wanglab/gogpt-training-data huggingface dataset:
Protein: Protein sprouty homolog 4 (Spry-4) (Q9WTP2)
Organism: Mus musculus (Mouse)
Function: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras (By similarity). Inhibits Ras-independent, but not Ras-dependent, activation of RAF1 (By similarity). Represses integrin-mediated cell spreading via inhibition of TESK1-mediated phosphorylation of cofilin (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9C004}. Cell projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor). Colocalizes with TESK1 in vesicular spots in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q9C004}.
Interaction partners:
- E3 ubiquitin-protein ligase CBL
- Growth factor receptor-bound protein 2
- Dual specificity protein phosphatase 6
Sequence:
MEPPVPQSSVPVNPSSVMVQPLLDSRAPHSRLQHPLTILPIDQMKTSHVENDYIDNPSLAPATGPKRPRGGPPELAPTPARCDQDITHHWISFSGRPSSVSSSSSTSSDQRLLDHMAPPPVAEQASPRAVRLQPKVVHCKPLDLKGPTAPPELDKHFLLCEACGKCKCKECASPRTLPSCWVCNQECLCSAQTLVNYGTCMCLVQGIFYHCTNEDDEGSCADHPCSCSGSNCCARWSFMGALSVVLPCLLCYLPATGCVKLAQRGYDRLRRPGCRCKHTNSVICKAASGDTKTSRSDKPF
Protein: Probable oxidoreductase (O33263)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable short-chain type dehydrogenase/reductase
- L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
Sequence:
MTSLQGKVVFITGAARGIGAEVARRLHNKGAKLVLTDLSKSELAVMGAELGGDDRLLTVVADVRDLPAMQAAAETAVERFGGIDVVVANAGIASYGSVLKVDPQAFRRVLDVNLLGNFHTVRATLPALIDRRGYVLIVSSLAAFAAPPGMAPYNMSKAGNEHFANALRLEVAHLGVSVGSAHMSWIDTALVRDTKADLPAFAELLARLPWPLNKTTSVNKCAAAFVNGIEGRKDRVYCPGWVALFRWLKPLLSTRVGQRPIRNTVAKLMPQMDAEVAALGRFASAYTESLENS
Protein: Rcn1p (A0A1D8PPK4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein phosphatase
- Calcineurin subunit B
- Vacuolar calcium ion transporter
- Calcium-transporting ATPase
Sequence:
MPRKPTNTLIITNIDDSLLSNPEPIISLLGDQPYMIELIVLMKFKRILLYCQTSKIATKTKTFLLNQWETTTIGGGGGGGGGGGSGGGNSISISYSLKDNSRILDPEEEDEEDGKDGGGKGGRFLDIPKDLEIKRFLISPPASPHSEWDDWDKVEEGPNETNIHDYLWEKLKTHENEEKEKDSGISEDDDGCESIKKVELPKIVLNATDN
Protein: Mitochondrial fission 1 protein B (FIS1 homolog B) (AtFIS1b) (Q94CK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the peroxisomal and mitochondrial division machineries. Plays a role in promoting the fission of mitochondria and peroxisomes. In association with PEX11C, PEX11D, PEX11E and DRP3A, is involved in cell cycle-associated constitutive self-replication of preexisting peroxisomes.
Subcellular location: Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Peroxisomal membrane protein 11E
- Peroxisomal membrane protein 11C
- Peroxisomal membrane protein 11D
- Dynamin-related protein 3A
- Dynamin-related protein 3B
- Peroxisomal membrane protein 11B
- Dynamin
- Peroxisome biogenesis protein 16
- Dynamin-like protein ARC5
- Peroxisomal membrane protein PEX14
Sequence:
MDAAIGKVFDSVSDFFSGAASASADEFPLCDSDIISGCEKELAEAQDEGRKKECIMRLSWALVHSKMPSDIQRGIAMLEALVVNDTSAMKLREKLYLLALGYYRSGDFSRSRDCIERCLEVEPESGQAQALKKAIEDRIVKDGVIGVGIAVTAVGVVAGIAAAILRS
Protein: ATP synthase F(0) complex subunit C1, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 1) (ATP synthase proteolipid P1) (ATPase protein 9) (ATPase subunit c) (Proton-conducting channel, ATP synthase F(0) complex subunit c) (P32876)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
Sequence:
MQTTGALLISPALIRSCTRGLIRPVSASFLSRPEIQSVQPSYSSGPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
Protein: Lysophosphatidic acid receptor 6 (LPA receptor 6) (LPA-6) (Oleoyl-L-alpha-lysophosphatidic acid receptor) (P2Y purinoceptor 5) (P2Y5) (Purinergic receptor 5) (RB intron encoded G-protein coupled receptor) (P43657)
Organism: Homo sapiens (Human)
Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18297070, ECO:0000269|PubMed:36173926}; Multi-pass membrane protein {ECO:0000269|PubMed:18297070}.
Interaction partners:
- Lysophosphatidic acid receptor 3
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 2
- Guanine nucleotide-binding protein subunit alpha-12
- Lipase member H
- Muscarinic acetylcholine receptor M1
- Lysophosphatidic acid receptor 5
- Lysophosphatidic acid receptor 4
- Angiotensinogen
- Proteinase-activated receptor 1
Sequence:
MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLAMSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCFCFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA
Protein: Staphylocoagulase (Q846V4)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
IVTKDYSKESRVNENSKYGTLISDWYLKGRLTSLESQFINALGILETYHYGEKEYKDAKDKLMTRILGEDQYLLERKKVQYEEYKKLYKKYKEENPTSKVKMKTFDQYTIEDLTMREYNELTESLKSAVKDFEKDVEIIENQHHDLKPFTDEMEEKATARVDDLANKAYSVYFAFVRDTQHKTEALELKAKVDLVLGDEDKPHRISNERIEKEMIKDLESIIEDFFIETGLNKPDNITSYDSSKHHYKNHSEGFEALVKETREAVTNANDSWKTKTVKKYGETVTKPPVVKEEKKVEEPQAPKVSEKVDVQETVGTEETTQPVAQPLVKIPQGTIYGETVKGPEYLTMENKTLQGEIVQGPDFPTMEQNRPSLSDNYTQPTTPNPILKGLEGSSSKLEIKPQGTESTLKGTQGESSDIEVKPQASETTEASHYPARPQFNKTPKYVKYRDAGTGIREYNDGTFGYEARPRFNKPSETNAYNVTTHANGQVSYGARPTQNKPSKTNAYNVTTHGNGQVSYGARPTYKKPSKTNAYNVTTHANGQVSYGARPTQNKPSKTNAYNVTTHGNGQVSYGARPTQNKPSKTNAYNVTTHGNGQVSYGARPTQNKPSKTNAYNVTTHANGQVSYGARPTYKKPSETNAYNVTTHADGTATYGSRVTK
Protein: Cysteine proteinase 2 (EC 3.4.22.-) (Prestalk cathepsin) (P04989)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cysteine proteinases 1 and 2 are believed to participate in the breakdown of protein during differentiation of Dictyostelium as a response to starvation.
Subcellular location: Lysosome.
Interaction partners:
- Cathepsin D
Sequence:
MRLLVFLILLIFVNFSFANVRPNGRRFSESQYRTAFTEWTLKFNRQYSSSEFSNRYSIFKSNMDYVDNWNSKGDSQTVLGLNNFADITNEEYRKTYLGTRVNAHSYNGYDGREVLNVEDLQTNPKSIDWRTKNAVTPIKDQGQCGSCWSFSTTGSTEGAHALKTKKLVSLSEQNLVDCSGPEENFGCDGGLMNNAFDYIIKNKGIDTESSYPYTAETGSTCLFNKSDIGATIKGYVNITAGSEISLENGAQHGPVSVAIDASHNSFQLYTSGIYYEPKCSPTELDHGVLVVGYGVQGKDDEGPVLNRKQTIVIHKNEDNKVESSDDSSDSVRPKANNYWIVKNSWGTSWGIKGYILMSKDRKNNCGIASVSSYPLA
Protein: Charged multivesicular body protein 3 (Chromatin-modifying protein 3) (Vacuolar protein sorting-associated protein 24) (rVps24p) (Q8CGS4)
Organism: Rattus norvegicus (Rat)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12878588}. Membrane {ECO:0000269|PubMed:12878588}; Lipid-anchor {ECO:0000269|PubMed:12878588}. Endosome {ECO:0000269|PubMed:12878588}. Late endosome membrane {ECO:0000250}. Note=Localizes to the midbody of dividing cells. {ECO:0000250}.
Interaction partners:
- Charged multivesicular body protein 6
- Similar to RIKEN cDNA 1500016L11
- Charged multivesicular body protein 1A
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 4B
- Charged multivesicular body protein 7
- Charged multivesicular body protein 4c
- Vacuolar-sorting protein SNF8
Sequence:
MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKEVCVVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEAAEMEIDRILFEITAGALGKAPSKVTDALPEPEPAGAMAASEGDEEDDEEDLEAMQSRLATLRS
Protein: Probable heat shock protein ssa1 (Q10265)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein psi1
- Hsp70 nucleotide exchange factor fes1
- Heat shock protein 104
- Heat shock protein 90 homolog
- Heat shock protein sti1 homolog
- Probable heat shock protein ssa2
- Mitochondrial protein import protein mas5
- Ribosome-associated molecular chaperone sks2
- Heat shock protein 16
- Zuotin
Sequence:
MSKSIGIDLGTTYSCVGHFSNNRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTIFDAKRLIGRRFNDPEVQSDMKHWPFKVIEKDGKPLIQVEFKGETKTFTPEEISSMVLLKMRESAEAFLGGKVTDAVVTVPAYFNDSQRQATKDAGLIAGLNVLRIINEPTAAAIAYGLDRSNQHETNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDSRLVNHFAQEFKRKNKKDITGNARAVRRLRTACERAKRTLSSSAQASIEIDSLYEGIDFYTSITRARFEELCADLFRNTMEPVEKVLRDSKIDKSSVNEIVLVGGSTRIPRIQKLVSDFFNGKEPCKSINPDEAVAYGAAVQAAILVGDTSEKTQDLLLLDVAPLSLGIETAGGVMTPLIKRNTTIPTKKSEVFSTYADNQPGVLIQVFEGERARTKDCNLLGKFELSGIPPAPRGVPQIEVTFDVDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDRMVSEAEKYKAEDEAETSRIQAKNHLESYAYSLRNSLDDPNLKDKVDASDKEAIDKAVKETIEWLDHNTTAAKDEYEDKQKELEGVANPIMAKIYQAGGAPGGAPGGMPGGAPGGAPGGADNGPEVEEVD
Protein: Protein FAM24B (Q8N5W8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MPVIAGGILAALLLLIVVVLCLYFKIHNALKAAKEPEAVAVKNHNPDKVWWAKNSQAKTIATESCPALQCCEGYRMCASFDSLPPCCCDINEGL
Protein: Protocadherin gamma A3 (Protocadherin gamma subfamily A, 3) (Q91XY5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MIRLGQGTAGALLCALLGTLCAAGFRQIRYSVPEELDKGSFVGNISKDLGLEPRELAERGVRIISRGKSQLFSLDPRSGSLVTRGRIDREELCAQSAPCLVSFNILVEDKLKIFEVEVDISDINDNAPSFPTEELEIKIGELTVPGTRFPLKTAFDPDVGMNALQNYKLNSNDYFSLAVNSVIDDAKYPELVLERALDREKKAVHQLDLIASDGGDPVHTSKLCIQVIVSDANDNPPVFTKPEYHVSVLENVPVGTRLITVNATDPDEGFNAQVSYILDKMPGKIAQVFHLNSVTGDISILKSLDYEDAVFYEIKIEAQDGPGLFSRAKVLVTVLDVNDNAPEVSVTSLTGSVPEEAPAGREIALINVHDRDSGQNGQVTVFVLGNLPFTLEKSIDQYYRLVTARSLDHEEVSQYNISLRATDGGSPPLSTETHITLHVSDINDNPPTFTHASYSAYIPENNARGASIFSVTAQDPDTDKNAQVTYSLAEDTLQGLPLSSYISINSNTGVLYALCSFDYEQFRDLQLQITARDSGTPPLSSNTTLNLFVLDQNDNTPEILYPTLPVDGSTGVELAPRSADPGYLVTKVVAVDKDSGQNAWLSYRLLKASEPGLFSVGLHTGEVRTARALLDRDALKQSLVVAVQDHGQPPLSATVTLTIAVADSIPDILGDLESIHTPANPQNSDLTLYLVVAVAVVSCIFLAFVIVLLALRLRRWYSSRLQASGNGLAGIPASHFVGLDGVQAFLQTYSQEVSLTAGSRKSHLIFPQPNYADTLISQESCGKSEPLIIPQDLLETKEDPTLPQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Iron(3+)-hydroxamate import ATP-binding protein FhuC (EC 7.2.2.16) (Ferric hydroxamate uptake protein C) (Ferrichrome transport ATP-binding protein FhuC) (Iron(III)-hydroxamate import ATP-binding protein FhuC) (P07821)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:1551849}; Peripheral membrane protein {ECO:0000269|PubMed:1551849}. Note=FhuB mediates the association of FhuC with the cytoplasmic membrane. {ECO:0000269|PubMed:1551849}.
Interaction partners:
- Iron
- Iron
- Ferrichrome outer membrane transporter/phage receptor
- Vitamin B12 import system permease protein BtuC
- Fe
- Fe
- Ferric enterobactin transport system permease protein FepD
- Ferric enterobactin transport system permease protein FepG
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Vitamin B12-binding protein
Sequence:
MQEYTNHSDTTFALRNISFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPPAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLSLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEIMRGETLEMIYGIPMGILPHPAGAAPVSFVY
Protein: Ubiquitin-conjugating enzyme E2 D2 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D2) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating enzyme E2(17)KB 2) (Ubiquitin-conjugating enzyme E2-17 kDa 2) (Ubiquitin-protein ligase D2) (p53-regulated ubiquitin-conjugating enzyme 1) (P62837)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 1
- CCR4-NOT transcription complex subunit 4
- E3 ubiquitin-protein ligase RBX1
- E3 ubiquitin-protein ligase NEDD4-like
- E3 ubiquitin-protein ligase Mdm2
- Polyubiquitin-C
- Baculoviral IAP repeat-containing protein 3
- Mitochondrial ubiquitin ligase activator of NFKB 1
- E3 ubiquitin-protein ligase RNF38
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM
Protein: Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (cp38a) (Q90336)
Organism: Cyprinus carpio (Common carp)
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Mapk14a is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSQKERPTFHRQEVNKTIWEVPVRYQNLSPVGSGAYGTVCSAYDEKTGLKVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPATSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNMTVDIWSVGCIMAELLTGRTLFPGTDHINQLQQIMRLTGTPPASLISRMPSHEARTYINSLPQMPKRNFSEVFIGANPQAVDLLEKMLVLDTDKRITAAEALAHPYFAQYHDPDDEPEAEPFDQSFESRELDIEEWKRQTYEEVISFEPPVFDGDEMES
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P00375)
Organism: Mus musculus (Mouse)
Function: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25980602}. Cytoplasm {ECO:0000269|PubMed:25980602}.
Interaction partners:
- Thymidylate synthase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Folylpolyglutamate synthase, mitochondrial
- Bifunctional purine biosynthesis protein ATIC
- Methionine synthase
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Trifunctional purine biosynthetic protein adenosine-3
- Sepiapterin reductase
Sequence:
MVRPLNCIVAVSQNMGIGKNGDLPWPPLRNEFKYFQRMTTTSSVEGKQNLVIMGRKTWFSIPEKNRPLKDRINIVLSRELKEPPRGAHFLAKSLDDALRLIEQPELASKVDMVWIVGGSSVYQEAMNQPGHLRLFVTRIMQEFESDTFFPEIDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVYEKKD
Protein: NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (F1QCG4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- S-phase kinase-associated protein 1
- Inhibitor of nuclear factor kappa B kinase subunit beta.
- Nuclear factor NF-kappa-B p105 subunit isoform X1
- Transcription factor p65
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa B kinase regulatory subunit gamma.
- Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon.
- NF-kappa-B inhibitor alpha
- F-box only protein 22
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MDLHRAAMLNFVDCNVDEMDTKNRKTQQCEDRVDSGVDSLKEEEYETREISEEMEKLTIASLKETICEPWAKVVTEDGDTYLHLAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIQTQHLRSILTFPNYSGHTCLHIAAINNYLSMVESLVQLGADVDAKEQCSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQLYSRTALKFTVMPESESEESEDELMSEDDCIYDDIRLCGR
Protein: Trimeric intracellular cation channel type B (TRIC-B) (TRICB) (Mitsugumin-33B) (Transmembrane protein 38B) (Q9DAV9)
Organism: Mus musculus (Mouse)
Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17611541}; Multi-pass membrane protein {ECO:0000269|PubMed:17611541}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Cartilage-associated protein
- Prolyl 3-hydroxylase 1
- Membrane-bound transcription factor site-2 protease
- Interferon-induced transmembrane protein 5
- SEC24 homolog D, COPII coat complex component)
- Cyclic AMP-responsive element-binding protein 3-like protein 1
Sequence:
MEYPWDDLTLAFSRTSMFPFFDIAHYLVSVMALKQRPGAVAAAWNNPLASWLSAMLHCFGGGILSCMLLAESPLKFLTNHTNILLASSIWYIVFFCPRDLVSQGYSYQPIQFLAAGMKEVTRTWKIVGGVSDANSYYRNAWIVMIVVGWARGAGGAVVTACEQLLKGDWKPEGDEWLKMSFPCKITLLGSIMFTFQHTRHLAISKHDLMFLYTIFLVTIKVTMMMTKDTAVTLTPFEDTLTRMLFGRRQQQQFSSSEKKTEVKPSSNGSASSASKRGAEPSGGAKRHAKKED
Protein: Cytosolic beta-glucosidase (EC 3.2.1.21) (Cytosolic beta-glucosidase-like protein 1) (Cytosolic galactosylceramidase) (EC 3.2.1.46) (Cytosolic glucosylceramidase) (EC 3.2.1.45) (Cytosolic glycosylceramidase) (Cytosolic GCase) (Glucosidase beta acid 3) (Glucosylceramidase beta 3) (Klotho-related protein) (KLrP) (Q9H227)
Organism: Homo sapiens (Human)
Function: Neutral cytosolic beta-glycosidase with a broad substrate specificity that could play a role in the catabolism of glycosylceramides. Has a significant glucosylceramidase activity in vitro. However, that activity is relatively low and its significance in vivo is not clear. Hydrolyzes galactosylceramides/GalCers, glucosylsphingosines/GlcSphs and galactosylsphingosines/GalSphs. However, the in vivo relevance of these activities is unclear. It can also hydrolyze a broad variety of dietary glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro and could therefore play a role in the metabolism of xenobiotics. Possesses transxylosylase activity in vitro using xylosylated ceramides/XylCers (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) as xylosyl donors and cholesterol as acceptor. Could also play a role in the catabolism of cytosolic sialyl free N-glycans.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12594539, ECO:0000269|PubMed:17595169}.
Interaction partners:
Sequence:
MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYYNKIIDDLLKNGVTPIVTLYHFDLPQTLEDQGGWLSEAIIESFDKYAQFCFSTFGDRVKQWITINEANVLSVMSYDLGMFPPGIPHFGTGGYQAAHNLIKAHARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQEAAKRAITFHLDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGTADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVPWGVCKLLKYIKDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQELFKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL
Protein: Retrotransposon hot spot (RHS) protein, putative retrotransposon hot spot protein 4 (RHS4), putative (Q8IFI8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Zinc-finger protein ZPR1, putative
Sequence:
MNQQFPIEGRGDIEGRRRENEEAARNDAEPPAVQQRVENNNQPQWRLFSRIDAVLLEGRVHPENVSVNDFLRRNLLDDMDLDQRLLRASMFAFVQRCEEYINDVNALNRIFATPEYKVYKRFVSVYGFFEDEGILDLQQWQQADEEAKVRLQADIRGLRDGERLWIVVNALLNNALNVALERAAQTAASAVEIKGVYDSIYNAKWSYVMSGYRREPLGMRVFDGKPQRIWTEAEVDINPDPANLDARVPERPYGLEIFVLTSEEGWPYDRFALGHTEMCGENFKHVYIRREIMRVWYIIQRGLQGRWVEKAEITPRHIVIGTPGIGKSYGVGSFLLHSLLHFNDGMLDVVAYFTDGIAYLIYNKKPGEEGRVERYKFPEDAVDAIAALVSKKKKGHIIVDICRNAQTPPDGLPVYAWGVTLLTSPDEAHFHHWAKDKRSRRVIINCDDVRDMKAFVAWKKLCVLSEEAPRDKTKQQLKEDLEKEWKIVEERIDMVGPLPRFVFSAPEYHERLESVRKEARQLDSDNGKKYGKIIGKSAGWQNDVVTHKLVKIVRVSSGTVNVDSYRCRSLSVTIGNMLICTLFGILIVEMTSKEITLSDECVGANAFERLALLSLLFPRVFKVIANNLKYLRRGGEIADRRSILNDMASQQLRLIGQKALPAARQRPIERCEYMVLYLPATGNEPVVDGFFFVEGRFRRNRDGTAAPIPSNIAVLLQVTKSDRHPTATDKVQKFRKNMARYFSDWGAFSRDMVWEMIYINSVNGGTITIRQLCEGPPDRARGGDGGPLGPQTFWESIDQFQVTLKETMQAELIRAYRRESGMRNAPGLMGLAGRRRAREEVVEGRGDVAMRRRGRR
Protein: Protein ripply (Protein AmphiSom) (Q5I2D0)
Organism: Branchiostoma belcheri (Amphioxus)
Function: May play a role in somitogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q2WG80}.
Interaction partners:
Sequence:
MEATRFTFNTATLCSAQHCNCHKLTTKASGMPVQPPVWRPWIVTERDILRRNAIRERRSKPYARPSSTSNGSTRGPEPGPTSFQHPVKLHWSKPVYDYMYQYGKQLLDAFPVQATICIVDEDPAQSDDSDFESDYEDDSDTDYKPLKRNAPILN