylmaleimide sensitive factor
- Paraflagellar rod component
- Vacuolar protein sorting-associated protein 45, putative
- Vesicle-associated membrane protein, putative
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
Sequence:
MDDPSWQRNCDMLTHALQSLERSTSQIKRSTNKLVTLRDIAQERDKVKKVTSAANAKDVHAVHDALAFLEKYMRLHPTQLRGQGVKLSTEAQVVLENYKKSCDVFYKKCISLEESLRKNSATTRVRIGTGDGSDVDDFDDEGESLLPRGATAGSAQRQAFEDDLHNEIMAERVRETSEIAESVRDINELFNHINSLVAEQGVGLEIIEENVTRSSAATRNAVGHLQQARDSQQRSGRDKMFIFLIVVLMIMLLLVAYHKV
Protein: Deoxyribonuclease Tat-D (EC 3.1.21.-) (P34220)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has both endo- and exonuclease activities. Incises double-stranded DNA without obvious specificity via its endonuclease activity and excises the DNA from the 3'-to 5'-end by its exonuclease activity. May have a role in apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pro-apoptotic serine protease NMA111
Sequence:
MWGILLKSSNKSCSRLWKPILTQYYSMTSTATDSPLKYYDIGLNLTDPMFHGIYNGKQYHPADYVKLLERAAQRHVKNALVTGSSIAESQSAIELVSSVKDLSPLKLYHTIGVHPCCVNEFADASQGDKASASIDNPSMDEAYNESLYAKVISNPSFAQGKLKELYDLMNQQAKPHDTSFRSIGEIGLDYDRFHYSSKEMQKVFFEEQLKISCLNDKLSSYPLFLHMRSACDDFVQILERFIAGFTDERDTFQLQKLGASSSSGFYKFHPDRKLVVHSFTGSAIDLQKLLNLSPNIFIGVNGCSLRTEENLAVVKQIPTERLLLETDAPWCEIKRTHASFQYLAKYQEVRDFEYPAFKSVKKNKLADKLNAEELYMVKGRNEPCNMEQVAIVVSEVKDVDLATLIDTTWKTTCKIFGE
Protein: Protein patched (Hedgehog receptor) (P18502)
Organism: Drosophila melanogaster (Fruit fly)
Function: Segmentation polarity protein. Acts as a receptor for the hedgehog protein (HH). Associates with the smoothened protein (SMO) to transduce the hedgehog signal leading to the activation of wingless, decapentaplegic and patched itself. Participates in cell interactions that establish pattern within the segment and the imaginal disks during development. In the absence of HH, represses the constitutive signaling activity of smo through fused (FU).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Protein hedgehog
- Interference hedgehog
- Protein smoothened
- Brother of ihog, isoform G
- Suppressor of fused homolog
- E3 ubiquitin-protein ligase Smurf1
- Transcriptional activator cubitus interruptus
- Kinesin-like protein costa
- Dally-like, isoform A
- Protein dispatched
Sequence:
MDRDSLPRVPDTHGDVVDEKLFSDLYIRTSWVDAQVALDQIDKGKARGSRTAIYLRSVFQSHLETLGSSVQKHAGKVLFVAILVLSTFCVGLKSAQIHSKVHQLWIQEGGRLEAELAYTQKTIGEDESATHQLLIQTTHDPNASVLHPQALLAHLEVLVKATAVKVHLYDTEWGLRDMCNMPSTPSFEGIYYIEQILRHLIPCSIITPLDCFWEGSQLLGPESAVVIPGLNQRLLWTTLNPASVMQYMKQKMSEEKISFDFETVEQYMKRAAIGSGYMEKPCLNPLNPNCPDTAPNKNSTQPPDVGAILSGGCYGYAAKHMHWPEELIVGGAKRNRSGHLRKAQALQSVVQLMTEKEMYDQWQDNYKVHHLGWTQEKAAEVLNAWQRNFSREVEQLLRKQSRIATNYDIYVFSSAALDDILAKFSHPSALSIVIGVAVTVLYAFCTLLRWRDPVRGQSSVGVAGVLLMCFSTAAGLGLSALLGIVFNAASTQVVPFLALGLGVDHIFMLTAAYAESNRREQTKLILKKVGPSILFSACSTAGSFFAAAFIPVPALKVFCLQAAIVMCSNLAAALLVFPAMISLDLRRRTAGRADIFCCCFPVWKEQPKVAPPVLPLNNNNGRGARHPKSCNNNRVPLPAQNPLLEQRADIPGSSHSLASFSLATFAFQHYTPFLMRSWVKFLTVMGFLAALISSLYASTRLQDGLDIIDLVPKDSNEHKFLDAQTRLFGFYSMYAVTQGNFEYPTQQQLLRDYHDSFVRVPHVIKNDNGGLPDFWLLLFSEWLGNLQKIFDEEYRDGRLTKECWFPNASSDAILAYKLIVQTGHVDNPVDKELVLTNRLVNSDGIINQRAFYNYLSAWATNDVFAYGASQGKLYPEPRQYFHQPNEYDLKIPKSLPLVYAQMPFYLHGLTDTSQIKTLIGHIRDLSVKYEGFGLPNYPSGIPFIFWEQYMTLRSSLAMILACVLLAALVLVSLLLLSVWAAVLVILSVLASLAQIFGAMTLLGIKLSAIPAVILILSVGMMLCFNVLISLGFMTSVGNRQRRVQLSMQMSLGPLVHGMLTSGVAVFMLSTSPFEFVIRHFCWLLLVVLCVGACNSLLVFPILLSMVGPEAELVPLEHPDRISTPSPLPVRSSKRSGKSYVVQGSRSSRGSCQKSHHHHHKDLNDPSLTTITEEPQSWKSSNSSIQMPNDWTYQPREQRPASYAAPPPAYHKAAAQQHHQHQGPPTTPPPPFPTAYPPELQSIVVQPEVTVETTHSDSNTTKVTATANIKVELAMPGRAVRSYNFTS
Protein: Cytochrome P450 4A12A (EC 1.14.14.1) (CYPIVA12) (Q91WL5)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids. May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney. Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Further catalyzes successive omega-oxidations of 20-HETE to the corresponding dicarboxylic acid, and may contribute to the degradation of PUFA by chain shortening. Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoc acid (EPA). Catalyzes stereoselective epoxidation of the last double bond of EPA, displaying a strong preference for the (R,S) stereoisomer. Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Prostaglandin G/H synthase 2
- Cytochrome P450 2U1
- Cytochrome P450 1A1
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Prostaglandin G/H synthase 1
- Polyunsaturated fatty acid lipoxygenase ALOX12
- Polyunsaturated fatty acid
Sequence:
MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKLQ
Protein: Probable G-protein coupled receptor 25 (O00155)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAPTEPWSPSPGSAPWDYSGLDGLEELELCPAGDLPYGYVYIPALYLAAFAVGLLGNAFVVWLLAGRRGPRRLVDTFVLHLAAADLGFVLTLPLWAAAAALGGRWPFGDGLCKLSSFALAGTRCAGALLLAGMSVDRYLAVVKLLEARPLRTPRCALASCCGVWAVALLAGLPSLVYRGLQPLPGGQDSQCGEEPSHAFQGLSLLLLLLTFVLPLVVTLFCYCRISRRLRRPPHVGRARRNSLRIIFAIESTFVGSWLPFSALRAVFHLARLGALPLPCPLLLALRWGLTIATCLAFVNSCANPLIYLLLDRSFRARALDGACGRTGRLARRISSASSLSRDDSSVFRCRAQAANTASASW
Protein: Alpha-tocopherol transfer protein (Alpha-TTP) (Q8BWP5)
Organism: Mus musculus (Mouse)
Function: Binds (+)-alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MAEMRPGPLVGKQLNELPDHSPLLQPGLAELRRRVQEAGVPQTPQPLTDAFLLRFLRARDFDLDLAWRLMKNYYKWRAECPELSADLRPRSILGLLKAGYHGVLRSRDSTGSRVLIYRIAYWDPKVFTAYDVFRVSLITSELIVQEVETQRNGVKAIFDLEGWQVSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKDRIHLHGNNYKSSMLQHFPDILPREYGGKEFSMEDICQEWTNFIMKSEDYLSSISETIQ
Protein: Spliceosome protein-like protein (Q9C5M7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small nuclear ribonucleoprotein SmD1a
- Small nuclear ribonucleoprotein SmD1b
Sequence:
MMTNSDSDHCTPAKTSISGDGLEKESDFKKQLNSEIDPQASSSQNDAITMEDGAVSVNNRDLQEIKESSFSKGSEQYRVDGALEESLNFEEKEQESEAQRLLEAEKRRLLAEIELGSIFRKSVDVDTLPKIEETMDNDVDKIELVDHTALVDVVHHPKRPGTAQNEKDTPRKLKKIGDKRNVIEGSGVENNGKQFRRLYTRKQLESMRFAHIVNQKNLWSEMYSRILPEVVTEYESLVYVKNYKSSKSNRVRGRTESGNEENLGTEEGTEDPEDYTDDNDDYNSILRPAFEVDGEPDFSTGPPEDGLEYLRRVRWEAKGIPNVRVAKIDESTYIKKEQSVYMPLIPEIPKCPEYLLPMKEWEDSLLLDFVHLRQTLTQSANSCEDEIISSQCVEDLLVEMFNKHLHTEEDESFGEVVTDIQGMDSVTRVSKLKKRICLVEKESGLQSSDCKWVVALCASLETPLDADTCACLRGLLRKCASVRAETSLEVGDEEVITMANMLITIAGRYFGQMGQ
Protein: Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)] (P61812)
Organism: Homo sapiens (Human)
Function: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Transforming growth factor beta receptor type 3
- Latent-transforming growth factor beta-binding protein 3
- Latent-transforming growth factor beta-binding protein 1
- Mothers against decapentaplegic homolog 3
- Transforming growth factor beta-1 proprotein
- Latent-transforming growth factor beta-binding protein 2
- Mothers against decapentaplegic homolog 2
- Transforming growth factor beta-3 proprotein
Sequence:
MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS
Protein: Large ribosomal subunit protein uL16m (60S ribosomal protein L16, mitochondrial) (Q2F932)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MEKHLVMYLTRKSIMLLRKYPLVTEFQVSKCGSHIVKIRRDVLYPKRTKYSKYSKCRCSRGCEPDGTQLGFGRYGTKSCRAGRLSYRAIEAARRATIGQFHRAMSGQFRRNCKIWVRVLADLPITGKPAEVRMGRGKGNPTGWIARVSTGQIPFEMDGVSLSNARQAARLAAHKPCSSTKFVQWS
Protein: 18 kDa seed maturation protein (Q01417)
Organism: Glycine max (Soybean) (Glycine hispida)
Interaction partners:
- Protein SLE3
- Abscisic acid receptor PYL4
- Abscisic acid receptor PYL4
- Abscisic acid receptor PYL4
- Uncharacterized protein
- Abscisic acid receptor PYL6
- Protein SLE2
- Seed maturation protein PM30
- Seed maturation protein PM28
- 51 kDa seed maturation protein
Sequence:
MQGGKKAGESIKETATNIGASAKAGMEKTKATVQEKAERMTARDPVQKELATQKKEAKMNQAELDKQAARQHNTAAKQSATTAGHMGHGHHTTGTGTGTATYSTTGEYGQPMGAHQTSAMPGHGTGQPTGHVTEGVVGSHPIGTNRGPGGTATAHNTRAGGKPNDYGYGTGGT
Protein: Cell division protein DivIC (P37471)
Organism: Bacillus subtilis (strain 168)
Function: Required for vegetative and sporulation septum formation. Required for the activation of genes expressed under the control of the sporulation transcription factors sigma F and sigma E.
Interaction partners:
- Cell division protein DivIB
- Cell division protein FtsL
- Septation ring formation regulator EzrA
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsZ
- Cell division protein FtsA
- Penicillin-binding protein 2B
- Cell division protein SepF
- Cell division protein ZapA
- Uncharacterized protein YabR
Sequence:
MNFSRERTITEIQNDYKEQVERQNQLKKRRRKGLYRRLTVFGALVFLTAIVLASSVWSQTSSLSAKEEKKEQLEKELKSLKTKQTDLKEEISKLKDEDYVTELARRDLFMSGDGEIIFNVEKKSK
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.109) (Q14U74)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}.
Interaction partners:
- Protein O-mannosyl-transferase 1
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Dystroglycan 1
- Ribitol-5-phosphate transferase
- Ribitol-5-phosphate transferase
- dolichol kinase
- Ribitol xylosyltransferase 1
- D-ribitol-5-phosphate cytidylyltransferase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
Sequence:
MFYASGRLLAAREATTLYAPPRARGPALRGKRRELQIPWHLETPSYDSLTGQRTRPGVPPARRVILRKGRMPPAIGGGLAGSELRPRRGRSVQQAARAVSRDVVPEAATRKLKRPAWSSRRFQAAGWWATLAVVTLLSFATRFHRLDQPAHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDRYEHHSYMGMRGFCAFLGSWLIPFAYLTVLDLSKSFPAALLTAALLTCDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSFANRPFSAPWWFWLSLTGISLAGALGVKFVGLFIIVQVGLNTISDLWHLFGDLSLSLVTVGKHLTARILCLIVLPLVLYVTIFAVHVMVLNKSGPGDGFFSSAFQARLSGNSLHNASIPEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKYNTNTDPLDPSFPVEFVRHGDIIRLEHKETTRNLHSHYHEAPLTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKILPKWGWEQLEVTCNPYLKETSNSIWNIEEHINPKLPNISLDVLQPSFPEILLESHMVMIRGNNGLKPKDNEFTSKPWHWPINYQGLRFSGANDTDFRVYLLGNPVVWWLNLVSLVLYLLTGSTIAIAMQRGIQLPAELQGLTKLLLRGGGQLLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGLLWDTLLRFCAWALAPSPLGRRIHMVGILSLLLATAYSFYLFHPLAYGMVGPLAQEPESPMAGLRWLESWDF
Protein: Mitochondrial sodium/calcium exchanger protein (Na(+)/K(+)/Ca(2+)-exchange protein 6) (Sodium/calcium exchanger protein, mitochondrial) (Sodium/potassium/calcium exchanger 6) (Solute carrier family 24 member 6) (Solute carrier family 8 member B1) (Q925Q3)
Organism: Mus musculus (Mouse)
Function: Mitochondrial sodium/calcium antiporter that mediates sodium-dependent calcium efflux from mitochondrion, by mediating the exchange of 3 sodium ions per 1 calcium ion. Plays a central role in mitochondrial calcium homeostasis by mediating mitochondrial calcium extrusion: calcium efflux is essential for mitochondrial function and cell survival, notably in cardiomyocytes. Regulates rates of glucose-dependent insulin secretion in pancreatic beta-cells during the first phase of insulin secretion: acts by mediating efflux of calcium from mitochondrion, thereby affecting cytoplasmic calcium responses (By similarity). Required for store-operated Ca(2+) entry (SOCE) and Ca(2+) release-activated Ca(2+) (CRAC) channel regulation: sodium transport by SLC8B1 leads to promote calcium-shuttling that modulates mitochondrial redox status, thereby regulating SOCE activity (By similarity). Involved in B-lymphocyte chemotaxis. Able to transport Ca(2+) in exchange of either Li(+) or Na(+), explaining how Li(+) catalyzes Ca(2+) exchange (By similarity). In contrast to other members of the family its function is independent of K(+) (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20018762, ECO:0000269|PubMed:24067497}; Multi-pass membrane protein {ECO:0000269|PubMed:20018762}. Note=Mainly localizes to mitochondrion inner membrane (PubMed:20018762).; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:14625281}; Multi-pass membrane protein {ECO:0000269|PubMed:14625281}.
Interaction partners:
- Calcium uptake protein 1, mitochondrial
- Mitochondrial proton/calcium exchanger protein/H
- Calcium uniporter protein
- Calcium uptake protein 2, mitochondrial
- Mitochondrial calcium uniporter regulator 1
Sequence:
MASRWLALLWAPVFLCVALILETASGTGDPSTKAHGHIQFSAGSVNQTAMADCRAVCGLNTSDRCDFVRRNPDCRSEAGYLDYLEGIFCYFPPNLLPLAITLYVFWLLYLFLILGVTAAKFFCPNLSAISTNLKLSHNVAGVTFLAFGNGAPDIFSALVAFSDPRTAGLAIGALFGAGVLVTTVVAGGITILHPFMAASRPFLRDIAFYMVAVFLTFTALYLGRITLTWALGYLGLYVFYVVTVIICTWVYQRQRSRSLVHSISETPELLSESEEDQMSSNTNSYDYGDEYRPLLLGRETTVQILIQALNPLDYRKWRTQSISWRVLKVVKLPVEFLLLLTVPVVDPDKDDRNWKRPLNCLQLVISPLVLVLTLQSGVYGIYEIGGLLPVWAVVVIVGTALASVTFFATSNREPPRLHWLFAFLGFLTSALWINAAATEVVNILRSLGVIFRLSNTVLGLTLLAWGNSIGDAFSDFTLARQGYPRMAFSACFGGIIFNILVGVGLGCLLQIIRNHVVEVKLEPDGLLVWVLASALGLSLIFSLVSVPLQCFQLSKAYGLCLLLFYICFLVVVLLTEFGVIHLKKA