wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial 3' processome subunit 2 (A0A120KVR5)
Organism: Trypanosoma brucei brucei
Function: As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26833087}.
Interaction partners:
Sequence:
MGLPFLCHTRVCLFSNKIPFVLCGSRFAPATLHAHHTAAGGGETLNFPELSSPSTSKEPSVGSDSPQKKNKKQAFDALARWCGGHQQLLMRIQQSAEDTSAGVVFETPLTEVDSAAIRWLQGSTEQLTCGQSLLVCSFVCEVLYCQLNSASGGIGVEEAQRLQIHALTNRIAALLQRADESNKLESQPLSVLMSCAYVVQRLKYVDNPLFGETQRSLVKVPPSIMFALLHKLRGDGLGKLFQLDERTATDVCLSFLFIATEEHRQAFFSSGDAALVSNVLRRLVRYTASKTRRMRIQKEGDIIDLLTVDSPSDGGARQTPVCTSGTGFTSPSMRECAMIMQNVSFSSPSNRLELLLYLLCVRRNLAQCSLKDIELVPTVLSTVANIRSAEACSIRKKIISQLWLPENNPTLVAQLLVHSGESIPRYVTYLQGVPASKLSPRDAAQVILCAGTYLSYESLQLYIMAALRDIMPSSSLVTLGAETTSASVPATASVPTRVPACDSLETVLSVLLMRVEEKGGSLSEVEKDACMEYIRRLNELIDWCASAPTSSPKPALQRLTLLTKLFNRGLVVHAPETVVELAVQSLQLDPGNTMMNTLKCVSEALPLVSDDKKRSIIIEKMISYSGTRTTSSVIRFLLLLAPLVDADSPHSCELVEQLLKFHTLNPHKLRQASVEGVAKGIDVYTLLLINGIDFLLASGDWRSSPSQLQNVITTWVRDYTLYVMDPARKQKIDDGAAAHVAPATKGEKTDVVQHQQPSRLNEGGELPTLSGPNDEELEQVFTCLLRAGVKLPHAFSSELLSRIRRLQAKRNPADGTDQQVVFPLPAHFVFCCKLDVPVEVSVTPEMMKYHIDACDYRIIHCVITAFFSAAGTFKHNINDLLLCNMRLASRSFELFIQRLGEEASRSFRPATVSSVVANTLRFVVNHITKQERCQRVLRKLNEKGGIEAGEEELEGDRSLIAEHTRLGELLTRMIAYLSGAHVKNVGLSVLDRLSLLSPACGEYLMMRLSTQLSEFTQVELLYLVQKYPKSQDLVAELLGKSDLVSSMDFGDYMRVMRNLPMPINALVIGAHLPGLNFQWCTRILSSLSVRHESVPLHLLASVLRRLNDVTESATLTDRNIAFVVLQKYLQFDQTSGDGGDLEERQRLIKCSCDKLLVLSRINSLDTLKEFLVEFPEALSGVICESLSKHVVQHIVGGLLKDLDGLLTLCRLLHRHKLLTSDVKVAIVDGFFMKTLQSEVEGRANIEGESSQGLQPLNSVRGASLKTTHPVSNVLALALLLSDGPLHFPGASNSSSTICGDNERCAVSSMFQVVKESYTSPRDRLLIANTLVGQKGPNALTVVAKEICTELIENCESVTSNDFSRLLQCISRLKCWSELDLANSRFDEVFQRSCTQADAHSRCVAFRAVSFEADIFRRYESFMIPLLQETVDVMSNEDLETVLSSVLSLPFTEALESLIDAIGTRLLRMIDQCRRSALIRLLQCHAAFGIQDDALVSVCVATLTDQCGRDFRLDTAQVLALLQAAVDLDFFLPPKLVTSCFTWLEHHVENMTITQLGHAVRLAVDVEVGYTAAVHTLTLRALEQRDAIRSNASFREAVEMLCDEFSAEIPWHLRAPVLRRRYQSERLLEYLDKRRLAVDSTVA
Protein: Phosphoglycolate phosphatase (PGP) (PGPase) (EC 3.1.3.18) (P32662)
Organism: Escherichia coli (strain K12)
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Tryptophan--tRNA ligase
- Glycolate oxidase subunit GlcD
- DNA adenine methylase
- Glyoxylate/hydroxypyruvate reductase B
- Glyoxylate/hydroxypyruvate reductase A
- Glycolate oxidase subunit GlcE
- Glycolate oxidase iron-sulfur subunit
- Lactaldehyde dehydrogenase
- Uncharacterized protein YhfY
Sequence:
MNKFEDIRGVAFDLDGTLVDSAPGLAAAVDMALYALELPVAGEERVITWIGNGADVLMERALTWARQERATQRKTMGKPPVDDDIPAEEQVRILRKLFDRYYGEVAEEGTFLFPHVADTLGALQAKGLPLGLVTNKPTPFVAPLLEALDIAKYFSVVIGGDDVQNKKPHPDPLLLVAERMGIAPQQMLFVGDSRNDIQAAKAAGCPSVGLTYGYNYGEAIDLSQPDVIYQSINDLLPALGLPHSENQESKND
Protein: 1,3-beta-glucanosyltransferase GAS1 (EC 2.4.1.-) (Glycolipid-anchored surface protein 1) (Glycoprotein GP115) (P22146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18434410, ECO:0000269|PubMed:3046936, ECO:0000269|PubMed:3072201}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2160276, ECO:0000269|PubMed:3046936}. Secreted, cell wall {ECO:0000269|PubMed:10564469, ECO:0000269|PubMed:15781460}. Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. {ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:3046936}.
Interaction partners:
- Deoxyribodipyrimidine photo-lyase, mitochondrial
- Cell wall protein ECM33
- Glucan 1,3-beta-glucosidase
- Plasma membrane ATPase 1
- Beta-glucan synthesis-associated protein KRE6
- Chitin synthase 3
- 1,3-beta-glucan synthase component FKS1
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Probable family 17 glucosidase SCW10
- 1,3-beta-glucan synthase component GSC2
Sequence:
MLFKSLSKLATAAAFFAGVATADDVPAIEVVGNKFFYSNNGSQFYIRGVAYQADTANETSGSTVNDPLANYESCSRDIPYLKKLNTNVIRVYAINTTLDHSECMKALNDADIYVIADLAAPATSINRDDPTWTVDLFNSYKTVVDTFANYTNVLGFFAGNEVTNNYTNTDASAFVKAAIRDVRQYISDKNYRKIPVGYSSNDDEDTRVKMTDYFACGDDDVKADFYGINMYEWCGKSDFKTSGYADRTAEFKNLSIPVFFSEYGCNEVTPRLFTEVEALYGSNMTDVWSGGIVYMYFEETNKYGLVSIDGNDVKTLDDFNNYSSEINKISPTSANTKSYSATTSDVACPATGKYWSAATELPPTPNGGLCSCMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDCSFSGSATLQTATTQASCSSALKEIGSMGTNSASGSVDLGSGTESSTASSNASGSSSKSNSGSSGSSSSSSSSSASSSSSSKKNAATNVKANLAQVVFTSIISLSIAAGVGFALV
Protein: Ribose-5-phosphate isomerase (EC 5.3.1.6) (D-ribose-5-phosphate ketol-isomerase) (Phosphoriboisomerase) (Q9UTL3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable transketolase
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Transaldolase
- Phosphoglucomutase
- Probable gluconokinase
- Ribokinase
- Probable phosphoribomutase
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 5
Sequence:
MDSAEKKLDLSPIELAKRLACHMAVDENYPENPKVIGIGSGSTVVYVVERLLTKPGVDSVVFIPTGFQSKQLIVNNGLRLGDPDCYPNVDVSFDGADEVDDNLQCIKGGGACLFQEKLIAFLAKRLVIVADSRKNSHVLGEYWKKGVPIEVMPMAYASILPQLVELGAIEPKLRMGAPGKAGPVVTDNGNFIIDAHFGLIKNPKELFAKIKLLVGVVEVGLFCDMISAVYFGSKDGSVTVKKASGEKHIIPAPVTAAANEVDAKVAETNAKPLN
Protein: Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (Q8JGR4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (By similarity). Plays an essential role in early embryonic development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P83731}.
Interaction partners:
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS2
- 60S ribosomal protein L29
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS12
Sequence:
MKVELCSFSGYKIYPGHGRRYARVDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEVSKKRTRRAVKFQRAITGASLAEILAKRNQKPEVRKAQREQAIRAAKEAKKAKQATKKQTTQSSKAPAKSAQKQKIAKPMKVSAPRVGGKR
Protein: Lantibiotic lichenicidin A1 (LchA1) (BliA1) (Q65DC4)
Organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA1 exhibits activity towards L.lactis HP. When combined with LchA2, it displays activity towards a broad spectrum of non-pathogenic and pathogenic Gram-positive bacteria including strains of L.monocytogenes, methicillin-resistant S.aureus, S.pneumoniae and strains of vancomycin-resistant enterococci, but not towards E.faecium L4001 and BM4147-1. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:19561184, ECO:0000269|PubMed:19707558}.
Interaction partners:
- Lantibiotic modifying enzyme
Sequence:
MSKKEMILSWKNPMYRTESSYHPAGNILKELQEEEQHSIAGGTITLSTCAILSKPLGNNGYLCTVTKECMPSCN
Protein: Plasmanylethanolamine desaturase (EC 1.14.19.77) (Carotenogenesis protein CarF) (CarF) (Q9AE87)
Organism: Myxococcus xanthus
Function: Plasmanylethanolamine desaturase involved in plasmalogen biogenesis in the membrane, required for light-induced carotenogenesis. Plasmalogens are glycerophospholipids with a hydrocarbon chain linked by a vinyl ether bond at the glycerol sn-1 position, and are involved in antioxidative and signaling mechanisms, most precisely in sensing photooxidative stress through singlet oxygen. Participates in the light-dependent inactivation of the antisigma factor CarR. Mediates signaling by singlet oxygen, generated via photoexcited protoporphyrin IX.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:18310035}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKTQEIEKKVRQQDAQVLAQGYSPAIRAMEIAAIVSFVSLEVALVYRLWGTPYAGTWLLLSAVLLGYLAADFVSGFVHWMGDTWGSTEMPVLGKALIRPFREHHVDEKAITRHDFVETNGNNCLISLPVAIIALCLPMSGPGWVFCASFLGAMIFWVMATNQFHKWSHMDSPPALVGFLQRVHLILPPDHHRIHHTKPYNKYYCITVGWMNKPLTMVHFFPTAERLITWATGLLPRQDDIGAEAARALVVAAGGSEAPVVQAAKELLTQATVQEKPASTRP
Protein: Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3) (E9PUL5)
Organism: Mus musculus (Mouse)
Function: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26797119, ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000305|PubMed:26797119}. Presynaptic cell membrane {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747}; Single-pass membrane protein {ECO:0000305|PubMed:26797119}. Synapse {ECO:0000269|PubMed:27052163, ECO:0000269|PubMed:29056747, ECO:0000305|PubMed:22632720}. Cell projection, axon {ECO:0000269|PubMed:29056747}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic density membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}.
Interaction partners:
- Synaptosomal-associated protein 25
- Synaptotagmin-1
Sequence:
MAASSSQVSEMKGVEDSSKTQTEGPRHSEEGLGPVQVVAEIPDQPEALQPGPGITAAPVDSGPKAELAPETTETPVETPETVQATDLSLNPEEGSKASPSPSPSEARQEPASKPDVNRETAAEEGSEPQSTAPPEPTSEPAFQINTQSDPQPTSQPPPKPPLQAEPPTQEDPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
Protein: Thioredoxin-like protein CXXS2 (AtCXXS2) (Mono-cysteine thioredoxin 2) (Q8GXV2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low disulfide reductase activity, but efficient protein disulfide isomerase activity. Does not possess deglutathionylation activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18384502}.
Interaction partners:
Sequence:
MGNHCTRIPCCKKVCSCICCCNRRNKTQARSQKGSYFIKGKVHPVSRMEKWEEKITEANSHGKILVVNFKASWCLPSKTILPIYQELASTYTSMIFVTIDVEELAEFSHEWNVDATPTVVFLKDGRQMDKLVGGDAAELQKKTAAAANLLLRQS
Protein: Progonadoliberin-1 (Progonadoliberin I) [Cleaved into: Gonadoliberin-1 (Gonadoliberin I) (Gonadotropin-releasing hormone I) (GnRH-I) (Luliberin I) (Luteinizing hormone-releasing hormone I) (LH-RH I); GnRH-associated peptide 1 (GnRH-associated peptide I)] (P37042)
Organism: Gallus gallus (Chicken)
Function: Stimulates the secretion of gonadotropins.
Subcellular location: Secreted.
Interaction partners:
- Type II GnRH receptor
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Gonadotropin-inhibitory hormone
- Small ribosomal subunit protein mS26
- Follitropin subunit beta
- Prolactin
- Uncharacterized protein.
- Pro-thyrotropin-releasing hormone
- VIP peptides
- Neuropeptide FF receptor 1
Sequence:
MEKSRKILVGVLLFTASVAICLAQHWSYGLQPGGKRNAENLVESFQEIANEMESLGEGQKAECPGSYQHPRLSDLKETMASLIEGEARRKEI
Protein: Dynein axonemal assembly factor 1 homolog (Defective transmitter-recycling protein) (Dynein regulatory complex subunit 3) (Leucine-rich repeat-containing protein 50 homolog) (Q9VL65)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- Serine/threonine-protein phosphatase
- Gustatory and pheromone receptor 32a
- GEO02361p1
- AT04270p
- AT29763p
- Glycerol-3-phosphate dehydrogenase
- FI08238p
- GH08353p
- FI08446p
- Reticulon-like protein
Sequence:
MDEPVSSQPGEDAVEETEEEPLRGFLEEINCPEPGIIDRQMIETAYLEEGKKGEARRLHQLEPVVYDRITTMRLEFKNILRIDHLWMMPNLTKLCLNCNKIEVIEHLEMLTALKDLNLSFNYITRIENLEKLVKLEKLSLFSNRIRKIENIHTLQNLVILSIGNNLIDTVEGIERLRFVSSLKVLNLEGNPIAKQPDFPLSLYVIAILPQLNYYEYVFIKTETREEAQKRFYRELREIEDKQEREIQGLETEAREMAEADRLASSFVEHLDGMQLYDSLWRDDEDGRILMLVGAPAQELCEEYSKDVYELTQQIYRLGLERFGERDEEIRDFNANLHEGQEELQAQGQRQIEDFLEYKERIFDEMRLKWRELDQRDDDLEQLQAQLDTLTANFEDSLNELWESLMAQELHLHEAVEDSTLKFNRKISDLMSNFVEQAQVIFLQLRDLCSYFADNMTDIVNQFLSTKLARNELNTIPEELKQCVDDREAVLQLVEGMRTTHTSRVDKREDRLAQRSRQFIDDMITNLNNKEVDRHRAKILEINSFMEMMTEALANLPGELHQEAPSD
Protein: Solute carrier organic anion transporter family member 4A1 (Organic anion-transporting polypeptide E) (OATP-E) (Sodium-independent organic anion transporter E) (Solute carrier family 21 member 12) (Q99N01)
Organism: Rattus norvegicus (Rat)
Function: Mediates the Na(+)-independent transport of organic anions such as the thyroid hormones T3 (triiodo-L-thyronine), T4 (thyroxine) and rT3, taurocholate, estrone 3-sulfate, estradiol-17beta-glucuronide and prostaglandin E2 (PGE2). Shows a pH-sensitive substrate specificity T4 and estrone 3-sulfate which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96BD0}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Monocarboxylate transporter 8
Sequence:
MPQHAMGDKHFLSLPKHLFTSTSSTTDSGCDTPPSSRASPASLRSAHGALGSSSQPLFEPQVEKRSSQAACEVQYLSSGPQSTLCGWQSFTPKCLQVFNTPKGFLFFLCAASFLQGMTVNGFINTVITSIERRFDLHSYQSGLIASSYDIAACLCLTFVSYFGGNGHKPRWLGWGALVLGIGSLVFALPHFTAGRYEVEIDDEGLGTETGTCLTNQSQVECKDRASGLSSYRLIFMLGQLLHGVGATPLYTLGVTYLDENVKSSYSPIYIAIFYTAAILGPAAGYLIGGAMLNVYTEVGQRTELTTDSPLWVGAWWIGFLGAGIAAFLIAIPILGYPRQLPGSQRYVVMRAAETQQLKDHSRDNPAFGKTVRDLPLSVWILLRNPTFILLCLAGATEATLIAGMSTFGPKFFEAQFSLSASEAATLFGYLVVPAGGGGTLLGGFLVNKFKLRGSGIIRFCLFCTLTSLLAFFVFLMHCPNVHMAGVTTGYVGSLLPKGQLDLKAACNALYCCQPRHYSPLCGSDGTMYYSPCYAGCPEGAVTGPGGQKVYRGCSCILEKASSGWGNATAGKCASTCQSKPLLLVLVFVVIIFTFLSSIPALTATLRCVCDRQRSFALGIQWIVVRTLGSIPGPIAFGWVIDKACLLWQDQCGHQGSCFVYKNEAMSRYLLIAGLTFKVLGFLFFVAAYFLYKSPSVSSDGLEASLPSQSSASDSPTEQLQSNV
Protein: Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa protein 1-Hom) (HSP70-Hom) (Heat shock protein family A member 1L) (P34931)
Organism: Homo sapiens (Human)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Stress-induced-phosphoprotein 1
- Glucocorticoid receptor
- DnaJ homolog subfamily B member 1
- DnaJ homolog subfamily A member 1
- DnaJ homolog subfamily B member 4
- DnaJ homolog subfamily A member 2
- Heat shock protein HSP 90-beta
- DnaJ homolog subfamily C member 7
- Toll-like receptor 2
Sequence:
MATAKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQADMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKVNKITITNDKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGLKGKISESDKNKILDKCNELLSWLEVNQLAEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTGYVPGRPATGPTIEEVD
Protein: RAB6-interacting golgin (Q8IQQ4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for centriole duplication likely through its interaction with Sas-6. During embryogenesis, maternally provided protein is required for centrosome duplication and nuclear division cycles of the syncytial embryos. In femoral chordotonal organs, required for sensory cilia structural integrity and functionality necessary for motor coordination. In male germline, has a role in cytokinesis which seems dependent on its localization to the Golgi.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:29892014}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}. Note=Co-localizes with the centriole in interphase and mitosis (PubMed:29892014). Mostly found in the Golgi, with a small amount detected in centrosomes (PubMed:29892014, PubMed:33704067). In spermatocytes, localizes to the trans-Golgi and inside the Golgi cisternae (PubMed:33704067). {ECO:0000269|PubMed:29892014, ECO:0000269|PubMed:33704067}.
Interaction partners:
- Ras-related protein Rab6
Sequence:
MTEKFNGFSHDEILKITGVKEGGVGKRPASLEAAKPALRIQPGIRRMPDKIFRQADQLRKQQQQQPQQPIQKPDVAKKTKSGTATPTEKPPTPTPAAEDDVANGSLNLDRPLSDSLIEALYHGNATARDKKTPATYADAETTSTDDSSILKISGGDSQTTSSTDDGSILPSTQDTSPRERLNTDSPFKGISLKDFEQHRRMIEEQNKQKKQMLYQAIEQHTQKTAAESRKIEEIRHELSKLESDLAVDVALLRKQIDNACIHFANVEKQYVKIEAQFLRAKIELHNASEKKELLTEHLCTVIAHNEDRKAQKLTELMQKVGLSPTDDCQPIDLTQQSP
Protein: C2 domain-containing protein (Q583I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQQVDFGQQPIFDDRQSIDELSDLCASLKEQLAAKELNEYEQEVRLRDLRQQLKELSDVEGKLILANRNARVLEEENNALLMKLKSGETADTSGTSFRAEAVKLIEENSSLRSEVHELRGLLNKAQQRESHLDQRCKNINEQQEKNDLQVSLLKKRNAELEEQLHEVQHQWLLAKETWENERSRNLQDYEELLASVKRFDGTAQQRENWDVKTRGSNQHLQQALLKEDIAELEEKLQLAEERYRAKEREWREMEAALRVEISTLQGNNIGTGGDVYRAIQHQLDSFKHEVTVFREERKPGRMKNKLRLGDPSVDDVDDKVSEIDDSDASRESRIQSLEVLNGNISRKNELLMRENEELHKEIEHLHLRNSRAEEEYNDLEVRVKELEIALVSTEKELSLQKGYNINREKDSRCYDVHEMKAVLDENEQLRDSLLEYTRQISSLKAANEEQLAASESSRSEYQAEIAKLLLQNESLQQRLLLRNSRNNSAGELAHDSNDLGNGENEQRPRTRGVSEATVIDKFLKDKLDSTEDFMRSLETAWSEEDEAKRKMRRMSLQDFYKETEQRQNSLQLLQSEKNRLSNEIVDLRHANKSKENRIHELQESLSVLKRHLTNDGLGIVQGEPMRGSGIESRMRRLEEALAQKEQSEVAEKRDKKLQELNDQLFALREANDGLWKQLVSIKDERQEGQRHQSRRNSRSTRRSARRRSMEQLAYPPASPHLADKKKNAVAAGAHLAVTIVELRDLMKNGRPIIEPGYVVIKVKSVKEKYKTSVKELSSAIRFNETFYFYLAQPDEDVITLHVFYKSKGNSREHHVGDAAFTMATLHRGVPRQRVAIVAQNPGTRDARRAAEVEVTLQSDDFGMLSTPTLAQIEEDNIRFKELQKRVEMNSPESLHCVDVLMAMNTH
Protein: Dymeclin (Q38FE7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGTSTKESLLYFMDVARGVSPPDEKDFSSHLGRCRKELCSGAELYRTLLPIMQTLMPANAQASQVQWVVRFCLKQVEHASCNYSQGVSDIFLTTVRAVQFVVRHACETSRGDASRLLWTIGEDLGESVHGALRVSTTGDSDTVFMNRWLSTGIGKLCIALEKFIVFVPLTVSTVEAHGEVVSLLLCMCSTALYHSTACDTNFTDPFTRLILASGDLHALVLVLLQRLMDWGEGRLPKTPVLYRCAQYSSLWTLYNMFAGGTENESITCGNHLGRHCAQLLSVLVSYGKGYRPNEALHYIASLGDSSQIQVKALLVTFNRHVLRCPALCILLYTLLHDNPTFIHTVMTAYPDEFLGVIQGVLRLSYTASSEAWASGFNSSDDDIDGGQCAIPIVEDAITPEAVASIVRRMTAFSYPFISFMTGTLVLVCSQDQVINKRMSNTIAETTFKVGRLVGRCPVIAVCIVIIVHSIARALNDGNEALAAVFIPCLANFAPFVHDIDVYTSQRLVGLLLLTLRKVQRTAEHARSGAGDCLGTLEGTTPAGGCSSADTSIQMFLRQLLALTEAVGGLLQGDCRNNYSFIYELVYQRSHLEEGAKLLSTVSCHSSEAQTALQSLLSVAKFYDEEIANSTATDSYGGALAVIRQVSQNKVVPTGPSSRLSVRTGTYAATASADVEYCTSLEMGEIPFLYEESTCSYDFFGPFLWSTLLSDAAYPGGILWATDLSTLGIFPH
Protein: Angiomotin-like protein 2 (Q8K371)
Organism: Mus musculus (Mouse)
Function: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC (By similarity).
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:A1YB07}. Cytoplasm {ECO:0000269|PubMed:24806444}. Cell projection, podosome {ECO:0000269|PubMed:23525008}. Cell junction {ECO:0000269|PubMed:24806444, ECO:0000269|PubMed:28842668}.
Interaction partners:
- Merlin
- InaD-like protein
- Multiple PDZ domain protein
- Angiomotin
- Rho GTPase-activating protein 17
- WW domain-containing transcription regulator protein 1
- Angiomotin-like protein 1
- Protein kinase C iota type
- Protein kinase C zeta type
- Transcriptional coactivator YAP1
Sequence:
MRTLEDSSGTVLHRLIQEQLRYGNLTETRTLLAIQQQALRGGAGAGGTGSPQASLEIGAPEDSQVLQQATRQEPQGQEHQGGETHLAENRLYRLCPQPSKGEELPTYEEAKAHSQYYAAQQAGSRPHVGDRDPRGGVSGGGRRQDEALRELRHGHVRSLSERLLQLSLERNGARVPSHMSSSHSFPQLARSQQGPQPRGPPAEGPEPRGPPPQYPHAVMAQETAAVTDPRYRPRSSPHFQHAEVRILQAQVPPVFLQQQQYQYLPQPQEHSPPLHPAALGHGPPSSFGPPAVEGPPSAQATLGSAHLAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQGLVSSERQTDARPAGDRVPAEEPPATAPLPAHTKHGSRDGSTQTDGPADNTSACLASEPDGLLGCNSSQRTPSLDSIAATRVQDLSDMVEILI
Protein: TIP41-like protein (F1QRY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tubulin folding cofactor E-like b
- Serine/threonine-protein phosphatase
- Major histocompatibility complex class II DBB gene.
- Neurogranin A
- Serine/threonine-protein phosphatase.
- Immunoglobulin
- Serine/threonine-protein phosphatase 4 catalytic subunit A
- Serine/threonine-protein phosphatase 4 catalytic subunit B
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
Sequence:
MSSVISQGFQSSKQEFSFGPWIISATKTHIMKSKDIERLAEAMQMPALPEMLFGDNVLRIWHSDGFGIEFNAIDALRRVNNLQESVKVACAQEWQDSRAQSEHSTEAVKRYDWTYTTDYRGTLIGEQTQMKVSPTAERIDMEKLKAREQIKFFEDVLLFEDELHDHGVSMISVKIRVMPSSFFLLLRFFLRVDGVLIRINDTRLYHEAGKKHMLREFSTRESNMADLQHIPPAVYTDPNEIAPHLPLRLTECEKLEFPEGDAPAHTHTQ
Protein: Uncharacterized protein YNL162W-A (Q3E7A8)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized transporter YNL095C
- Uncharacterized membrane protein YNL019C
- Putative uncharacterized protein YAL066W
Sequence:
MSDKPDSQVFCPNCNERLQKCLVQQNYAIIICPSLVCGYPFNQREVLENLTYVDDNDVLKVAKKRLSSRSKP