wanglab/gogpt-training-data huggingface dataset:
Protein: Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (L-PGDS) (PGD2 synthase) (PGDS2) (O09114)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system. Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR.
Subcellular location: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
Interaction partners:
- Hematopoietic prostaglandin D synthase
- Prostaglandin E synthase
- Prostacyclin synthase
- Thromboxane-A synthase
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase 3
- Prostaglandin G/H synthase 2
- Prostamide/prostaglandin F synthase
- Transcription factor SOX-9
Sequence:
MAALRMLWMGLVLLGLLGFPQTPAQGHDTVQPNFQQDKFLGRWYSAGLASNSSWFREKKAVLYMCKTVVAPSTEGGLNLTSTFLRKNQCETKIMVLQPAGAPGHYTYSSPHSGSIHSVSVVEANYDEYALLFSRGTKGPGQDFRMATLYSRTQTLKDELKEKFTTFSKAQGLTEEDIVFLPQPDKCIQE
Protein: Spermatogenesis-associated protein 16 (Testis development protein NYD-SP12) (Q9BXB7)
Organism: Homo sapiens (Human)
Function: Essential for spermiogenesis and male fertility (By similarity). Involved in the formation of sperm acrosome during spermatogenesis.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:12529416}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8C636}. Note=Shift from Golgi to sperm acrosome. {ECO:0000250|UniProtKB:Q8C636}.
Interaction partners:
- Probable C-mannosyltransferase DPY19L2
- Golgin subfamily A member 3
- Male-enhanced antigen 1
- Golgi-associated PDZ and coiled-coil motif-containing protein
- Zona pellucida-binding protein 1
- PRKCA-binding protein
- Acrosin
Sequence:
MDAGSSRSLENAVNRIYHDQLVPKINTSKKMSTLAHPPNILEMSQEIKKNCGGKQVEITLERTKMTKGIKEKQSNDLEKAAFKRKAEGEEKPTRKKQAKITELDNQLITMPLPHIPLKNIMDVEMKLVYIDEMGVRYEFVESFMSTGSQPTCQAAEIVDPLSVHNFSFLPQIDKWLQVALKDASSCYRQKKYALAAGQFRTALELCSKGAVLGEPFDAPAEDIASVASFIETKLVTCYLRMRKPDLALNHAHRSIVLNPAYFRNHLRQATVFRCLERYSEAARSAMIADYMFWLGGGREESISKLIKLYWQAMIEEAITRAESFSVMYTPFATKIRADKIEKVKDAFTKTHPAYAEYMYTDLQALHMLPQTVDWSSFPPQQYLLTLGFKNKDDGKFLEKISSRKLPIFTEHKTPFGLTREDTVRQMETMGKRILPILDFIRSTQLNGSFPASSGVMEKLQYASLLSQLQRVKEQSQVINQAMAELATIPYLQDISQQEAELLQSLMADAMDTLEGRRNNNERVWNMIQKVGQIEDFLYQLEDSFLKTKKLRTARRQKTKMKRLQTVQQR
Protein: Prokineticin 1-like protein (P84909)
Organism: Pelophylax saharicus (Sahara frog) (Rana saharica)
Function: Stimulates insulin secretion by BRIN-BD11 cells in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:16269346}.
Interaction partners:
Sequence:
AVITGACERDVQCGGGTCCAVSLI
Protein: Copper transport protein (F1QKH1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Membrane {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367022}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
- ATPase copper-transporting alpha.
- Copper transport protein ATOX1
- ATPase copper-transporting beta.
- Copper chaperone for superoxide dismutase
- Copper chaperone for superoxide dismutase.
- Cytochrome c oxidase copper chaperone
Sequence:
MDMSHSHHHVEETTMPSPASDDHGGHLTTSGNGHGDHMMMMQMTFYFGYKNVELLFAGLVINTPGEMAGACIGVFLLAVLYEGLKIGREVLLRRNQVNVRYNSMPVPGSDGTVLMETHKTVGQRMLSMAHFLQTLLHIIQVVVSYFLMLVFMTYNGYLCIAVAAGAGLGYFLFSWKKAVVVDITEHCH
Protein: Afadin/alpha-actinin-binding protein (At2g18870) (Q8GW47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g07590
- VIN3-like protein 3
- Vernalization5/VIN3-like protein
Sequence:
MSLTVPEFDFRLTPQFGFSQSPIGERNFADVDNLENCIKYLNQSLVTSGFSASLDLFATDPVSIARTCNCVYALIQQRQRDVEFRESANDQRQRLLSDMARLEAKVERLETQLQAKERELGSVTRTEAKNTAALKTQNEKLQKERDEFQRMVIANQQVKTQQLHETKKKEKEYIKLQERLNQVLMEKKKETRSGMEIMNLLQKEGRQRGTWSGKKTDSDFYKKIVDAYEAKNQELMAENTDLRALLRSTQGDMRSFLNASGGLTNQSLVANGRHGADPSQSPLGGKTDVFDLPFRMARGQIEDSLRSKMVSIKERMGQLVDAQKEVSITSEASERELELEAQLVEARSIIQEQESIMSKHLPKTDRRRNSAPPHSSVNGLRG
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (Dioxygenase-like protein) (F7A19.20 protein) (Putative dioxygenase) (Q9XI76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 3 member F1
- Nitrilase 3
- Indole-3-acetaldehyde oxidase
- 2-oxoglutarate-dependent dioxygenase DAO
- Indole-3-acetaldehyde oxidase
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Nitrilase 1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Nitrilase 2
Sequence:
MAEVNGVIPTIDLEEVNDQILNEKIREASERWGCFTVINHGVSLSLMAEMKKTVRDLHERPYEMKLRNTDVLLGNGYKPLSEFNPFYESFGLFDMASPQAVNSFCDKLDASPDQREILLKYAKATDDLARSLARRLAESYGVVEPNFLRGWPSQFRMNKYHFKPDSVGKLGVILHTDPGFLTILQGDEDVGGLEAMDNSSGSFFPIHTLPNTLLVNLGDMATIWSNGRLCNVKHRVQCIEAKMRITIASFLLGPVDRDLEAPDEFVDAEHPRLYKPISDGGLRKIRLSKHLHAGESLKFITINELSDVPKID
Protein: Putative AcsD (E0SIF0)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Diaminopimelate decarboxylase
- Achromobactin siderophore NIS synthase
- Inner membrane component of tripartite multidrug resistance system
- TonB-dependent receptor
- Achromobactin siderophore NIS synthase
Sequence:
MNNRNHDVLSRMISEKAALHGLLNCLIKEFAIPEGYLRYEWPDEMKGIPPGAYFDGADWKGIPMMIGLPDQLQLFVMVDRRDTFGSQHYLSDVYLRQAQGDWQCPDFEPLVARLLAACEHIAGRKNPELYEQILQSQRLVSAIVSHNGRQRADAPLQHYLQSEQGLWFGHPSHPAPKARLWPAHLGQEQWAPEFQARAALHQFEVPVDGLHIGANGLTPQQVLDGFADQQPASPGHAIICMHPVQAQLFMQDARVQQLLRDNVIRDLGQSGRVASPTASIRTWFIDDHDYFIKGSLNVRITNCVRKNAWYELESTVLIDRLFRQLLDQHADTLGGLVAAAEPGVVSWSPAAAGELDSHWFREQTGGILRENFCRRTGAERSIMAGTLFARGVDLQPMIQTFLRTHYGEALDDNALLYWFDDYQTRLLRPVLSLFFNHGVVMEPHLQNSVLVHQQGRPQQVLLRDFEGVKLTDDLGIRYIDDDIHPRVRQSLLYSREQGWNRIMYCLFINHLSETILALSQGRPQLAPLMWRRVQQQLRAIQGELKQPSPELDALIAGHPVACKTNLKVRLAAEADRQASYVRLPSPWGHAVQHGSEVQHDERRHGDVRHEEARHGEVQHG
Protein: Proteasome subunit alpha type-4 (PROS-Dm29) (Proteasome 29 kDa subunit) (P18053)
Organism: Drosophila melanogaster (Fruit fly)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-5
- Proteasome subunit beta
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-3
- Proteasome subunit beta
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-7-1
Sequence:
MARRYDSRTTIFSPEGRLYQVEYAMEAISHAGTCLGILAEDGILLAAECRSTNKLLDSAIPSEKIYRLNDNMVCSVAGITSDANVLTSELRLIAQRYQFSYGEVIPCEQLVSHLCDIKQAYTQYGGKRPFGVSLLYMGWDNKYGYQLYQSDPSGNYGGWKATCIGNNFGAAISMLKQELADKENVKLTLADAKDLAIKVLSMTLDTTKLTPEKVEMATLQRVDNKTVYSVLEKPDVEKLIEKYTKVQAEAEAAKKEKQAKQPTK
Protein: LanC-like protein GCR2 (G-protein coupled receptor 2) (F4IEM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in abscisic acid (ABA) signaling.
Interaction partners:
- GPCR-type G protein 1
- GPCR-type G protein 2
- Guanine nucleotide-binding protein alpha-1 subunit
- G-protein coupled receptor 1
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 2
- Magnesium-chelatase subunit ChlH, chloroplastic
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 6
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 8
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
Sequence:
MGERFFRNEMPEFVPEDLSGEEETVTECKDSLTKLLSLPYKSFSEKLHRYALSIKDKVVWETWERSGKRVRDYNLYTGVLGTAYLLFKSYQVTRNEDDLKLCLENVEACDVASRDSERVTFICGYAGVCALGAVAAKCLGDDQLYDRYLARFRGIRLPSDLPYELLYGRAGYLWACLFLNKHIGQESISSERMRSVVEEIFRAGRQLGNKGTCPLMYEWHGKRYWGAAHGLAGIMNVLMHTELEPDEIKDVKGTLSYMIQNRFPSGNYLSSEGSKSDRLVHWCHGAPGVALTLVKAAQVYNTKEFVEAAMEAGEVVWSRGLLKRVGICHGISGNTYVFLSLYRLTRNPKYLYRAKAFASFLLDKSEKLISEGQMHGGDRPFSLFEGIGGMAYMLLDMNDPTQALFPGYEL
Protein: Euchromatic histone lysine methyltransferase 1 (A0A0G2K889)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- [histone H3]-lysine
- Histone deacetylase 1
- PR/SET domain 16.
- Chromobox 3)
- Cellular tumor antigen p53
- WIZ zinc finger
- DNA
- Chromodomain Y-like protein
- Histone deacetylase 2
- Lysine-specific histone demethylase
Sequence:
MARGRGGATLRARAMAAADAEAVLAKQETKQDCCMKTELLREDTLMAADEGSTEKQAGETPMAADGETNGSCEKSGDISHPNAPKHTQENTRASPQEGTNRVSRVAENGVSERDTEVGKQNHVTADDFMQTSVIGSNGYFLNKPALQGQPLRTPNTLNSSLPGHAAKTLPGGASKCRTPSALPQTPTTAPTVPGEGSADTEDRKPTASGTDVRVHRARKTMPKSILGLHAASKDHREVQDHKEPKEDINRNISECGRQQLLPTFPALHQSLPQNQCYMATTKSQTAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGAKGEKVLDDSALHVNGESLEMDSEEEDSEELEDEEDRGAEQAAAFPTEDSRTSKESMSETDRAAKMDGDSEEEQESPDTGEDEDGGDESDLSSESSIKKKFLKRRGKTDSPWIKPARKRRRRSRKKPSSMLGSEACKSSPGSMEQAALGDSAGYMEVSLDSLDLRVRGILSSQTENEGLANGPDVLETDGLHEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEETSKAKEVTIAKADTTSTVTLAPGQEKSLAAEGRADTTTGSIAGAPEDEKSQSTVTQAPECFDPAGPAGFVRPTSGFSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDKPVAVEKTVSRDIARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQENGLPDTSSAAAADPL
Protein: AT27014p (Q8T3X1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDSGNCASSACLGDCKGDGKTAIKEEGYEHLRKIFIGGLSTQTTVETLRGFFSQFGIVADAVVLRDPVSNHSRGFGFVTYVDPKSVEIVQRARPHTIDNKIVETKHALPRQDFKRGGGVGSVVGSFGCEAGFMNSKRIFLGGLKEYHDENIVREYFSQFGPVASVKLLMDRETGRQRAFGFLEFVDPSSAEKALAPRKHWILQTLVEVKRSTQKADRRFRFPIFSSVRAGYIPPQPATADSYNYNNPNYNPYLAQSVLPPSAFTNGWAHYVIPMAPKPTPGQNMAASLPSQQLAEHSLNGHGPDMWSSYPKTGIYSAQEWTSSKVAEWGPKAGHKHAQTSTNDRAKIDLKELQAATFNDKLDFGARGDADRMSGAGLGLGLTGGAAVGVGAIKKWPTQDYKVFKPAKSPTNGVIPKIGKEATTPPYGI
Protein: cAMP-dependent protein kinase type II-alpha regulatory subunit (P00515)
Organism: Bos taurus (Bovine)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Protein kinase cAMP-dependent type I regulatory subunit beta
- Hormone-sensitive lipase
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Protein kinase cAMP-dependent X-linked catalytic subunit
- A-kinase anchoring protein 1
- A-kinase anchor protein 10, mitochondrial
Sequence:
MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQDFDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIESGEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ
Protein: Phosphate-binding protein PstS (G3XDA8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Binds 1 inorganic phosphate per subunit with a KD of 0.34 uM. Required for phosphate transport (Ref.5). In strain PAO1 implicated in host cell adhesion; in some virulent strains (e.g. MDR25 which expresses very high levels of this protein) antibody fragments against this protein decrease host cell adhesion and increase transepithelial resistance of human epithelial cell monolayers. Its ability to bind phosphate may allow it to acquire phosphate from its host.
Subcellular location: Periplasm {ECO:0000269|PubMed:6436026, ECO:0000269|Ref.5}. Secreted {ECO:0000269|PubMed:18282104}. Note=In some strains (e.g. non-MDR PAO1 and virulent clinical strain MDR25) forms long appendages distinct from flagella or pili on the cell surface: cell surface expression depends on type II secretion effector hxcR (PubMed:18282104). {ECO:0000269|PubMed:18282104}.
Interaction partners:
- Phosphate transport system permease protein PstA
- Membrane protein component of ABC phosphate transporter
- Phosphate import ATP-binding protein PstB
- Phosphate-specific transport system accessory protein PhoU homolog
- Phosphate regulon transcriptional regulatory protein PhoB
- Phosphate regulon sensor protein PhoR
- OmpA-like domain-containing protein
- Phosphate transporter
- Phosphate transporter
- Phosphate transporter
Sequence:
MKLKRLMAALTFVAAGVGAASAVAAIDPALPEYQKASGVSGNLSSVGSDTLANLMTMWAEEYKRLYPNVNIQIQAAGSSTAPPALTEGTANLGPMSRKMKDVELQAFEQKYGYKPTAVPVAVDALAIFVHKDNPIKGLTMQQVDAIFSATRLCGSKQDVKTWGDLGLTGDWAKKPVQLFGRNSVSGTYGYFKEEALCKGDFRPNVNEQPGSASVVQSVSQSLNGIGYSGIGYKTASVKTVALAKKEGAAFVEDNEQNALNGTYPLSRFLYVYVNKAPNKPLDPLEAQFLKLVLSKTGQQVVVKDGYIPLPAKVAEKAIKELGL
Protein: Histone H4 (H4.1) (P62803)
Organism: Bos taurus (Bovine)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62806}. Chromosome. Note=Localized to the nucleus when acetylated in step 11 spermatids. {ECO:0000250|UniProtKB:P62806}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- DNA
- Histone H4
- Histone H4
- Histone H4
- Histone H4
- Histone H4
- Histone H4
- Histone H4
- Histone H4
Sequence:
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Protein: Peptide chain release factor subunit 1 (Translation termination factor aRF1) (Q9YAF1)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Elongation factor 1-alpha
- ABCE1 homolog
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein eS1
- Translation initiation factor 2 subunit alpha
- Translation initiation factor 2 subunit beta
- Translation initiation factor 2 subunit gamma
- Large ribosomal subunit protein uL10
- Methyltransferase
- Large ribosomal subunit protein uL24
Sequence:
MSQGRLEERLTISKRELARLLKELKKWSAPATVLLSLYIPPGRPLSDVMTLLRQEYSITDNIKLKRTRQAVKRALSAAMDRLQMLTSTPPNGLVLFCGEDMSTGKFECFMFSPPEPIRVFYYRTDKRFITDFLEDMVEDNNAIGIIIVERDQATIGLLKGARLEVLKELEGFVPGKHKMGGQSQRRYERIIEQMVDEFFKKVGEEASNLLVPLAEKGVLKGVIVAGPGLAKQEFVEGNYLDYRLKKILAPELVDVAYQGLQGLKEAVMKAEKVVEAQMYRDAVNAMEEFKLHLAKGTGMIVYGEKDVEAALEMGAVKTLLIHESREDLEEWVEKAKSSGAQVIVVPESLAEAEWFLKTFGGLAGILRFRISTV
Protein: STAG3 cohesin complex component (C9J3T3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSPLQRAVGDTKRALSASSSSSASLPFDDRDSNHTSEGNGDSLLADEDTDFEDSLNRNVKKRAAKRPPKTTPVAKHPKKGSRVVHRHSRKQSEPPANDLFNAVKAAKSDMQDSGDYPLIAPGPSWKKFQGSFCEFVRTLVCQCQYSLLYDGFPMDDLISLLTGLSDSQVRAFRHTSTLAAMKLMTSL
Protein: Signal recognition particle receptor subunit beta (SR-beta) (Q4FZX7)
Organism: Rattus norvegicus (Rat)
Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O13950}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASANTRRVGDGAGGAFQPYLDSLRQELQQRDPTLLSVAVAVLAVLLTLVFWKFIWSRKSSQRAVLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNSLTLIDLPGHESLRLQFLDRFKSSARAVVFVVDSATFQREVKDVAEFLYQVLIDSMALKNTPAFLVACNKQDIAMAKSAKLIQQQLEKELNTLRVTRSAAPSTLDSSSTAPAQLGKKGKEFEFSQLPLKVEFLECSAKGGRGDAGSADVQDLEKWLAKIA
Protein: Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (Valyl-tRNA synthetase-like) (Q5ST30)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Alanine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Aspartate--tRNA ligase, mitochondrial
- Lysine--tRNA ligase
- Ribosome production factor 2 homolog
Sequence:
MPHLPLASFRPPFWGLRHSRGLPRFHSVSTQSEPHGSPISRRNREAKQKRLREKQATLEAEIAGESKSPAESIKAWRPKELVLYEIPTKPGEKKDVSGPLPPAYSPRYVEAAWYPWWVREGFFKPEYQARLPQATGETFSMCIPPPNVTGSLHIGHALTVAIQDALVRWHRMRGDQVLWVPGSDHAGIATQAVVEKQLWKERGVRRHELSREAFLREVWQWKEAKGGEICEQLRALGASLDWDRECFTMDVGSSVAVTEAFVRLYKAGLLYRNHQLVNWSCALRSAISDIEVENRPLPGHTQLRLPGCPTPVSFGLLFSVAFPVDGEPDAEVVVGTTRPETLPGDVAVAVHPDDSRYTHLHGRQLRHPLMGQPLPLITDYAVQPHVGTGAVKVTPAHSPADAEMGARHGLSPLNVIAEDGTMTSLCGDWLQGLHRFVAREKIMSVLSEWGLFRGLQNHPMVLPICSRSGDVIEYLLKNQWFVRCQEMGARAAKAVESGALELSPSFHQKNWQHWFSHIGDWCVSRQLWWGHQIPAYLVVEDHAQGEEDCWVVGRSEAEAREVAAELTGRPGAELTLERDPDVLDTWFSSALFPFSALGWPQETPDLARFYPLSLLETGSDLLLFWVGRMVMLGTQLTGQLPFSKVLLHPMVRDRQGRKMSKSLGNVLDPRDIISGVEMQVLQEKLRSGNLDPAELAIVAAAQKKDFPHGIPECGTDALRFTLCSHGVQAGDLHLSVSEVQSCRHFCNKIWNALRFILNALGEKFVPQPAEELSPSSPMDAWILSRLALAAQECERGFLTRELSLVTHALHHFWLHNLCDVYLEAVKPVLWHSPRPLGPPQVLFSCADLGLRLLAPLMPFLAEELWQRLPPRPGCPPAPSISVAPYPSACSLEHWRQPELERRFSRVQEVVQVLRALRATYQLTKARPRVLLQSSEPGDQGLFEAFLEPLGTLGYCGAVGLLPPGAAAPSGWAQAPLSDTAQVYMELQGLVDPQIQLPLLAARRYKLQKQLDSLTARTPSEGEAGTQRQQKLSSLQLELSKLDKAASHLRQLMDEPPAPGSPEL
Protein: Keratin, type II cytoskeletal 2 oral (Cytokeratin-2P) (CK-2P) (K2P) (Keratin-76) (K76) (Type-II keratin Kb9) (Q01546)
Organism: Homo sapiens (Human)
Function: Probably contributes to terminal cornification.
Interaction partners:
- Potassium channel subfamily K member 18
- Potassium channel subfamily K member 6
- Potassium channel subfamily K member 1
- Potassium channel subfamily K member 7
- Potassium channel subfamily K member 2
- Cytochrome c oxidase subunit 1
- Potassium channel subfamily K member 4
- Potassium channel subfamily K member 10
- Potassium channel subfamily K member 9 channel 3)
- Potassium channel subfamily K member 3 channel 1)
Sequence:
MNRQVCKKSFSGRSQGFSGRSAVVSGSSRMSCVARSGGAGGGACGFRSGAGSFGSRSLYNLGSNKSISISVAAGSSRAGGFGGGRSSCGFAGGYGGGFGGSYGGGFGGGRGVGSGFGGAGGFGGAGGFGGPGVFGGPGSFGGPGGFGPGGFPGGIQEVIVNQSLLQPLNVEIDPQIGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWELLQQQTTGSGPSSLEPCFESYISFLCKQLDSLLGERGNLEGELKSMQDLVEDFKKKYEDEINKRTAAENEFVGLKKDVDAAFMNKVELQAKVDSLTDEVSFLRTLYEMELSQMQSHASDTSVVLSMDNNRCLDLGSIIAEVRAQYEEIAQRSKSEAEALYQTKLGELQTTAGRHGDDLRNTKSEIMELNRMIQRLRAEIENVKKQNANLQTAIAEAEQRGEMALKDANAKLQDLQTALQKAKDDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRMSGECQSAVCISVVSNVTSTSGSSGSSRGVFGGVSGSGSGGYKGGSSSSSSSGYGVSGGSGSGYGGVSSGSTGGRGSSGSYQSSSSGSRLGGAGSISVSHSGMGSSSGSIQTSGGSGYKSGGGGSTSIRFSQTTSSSQHSSTK