wanglab/gogpt-training-data huggingface dataset:
Protein: MAP kinase kinase skh1/pek1 (EC 2.7.12.2) (Q9Y884)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the mkh1 signal transduction pathway that plays a role in cell wall integrity. Activates spm1/pmk1 via phosphorylation.
Interaction partners:
- MAP kinase kinase kinase mkh1
- Mitogen-activated protein kinase spm1
- GTP-binding protein rho1
- Cell wall integrity and stress response component 1
- Protein kinase byr2
- Protein kinase byr1
- Mitogen-activated protein kinase sty1
- Mitogen-activated protein kinase spk1
- Stretch-activated cation channel yam8
- GTP-binding protein rho2
Sequence:
MSKKPVLNLDTSNGFSEEYISHPERNDNQGIVEITDLVFSSESKLTQRKESRDSKTFVPSFLEELDDDHLHELVTNGGILYMNSLGEGVSGSVRKCRIRGTQMIFAMKTVLAAPNTALQKQLLRELKINRSCTSPYIVKYYGACYNNAECQLNIAMEYCGAGSLDAIYKRVRSQGGRTGERPLGKIAFGVLSGLSYLHDRKIIHRDIKPSNILLTSKGQVKLCDFGVSGELVNSLAGTFTGTSYYMAPERISGGSYTISSDIWSLGLTLMEVALNRFPFPPEGSPPPMPIELLSYIINMPPPLLPQEPGIKWSKSFQHFLCVCLDKDKTRRPGPQKMLTHPWVKAFERIHVDMEEFLRQVWSD
Protein: Non-specific lipid transfer protein GPI-anchored 15 (AtLTPG-15) (Protein LTP-GPI-ANCHORED 15) (Xylogen-like protein 10) (AtXYLP11) (AtXYP7) (Q7EB72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable lipid transfer protein.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- GDSL esterase/lipase At2g23540
- GDSL esterase/lipase At3g50400
- Glycerol-3-phosphate acyltransferase 7
- Non-specific lipid-transfer protein 6
- Non-specific lipid-transfer protein 2
Sequence:
MGYRRSYAITFVALVAALWSVTKAQPSSSCVSTLTTLSPCLSYITGNSTTPSQPCCSRLDSVIKSSPQCICSAVNSPIPNIGLNINRTQALQLPNACNIQTPPLTQCNAATGPTAQPPAPSPTEKTPDVTLTPTSLPGARSGVGGGSKTVPSVGTGSSSRNVDPLPLHFLMFAVLVVCTSSFL
Protein: BET1 homolog (mBET1) (Golgi vesicular membrane-trafficking protein p18) (O35623)
Organism: Mus musculus (Mouse)
Function: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus (By similarity). {ECO:0000250}.
Interaction partners:
- Synaptobrevin homolog YKT6
- Golgi SNAP receptor complex member 2
- Syntaxin-5
- Vesicle-trafficking protein SEC22b
- Golgi SNAP receptor complex member 1
- Sec1 family domain-containing protein 1
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 7
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Vesicle-trafficking protein SEC22a
Sequence:
MRRAGLGDGAPPGSYGNYGYANTGYNACEEENDRLTESLRSKVTAIKSLSIEIGHEVKNQNKLLAEMDSQFDSTTGFLGKTMGRLKILSRGSQTKLLCYMMLFSLFVFFVIYWIIKLR
Protein: cAMP-responsive element-binding protein-like 2 (Q0VD32)
Organism: Bos taurus (Bovine)
Function: Probable regulator of CREB1 transcriptional activity which is involved in adipose cells differentiation. May also play a regulatory role in the cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:16352405}.
Interaction partners:
Sequence:
MDDSKVVGGKVKKPGKRGRKPAKIDLKAKLERSRQSARECRARKKLRYQYLEELVSSRERAICALREELEMYKQWCMAMDQGKIPSEIKALLTGEEQSKSQQNSSRHMKAGKTDANSNSW
Protein: F-box only protein 39 (Q8N4B4)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- Ribonuclease inhibitor
Sequence:
MDEESELIQPQDQSCWAFLPDLCLCRVFWWLGDRDRSRAALVCRKWNQMMYSAELWRYRTITFSGRPSRVHASEVESAVWYVKKFGRYLEHLEVKFMNPYNAVLTKKFQVTMRGLLSCLSKSNNRLKSLSIQYLELDRLVWRNSIRSSFISSLSFFLKKMGKRLDYLNLKGARLTVEQGCQILDSLSYMRNENVISELNIEDYFSHHLAVYNSPQFKKTMSTFHNLVSLNLNYNCISDELLENLCENASTLRTINIKCHVHDPHGQVIWGMSWAKLARQATNLKVNFFFERIMKYERLARILLQEIPIRSISLRSCYFSDPDCSMRPTLIDLLPTFRHTLQKLTCEFNNNHESLDEELHLLIISCRKLFYFKIWAFLDVSFVERILKSQKERQCALRVFKARIYTNRYETNEEDKTLQEIYRKYRKLIESELSYFVIVYSVM
Protein: GH02708p (Q8IH74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPITMAKNKVLRMLEMKRAQQLKIIDSRVSAKVPRVTKLPPLKDIVKDTYCMETEDPGTEIAPLSNKLHPDYEEIIIVSASCNTDITIPPNQLSKASPRSLLKSSVLLYNISNGQDANKNMSNSLIASIQSEVARQTSNTTLSTIQSNATKVMSSADKNCQHGEDMVIMHLPKDRVRKTLVSIATQTDLQPEFPLLTLPPKRQSRERTRRNYRRRRTQGSGSNMSTSSSDFSSDCSSLVSHRSRSQYDSIDQLRNLDVAATCGGSIGNGGYSSRSTQRHRSSVSSSSYSENGQYRRRQRRTSYNKRRSRNQKRGSTSSSCSGSEKSDRERSRSPHRKLRHSRSRSRSKSDTRYPNNNSSSNNNNRRGFFDRNVSQPAVEERRIVYVGRIEQETTKEILRRKFLPYGSIKQITIHYKENGMKYGFVTYERAQDAFTAIDTSHRDSQISMYDISFGGRRAFCRSSYADLGEFFFTFYIILCTILSNLSFIDNAGINNYNSYVFPKEAPAPNVVEDSFEALLLQVKAKLNAGKSPVGSSTLEAPSASGTVLQGHSQM
Protein: nitric oxide dioxygenase (EC 1.14.12.17) (Q6FL28)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MLSEQTRTIIKATVPVLEKQGTQITKCFYGHMLTEHEELLNIFNRTNQKIGAQPTALATTVLAAAKHIDNLAALLPHVEQIGHKHRALQILPEHYPIVGKYLLIAIKEVLGDVATPEIITAWGEAYQEIADVFISVEAKMYKEAAWPGWKQFEVVGKDKVAEDIYEFTVKPTGDSGVDLAKLPIIPGQYITVNSHPVRQDNKYDALRHYSICSADTTNGLKFAVKLQTSTNNPDGLVSEFLHKDVKVGDVLKLSAPAGDFAVNKDLINQNDIPLVLLSSGVGVTPIVSMLEAQVKENPSRPIVWIQSAYNEPHVAFKNHVDNLLKQAKDAKKVVVLTDSQPRIDDKFLKENVPAHADVYICGSLNFMQSMIDHFQVLEHKNDMIHYEPFGPKMSTVKV
Protein: Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10] (Q9JHX4)
Organism: Rattus norvegicus (Rat)
Function: Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (By similarity). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (By similarity). Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (By similarity). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (By similarity). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-325', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (By similarity). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis (By similarity). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (By similarity). Cleaves PARP1 and PARP2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10197541}. Nucleus {ECO:0000269|PubMed:10197541}.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 1
- Receptor-interacting serine/threonine-protein kinase 3
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- FAS-associated death domain protein
- Tumor necrosis factor receptor superfamily member 6
- CASP8 and FADD-like apoptosis regulator
- Caspase-3
- Caspase-1
- Tumor necrosis factor ligand superfamily member 6
- B-cell lymphoma/leukemia 10
Sequence:
MDFHSCLYDIAERLGNEELAALKFLCLDHIPQKKQESINDVLVLFQRLQEEGMLEEDNLSFLKELLFHISRRDLLSRVLKSSPEEMVRELQVLGKAQVSAYRVMLFKLSEDMDKEDLKSFKFLLITEIPKCKLQDNSSLLDIFVEMEKRTILAENNLVTLKSICFRVNRSLLGRIDDYERSSTERRMSTEGGEELPVSVLDEVTIKMQDMWDSPGEQESESLNSDNVYQMKSKPRGYCLIFNNNNFSKAREDIPKLSNMRDRKGTNYDEEALSKTFKELHFEIVSFSDCTASQIHEVLVSYQSKDHKGKDCFICCILSHGDKGIVYGTDGKEASIYELTSYFTGSKCPSLAGKPKIFFIQACQGNNFQKAVPVPDETGLEQEHVLEEDSSSYKNYIPDEADFLLGMATVKNCVSYRDPTRGTWYIQSLCQSLRERCPRGEDILSILTGVNYDVSNKDNPRNMGKQMPQPIFTLRKKLFFPPN
Protein: Transient receptor potential cation channel subfamily M member 5 (A0A455XI77)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPMAQSSCPGSPPDTGDGWEPVLCKGEVNFGGSGKKRSKFVKVPSNVAPSMLFELLLTEWHLPAPNLVVSLVGEERLFAMKSWLRDVLRKGLVKAAQSTGAWILTSALHVGLARHVGQAVRDHSLASTSTKVRVVAIGMASLDRILHRQLLDGVQEDTPIHYPADEGSTQGPLCPLDSNLSHFILVEPGTLGSGNDGLAELQLSLEKHISQQRTGYGGTSSIQIPVLCLLVNGDPSTLERMSRAVEQAAPWLILAGSGGIADVLAALVGQPHLLVPQVTEKQFREKFPSECFSWEAIVHWTELLQNIAAHPHLLTVYDFEQEGSEDLDTVILKALVKACKSHSRDAQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMTDALVSNKPDFVRLFVDSGADMAEFLTYGRLQQLYHSVSPKSLLFELLERKHEEGRLTLAGLGAQQTRELPVGLPAFSLHEVSRVLKDFLHDACRGFYQDGRRMEERGPPKRPAGQKWLPDLSRKSEDPWRDLFLWAVLQNRYEMATYFWAMGREGVAAALAACKIIKEMSHLEKEAEVARTMREAKYEQLALDLFSECYSNSEDRAFALLVRRNHSWSRTTCLHLATEADAKAFFAHDGVQAFLTKIWWGDMATGTPILRLLGAFTCPALIYTNLISFSEDAPQRMDLEDLQEPDSLDMEKSFLCSHGGQLEKLTEAPRAPGDLGPQAAFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFSYVLLVDFRPPPQGPSGSEVTLYFWVFTLVLEEIRQGFFTNEDTRLVKKFTLYVEDNWNKCDMVAIFLFIVGVTCRMVPSVFEAGRTVLAIDFMVFTLRLIHIFAIHKQLGPKIIIVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSLHPLLLDSSASCPNLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYHLIVEYHGRPALAPPFILLSHLSLVLKQVFRKEAQHKQQHLERDLPDPVDQKIITWETVQKENFLSTMEKRRRDSEEEVLRKTAHRVDLIAKYIGGLREQEKRIKCLESQANYCMLLLSSMTDTLAPGGTYSSSQNCGRRSQPASARDREYLEAGLPHSDT
Protein: Cytochrome P450 2C40 (EC 1.14.14.-) (CYPIIC40) (P56657)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase that may play a major role in the metabolism of arachidonic acid in the intestinal tract. Exhibits regioselective hydroxylase and epoxidase activity toward arachidonic acid, producing 16(R)-hydroxyeicosatetraenoic acid (HETE) and (14R,15S)-epoxyeicosatrienoic acid (EpETrE) as major products. 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).
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Cytochrome P450 2U1
- Epoxide hydrolase 1
- Arachidonate 12-lipoxygenase, 12R-type
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 7A1
- Cytochrome P450 3A25
Sequence:
MDPFVVLVLCLSFLLVLSLWRQRSARGNLPPGPTPLPIIGNYHLIDMKDIGQCLTNFSKTYGPVFTLYFGSQPIVVLHGYEAIKEALIDHGEEFSGRGRIPVFDKVSTGKGIGFSHGNVWKATRVFTVNTLRNLGMGKRTIENKVQEEAQWLMKELKKTNGSPCDPQFIIGCAPCNVICSIVFQNRFDYKDKDFLSLIGKVNECTEILSSPGCQIFNAVPILIDYCPGSHNKLFKNHTWIKSYLLGKIKEHEESLDVTNPRDFIDYFLIQRRQKNGIEHMDYTIEHLATLVTDLVFGGTETLSSTMRFALLLLMKHTHITAKVQEEIDNVIGRHRSPCMQDRNHMPYTNAMVHEVQRYIDLGPNGVVHEVTCDTKFRNYFIPKGTQVMTSLTSVLHDSTEFPNPEVFDPGHFLDDNGNFKKSDYFVPFSAGKRICVGESLARMELFLFLTTILQNFKLKPLVDPKDIDMTPKHSGFSKIPPNFQMCFIPVE
Protein: Subtilisin-like protease 1 (EC 3.4.21.62) (PfSUB1) (Q8I0V0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.
Subcellular location: Secreted {ECO:0000269|PubMed:18083098}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:18083098}. Note=At the schizont stage, in merozoites, localizes to dense secretory granules called exonemes (PubMed:18083098). Just prior to egress secreted into the parasitophorous vacuole (PubMed:18083098). {ECO:0000269|PubMed:18083098}.
Interaction partners:
- Subtilisin-like protease 2
Sequence:
MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH
Protein: Threonine-phosphate decarboxylase (EC 4.1.1.81) (L-threonine-O-3-phosphate decarboxylase) (P97084)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Interaction partners:
- Cobyrinate a,c-diamide synthase
- L-threonine kinase
- Cobalamin biosynthesis protein CbiB
- Cobalt-precorrin-8 methylmutase
- Histidine biosynthesis bifunctional protein HisIE
- Cobyric acid synthase
- Cobalt-precorrin-5B C
- Histidine biosynthesis bifunctional protein HisB
- Bifunctional adenosylcobalamin biosynthesis protein CobU
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
Sequence:
MALFNSAHGGNIREAATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERYPDADYFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAMIVTPGFAEYGRALAQSGCEIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPNNPTGLLPERPLLQAIADRCKSLNINLILDEAFIDFIPHETGFIPALKDNPHIWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMRRQQMPWSVNALAALAGEVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYLLLRCEREDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNVLTGIAPAD
Protein: Mitochondrial ribosomal protein S9 (RH44312p) (Q8SXF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS5m
- Elongation factor Ts, mitochondrial
- Small ribosomal subunit protein uS7m
- 40S ribosomal protein S15
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL21m
- 28S ribosomal protein S14
Sequence:
MALRVFGLNIVKNNRNLLQNACKSRAPMPCYMAAAPFATDVTVQAAPAAVQKQRVSKAMRAYLKRATEHDEFMKTQHLEFQIGKRHLANMMGADAETFTQEDIDEAISYLFPSGLYDQKARPAMKSPEVVFPARKAAEFDETGRPFHSMFYTGKPNFFQLLHDIVEETNKLADLEERMLRRGNKPDENQKLEIAGFQLLPKDQLELLLVESIADIEYSNFTNSMDRLIASPYAYKSKAFIERYMKPLMDQSKQLEVPKPRIDEEGRQYITTYECLRKTARADVTVRLPGTGKISINGKDISYFEDENCREQLLFPLQFSELLGKVDVEANVEGGGPSGQAGAIRWGIAMSLRSFVDQEMIESMRLAGLLTRDYRRRERKKFGQEGARRKYTWKKR
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 (Complex I-B22) (CI-B22) (LYR motif-containing protein 3) (NADH-ubiquinone oxidoreductase B22 subunit) (Q9Y6M9)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Acyl carrier protein, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 beta subcomplex subunit 2, mitochondrial
Sequence:
MAFLASGPYLTHQQKVLRLYKRALRHLESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKKLRRESWEREVKQLQEETPPGGPLTEALPPARKEGDLPPLWWYIVTRPRERPM
Protein: Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics) (Q5PR69)
Organism: Mus musculus (Mouse)
Function: Involved in epithelial cell integrity by acting on the dynamics of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:30361697}.
Interaction partners:
Sequence:
MGARAFSHDSIFIPDGGAESEQTVQAMSQDNILGKVKTLQRQLGKNIKFGQRPSNAIPMKKAGSTDASSEEDFVLTSPMEIVTQQDIVPSDTENKSSDTPSSSSPLNLPEAGSDMEEKVAPVKPSRPKRHLSSAGTIESVNLDAIPLAIARLDNSAARHKLAVKPKNQRVSRKHRWLAQDRQNEPGSFESQSSLDQNGQLGEDKHIWHGEEPEPLESHEEKRLHEEYWRELEAKCKRQKAEAAEKRRQEEQRRQALERRLWEESLRQELLEEEEEGEEEEEVKEEGEEGEEVGLQPRAGKVPPEEGHQSGPEEQRCTEQELGGADDPARLEAEERRREQEEAERQAEKLRQREAERQEEEQKQREAERQEEEARQCEAERQAEKLRQREAERQEEEARQREAERQAEKLRQREAERQEEELRQREEAERQEKLRQRDAESQEEELRQREAERQRAQEEDAKGMLQEEEEEAKRIEELKGKETPEPLVEEGPQSPEGESQPWLTDDADQRSPLQRDLEKPGEREREDLESAGQREIAEEPRGEGEPAEQSGDLDAHCGGVDGEGKETAQTDSPQPQERQMEGTPAPEENEATAADIDRKVEELRWQEVDERQTMPRPYTFQVSSGSRQILFPKVNLSPVTPAKDASLAPAAQEPPAPRGAASHALPSALSIPHTAILVTGAQLCGPAVNLSQIKDTACKSLLGLSEEKRPMDVPTVESRAGSGKSRPAPESPSNAAALAEWASIRSRILKNSEGDQRGDREPARAGDEPVPRARCDSRGNVRRTPPVNAKFSIMPAWQKFSDSGAETFRQSLDGESGRKKPGLAPSEETAPQPHAAAQQEVSQEPPDTTDGCKFAKDLPSFLVPGLPSPQKAASRTESTTTLDSETTSDVGNPDPAMPGGEEKASPFGIKLRRTNYSLRFHCDQQAEQKKKKRHSSTGDSVGGATPATGSVSGESEPEATFLKHGPSLPQERKPALSPRKDSAESHSSGHYVAVAQSGLPPASGQTPAPEQDRAVSKMPSMQKPALAPKPASQTPPSSPLSKLSRPHLVELLARRAGKLDSEPSETAKESSDNQPPSPSLPEELKGQKRDEKDVPEKKPASPPLPAGQQERPSLIPETGRKEKPVLQSRHSLDGSKVTEKVETAQPLWITLALQKQKGFREQQATREERKQAREAKQAEKLSKETVSVSLQPGSSRASKTAPVHKPAAPSEEKKPETAVSRLQRREQLKKSNTLPTSVTVEISDSAPSAALVKDVTKRFSTPDAAPVSTEPAWLALAKRKAKAWSDCPQIIK
Protein: Sideroflexin-2 (Q96NB2)
Organism: Homo sapiens (Human)
Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria. Involved in mitochondrial iron homeostasis by regulating heme biosynthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30442778}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:30570704}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEADLSGFNIDAPRWDQRTFLGRVKHFLNITDPRTVFVSERELDWAKVMVEKSRMGVVPPGTQVEQLLYAKKLYDSAFHPDTGEKMNVIGRMSFQLPGGMIITGFMLQFYRTMPAVIFWQWVNQSFNALVNYTNRNAASPTSVRQMALSYFTATTTAVATAVGMNMLTKKAPPLVGRWVPFAAVAAANCVNIPMMRQQELIKGICVKDRNENEIGHSRRAAAIGITQVVISRITMSAPGMILLPVIMERLEKLHFMQKVKVLHAPLQVMLSGCFLIFMVPVACGLFPQKCELPVSYLEPKLQDTIKAKYGELEPYVYFNKGL
Protein: Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (Q8JHF2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Involved in the correct formation of boundaries in the somites and hindbrain (By similarity). Required for Delta-Notch-mediated induction of hypochord cells at the lateral borders of the midline precursor domain.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 2 precursor
- Notch receptor 1b.
- Notch receptor 3.
- Beta-1,3-N-acetylglucosaminyltransferase manic fringe
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- Hairy-related 1.
- Mesoderm posterior ab.
- Homeobox protein unc-4 homolog
Sequence:
MLKTYRGKVVVSLAGATVTCLGFLLFLSQHQRIQADGMQNESEVGLRSLQSLGDSETDDGAQPEQNAKKGFSAYFSKLTRSRREADKPSEAPGAATDAPPAEDISADDIFIAVKTTKKFHRSRLDLLLDTWISRNMRQTYIFTDGEDEELKKKIGSHAINTNCSAAHSRQALSCKMAVEYDKFIESGKKWFCHVDDDNYVNTKTLVKLLSNYPHTQDMYIGKPSLDRPIEATERLGDNKMRPVNFWFATGGAGFCISRGLALKMSPWASGGHFMNTAEKIRLPDDCTIGYIIESVLGVSLTRSSLFHSHLENLQQVSKSEVHKQITLSYGMFENKRNIINMKGAFSVEEDPSRFKSVHCLLYPDTPWCPPQVAY
Protein: Cytochrome P450, family 702, subfamily A, polypeptide 8 (F4J5G3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Casein kinase 1-like protein 10
- non-specific serine/threonine protein kinase
- At3g16760
- At5g26610
- Protein FIP2
- DExH-box ATP-dependent RNA helicase DExH14
- non-specific serine/threonine protein kinase
- Nuclear pore complex protein NUP35
- Serine/threonine-protein kinase AFC3
Sequence:
MDRFFRTSLFGGKVIISMDNELNMEMAKTNRTPGITKSIARLFGEDNNLFLQSTESHKHVRNLTVQMLGSQSLKLRIMENIDLLTRTHMEEGARDGSLDVKETTSKILIECLAKKVMGEMEPEAAKKLALCWRYFPSGWFRLPFNLPGIGVYNMMKARKRMKTLLKEEVLKKREAGEEFGEFSKIIFGEKEGEKETMSMKNVIEYIYTFFVIANETTPRILAATVKFISENPKVMQELQREHAMIFENKSEEAGLTWEDYKSMTFTNMVINESLRISTTVPVILRKPDHDTKVGDYTIPAGWNFMGYPSAHFDPTKYEDPLEFNPWRWKGNDLDAIVSTNYIPFGAGPRLCVGAYFAKLLMAIFIHHLCRYRWSMKAEVTVTRSYMLMFPRGCDVQISKDTQEHDSDG
Protein: Growth hormone secretagogue receptor type 1 (GH-releasing peptide receptor) (Ghrelin receptor) (C7G181)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRSRSGTMREGSAENRTGGESPLRLFPAPVLTGITVACVLLFVVGVLGNMMTMLVVSRFRDMRTTTNFYLSSMAFSDLLIFLCMPLDLFRLWQYRPWNFGDLLCKLFQFISESCTYSTILNITALSVERYVAICFPLRAKVIITKRKVKLVILILWAISFISAGPIFVLVGVEHENGTNPLSTNECRATEYAIRSGLLTIMVWISSIFFFLPVFCLTVLYSLIGRKLWRRKRKNIGPSTVIRDKNNKQTVKMLVVVVFAFILCWLPFHVGRYLFSKSFEAGSLEIAVISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAACRLFGLKTLPKKRLSSTKQDSSRVWTEPTVAT
Protein: FAD-binding PCMH-type domain-containing protein (Q5BA56)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MRLTPAAAAASLLSLSAPELTVATAAESYSADQCCAALFSSSIGDKVVFPGNAAYRDSVTSYWAVNVQLEPTCIVQPQSADDVSVAVQTLAGAGGNSRCKFAVRSGGHMTWAGSNNIETGVTIDLSLMNSTIYDKEAKVATILPGSRWEAVYKTLEEYNVVVPGGRTGPVGVGGFLLGGGNSFHAARVGLACDNVINYEVVLASGRIVNANNNTNVELFKALKGGSNNFGIVTKYELKAIDNAHLWGGINVFDNSTTNQQIDALVKFIDNIENDPYASWIGLWQYNSTTRKTLISSPWDYTKPVAHPAAFDDFSKIPRISSSNRFATLYNLTSELQQAAGYRWTHPANGNSDIFLTSTYLNSAAVLHKTIEILNKKIEAAVPVAQGKDWSIMVIIQPWPKIYWQRNQNNGVGNVLGLDRFDENMLQVLYDYSWDNAADDELFQRLCREAMAELDEYAKSIGKYNEYIYLNYADVSQNPLRGYGDENVEFIRQVAERYDPDGVFQSQVPGGFKVSEA
Protein: Enhancer of filamentation 1 homolog (Q9YHC0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MKYKNLMARALYDNVPECAEELAFRKGDILTVIEQNTEGLEGWWLCSLHGRQGIVPGNRVKLLIGPVVQDGPSSQDMSNSGLTHQSFNQQKIYQVPSSHASARDPVYQVPPSHTNQGIYQIPTGHGVAGQDIYQVPPSTQRCLDGPPLTNKVVTPVRSGQGYVYEFPSKYQKDTYXIPPVRPLQGIYDIPPTSAKGTAHSVPTGDAKALGVYDVPPAKGMYATPPSTCRDDVGLRDNLQDFSSPAGHNARQEGVYDIPPPITKATGKELIKKFSSEGLALTDGAPHKQSVYDIPVNHHNHFLGQQIAPQKDVYDTP