wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase TAO2 (EC 2.7.11.1) (Thousand and one amino acid protein 2) (Q9JLS3)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization and stability. May play a role in the osmotic stress-MAPK8 pathway. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14/p38 MAPK activation.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Found to be perinuclear and localized to vesicular compartment. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, dendrite. Note=In dendrites, colocalizes with PCDH8.
Interaction partners:
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- Serine/threonine-protein kinase TAO1
- Serine/threonine-protein kinase TAO3
- Potassium channel tetramerization domain-containing 13.
Sequence:
MPAGGRAGSLKDPDVAELFFKDDPEKLFSDLREIGHGSFGAVYFARDVRNSEVVAIKKMSYSGKQSNEKWQDIIKEVRFLQKLRHPNTIQYRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAVTHGALQGLAYLHSHNMIHRDVKAGNILLSEPGLVKLGDFGSASIMAPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPALQSGHWSEYFRNFVDSCLQKIPQDRPTSEVLLKHRFVLRERPPTVIMDLIQRTKDAVRELDNLQYRKMKKILFQEAPNGPGAEAPEEEEEAEPYMHRAGTLTSLESSHSVPSMSISASSQSSSVNSLADASDNEEEEEEEEEEEEEEEEEGPESREMAMMQEGEHTVTSHSSIIHRLPGSDNLYDDPYQPEMTPGPLQPPAAPPTSTSSSSARRRAYCRNRDHFATIRTASLVSRQIQEHEQDSALREQLSGYKRMRRQHQKQLLALESRLRGEREEHSGRLQRELEAQRAGFGTEAEKLARRHQAIGEKEARAAQAEERKFQQHILGQQKKELAALLEAQKRTYKLRKEQLKEELQENPSTPKREKAEWLLRQKEQLQQCQAEEEAGLLRRQRQYFELQCRQYKRKMLLARHSLDQDLLREDLNKKQTQKDLECALLLRQHEATRELELRQLQAVQRTRAELTRLQHQTELGNQLEYNKRREQELRQKHAAQVRQQPKSLKVRAGQLPMGLPATGALGPLSTGTLSEEQPCSSGQEAILGQRMLGEEEEAVPERMILGKEGTTLEPEEQRILGEEMGTFSSSPQKHRSLVNEEDWDISKEMKESRVPSLASQERNIIGQEEAGAWNLWEKEHGNLVDMEFKLGWVQGPVLTPVPEEEEEEEEEGGAPIGTPRDPGDGCPSPDIPPEPPPSHLRQYPASQLPGFLSHGLLTGLSFAVGSSSGLLPLLLLLLLPLLAAQGGGGLQAALLALEVGLVGLGASYLFLCTALHLPPSLFLLLAQGTALGAVLSLSWRRGLMGVPLGLGAAWLLAWPSLALPLAAMAAGGKWVRQQGPQMRRGISRLWLRVLLRLSPMVFRALQGCAAVGDRGLFALYPKTNKNGFRSRLPVPWPRQGNPRTTQHPLALLARVWALCKGWNWRLARASHRLASCLPPWAVHILASWGLLKGERPSRIPRLLPRSQRRLGLSASRQLPPGTVAGRRSQTRRALPPWR
Protein: Gamma-taxilin (Factor inhibiting ATF4-mediated transcription) (FIAT) (Lipopolysaccharide-responsive gene protein) (Q8BHN1)
Organism: Mus musculus (Mouse)
Function: May be involved in intracellular vesicle traffic (By similarity). Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:19913514}. Cytoplasm, cytosol {ECO:0000269|PubMed:19913514}.
Interaction partners:
- Tetratricopeptide repeat protein 27
Sequence:
MATRLEEVTRGRGGGTEEASEGGRGGRRRSPPQKFEIGTMEEARICGLGVKADMVCNSQANDILQHQDPSCGGTTKKHSLEGDEGSDFITKNRNLVSSVFCTQEKREEIPGREARTGPPDGQQDSECSRNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRNVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKAFQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAADGDLVSPATQPCAVLDSFKETSRRTLGMHLEARAKSVCEKSAAQKPSSSGSPAQGIESVD
Protein: BRO1 domain-containing protein BROX (BRO1 domain- and CAAX motif-containing protein) (Q5VW32)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus membrane {ECO:0000305|PubMed:34818527}; Lipid-anchor {ECO:0000305|PubMed:18190528}. Note=During nuclear envelope repair, localizes at rupture sites where it is recruited by the CHMP7/ESCRT-III axis. {ECO:0000269|PubMed:34818527}.
Interaction partners:
- Charged multivesicular body protein 4b
- Charged multivesicular body protein 5
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 4a
Sequence:
MTHWFHRNPLKATAPVSFNYYGVVTGPSASKICNDLRSSRARLLELFTDLSCNPEMMKNAADSYFSLLQGFINSLDESTQESKLRYIQNFKWTDTLQGQVPSAQQDAVFELISMGFNVALWYTKYASRLAGKENITEDEAKEVHRSLKIAAGIFKHLKESHLPKLITPAEKGRDLESRLIEAYVIQCQAEAQEVTIARAIELKHAPGLIAALAYETANFYQKADHTLSSLEPAYSAKWRKYLHLKMCFYTAYAYCYHGETLLASDKCGEAIRSLQEAEKLYAKAEALCKEYGETKGPGPTVKPSGHLFFRKLGNLVKNTLEKCQRENGFIYFQKIPTEAPQLELKANYGLVEPIPFEFPPTSVQWTPETLAAFDLTKRPKDDSTKPKPEEEVKPVKEPDIKPQKDTGCYIS
Protein: Thymosin beta-4 (T beta-4) [Cleaved into: Hemoregulatory peptide AcSDKP (N-acetyl-SDKP) (AcSDKP) (Seraspenide)] (Q95274)
Organism: Sus scrofa (Pig)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P62328}.
Interaction partners:
- Actin gamma 1
- Actin, cytoplasmic 1
- Thymosin beta
Sequence:
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Protein: Poly(A) polymerase gamma (A0A0C4DH56)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
RTVMVEEFKQGLAVTDEILQGKSDWSKLLEPPNFFQKYRHYIVLTASASTEENHLEWVGLVESKIRVLVGNLERNEFITLAHVNPQSFPGNKEHHKDNNYVSMWFLGIIFRRVENAESVNIDLTYDIQSFTDTVYRQANNINMLKEGMKIEATHVKKKQLHHYLPAEILQKKKKQSLSDVNRSSGGLQSKRLSLDSSCLDSSRDTDNGTPFNSPASKSDSPSVGETERNSAEPAAVIVEKPLSVPPAQGLSIPVIGAKVDSTVKTVSPPTVCTIPTVVGRNVIPRITTPHNPAQGQPHLNGMSNITKTVTPKRSHSPSIDGTPKRLKDVEKDAIGGESMPIPTIDTSRKKRLPSKELPDSSSPVPANNIRVIKNSIRLTLNR
Protein: Intron-encoded endonuclease I-SceI (EC 3.1.-.-) (21S rRNA intron maturase) (Homing endonuclease omega) (P03882)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the 21S rRNA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Specifically recognizes and cleaves the sequence 5'-TAGGGATAACAGGGTAAT-3'.
Subcellular location: Mitochondrion.
Interaction partners:
- Intron-encoded DNA endonuclease aI4
- V-type proton ATPase catalytic subunit A
- Protein transport protein SEC61
- ATP-dependent DNA helicase II subunit 1
- Uncharacterized mitochondrial protein RF1
- DNA repair and recombination protein RAD52
- Orotidine 5'-phosphate decarboxylase
- Homothallic switching endonuclease
- Intron-encoded DNA endonuclease aI3
- Intron-encoded RNA maturase bI4
Sequence:
MKNIKKNQVMNLGPNSKLLKEYKSQLIELNIEQFEAGIGLILGDAYIRSRDEGKTYCMQFEWKNKAYMDHVCLLYDQWVLSPPHKKERVNHLGNLVITWGAQTFKHQAFNKLANLFIVNNKKTIPNNLVENYLTPMSLAYWFMDDGGKWDYNKNSTNKSIVLNTQSFTFEEVEYLVKGLRNKFQLNCYVKINKNKPIIYIDSMSYLIFYNLIKPYLIPQMMYKLPNTISSETFLK
Protein: Caltractin (20 kDa calcium-binding protein) (Centrin) (P05434)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: This calcium-binding protein is found in the basal body complexes (the functional homolog of the centrosome in animal cell). In mitotic cells it is specifically associated with the poles of the mitotic spindles at the sites of the duplicated basal body complexes.
Interaction partners:
Sequence:
MSYKAKTVVSARRDQKKGRVGLTEEQKQEIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMISEIDKDGSGTIDFEEFLTMMTAKMGERDSREEILKAFRLFDDDNSGTITIKDLRRVAKELGENLTEEELQEMIAEADRNDDNEIDEDEFIRIMKKTSLF
Protein: Monoglyceride lipase (MGL) (EC 3.1.1.23) (HU-K5) (Lysophospholipase homolog) (Lysophospholipase-like) (Monoacylglycerol lipase) (MAGL) (Q99685)
Organism: Homo sapiens (Human)
Function: Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35678}. Membrane {ECO:0000250|UniProtKB:O35678}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35678}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Patatin-like phospholipase domain-containing protein 2
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Fatty-acid amide hydrolase 1
- Lipoprotein lipase
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Neutral cholesterol ester hydrolase 1
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP
Protein: Transmembrane and immunoglobulin domain-containing protein 2 (CD28 homolog) (Immunoglobulin and proline-rich receptor 1) (IGPR-1) (Q96BF3)
Organism: Homo sapiens (Human)
Function: Plays a role in cell-cell interaction, cell migration, and angiogenesis. Through interaction with HHLA2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22419821}; Single-pass type I membrane protein {ECO:0000269|PubMed:22419821}.
Interaction partners:
- HERV-H LTR-associating protein 2
- Cytotoxic T-lymphocyte protein 4
- V-set domain-containing T-cell activation inhibitor 1
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- V-type immunoglobulin domain-containing suppressor of T-cell activation
- T-lymphocyte activation antigen CD80
- Small nuclear ribonucleoprotein G
Sequence:
MGSPGMVLGLLVQIWALQEASSLSVQQGPNLLQVRQGSQATLVCQVDQATAWERLRVKWTKDGAILCQPYITNGSLSLGVCGPQGRLSWQAPSHLTLQLDPVSLNHSGAYVCWAAVEIPELEEAEGNITRLFVDPDDPTQNRNRIASFPGFLFVLLGVGSMGVAAIVWGAWFWGRRSCQQRDSGNSPGNAFYSNVLYRPRGAPKKSEDCSGEGKDQRGQSIYSTSFPQPAPRQPHLASRPCPSPRPCPSPRPGHPVSMVRVSPRPSPTQQPRPKGFPKVGEE
Protein: Sucrose synthase (EC 2.4.1.13) (G1JRK6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASISVCERLGESLATHPQQAKSILSRIESLGKGIHKSQKLLSVLDKEAGNQALDGMVVGVLRSTQEAVVSSPLVALAIRSAPGVWEYIAVEVQKLFVEEMPVAEYLRLKEELVDGSSNGEFMLELDFGAFNNSVPRPSLSKSIGNGMDFLNRHLSAKLFQDKENLNLLLEFLQIHCQKGKGMLLNDRIQDVNSLQHALRKAEEYLTPLSSDTPYSVFEKRFLGIGLEKGWGDNAEHVLEMIHLLLDLLQAPDPVALESFLGRIPLVANVVIMTPHGYFAQDNVLGYPDTGGQVVYILDQVRALEEELLHRFKLQGLDITPRILVITRLLPDAVGTTCGQRLEKVYGTKYSDILRVPFRTEKGIVRPWISRFKVWPYLETYTKDVAAEITKEFQGKPDLIVGNYSDGNIVASLLAHKFDVTQCTIARALEKTKYPDSDINWKQLEDKYHFSCQFTADLIAMNHTDFIITSTFQEIAGSKDTLGQYESHIAFTLPGLYRVVDGIDVFDPKFNIVSPGADMSIYFPYTEEKRRLKKFHPEIEELLYSPVENTEHLCVLKDRNKPILFTMARLDRVKNLTGLVEFYAKNSRLRELVNLVVVGGDRRKESKDLEEKAEMKKMYELIEKYKLNGQFRWISSQMNRVRNGELYRYICDTKGAFVQPPIYEAFGLTVVEAMTCGLPTFATCYGGPAEIIVHGKSGFNIDPYNGDLAAETLANFFEKCKADPSYWDEISQGGLKRIQEKYTWQIYSEKLLTLTGVYGFSKHVAYQEQRGRKRYIEMLHAWMYNNRVKTVPLAVE
Protein: Thiosulfate/3-mercaptopyruvate sulfurtransferase 2 (EC 2.8.1.1) (EC 2.8.1.2) (Rhodanese homolog protein 2) (AtRDH2) (Sulfurtransferase 2) (AtStr2) (Q24JL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10734224, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:15181206}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase MOCS3
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- Cysteine desulfurase, mitochondrial
- Cystathionine beta-lyase, chloroplastic
- Aspartate aminotransferase, chloroplastic
- Aspartate aminotransferase, cytoplasmic isozyme 1
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic isozyme 2
Sequence:
MKRAFSSQLRSAYPASKSTHFGRVMASSGSEAKANYAPISTNEPVVSVDWLHSNLGDADIKVLDASWYMAHEQRNPIQEYQVAHIPGALFFDLNGIADRKTNLRHMLPSEEAFAAGCSALGIENNDGVVVYDGMGLFSAARVWWMFRVFGHDKVWVLDGGLPKWRASGYDVESSVSNDAILKASAATEAIEKIYQGQTISPITFQTKFRPHLVLALDQVKENIEDKTYQHIDARSKARFDGIAPEPWKGLPSGHIPGSKCVPFPLMFDSSQTLLPAEELKKQFEQEDISLDSPIAASCGTGVTACILALGLYRLGKTNVAIYDGSWTEWATAPNLPIVGSSS
Protein: X-ray repair cross complementing 6 (E9PT85)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- X-ray repair cross-complementing protein 5
- DNA-dependent protein kinase catalytic subunit
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Non-homologous end-joining factor 1
- DNA ligase
- Serine-protein kinase ATM
- TP53-binding protein 1
- DNA repair protein XRCC1
- Double-strand break repair protein MRE11
- Protein artemis
Sequence:
MSEWESYYKTEGEEEEEEEQSPDTNGEYKYSGRDSLIFLVDASRAMFESQGEDELTPFDMSIQCIQSVYTSKIISSDRDLLAVVFYGTEKDKNSVNFKSIYVLQDLDNPGAKRVLELDRFKGQQGKKHFRDTIGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDDPHGNDSAKASRARTKASDLRDTGIFLDLMHLKKRGGFDVSLFYRDIISIAEDEDLGVHFEESSKLEDLLRKVRAKETKKRVLSRLKFKLGKDVALMVGVYNLVQKANKPFPVRLYRETNEPVKTKTRTFNVNTGSLLLPSDTKRSLTFGTRQIVLEKEETEELKRFDEPGLILMGFKPMVMLKNHHYLRPSLFLYPEESLVNGSSTLFSALLTKCVEKEVIAVCRYTARKNVSPYFVALVPQEEELDDQNIQVTPAGFQLVFLPYADDKRKVPFTEKVMANPEQIDKMKAIVQKLRFTYRSDSFENPVLQQHFRNLEALALDMMESEQVVDLTLPKVEAIKKRLGSLADEFKELVYPPGYNPEGKIAKRKADNEGSASKKPKVELSEEELKDLFAKGTLGKLTVPALRDICKAYGLKSGPKKQELLEALSRHLEKTD
Protein: EC1-V2R pheromone receptor protein (Vomeronasal 2, receptor 81) (Q80Z09)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLLSWLLIVWFLQMPTFTWIIATHICPTDTKYLIYSDGTVVIGAFFPILHNSLVRTTTDWKYFPMDSDNYFGMSGRNYQLVLAMLFAINEINLNSHILPNTSLGLEIYNLPAIGRNIFRTVFSWLTGLSSVIPNYTCRKESNSAATLTGVSWKTSETIWTILDLYKFPQLTFGPFDPVQIDRNQFQSLYQVAPKDTALLSGIASLMLHFNWNWVGLLIPDDQRGAQFLSDFRKELDKTKICIAFVKTVLYLGETLLRLISQDHIHIIESSTADVIVIYGPTSILLTLIENTYRTYNKKKIWVMSTKWFCPNLELYNMLELTHGALIFSPHYKEIVGFKKFMLEATPIKYPEDIFLHLLWYWHFNCSFLHSECKIFENCLQNASLELLPGNIFTMTMTEESYNVYNAVYAVAHSLHEETLSQIQFQPQANIDRTLLFPWQLHPFLKKIQVKNSVGDHVVLDWKRKADPEYDITNIWNFPTGLSLLVKVGTFVPSAPKGEQLSMSEYMISWPIGFTEIPHSVCTESCNPGFRKVVLESKPTCCFDCTPCPDNEISNETGLDHCVHCPETHYANAEKRHCLKKTVTFLYYNDPLGKGITLLSIGFSTLTALFIWVFVDHRGTPIIKANNRSLSYILLITLILCFLCPLLFIGLPNTATCIMQQYMFGLLFTVALSTVLAKTITVVMAFKITAPGRKIRWLLTSQVPKFAIPICTLIQVLLSGIWLGTSPPFIDKDYHSEHGHIIILCNKGSYIYFYCTLAYLGVMAFGSYLLAFLSRRLPDRFNESKSLAFSMLVFCSVWVMFLPVYHSTSGKVMVAMEMFSILASSASILIIVFAPKCYIVLFRPELNILTHNRDKRHHRSKTFLKT
Protein: G_PROTEIN_RECEP_F1_2 domain-containing protein (Q93174)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTRCSAPREISVSEETTEKSGRKSPKSPIECRKLSKAPPLCCKNGEECKVAGNCVCKPPKPTGPNDEKPTSSRETYDVFLGGSCGTTVWRRQSVIPFLKKRGITYYDPQRSFWSENMIYEESIAKESSSLFLFVIDPATVNATSFLEIAYFAARKSPKLVVVFLGKTEWAEKAHPDDLPDRNRTCQLLDRILECHQVPMLHTIPDALEFIEEEMLGRQSLTEAMRSKNNRLPYLQIRARRVVRNVKSLAAQTIKVCKNYATKTVVTGLIDLTVLLSISFAFPALPLFYILVPLLMLNIVFFGVIYKVQELRKRYPRMIADSSAVMYHATAAIPSPRVTLKATNVNGTISSKTLVRRRSKQNFEKFFPDDSGASSFIVPSSFLPKQHETKVNIDCSVVELCSSSPDDNSWVQELAAPTLDGKGTPYSYVLATPNFQLDNRMNCLRTWFHHHKKFFYYIPSTTTFLSGMVEIAYILGHTNWEGTVCVPATSQILEGPDDMTADEKDHARAARRRRNDCYQIAFCYLKDMAKRRQCRVFTDIGVAVKALVDPAIRGV
Protein: Actin cytoskeleton-regulatory complex protein end3 (Cytoskeletal adapter protein sagA) (Endocytosis protein 3) (Q5BEK7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch {ECO:0000250}. Note=Cytoplasmic and cortical actin patches. {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 27
Sequence:
MSNKKIEQWEVERYWEIFSSLAGGQPHLNNSQAASVLRNSRLRDDQLEKVWDLADLDGDGELDFEEFCVAMRLVFDLVNGELPQVPKSLPDWLVPESKAHLVQATRALSGGQEQFERIEDEDSTPGLKDGFDWYMSPEDKAKYEEIYSANKNQRGEIAFGSLEPLYESLDVPDTDIRSAWNLVNPSAAPEINKDATLAFLHILNYRHEGYRIPRTIPASLRASFENNKIDYQLDSARPAQKWGTNGDTETSTGRKAKFGDTYLSRLGVAGKTSYTPKGTDFSDTIQDEEWEKVRLRRELAELDAKLQAANKAVEGRKAGNRNDGRPNWVLIKKEALQLLEYKERELRELREGSGRAKAGGDVERLREDVRTVGEQVDGLKNHLIQRKGVLEDLRREIEDERASR
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) (P08165)
Organism: Bos taurus (Bovine)
Function: Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Adrenodoxin, mitochondrial
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Ferredoxin-2, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
- Cytochrome P450 11B1, mitochondrial
- Dihydropyrimidine dehydrogenase [NADP
- Cytochrome b5 reductase 4
- Dihydroorotate dehydrogenase
- Cysteine desulfurase
Sequence:
MAPRCWRWWPWSSWTRTRLPPSRSIQNFGQHFSTQEQTPQICVVGSGPAGFYTAQHLLKHHSRAHVDIYEKQLVPFGLVRFGVAPDHPEVKNVINTFTQTARSDRCAFYGNVEVGRDVTVQELQDAYHAVVLSYGAEDHQALDIPGEELPGVFSARAFVGWYNGLPENRELAPDLSCDTAVILGQGNVALDVARILLTPPDHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQVAFTIKELREMIQLPGTRPMLDPADFLGLQDRIKEAARPRKRLMELLLRTATEKPGVEEAARRASASRAWGLRFFRSPQQVLPSPDGRRAAGIRLAVTRLEGIGEATRAVPTGDVEDLPCGLVLSSIGYKSRPIDPSVPFDPKLGVVPNMEGRVVDVPGLYCSGWVKRGPTGVITTTMTDSFLTGQILLQDLKAGHLPSGPRPGSAFIKALLDSRGVWPVSFSDWEKLDAEEVSRGQASGKPREKLLDPQEMLRLLGH
Protein: Tubulin alpha-8 chain (EC 3.6.5.-) (Alpha-tubulin 8) [Cleaved into: Dephenylalaninated tubulin alpha-8 chain] (Q9JJZ2)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-4A chain
- Tubulin beta-6 chain
- Tubulin beta-4B chain
- Tubulin beta-1 chain
- Tubulin beta-2B chain
- Tubulin beta-5 chain
- Tubulin beta-2A chain
- Tubulin beta-3 chain
- Microtubule-associated protein
- Cell division control protein 42 homolog
Sequence:
MRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFGTQASKINDDDSFTTFFSETGNGKHVPRAVMVDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEENEGEEF
Protein: Gephyrin a (A0A0R4INA6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Glycine receptor subunit beta
- Disks large homolog 4
- Glycine receptor subunit beta
- Molybdenum cofactor biosynthesis protein 1
- Glycine receptor subunit alphaZ1
- Gephyrin
- Glycine receptor, alpha 3
- Sulfite oxidase, mitochondrial
- Glycine receptor, alpha 4a
Sequence:
MASDGMILTNHDHQIRVGILTVSDSCFRNLAEDRSGINLKDLVHDPSLLGGIISAYKIVPDEIDEIKEILVDWCDEKELNLILTTGGTGFAPRDVTPEATREVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDALEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEDEEKKDSGVASTEDSGSSHITAAAIAAKSMTSHLSHAVVMAKGGQPLSGFIPSTSIPSHFTCSCSDTIPESIISRGVQVLPRDTASLSTTPSESPCAQQSRLSTASCPTPKARLTSCSSTYSVTEASRREFRAHLDDVISHKSRYSTLDQLHSRLEGLKDDRRNHRTFDSRVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTLTVMPGQVMRVTTGAPIPCGADAVVQVEDTELLRESEDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVQKFPVVAVMSTGNELLNPEDDLHPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGARKLIFALPGNFTYRDTGATLLEAVPLSDTEACRMPVPPPPRGSNPVSAVVTCNLFVIPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) (Stationary phase enzyme) (P25516)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.
Interaction partners:
- Citrate synthase
- Isocitrate dehydrogenase
- Aconitate hydratase B
- Isocitrate lyase
- Fumarate hydratase class II
- Fumarate hydratase class I, aerobic
- 2-methylcitrate synthase
- Succinate dehydrogenase flavoprotein subunit
- Uncharacterized protein YbhJ
- Superoxide dismutase
Sequence:
MSSTLREASKDTLQAKDKTYHYYSLPLAAKSLGDITRLPKSLKVLLENLLRWQDGNSVTEEDIHALAGWLKNAHADREIAYRPARVLMQDFTGVPAVVDLAAMREAVKRLGGDTAKVNPLSPVDLVIDHSVTVDRFGDDEAFEENVRLEMERNHERYVFLKWGKQAFSRFSVVPPGTGICHQVNLEYLGKAVWSELQDGEWIAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPDVVGFKLTGKLREGITATDLVLTVTQMLRKHGVVGKFVEFYGDGLDSLPLADRATIANMSPEYGATCGFFPIDAVTLDYMRLSGRSEDQVELVEKYAKAQGMWRNPGDEPIFTSTLELDMNDVEASLAGPKRPQDRVALPDVPKAFAASNELEVNATHKDRQPVDYVMNGHQYQLPDGAVVIAAITSCTNTSNPSVLMAAGLLAKKAVTLGLKRQPWVKASLAPGSKVVSDYLAKAKLTPYLDELGFNLVGYGCTTCIGNSGPLPDPIETAIKKSDLTVGAVLSGNRNFEGRIHPLVKTNWLASPPLVVAYALAGNMNINLASEPIGHDRKGDPVYLKDIWPSAQEIARAVEQVSTEMFRKEYAEVFEGTAEWKGINVTRSDTYGWQEDSTYIRLSPFFDEMQATPAPVEDIHGARILAMLGDSVTTDHISPAGSIKPDSPAGRYLQGRGVERKDFNSYGSRRGNHEVMMRGTFANIRIRNEMVPGVEGGMTRHLPDSDVVSIYDAAMRYKQEQTPLAVIAGKEYGSGSSRDWAAKGPRLLGIRVVIAESFERIHRSNLIGMGILPLEFPQGVTRKTLGLTGEEKIDIGDLQNLQPGATVPVTLTRADGSQEVVPCRCRIDTATELTYYQNDGILHYVIRNMLK