wanglab/gogpt-training-data huggingface dataset:
Protein: CBL-interacting serine/threonine-protein kinase 5 (EC 2.7.11.1) (SNF1-related kinase 3.24) (SOS2-like protein kinase PKS19) (Q9LEU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Interaction partners:
- Calcineurin B-like protein 1
- Calcineurin B-like protein 9
- Potassium channel GORK channel)
- Calcineurin B-like protein 2
- Calcineurin B-like protein 4
- Calcineurin B-like protein 3
Sequence:
MEEERRVLFGKYEMGRLLGKGTFAKVYYGKEIIGGECVAIKVINKDQVMKRPGMMEQIKREISIMKLVRHPNIVELKEVMATKTKIFFVMEFVKGGELFCKISKGKLHEDAARRYFQQLISAVDYCHSRGVSHRDLKPENLLLDENGDLKISDFGLSALPEQILQDGLLHTQCGTPAYVAPEVLKKKGYDGAKADIWSCGVVLYVLLAGCLPFQDENLMNMYRKIFRADFEFPPWFSPEARRLISKLLVVDPDRRISIPAIMRTPWLRKNFTPPLAFKIDEPICSQSSKNNEEEEEDGDCENQTEPISPKFFNAFEFISSMSSGFDLSSLFESKRKVQSVFTSRSSATEVMEKIETVTKEMNMKVKRTKDFKVKMEGKTEGRKGRLSMTAEVFEVAPEISVVEFCKSAGDTLEYDRLYEEEVRPALNDIVWSWHGDNNNTSSEDC
Protein: Complement factor properdin (Properdin isoform X1) (Properdin precursor) (B0S697)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Complement C3a, tandem duplicate 6
- Complement component c3a, duplicate 1.
- Complement C3a, tandem duplicate 3
- Complement component c3a, duplicate 2.
- Si:ch73-237c6.1.
Sequence:
MNLNLLWILLLGIYVQQSASQMVQCFSAFSISTGKCADLLGEIEKDFCCINPSYGFAEADGVCRSCGHAAWSEWSSWSQCSVSCTEGVTQRRRFCYGNGNCSDPEDLGTIQTKPCVKKDCCPEDGGWSKWGNWQPCSVTCENGQKKRQRACSNPAPKCGGSCSGEPQEIEPCSADTVCPTHGGWSTWGNWGRCPVTCIEEGRNTQKEVRTRTCTNPSPSTAPPGRFCEGSEKDTRPCSGLPFCPIDGSWGSWSGSSACSVTCGVGRQMQSRICDSPSPKHGGKPCHGIEQKSGLCRTLAKCPIHGRWTEWSEWSICKSPSTRKITCRTREGTRRKLRDCVGTEHEGKLCDGEIVEHGSCFDIDKCDMEAILSEWSEWSYCKPDCGQDSKQTRSRKCVPDISEYQSDDYSLFYGKPVINCEKVKDETETRPCKNVPQC
Protein: Large ribosomal subunit protein eL15A (60S ribosomal protein L15-A) (L13) (RP15R) (YL10) (YP18) (P05748)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL13A
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS10
Sequence:
MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRAARPTRPDKARRLGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRAANLRVLNSYWVNQDSTYKYFEVILVDPQHKAIRRDARYNWICDPVHKHREARGLTATGKKSRGINKGHKFNNTKAGRRKTWKRQNTLSLWRYRK
Protein: Protein with SprT-like domain at the N terminus (Q9VXU6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Proliferating cell nuclear antigen
- Cyclin-G-associated kinase
- Proliferating cell nuclear antigen 2
- GH21160p
- Transitional endoplasmic reticulum ATPase TER94
Sequence:
MSDADYLFALNLQNQLNAESDQSYTAADASNDRDYQLARRIQNLINEGDEDGASELDSSIQFVYPKSNQPKSTKMENSEIKNKKREAAKKKPVRAIQASHDDYLNKTMNLVDPEWELVDPTPDIYAMFIRFDEKFFQERLGAVSLEWSKKMYSCAGICYQRGNRFVKQVTIRLSEPLLKLRPRKDLVETLLHEMIHAYCFVLNIREGNGGHGPNFKRIMETINKVAGTNITVYHTFHDEVASYRTHIWRCTGICRERSPFWGYVKRTSNRAPGPNDQWWKMHQRECSGTFLKLSEPPKAPKPETKSRAKKSTPAVAAPKEDIRNWFGQPSAKKAATGTVLLGDLAKAVPPTSYPGLSSEPFALPKTPAAGTKGNKSGGFNELDKSGSKATTEMSGQGYSLGGSSAIEHIDLSDTDVPDSAKLRQIRLQRFSEDASNKRQNKKKRRRVSSDSEIINWESYDDDVMVRDVHTPIVNLVESSSDEEEMKMPAGRKTMTSQERTQIIKRQVMEDELTLCEDDILLIDDEYDDEVAANESLTAATELADQSIIDDIFGEDTLLKEFQRENDVQPSCSSYAKRIENDIVSCPICFEKMRRTELSNHFDGCAIMVRLEPPSFKPKNRRTTASLTSKDSSGASTSRRAKSKAKSSKGILRSSGYTEGEIDKLNLSSSTDSSTLPSSEDELTPRQRRQRNLFKETVGCPRCGLEIMPLHLKVHGSVCAGRKKR
Protein: Guanine nucleotide-binding protein alpha-5 subunit (G alpha-5) (P34043)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- Latrophilin receptor-like protein A
- Guanine nucleotide-binding protein subunit beta
Sequence:
MGCILTIEAKKSRDIDYQLRKEEGSKNETKLLLLGPGESGKSTIFKQMKIIQDDGGFSIDERLEYRYIIYGNCISQMKVLVTAAISQDLKPNNPDNETRFEKFSKISPGGNSWTLEIAEDIKQLWSDDSIQNIYRMKDKFYQLNDSAAYFFDNIGRFANENYVPTQDDVLRSRVRTTGIQEAHFKFINIEFRMLDVGGQRSERRKWIHCFDSVTAVIFCVALSEYDQTLREEESQNRMKESLMLFDEIVNSHWFRNTAFIIFFNKVDLFREKIAKIDLGDYFPAYTGGLSFDNSTQFIKKMFLDLSTGNQRIFAHFTCAIDTANIQFVFHAVRETLLKNIFNTIINY
Protein: Huntingtin interacting protein 1 (A0A8I6AA26)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDVNKMTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTTAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFQRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEVSSPDSEPVLEKDDLMDMDASQQSLFDNKFDDIFGSSLSSDPFNFNNQNGVNKDEKDHLIERLYREISGLTGQLDNVKIESQRAMLQLKGRVSELEAELAEQQHLGRQATDDCEFLRTELDELKRQREDTEKAQRSLTEIEKKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARVSEQTQRKTQEQQDVLETLKHELATSRQELQVLHGNLETSAQSEAKWLTQIAELEKEQGSLATAAAQREEEFSALRDQLESTQLKLAGAQDSMCQQIKDQRRILLAGARKAAELEIQEALGQLEEPALLISCAGATDHLLSKVNSVSSCLEQLEKSRSQYLACPEEISELLHSITLLGHLTSDTIIQGTATSLRAPPESADSLTEACRQYGRETLAYLSSLEEEGAMEKADTTAIANCLGKIKTIGEELLPRGLDIKQEELGDLVDKEMAATSAAIEAATTRIEEILSKSRAGDTGVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSHEIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQIEETDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELAGVAEGWEEGTEASPSAVQEAVPDKE
Protein: Phosphatidylethanolamine N-methyltransferase (PEAMT) (PEMT) (EC 2.1.1.17) (EC 2.1.1.71) (PEMT2) (Phospholipid methyltransferase) (PLMT) (Q9UBM1)
Organism: Homo sapiens (Human)
Function: Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure. Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step. Responsible for approximately 30% of hepatic PC with the CDP-choline pathway accounting for the other 70% (Probable).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:15927961}. Note=localized in the endoplasmic reticulum (ER) of the liver and in a lipid metabolism-rich region of the ER known as mitochondria-associated membranes (PubMed:15927961). Adopts a topography within the ER membrane that positions both termini in the cytosol (PubMed:12431977). {ECO:0000269|PubMed:12431977, ECO:0000303|PubMed:15927961}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Note=Found in endoplasmic reticulum where most PEMT activity is generated and in mitochondria. {ECO:0000269|PubMed:12431977}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20860552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
- Ethanolaminephosphotransferase 1
- Phosphatidylserine synthase 1
- Phosphatidylserine synthase 2
- Phosphatidylcholine-sterol acyltransferase
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase D1
- Choline dehydrogenase, mitochondrial
Sequence:
MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTILLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYEEPFTAEIYRQKASGSHKRS
Protein: Indoleamine 2,3-dioxygenase 2 (IDO-2) (EC 1.13.11.-) (Indoleamine 2,3-dioxygenase-like protein 1) (Indoleamine-pyrrole 2,3-dioxygenase-like protein 1) (Q8R0V5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism. Involved in immune regulation.
Interaction partners:
- Tryptophan 2,3-dioxygenase
- Kynureninase
- Kynurenine formamidase
- Tryptophan 5-hydroxylase 2
- Tryptophan 5-hydroxylase 1
- Cytochrome P450 1A1
- Cytochrome P450 1A2
- Cytochrome P450 1B1
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
Sequence:
MEPQSQSMTLEVPLSLGRYHISEEYGFLLPNPLEALPDHYKPWMEIALRLPHLIENRQLRAHVYRMPLLDCRFLKSYREQRLAHMALAAITMGFVWQEGEGQPQKVLPRSLAIPFVEVSRNLGLPPILVHSDLVLTNWTKRNPEGPLEISNLETIISFPGGESLRGFILVTVLVEKAAVPGLKALVQGMEAIRQHSQDTLLEALQQLRLSIQDITRALAQMHDYVDPDIFYSVIRIFLSGWKDNPAMPVGLVYEGVATEPLKYSGGSAAQSSVLHAFDEFLGIEHCKESVGFLHRMRDYMPPSHKAFLEDLHVAPSLRDYILASGPGDCLMAYNQCVEALGELRSYHINVVARYIISAATRARSRGLTNPSPHALEDRGTGGTAMLSFLKSVREKTMEALLCPGA
Protein: Cathepsin L-like (EC 3.4.22.15) (O45734)
Organism: Caenorhabditis elegans
Function: Cysteine protease which plays an essential role in the degradation of proteins in lysosomes. During early embryogenesis, maternally required for the proteolytic processing of yolk proteins in platelets, a lysosome-like structure where a slow and controlled degradation of yolk proteins occurs. In the gonad, required for the clearance of apoptotic germ cells in the engulfing cell phagolysosomes. In embryos, required for the degradation of endocytic and autophagic cargos. In embryos, may play a role in the degradation of lipid-containing droplets. Required for larval development.
Subcellular location: Secreted {ECO:0000269|PubMed:11707440, ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685}. Lysosome {ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:24829385}. Endosome {ECO:0000269|PubMed:22768338}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:24829385}. Note=The zymogen form localizes to yolk platelets/granules in the developing oocyte and in the pseudocoelom (PubMed:15456850, PubMed:16857685). Following cell corpse phagocytosis, recruited to phagosomes during the late stages of phagolysosome formation (PubMed:24829385). {ECO:0000269|PubMed:15456850, ECO:0000269|PubMed:16857685, ECO:0000269|PubMed:24829385}.
Interaction partners:
- Peptidase C1A papain C-terminal domain-containing protein
- Aspartic protease 4
- Aspartic protease 3
- legumain
- Cathepsin B-like cysteine proteinase 6
- Calreticulin
Sequence:
MNRFILLALVAAVVAVNSAKLSRQIESAIEKWDDYKEDFDKEYSESEEQTYMEAFVKNMIHIENHNRDHRLGRKTFEMGLNHIADLPFSQYRKLNGYRRLFGDSRIKNSSSFLAPFNVQVPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKYGNHGCNGGLMDQAFEYIRDNHGVDTEESYPYKGRDMKCHFNKKTVGADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHRSFQLYKKGVYYDEECSSEELDHGVLLVGYGTDPEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHCGVATKASYPLV
Protein: Rho GTPase-activating protein 10 (PH and SH3 domain-containing rhoGAP protein) (PS-GAP) (PSGAP) (Rho-type GTPase-activating protein 10) (Q6Y5D8)
Organism: Mus musculus (Mouse)
Function: GTPase activator for the small GTPases RhoA and Cdc42 by converting them to an inactive GDP-bound state. Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death.
Subcellular location: Cytoplasm. Cytoplasm, perinuclear region. Cell membrane. Endosome membrane {ECO:0000250|UniProtKB:A1A4S6}. Note=Association to cell membrane is dependent on PH domain. Colocalized with MICAL1, RAB8A, RAB8B and RAB10 on endosomal tubules (By similarity). {ECO:0000250|UniProtKB:A1A4S6}.
Interaction partners:
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Catenin beta-1
Sequence:
MGLQPLEFSDCYLDSPWFRERIRAHEAELERTNKFIKELIKDGKNLISATKSLSAAQRKFAHSLRDFKFEFIGDAETDDERCIDASLREFSNFLKNLEEQREIMALSVTETLIKPLEKFRKEQLGAVKEEKKKFDKETEKNYSLIDKHLTLSARKKDSHLQEADLQVEQNRQHFYELSLEYVCKLQEIQERKKFEFVEPMLSFFQGMFTFYHQGHELSKDFNHYKMELQINIQNTRNRFEGTRSEVEELMNKIRQNPKDQKRASQFTAEGYLYVQEKRPAPFGSSWVKHYCMYRKTAKKFNMIPFEHRSGGKLGDGEAFFLKECTKRHMDSTDRRFCFDIEAADRPGVPLTVQAFSEEERKQWLEALGGKEALFHTFNRAIVPRPEGGAQLDKMGFTILRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKMCNELDLENSADWEVKTVTSALKQYLRSLPEPLMTYELHRDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSSHSKQNLMTVANLGVVFGPTLMRPQEETVAAIMDLKFQNIVVEILIENHEKIFRTSPDTTFAEPTCLSASPPNAPPRQSKRQGQRTKRPVAVYNLCLELEEGDSPSPLKEDPPSSSQDSLSTPSPTTSAAHGPPGLDGNHLAADGGSCGDATATTPSQTRPSMVQWLNMQSPTTPSSNPAGTPPSPRMSPFPLSPAASIVDKLPECVINRKARAVYPCEAEHSSELSFEIGAIFEDVQTSREPGWLEGTLNGKRGLIPQNYVKLL
Protein: Ferritin, mitochondrial (EC 1.16.3.1) (Q8N4E7)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidation of ferrous iron(II) to ferric iron(III) and stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11323407}.
Interaction partners:
- Frataxin, mitochondrial
- Cytoplasmic aconitate hydratase
Sequence:
MLSCFRLLSRHISPSLASLRPVRCCFALPLRWAPGRPLDPRQIAPRRPLAAAASSRDPTGPAAGPSRVRQNFHPDSEAAINRQINLELYASYVYLSMAYYFSRDDVALNNFSRYFLHQSREETEHAEKLMRLQNQRGGRIRLQDIKKPEQDDWESGLHAMECALLLEKNVNQSLLELHALASDKGDPHLCDFLETYYLNEQVKSIKELGDHVHNLVKMGAPDAGLAEYLFDTHTLGNENKQN
Protein: NGFI-A-binding protein 2 (EGR-1-binding protein 2) (Melanoma-associated delayed early response protein) (Protein MADER) (Q15742)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Isoform 2 is not localized to the nucleus. {ECO:0000250}.
Interaction partners:
- E3 SUMO-protein ligase EGR2
- Early growth response protein 1
- Early growth response protein 3
- Chromodomain-helicase-DNA-binding protein 4
- Signal transducer and activator of transcription 6
- Early growth response protein 4
- Zinc finger CCCH domain-containing protein 14
- Chromodomain-helicase-DNA-binding protein 3
- Nuclear RNA export factor 1
- Cyclin-dependent kinase 5 activator 1
Sequence:
MHRAPSPTAEQPPGGGDSARRTLQPRLKPSARAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGRSTPESDVGAGGEEEAGSPPFSPPAGGGVPEGTGAGGLAAGGTGGGPDRLEPEMVRMVVESVERIFRSFPRGDAGEVTSLLKLNKKLARSVGHIFEMDDNDSQKEEEIRKYSIIYGRFDSKRREGKQLSLHELTINEAAAQFCMRDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHPEELGGPPLKKLKQEVGEQSHPEIQQPPPGPESYVPPYRPSLEEDSASLSGESLDGHLQAVGSCPRLTPPPADLPLALPAHGLWSRHILQQTLMDEGLRLARLVSHDRVGRLSPCVPAKPPLAEFEEGLLDRCPAPGPHPALVEGRRSSVKVEAEASRQ
Protein: Protein disulfide-isomerase A6 (EC 5.3.4.1) (Calcium-binding protein 1) (CaBP1) (Protein disulfide isomerase P5) (Thioredoxin domain-containing protein 7) (Q63081)
Organism: Rattus norvegicus (Rat)
Function: May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q15084}. Cell membrane {ECO:0000250|UniProtKB:Q15084}. Melanosome {ECO:0000250|UniProtKB:Q15084}.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- DnaJ homolog subfamily B member 11
- ERO1-like protein alpha
- Protein disulfide-isomerase A4
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase
- DnaJ homolog subfamily C member 3
- Peptidyl-prolyl cis-trans isomerase B
- Calreticulin
Sequence:
MARLVLGLVSCTFFLAVSALYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAASALKDVVKVGAVNADKHQSLGGQYGVQGFPTIKIFGANKNKPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRGDSSSKKDVVELTDDTFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAATEVKEQTKGKVKLAAVDATVNQVLASRYGIKGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKKTCEEHQLCVVAVLPHILDTGATGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQYELENALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGSFPNITPREPWDGKDGELPVEDDIDLSDVELDDLEKDEL
Protein: Stomatin-like protein 2, mitochondrial (SLP-2) (EPB72-like protein 2) (Paraprotein target 7) (Paratarg-7) (Q9UJZ1)
Organism: Homo sapiens (Human)
Function: Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}; Peripheral membrane protein {ECO:0000269|PubMed:10713127}. Mitochondrion {ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:19597348, ECO:0000269|PubMed:22623988}. Mitochondrion inner membrane {ECO:0000269|PubMed:17121834, ECO:0000269|PubMed:18339324, ECO:0000269|PubMed:21746876}; Lipid-anchor {ECO:0000269|PubMed:21746876}. Mitochondrion intermembrane space {ECO:0000269|PubMed:17121834}. Membrane raft {ECO:0000269|PubMed:18641330}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330}. Note=Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain (PubMed:21746876). Also associates with the actin cytoskeleton and membrane rafts in activated T-cells (PubMed:10713127, PubMed:18641330). A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells (PubMed:22623988). {ECO:0000269|PubMed:10713127, ECO:0000269|PubMed:18641330, ECO:0000269|PubMed:21746876, ECO:0000269|PubMed:22623988}.
Interaction partners:
- Prohibitin 1
- Prohibitin-2
- Presenilin-associated rhomboid-like protein, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- Splicing factor Cactin
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein mL37
Sequence:
MLARAARGTGALLLRGSLLASGRAPRRASSGLPRNTVVLFVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTKAPVPGTPDSLSSGSSRDVQGTDASLDEELDRVKMS
Protein: Pyramus (B9ZW35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fibroblast growth factor receptor homolog 1
- Fibroblast growth factor
- Fibroblast growth factor receptor homolog 2
- Thisbe
Sequence:
MFHKFMPNVRTYIILMSFVAAIAWSASAAKNVLTLSKHSELALHINSHGKVTAENILRTYQYFNMEAVNDVFSLDFKITIYSADVDYYLCFHHGRLVGKRNATKECHFKEGIFMGNQNFSSAYNPVLRVGFKGNFKPIGLNDFSKPKVMKKAILFFFPLNEEKFNLHLAEVLSSSTTTTTTTTTTTSTTTTTTTPPPSTTTTTTTTTTTPASPVAVTKRTRSKSRRPTSINSNSSNSNIPDKISRHNSNSLKSYNQANSNNNNNNNNNNSSNNNELDLQQQQVILQRNRKLHRRHRLQQKKRQLQLQQQQRRRQRQYGTMGVMAQPQPKNLVVRHHHNNATIMERRRRRRLERQQHKLQRELWEREQREAGDKERERERVEHLPKATSSASSSSSSSSTATSTALTATAASLAPSAFNLVAIMAASRRKRDRRKRSAGATGAGAGATGAGATRGGGSSSSPPDADMQLVELPSQRLQQQDEQHPQNEYSKPYVNSNLNLDLDLNVNVKQLIDSSSVSVNHAIPALPKNYNYLYSNEHYNLNTKSSTTDSSSLDDSTKFDSPNSHSHSHSAFNQNIDNNLKQLTDRIELASAESQVETTANPEGETETVTTETVMQNRNHIDANNIIDDSYPNDEEHEELILKKLLRGLRLQQQHQQQQLQQQQQQPNIENPNENINVVNNNQNHNDGGLLTNNNHNSNYNEQFANDDETIRIQNNKYETHIVQYKHAVFIWKILGVSRRYDNPIIIAWQFACHCGKYFVSLYYIDL
Protein: HTH APSES-type domain-containing protein (F9XD62)
Organism: Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch fungus) (Septoria tritici)
Interaction partners:
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
Sequence:
MSAQPQPPAGANQQYPSSFDQTGQVAPHGMKPRVTATLWEDEGSLCFQVEANGVCVARREDNHMINGTKLLNVAGMTRGRRDGILKSEKTRHVVKIGPMHLKGVWIPFDRALDFANKEKITELLYPLFVHNIGALLYHPSNAARQSVGGAAMASAARRSDQQDYMRTPQGSQPPTLTHHHSMSTPGGGSMPQPPHSIAPHPASGRPGLDRAHTFPTPPTSASSLNMNMGHQGSSYGYGEQNGAIQSAATPPNHAQGIQYQTSQAPYDSQRQMYAPAPGAYGQQYAQQPSMNRYGQMQTSPDGVKSEMGPPARAGAENENAEAKPHGGYGGQHDVEGEHEGEYTHSSASFGARRPTYDYNPNPASGPVHTDPSHISPEMTHSPHQNGSGRATPRTTTTYAGYNTTTQRPTQLPQSNLNYVMSNDTRAGAPNGADTGYQPAYQASQYAAMNGTPVANNKRMREDESEDPYGRPPSANGDHKRQRTDSVSTRPIAQPQSLKAGGMRR
Protein: Transcription factor bHLH48 (Basic helix-loop-helix protein 48) (AtbHLH48) (bHLH 48) (Transcription factor EN 97) (bHLH transcription factor bHLH048) (Q8VZ02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor bHLH147
- Protein Brevis radix-like 4
- Probable WRKY transcription factor 12
- Protein EMSY-LIKE 3
Sequence:
MDLTQGFRARSGVVGPVAGLESLNFSDEFRHLVTTMPPETTGGSFTALLEMPVTQAMELLHFPDSSSSQARTVTSGDISPTTLHPFGALTFPSNSLLLDRAARFSVIATEQNGNFSGETANSLPSNPGANLDRVKAEPAETDSMVENQNQSYSSGKRKEREKKVKSSTKKNKSSVESDKLPYVHVRARRGQATDNHSLAERARREKINARMKLLQELVPGCDKIQGTALVLDEIINHVQTLQRQVEMLSMRLAAVNPRIDFNLDSILASENGSLMDGSFNAESYHQLQQWPFDGYHQPEWGREEDHHQANFSMGSATLHPNQVKMEL
Protein: Runt related A, isoform B (Q0KHQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHLTTTSSNSTASNANNNNNNTANNNNTSSNNNTTNTNGSSNNNTSGNNNNSSGNNSNTEQNTPPTPAQLLNEAYTKMTSDILAERTLGDFLTEHPGELIRTSSPLFVCTVLPPHWRSNKTLPVAFKVVSLGDIMDGTMVTVRAGNDENYCAELRNCTAVMKNQVAKFNDLRFVGRSGRGKSFTLTITVSTNPPHIATYNKAIKVTVDGPREPRSKTRQQQQFHFAFGQRPFHFSTDPLSGFRMPPIGNCQSASNTHWGYGSAASAYSPYLASSGLSSCTTPTSAQFNNPALGFTCSSNDQSNNQDFGGATNRDCVPMLPDSTASDLDQHLSSLVGSTSGQMTHHSLLGAGGQTSISSTVNGASGGGSAGAGTAGGGAGSGGGAGGGAGGNSILVPRYHTNASNEYNVHSSQNGPRSLSDSSQAESPVQEDLLTTNTPNLGSTAGGGAANGGAGSNAGSGAAGSGAGGAGGASSAVGNPAMLGANQNFPGIVNQAQHSAASAYGGGTGVVGGGHGSAAAAAAGCNGSLYPVLPASLLYSQLYTAANQSAHGFHSHTLPAHASPNSSVHGELQSVMDHISNVGVRQQHNIMAGGGVTHPGDLTLIGNCGASVRNIEDGNSNRQVAALAAHRGHHNPTDNGGSVWRPY