wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division control protein 42 homolog (EC 3.6.5.2) (Q8CFN2)
Organism: Rattus norvegicus (Rat)
Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase (By similarity). Regulates cell migration (By similarity). In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections (By similarity). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. Facilitates filopodia formation upon DOCK11-activation (By similarity). Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling. Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P60766}; Lipid-anchor {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side {ECO:0000250|UniProtKB:P60766}. Midbody {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P60953}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P60953}. Cytoplasm {ECO:0000250|UniProtKB:P60766}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P60766}; Peripheral membrane protein {ECO:0000250|UniProtKB:P60766}; Cytoplasmic side {ECO:0000250|UniProtKB:P60766}. Cell projection, dendrite {ECO:0000305|PubMed:21423166}. Note=Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells. Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome. In its active GTP-bound form localizes to the leading edge membrane of migrating dendritic cells. {ECO:0000250|UniProtKB:P60766, ECO:0000250|UniProtKB:P60953}.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- Serine/threonine-protein kinase PAK 1
- Ras GTPase-activating-like protein IQGAP1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- BAR/IMD domain-containing adapter protein 2
- Par-6 family cell polarity regulator beta
- Dedicator of cytokinesis 8
- Partitioning defective 6 homolog alpha
- non-specific serine/threonine protein kinase
Sequence:
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL
Protein: Interferon-induced protein with tetratricopeptide repeats 2 (IFIT-2) (Glucocorticoid-attenuated response gene 39 protein) (GARG-39) (Interferon-induced 54 kDa protein) (IFI-54K) (P54) (Q64112)
Organism: Mus musculus (Mouse)
Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Subcellular location: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Interferon-induced protein with tetratricopeptide repeats 3
- Signal transducer and activator of transcription 1
- 2'-5'-oligoadenylate synthase-like protein 2
- Interferon-induced protein 44
- Ubiquitin-like protein ISG15
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced helicase C domain-containing protein 1
- Antiviral innate immune response effector IFIT1
- Antiviral innate immune response receptor RIG-I
- C-X-C motif chemokine 10
Sequence:
MSTTSKESLVCNLRQLKCHFTWNLIAEDESLDEFEDRVFNKDEFQNSEFKATMCNILAYVKHCRGLNEAALQCLGEAEGFIQQQHPDQVEIRSLVTWGNYAWVYYHMGQFSKAQAYLDKVKQVCKKFSSPYRIENPALDCEEGWARLKCTKNQNERVKVCFQKALEKDPKNPEFTSGWAIAFYRLDDWPARNYCIDSLEQAIQLSPDNTYVKVLLALKLDAVHVHKNQAMALVEEALKKDPSAIDTLLRAARFYCKVYDTDRAIQLLRKALEKLPNNAYVHYYMGCCYRSKVHHMLNRREMVFSGDRKKLEELIQLAVNHLRKAEEIKEMLEYSCSFLADLYIIAKKYDEADYYFQKELSKDLPPGPKQLLHLRYGNFQFFQMKRQDKAIYHYMEGVKIKKKTIPQKKMREKLQRIALRRLHEDESDSEALHILAFLQENGGGQQADKDSERGVDSANQVPSASLDEDGAEY
Protein: Ras-related protein RABH1e (AtRABH1e) (Q9LFT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Ran-binding protein 1 homolog b
- Vacuolar protein-sorting-associated protein 33 homolog
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Ran-binding protein 1 homolog c
- ADP-ribosylation factor
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- Guanosine nucleotide diphosphate dissociation inhibitor At5g09550
- ADP-ribosylation factor
- Conserved oligomeric Golgi complex subunit 6
- At5g52210
Sequence:
MASVSPLAKYKLVFLGDQSVGKTSIITRFMYDKFDTTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAVIVYDVANRQSFLNTSKWIEDVRTERGSDVIIVLVGNKTDLVDKRQVSIEEGDNKARDYGVIFIETSAKAGFNIKPLFRKIAAALPGMETLSSTKQEDMVDVNLKTSSNSAQGEQQRGGCAC
Protein: Growth factor independent 1 (Growth factor-independent 1A transcription repressor b) (Q7SZV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPRSFLVKSKKAHSYHQPRSLEDDFNRLDNILAHICAESKTSDESECCADALTGDTTGAGSPDSHLLDQADLSSKSPLSCEESVCDRSSDYEDFWRPPSPSASPESEKSFSPSVEETQPFAVPFRPYAWSRYSGCEIRQLVQHTLNHHRSLELERPTPTYYNERVTEPSIFTERGSGARIYNSYGSTASLFERATASGLFDDSSMLGKGTEMKSSSDVICSRLLLNGAYKCIKCSKVFSTPHGLEVHVRRSHSGTRPFACDICGKTFGHAVSLEQHRAVHSQERSFDCKICGKSFKRSSTLSTHLLIHSDTRPYPCQYCGKRFHQKSDMKKHTFIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFGCDLCGKGFQRKVDLRRHKETQHGLK
Protein: Voltage-gated hydrogen channel 1 (Hydrogen voltage-gated channel 1) (D3ZIU8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTSHDQKAVTRRTKVAPTKRMSRFLKHFTVVGDDYHTWNVNYKKWENEEDEEEPAPTSAEGEGSAVGPDAEAGSASTPRPSLDFRSRLRKLFSSHRFQVIIICLVVLDALLVLAELLLDLRIIEPDLSVKKYSTKVFHYLSLAILAFFVLEISLKVFVFRLEFFHHKFEILDAIVVVVSFVLDLILLFKNHHFEALGLLILLRLWRVARIINGIIISVKTRSERQILRLKQINLQLATKIQHLEFSCSEKEQEIERLSKLLRQNGLLEDVNVN
Protein: Acireductone dioxygenase (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53) (Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1) (MTCBP-1) (Submergence-induced protein-like factor) (Sip-L) (Q9BV57)
Organism: Homo sapiens (Human)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site (By similarity). Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (By similarity). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.
Subcellular location: Cytoplasm {ECO:0000303|PubMed:14718544}. Nucleus {ECO:0000303|PubMed:14718544}. Cell membrane {ECO:0000303|PubMed:14718544}; Peripheral membrane protein {ECO:0000303|PubMed:14718544}; Cytoplasmic side {ECO:0000303|PubMed:14718544}. Note=Localizes to the plasma membrane when complexed to MMP14. {ECO:0000303|PubMed:14718544}.
Interaction partners:
- Enolase-phosphatase E1
- Methylthioribulose-1-phosphate dehydratase
- Tyrosine aminotransferase
- Matrix metalloproteinase-14
- L-amino-acid oxidase
- Methylthioribose-1-phosphate isomerase
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 5
- Ribonuclease H1
- NADH-ubiquinone oxidoreductase chain 6
Sequence:
MVQAWYMDDAPGDPRQPHRPDPGRPVGLEQLRRLGVLYWKLDADKYENDPELEKIRRERNYSWMDIITICKDKLPNYEEKIKMFYEEHLHLDDEIRYILDGSGYFDVRDKEDQWIRIFMEKGDMVTLPAGIYHRFTVDEKNYTKAMRLFVGEPVWTAYNRPADHFEARGQYVKFLAQTA
Protein: Intraflagellar transport protein 70A (Protein fleer) (Tetratricopeptide repeat protein 30A) (TPR repeat protein 30A) (A7YE96)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip (By similarity). Required for polyglutamylation of axonemal tubulin, which is a prerequisite for correct assembly of cilia and for normal cilia beat amplitude. Does not seem to be required for neuronal microtubule polyglutamylation.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:17761526}.
Interaction partners:
- Intraflagellar transport 52 homolog
- Intraflagellar transport 88 homolog.
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport 81 homolog.
- Intraflagellar transport protein 56
- Intraflagellar transport 80 homolog
- Intraflagellar transport 74.
- Intraflagellar transport protein 172 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 57 homolog
Sequence:
MPPMTIKDGEYTATVYKMIKEGRYGDAIHILSKEHQKHTKSRAALSLLGYCYYHMQDFTNAAECYEQLTQLHPEVEDYKLYYAQSLYGACAFPEAMKSTFLLDNTTSHTKMIKLQAAIKYGEEDYSGAKTLVEQLPQEDPDYDVDLGCLLYKEGEFEEACKKFMSSMNVLGYQPDLAYNIALCYYSLKQYASALKYIAEIIERGIREHPELSIGMTTEGIDVRSVGNTLILHETALIEAFNLKAAIEYQLKNYAAAQEALTDMPPRSEEELDPVTLHNQALMNMDTKPTEGFEKLAFLLQQNPFPPVTFGNLLLLYCKYEYFDLAADVLAENAHLTYKFLTPYLYEFLDAMITCQTAPEEAFRKFDENAGKLTEQLRKVTKQVQEARHNRDDESLKKYVQDYDEVLEKYIPVLMAQAKIYWNRENYSMVEKIFHKSLEFCNEHDTWKLNVAHVLFMQDNKYKEAIGFYEPIVKKHYENILNVSAIVLANLCVSYIMTSQNEEAEELMRKIEKEEEQISYDDPDKKIFHLCIVNLVIGTLYCAKGNYDFGISRVIKSLEPYNKKLGTDTWFYAKRCFLSLLENMAKHMIMLRDSVVQECIQFLEHCELYGKDVLAIIEQPLEEDRMHIGKNTVTYESRLIKALFYEVTGWNE
Protein: 28 kDa inner dynein arm light chain, axonemal (p28) (Q39604)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Plays a dynamic role in flagellar motility. May be necessary for stable assembly of a subset of inner dynein arms or for the binding of these arms to the outer doublet microtubules of the axoneme.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme. Note=Present along the entire length of the axoneme.
Interaction partners:
Sequence:
MIPPLSSLVRYDNPVLVSTSKDKGKGAKGTPGKKGALPPVEQKPGLTQTEDILNSILPPREWTEDGQLWVQYVSSTPATRLDVINLQEKLDQQLQQRQARETGICPIREELYAQTFDELIRQVTINCAERGLLLLRVRDEMRMTIAAYQTLYESAVAFGIRKALQTEQGKSEMESRITQLEGDVKDLERQVQEWKFKCEAIEKRESERREVEAKKHKDEVAYLENYAKQLKQQLETFLVPAKKGAPGAPAAAT
Protein: Proteasome subunit alpha type-3 (20S proteasome alpha subunit G-1) (DiDi 17A-2a) (Proteasome component 8) (Proteasome subunit alpha type-7) (O23715)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 alpha type-6-B
- Proteasome subunit alpha type-5-B
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-4-A
- Proteasome subunit beta type-6
- Proteasome subunit beta type-3-B
- Proteasome subunit alpha type-1-B
- Proteasome subunit alpha type-7-B
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Proteasome subunit beta type-3-A
Sequence:
MSSIGTGYDLSVTTFSPDGRVFQIEYAAKAVDNSGTVVGIKCKDGIVMGVEKLIASKMMLPGSNRRIHSVHRHAGMAVAGLAADGRQIVARAKSEARSYESVYGDAVPVKELSERVASYVHLCTLYWWLRPFGCGVILGGYDRDGPQLYMIEPSGISYRYFGAAIGKGKQAAKTEIEKLNLSEMTCKEGVIEVAKIIYKLHDEAKDKAFELEMSWICEESKREHQKVPDDLLEEAKTAAKTALEEMDAD
Protein: Transducin/WD40 repeat-like superfamily protein (Q84J57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At4g35930
- F-box protein SKIP27
- F-box protein At4g05010
- F-box protein At1g61340
Sequence:
MMEGRRIIANPRPCSGSRRVIAKKRSRPDGFVNSVKKLQRREISSRMDRAFSISTAQERFRNMRLVEQYDTHDPKGYCLVSLPNLLKRSKVIEIVAARDIVFALTLSGVCASFSRETNKKVCFLNVSPDEVIRSLFYNKNNDSLITVSVYASDNYSSLKCRSTRIEYILRGQADAGFPLFESESLKWPGFVEFDDVNGKVLTYSAQDSVYKVFDLKNYALLYSISDKNVQEIKISPGIMLLIFKRAASHVPLKILSIEDGTLLKSFHHLLHRNKKVDFIEQFNEKLLVKQENENLQILDVRNAELIEVSRTDFMTPSAFIFLYENQLFLTFRNRNVSVWNFRGELVTSFEDHLLWHPDCNTNNIYITSDQDLIISYCKADTEDQWIEGNAGSINISNILTGKCLAKIKANNGPPKEEDCSSSDLGNSSRRRSAVAEALEDITALFYDEERNEIYTGNRHGLLHVWSN
Protein: Ras-associating and dilute domain-containing protein (Q96JH8)
Organism: Homo sapiens (Human)
Function: Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development.
Interaction partners:
Sequence:
MFYGTHFIMSPPTKSKLKRQSQLLSSMLSRTLSYKYRDLDSTFSSLGASDDPAELSTQLSAPGVLKVFGDSVCTGTHYKSVLATGTSSARELVKEALERYALDPRQAGQYVLCDVVGQAGDAGQRWQARCFRVFGDSEKPLLIQELWKPREGLSRRFELRKRSDVEELAAKEVDTITAGINAQARRLQRSRAKGTPTPALGDARSSPPPRLRRTVSETSLSPVNALPAAAQGPEEPGPDAMRYSLYQSPHLLLLQGYSQQHDSLVYVLNRDRHTVGQRTPSSKPSISLSAPDILPLHCTIRRQPLPDSGQAAGRLVLEPIPGAHISVNFSEVGHRTVVLHHGDLLSLGLYYLLLFKDPAQAQPLPARALARLRAVPQSCRLCGAALGARGAASPTQAALPRRQQLLLEFEPHLEDTLLQRIMTLIEPGGDDHKLTPAFLLCLCIQHSATHFQPGTFGQLLLKIARLIRETVWEKTKELAEKQAQLQEPISLASCAMADLVPDLQPILFWMSNSIELLYFIQQKCPLYMQSMEEQLDITGSKESLFSCTLTASEEAMAVLEEVVLYAFQQCVYYVSKSLYICLPALLECPPFQTERRESWSSAPELPEELRRVVSVYQAALDLLRQLQVHPEVASQMLAYLFFFSGTLLLNQLLDRGPSLSCFHWPRGVQACARLQQLLEWMRSAGFGAAGEHFFQKLSCTLNLLATPRAQLIQMSWTALRAAFPALSPAQLHRLLTHYQLASAMGPMSTWEPGAQDSPEAFRSEDVLESYENPPPIVLPSDGFQVDLEANCLDDSIYQHLLYVRHFLWGLRSRASPGSPGRPGSGASQPVCPEGMHHVVLDGHLEAPSCPLAPRDPGPAAREVAPERTLPLRGAPWAQAPPGRQPSRGGSQAGPPHTDSSCLLTPPSTPLGPEPGDPDWPESGGPCGKALPERQRNGLSGLRGAAPEGDSAALAEESPPAPSSRSSSTEDFCYVFTVELERGPSGLGMGLIDGMHTHLGAPGLYIQTLLPGSPAAADGRLSLGDRILEVNGSSLLGLGYLRAVDLIRHGGKKMRFLVAKSDVETAKKIHFRTPPL
Protein: Synaptogyrin-2 (Cellugyrin) (O55101)
Organism: Mus musculus (Mouse)
Function: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12928441}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. {ECO:0000250|UniProtKB:O54980}.
Interaction partners:
Sequence:
MESGAYGAANAGGSFDLRRFLSQPQVVTRLVSMVLALIVFSCIFGEGYTNIHTSDQLYCVFNQNEDACRYGSAIGVLAFLASAFFLVVDAFFSQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAATKPQDVRVGADSARAAITFSFFSIFSWGVLASLAYQRYKAGVDAFIQNYVDPTPDPNTAYASYPSASVENYQQPPFTQNVETTEGYQPPPVY
Protein: Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha) (Q63787)
Organism: Rattus norvegicus (Rat)
Function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit.
- Insulin receptor substrate 1
- phosphatidylinositol-4,5-bisphosphate 3-kinase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- E3 ubiquitin-protein ligase CBL
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQPVLTLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDPPSVDLDVFDEHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQEVPSSEDYIQLLKKLIRSPNIPHQYWLTLQYLLKHFFKLSQASSKNLLNARALSEIFSHVLFRFPAASSDNTEHLIKAVELLISAEWSERQPAPALPPKPPKPTSIANNSMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNDTIKIFEEQCHPQERYSKDYIEKFKREGNEKEIQRIMHNHDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVDDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
Protein: Mitochondrial inner membrane protein oxa1-2 (Cytochrome oxidase biogenesis protein 1-2) (Sp2) (O43092)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the insertion of integral membrane proteins into the mitochondrial inner membrane. Essential for the activity and assembly of cytochrome c oxidase. It is essential for viability while oxa101 is not. When both are deleted the cell is non-viable, suggesting that oxa101 act as a back-up for oxa102.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial inner membrane protein oxa1-1
- Protein sco1
- Metal homeostasis factor atx1
- Large ribosomal subunit protein eL20B
- Cytochrome c oxidase subunit 2
- Tryptophan synthase
Sequence:
MFSVIGRGIKFSSKSHYSVSCFLIATQGAKIRQIHTHNTFFKNFSFAKLGRNQRTSSLIKIHNSSTSFPKSRSEKVVYTPSLPLSSSVLASFSFLPHNILQNGLNTLHIWSGLPWWASIAACAVAMRIAVFPIMLKMMKTSAKLAIINPKVAEHMSVLSKAKAEGNSELMMQATTQIQNLYKVNNVNPLNLLSAPVFQGILFISFFYALKTMAGVPVEGFTDGGFWWVNDLSQPDPLHIFPVANGLLMLLNIELGSETGSNKVAMSPSMKKFFRFLCLASPLFTMNFPMAIFMYWFPSNVFSVFQGAFLRSSTIRHKLGLPEVPSAMPVPNAQNESFVKSFTDIVHGVQEKGKYPQASEILDATRFLKTDTNNEQKPTNNSTITKATTLSDNSQNDKSSSVTKPTEKKD
Protein: Eye-enriched kainate receptor, isoform D (A0A023GQ97)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
Sequence:
MLIASGFLLFQFLSYGLGVPPLVRIGAIFSNQPGMYNSELAFRYAIHRLNMDKSLLPETTVDYYVEYVNRFDSFETVQKVCKLIRVGVQAVFSPTDSVLATHINSICDALDIPNIGRSAHDFSINVYPSKQLVNYAFNDVIQYLNWTRFGILHEKENGIINLHQLSRSFHGEVHMRQVSRDSYVSALNEFKGKEIHNIIIDTNSNGISILLKNILQQQMNEYKYHYLFTSFDLETYDLEDFKYNFVNITSFRLVDTADVGVKQILKDIGLYSHHIFKKPYLNLHIKKSTILESEPALMFDSVYVFAIGLQTLEQSHSLTLLNISCEEENSWDGGLSLINYLNAVEWKGLTGPIQFKDGQRVQFKLDLIKLKQHSIVKVGEWTPHGHLNITEPSMFFDAGSMNVTLVVITILETPYVMMHYGKNFTGNERFYGFCVDILETISREVGFDYILDLVPDRKYGAKDPETGEWNGMVAQLMKYADLAVGSMTITYARESVIDFTKPFMNLGISILFKVPTSEPTRLFSFMNPLAIEIWIYVLIAYFLVSLCIYIVGKLSPIEWKCINACDLENISIGNQFSLTDSFWFTIGTFMQQSPDIYPRAMSTRIISSTWGFFSLIIVASYTANLAAFLTTERMINPIENAEDLASQTEISYGTLDSGSTMTFFRDSVIETYKKIWRSMDNKKPSAFTTTYEDGIKRVNQGNYAFLMESTMLDYIVQRDCNLTQIGGLLDTKGYGIATPKGSPWRDKISLAILELQERGDIQMLYDKWWKNTDETCTRKNTSKQSKANSLGLESIGGVFVVLIAGIIVAAVVAFFEFWYNFRYNYEATPSQSVVNNKYNQDGILESERNYTPPDRSFWIEIAEELRYASWCMNKQKRPALTRTCSKCTIPKGQRINKL
Protein: LIM domain-containing protein WLIM1 (Widely-expressed LIM protein 1) (AtWLIM1) (Q94JX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to actin filaments and promotes cross-linking into thick bundles. Has an actin-stabilizing activity. The actin regulatory activities are not regulated by pH and [Ca(2+)].
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20817848}.
Interaction partners:
- Uncharacterized GPI-anchored protein At5g19230
- Uncharacterized GPI-anchored protein At5g19240
- LIM domain protein
- Protein DA1-related 7
- Actin binding protein family
- Uncharacterized GPI-anchored protein At5g19250
- Uncharacterized protein At4g15545
- Propionyl-CoA carboxylase
- Regulator of chromosome condensation
Sequence:
MAFAGTTQKCMACDKTVYLVDKLTADNRVYHKACFRCHHCKGTLKLSNYNSFEGVLYCRPHFDQNFKRTGSLEKSFEGTPKIGKPDRPLEGERPAGTKVSNMFGGTREKCVGCDKTVYPIEKVSVNGTLYHKSCFKCTHGGCTISPSNYIAHEGKLYCKHHHIQLIKEKGNLSQLEGGGENAAKDKVVAA
Protein: Alanine--tRNA ligase, cytoplasmic (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Protein lactyltransferase AARS1) (EC 6.-.-.-) (Renal carcinoma antigen NY-REN-42) (P49588)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:27911835, ECO:0000269|PubMed:38512451}. Nucleus {ECO:0000269|PubMed:38512451}. Note=Translocates to the nucleus in response to increased levels of lactate; nuclear translocation is dependent on KPNA4. {ECO:0000269|PubMed:38512451}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Glycine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Threonine--tRNA ligase 2, cytoplasmic
- Asparagine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEVTDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGGQIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRPIMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMIEAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKRVLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQLRLGDVKN