wanglab/gogpt-training-data huggingface dataset:
Protein: Discoidin, CUB and LCCL domain-containing protein 2 (CUB, LCCL and coagulation factor V/VIII-homology domains protein 1) (Endothelial and smooth muscle cell-derived neuropilin-like protein) (Q96PD2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000269|PubMed:11973641}; Single-pass type I membrane protein {ECO:0000269|PubMed:11973641}.
Interaction partners:
- Semaphorin-4B
Sequence:
MASRAVVRARRCPQCPQVRAAAAAPAWAALPLSRSLPPCSNSSSFSMPLFLLLLLVLLLLLEDAGAQQGDGCGHTVLGPESGTLTSINYPQTYPNSTVCEWEIRVKMGERVRIKFGDFDIEDSDSCHFNYLRIYNGIGVSRTEIGKYCGLGLQMNHSIESKGNEITLLFMSGIHVSGRGFLASYSVIDKQDLITCLDTASNFLEPEFSKYCPAGCLLPFAEISGTIPHGYRDSSPLCMAGVHAGVVSNTLGGQISVVISKGIPYYESSLANNVTSVVGHLSTSLFTFKTSGCYGTLGMESGVIADPQITASSVLEWTDHTGQENSWKPKKARLKKPGPPWAAFATDEYQWLQIDLNKEKKITGIITTGSTMVEHNYYVSAYRILYSDDGQKWTVYREPGVEQDKIFQGNKDYHQDVRNNFLPPIIARFIRVNPTQWQQKIAMKMELLGCQFIPKGRPPKLTQPPPPRNSNDLKNTTAPPKIAKGRAPKFTQPLQPRSSNEFPAQTEQTTASPDIRNTTVTPNVTKDVALAAVLVPVLVMVLTTLILILVCAWHWRNRKKKTEGTYDLPYWDRAGWWKGMKQFLPAKAVDHEETPVRYSSSEVNHLSPREVTTVLQADSAEYAQPLVGGIVGTLHQRSTFKPEEGKEAGYADLDPYNSPGQEVYHAYAEPLPITGPEYATPIIMDMSGHPTTSVGQPSTSTFKATGNQPPPLVGTYNTLLSRTDSCSSAQAQYDTPKAGKPGLPAPDELVYQVPQSTQEVSGAGRDGECDVFKEIL
Protein: Ras-related protein Rab-1A (EC 3.6.5.2) (YPT1-related protein) (P62821)
Organism: Mus musculus (Mouse)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion (By similarity). Required to modulate the compacted morphology of the Golgi. Regulates the level of CASR present at the cell membrane (By similarity). Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria (By similarity). Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P62820}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62820}. Membrane {ECO:0000250|UniProtKB:P62820}. Melanosome {ECO:0000269|PubMed:22854043}. Note=Alternates between membrane-associated and cytosolic forms. {ECO:0000250|UniProtKB:P62820}.
Interaction partners:
- General vesicular transport factor p115
- Guanine nucleotide exchange factor C9orf72 homolog
- Ras-related protein Rab-1B
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex 8
- Rab GDP dissociation inhibitor beta
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 3
- TBC1 domain family member 20
Sequence:
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC
Protein: Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) (O14241)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, actin patch.
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1
- Actin
- Protein dip1
- Actin-binding protein wsp1
- Structure-specific endonuclease subunit slx4
Sequence:
MLSLDYNNIFIYELLTERFSSENPSSIDQVVTDFDGVTFHISTPEEKTKILISLSMKCYPELVNYGTLDLLKQIYGAYVHEPEMGYNFSILIDLQQLPATDEEKEQLAMSISMLKRNVLAAPFHRAFTKQAELADLARKDPENAPMLDKQATSQELMAIHYRDEETIVLWPEHDRVTVVFSTKFREETDRIFGKVFLQEFVDARRRPAIQTAPQVLFSYRDPPLEIRDIQGIQKGDDFGFVTFVLFERHFTPQNREDCISHIQVFRNTLHFHIKASKAYMHQRMRKRVADFQKVLNRAKPDVELERKTATGRSFVRA
Protein: Phosphate regulon transcriptional regulatory protein PhoB (P0AFJ5)
Organism: Escherichia coli (strain K12)
Function: This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphate regulon sensor protein PhoR
- Phosphate-specific transport system accessory protein PhoU
- RNA polymerase sigma factor RpoD
- Phosphate-binding protein PstS
- Alkaline phosphatase
- Sensor protein PhoQ
- Sensor protein CreC
- Outer membrane porin PhoE
- Phosphate import ATP-binding protein PstB
- Sensor histidine kinase EnvZ
Sequence:
MARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDPTSHRVMAGEEPLEMGPTEFKLLHFFMTHPERVYSREQLLNHVWGTNVYVEDRTVDVHIRRLRKALEPGGHDRMVQTVRGTGYRFSTRF
Protein: Peroxiredoxin-1 (EC 1.11.1.24) (Macrophage 23 kDa stress protein) (Osteoblast-specific factor 3) (OSF-3) (Thioredoxin peroxidase 2) (Thioredoxin-dependent peroxide reductase 2) (Thioredoxin-dependent peroxiredoxin 1) (P35700)
Organism: Mus musculus (Mouse)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
Interaction partners:
- Sulfiredoxin-1
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- Tyrosine-protein kinase ABL1
- Thioredoxin, mitochondrial
- Cyclin-dependent kinase 5
- Thioredoxin reductase 1, cytoplasmic
- Peroxiredoxin-2
- Glutathione peroxidase 1
- Cyclin-dependent kinase 5 activator 1
Sequence:
MSSGNAKIGYPAPNFKATAVMPDGQFKDISLSEYKGKYVVFFFYPLDFTFVCPTEIIAFSDRADEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLISDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEIIRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK
Protein: MAGUK p55 subfamily member 7 (Q5T2T1)
Organism: Homo sapiens (Human)
Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact.
Subcellular location: Membrane; Peripheral membrane protein {ECO:0000269|PubMed:17332497}. Lateral cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:17332497}. Cell junction, tight junction {ECO:0000269|PubMed:17237226, ECO:0000269|PubMed:17332497}. Cell junction, adherens junction {ECO:0000269|PubMed:17237226, ECO:0000269|PubMed:17332497}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:26481050}. Note=In epidermal cells, detected primarily at the lateral cell membrane. {ECO:0000269|PubMed:17332497}.
Interaction partners:
- Protein lin-7 homolog C
- Protein lin-7 homolog A
- Disks large homolog 1
Sequence:
MPALSTGSGSDTGLYELLAALPAQLQPHVDSQEDLTFLWDMFGEKSLHSLVKIHEKLHYYEKQSPVPILHGAAALADDLAEELQNKPLNSEIRELLKLLSKPNVKALLSVHDTVAQKNYDPVLPPMPEDIDDEEDSVKIIRLVKNREPLGATIKKDEQTGAIIVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIQILAQSQGAITFKIIPGSKEETPSKEGKMFIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEADANPRAGLIPSKHFQERRLALRRPEILVQPLKVSNRKSSGFRKSFRLSRKDKKTNKSMYECKKSDQYDTADVPTYEEVTPYRRQTNEKYRLVVLVGPVGVGLNELKRKLLISDTQHYGVTVPHTTRARRSQESDGVEYIFISKHLFETDVQNNKFIEYGEYKNNYYGTSIDSVRSVLAKNKVCLLDVQPHTVKHLRTLEFKPYVIFIKPPSIERLRETRKNAKIISSRDDQGAAKPFTEEDFQEMIKSAQIMESQYGHLFDKIIINDDLTVAFNELKTTFDKLETETHWVPVSWLHS
Protein: BTB domain-containing protein (Q18030)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLINTNSTSDATTIIDLQNRYYHVNAALEKTSFDVDGFKWQIVFDCQQIIFTLISEMAEFCSIDLIIHCTDFKSSSTFTSQFERSGESVVHEWLPGGRHVQLEIDQTIHESQFSGLDFSQPFDSSNVVLKVEDEEFHVHTFVLSMASQYFKVLFNGSFIESSDLTKPIELKGISSCSFRNLLNCIYGYPSVFRITRGNIVELLELSHFFDCKNVTMFCEYNLCNDTCYNIRSTQKMEWAIRYNLNTLKNKLLRHEPYLVDLLSLT
Protein: ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 (F8VVT9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRGAGALQRRTTTYLISLTLVKLESVPPPPPSPSAAAAGAAGARGSETGDPGSPRGAEEPGKKRHERLFHRQDALWISTSSAGTGGAEPPALSPAPASPARPVSPAPGRRLSLWAVPPGPPLSGGLSPDPKPGGAPTSSRRPLLSSPSWGGPEPEGRAGGGIPGSSSPHPGTGSRRLKVAPPPPAPKPCKTVTTSGAKAGGGKGAGSRLSWPESEGKPRVKGSKSSAGTGASVSAAATAAAAGGGGSTASTSGGVGAGAGARGKLSPRKGKSKTLDNSDLHPGPPAGSPPPLTLPPTPSPATAVTAASAQPPGPAPPITLEPPAPGLKRGREGGRASTRDRKMLKFISGIFTKSTGGPPGSGPLPGPPSLSSGSGSRELLGAELRASPKAVINSQEWTLSRSIPELRLGVLGDARSGKSSLIHRFLTGSYQVLEKTESEQYKKEMLVDGQTHLVLIREEAGAPDAKFSGWADAVIFVFSLEDENSFQAVSRLHGQLSSLRGEGRGGLALALVGTQDRISASSPRVVGDARARALCADMKRCSYYETCATYGLNVDRVFQEVAQKVVTLRKQQQLLAACKSLPSSPSHSAASTPVAGQASNGGHTSDYSSSLPSSPNVGHRELRAEAAAVAGLSTPGSLHRAAKRRTSLFANRRGSDSEKRSLDSRGETTGSGRAIPIKQSFLLKRSGNSLNKEWKKKYVTLSSNGFLLYHPSINDYIHSTHGKEMDLLRTTVKVPGKRPPRAISAFGPSASINGLVKDMSTVQMGEGLEATTPMPSPSPSPSSLQPPPDQTSKHLLKPDRNLARALSTDCTPSGDLSPLSREPPPSPMVKKQRRKKLTTPSKTEGSAGQAEAKRKMWKLKSFGSLRNIYKAEENFEFLIVSSTGQTWHFEAASFEERDAWVQAIESQILASLQCCESSKVKLRTDSQSEAVAIQAIRNAKGNSICVDCGAPNPTWASLNLGALICIECSGIHRNLGTHLSRVRSLDLDDWPRELTLVLTAIGNDTANRVWESDTRGRAKPSRDSSREERESWIRAKYEQLLFLAPLSTSEEPLGRQLWAAVQAQDVATVLLLLAHARHGPLDTSVEDPQLRSPLHLAAELAHVVITQLLLWYGADVAARDAQGRTALFYARQAGSQLCADILLQHGCPGEGGSAATTPSAATTPSITATPSPRRRSSAASVGRADAPVALV
Protein: cAMP-dependent protein kinase inhibitor beta (PKI-beta) (cAMP-dependent protein kinase inhibitor, testis isoform) (Q04758)
Organism: Mus musculus (Mouse)
Function: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Interaction partners:
- cAMP-dependent protein kinase inhibitor gamma
Sequence:
MGGGTSPEAQQDSVMRTDSSEMTDVESVITSFASSARAGRRNALPDIQSSLATSGSSDLPLKLEALAVKEDAKTKNEEKDQGQPKTPLNEGK
Protein: Polyketide cyclase (O69685)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MGQVSAASTILINAEPTATLDALADYETVRPKILSPHYSEYQVLEGGKGRGTVAKWRLQATQSRVRDVQVNVDVAGHTVIEKDMNSSMVTNWTVAPAGPGSSVTVKTTWTGAGGVKGFFEKTFAPLGLKKIQAEVLSNLKTELEGDA
Protein: Ribosomal protein L37 (Q386L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L17, putative
- 40S ribosomal protein S25
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L28, putative
- 60S ribosomal protein L13a, putative
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L44
- 60S ribosomal protein L6, putative
- 40S ribosomal protein S17, putative
Sequence:
MTKGTTSMGQRHGRTHILCRRCGRNAYHVQWERCAACAYPRAQRRRYNWSVKAIKRRRTGTGRCRYLKVVHRRIRNHFKTDIKA
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (Q95T90)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MARIVESNFVPLAVGVVAVLAGALIVHYLLNKKSTKPRREPNRTARLRTLVDPNDKYLLPLIEKENLSHDTRRFQFGLPSKQHVLGLPVGQHIHLIATIDNELIIRPYTPISSDEDVGYVDLVVKVYFKDSHPKFPAGGKMTQHLEQLELGDKISFRGPSGRLQYLGNGTFSIKKLRKDPPKHVTAKRVNMIAGGTGITPMLQLAREVLKRSDKDKTELALLFANQSEKDILLRAELDELAQKHPDQFKIWYTVDKANEGELQ
Protein: Dickkopf long isoform (Dickkopf-related protein 3a precursor) (C1K6H6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFLLGFSLCLAVVHGIVPEIPKTDMDIIANMETNAAQEQTMSDVLKEVEELMEDTQHKLEDAVHQMDNETAKSSLHPQNVSSNLQNYSAIETIAGNQTISIGERINKTTDNSTEETNNLSSIQPRDKENIVDHECVIDEDCEKGKYCLYETHSSKCLPCKQLDASCTKDEECCAGQLCVWGQCTINITKGDAGTICQYQTDCKEDFCCAFHKALLFPVCIAKPIERERCIISANHLMELLSWDMDGEGPQEHCPCAGELQCQHRGRGALCLKSQNSSEEELTDTLYSEIDYIV
Protein: Type-4 uracil-DNA glycosylase (EC 3.2.2.27) (TTUDGA) (TthUDG) (Q5SKC5)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair as well as from single-stranded DNA. Specifically recognizes uracil that is flipped out from double-stranded DNA.
Interaction partners:
Sequence:
MTLELLQAQAQNCTACRLMEGRTRVVFGEGNPDAKLMIVGEGPGEEEDKTGRPFVGKAGQLLNRILEAAGIPREEVYITNIVKCRPPQNRAPLPDEAKICTDKWLLKQIELIAPQIIVPLGAVAAEFFLGEKVSITKVRGKWYEWHGIKVFPMFHPAYLLRNPSRAPGSPKHLTWLDIQEVKRALDALPPKERRPVKAVSQEPLF
Protein: Sperm mitochondrial-associated cysteine-rich protein (P15265)
Organism: Mus musculus (Mouse)
Function: Involved in sperm motility. Its absence is associated with genetic background dependent male infertility. Infertility may be due to reduced sperm motility in the female reproductive tract and inability to penetrate the oocyte zona pellucida.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8916043}. Mitochondrion membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Becomes associated with the spermatid mitochondrion capsule at step 16 of spermatogenesis.
Interaction partners:
- Outer dense fiber protein 1
Sequence:
MSDPSKTNQCPPPCCPPKPCCPPKPCCPQKPPCCPKSPCCPPKSPCCPPKPCPCPPPCPCPCPATCPCPLKPPCCPQKCSCCPKKCTCCPQPPPCCAQPTCCSSENKTESDSDTSGQTLEKGSQSPQSPPGAQGNWNQKKSNK
Protein: Mitochondrial import inner membrane translocase subunit TIM22-1 (Protein MATERNAL EFFECT EMBRYO ARREST 67) (A2RVP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM23-2
- Chloroplastic import inner membrane translocase subunit HP30-2
- Mitochondrial import inner membrane translocase subunit TIM17-2
- Mitochondrial import inner membrane translocase subunit TIM23-3
- Mitochondrial import inner membrane translocase subunit TIM23-1
- MICOS complex subunit, putative
- Outer envelope pore protein 16-3, chloroplastic/mitochondrial
- Outer envelope pore protein 16-4, chloroplastic
Sequence:
MADSSAAEPTTGASSPPVASDENSTQIQPIRMPTIEEIRAQEVWNNCAVRAVTSGVMGGGLGLMMGLFLGALDNPITHDTMTARQQFVFTAKQMGQRSWNSCKTFAVMGLVFSAAECIVEKARAKHDTVNTAIAGCVTGGSMSARGGPKAACIGCAGFATFSVLIEKFFDRHT
Protein: Cytosolic Fe-S cluster assembly factor NBP35 (Nucleotide binding protein 35) (AtNBP35) (Q8H1Q2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. Functions as Fe-S scaffold, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Essential for embryo development.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:18957412, ECO:0000269|PubMed:19084504}.
Interaction partners:
- Protein NAR1
- MMS19 nucleotide excision repair protein homolog
- Protein AE7
- Iron-sulfur cluster assembly protein 1
- Cysteine desulfurase, mitochondrial
- Protein CHLOROPLAST IMPORT APPARATUS 2
- Protein CIA1
- Anamorsin homolog
- ABC transporter B family member 25, mitochondrial
- NADPH-dependent diflavin oxidoreductase 1
Sequence:
MENGDIPEDANEHCPGPQSESAGKSDSCAGCPNQEACATAPKGPDPDLVAIAERMSTVKHKILVLSGKGGVGKSTFSAQLSFALAGMDHQVGLMDIDICGPSIPKMLGLEGQEIHQSNLGWSPVYVEDNLGVMSIGFMLPNSDEAVIWRGPRKNGLIKQFLKDVYWGEIDYLVVDAPPGTSDEHISIVQYLLPTGIDGAIIVTTPQEVSLIDVRKEVSFCKKVGVPVLGVVENMSGLSQPLKDVKFMKLATETGSSINVTEDVIACLRKNAPELLDIVACSEVFDSSGGGAERMCREMGVPFLGKVPMDPQLCKAAEQGKSCFEDNKCLISAPALKSIIQKVVPSTVMTE
Protein: Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12] (P70677)
Organism: Mus musculus (Mouse)
Function: Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis. Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42574}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Caspase-9
- Caspase-8
- Apoptotic protease-activating factor 1
- Poly [ADP-ribose] polymerase 1
- Cytochrome c, somatic
- Cytochrome c, testis-specific
- Baculoviral IAP repeat-containing protein 3
- Actin, cytoplasmic 1
- Granzyme B
Sequence:
MENNKTSVDSKSINNFEVKTIHGSKSVDSGIYLDSSYKMDYPEMGICIIINNKNFHKSTGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVCVILSHGDEGVIYGTNGPVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH
Protein: ATP synthase subunit alpha, mitochondrial (ATP synthase subunit atp-1) (Q9XXK1)
Organism: Caenorhabditis elegans
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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (Probable). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and is required for the assimilation of enterobactin-bound iron from non-pathogenic bacteria. Promotes mitochondrial accumulation of enterobactin-derived iron ions.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:30146159}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}.
Interaction partners:
- Oligomycin sensitivity conferral protein
- F-ATPase gamma subunit
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit d
- ATP synthase F
- ATP synthase c subunit
- ATP synthase-coupling factor 6
- ATP synthase F
Sequence:
MLSKRIVTALNTAVKVQNAGIATTARGMAGASGSEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNDAGDDKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIREEGQISPQTDAQLKDVVVNFLATFKP
Protein: Netrin-1 (O09118)
Organism: Mus musculus (Mouse)
Function: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Involved in dorsal root ganglion axon projection towards the spinal cord. It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:7604039}. Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted. {ECO:0000269|PubMed:7604039}.
Interaction partners:
- Netrin receptor UNC5A
- Cell adhesion molecule DSCAM
- Netrin receptor DCC
- Neogenin
- Netrin receptor UNC5C
- Netrin receptor UNC5B
- Netrin receptor UNC5D
- Draxin
- Slit homolog 1 protein
- Slit homolog 3 protein
Sequence:
MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKMNMKKYCRKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA