wanglab/gogpt-training-data huggingface dataset:
Protein: separase (EC 3.4.22.49) (G0SHM3)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Interaction partners:
- Serine/threonine protein kinase-like protein
- Putative cohesin complex protein
- Structural maintenance of chromosomes protein
- SCD domain-containing protein
- Protein phosphatase PP2A regulatory subunit B
- Structural maintenance of chromosomes protein
- protein-tyrosine-phosphatase
- non-specific serine/threonine protein kinase
- Uncharacterized protein
- Kinetochore protein NDC80
Sequence:
MDSLQAQADAVRSAVTSVTTCSPATSSLLKTLLLDINNSATINSDSDSRPSSKTSNSRSRASTNTRAPSRRGKCDSPTPTSLSPREKAALATHVVNAALKALAEAAKTASPAPAPANSEPLSPARQQKGQEDSDLVKTVTKNNAAAIRRSSSAPMSPLQPRSLNRQTTPPAPTGSRPPSRGSNHSTNNNNNNNSSSSSSSSSSSSSSSSSSSSNSNNNSNSNSTNVNLLATVECARVALAALRQLPSTGKISPPELQLESGMSALIGRLITLGLHEQAIKELRILRKKLDTSSDKKTSSKSTEAKTTTTTTAAQVFTEILDFGSVAATGAKLLLIIQTQLHALRILATTTFTSKKPSTIAAILPLLRLDSHTSPLNLLLTASKEKGADTAKIARHTETLSQVLLALTPSVSSKDDTLALEPRLSIPPLAALELQALALEARIEWWRLAGHKGDAEKDIMIPLSRCLAAFARRSQDRSREAWGVCVRAFERVYKGVKNLGMSVAKGGRSALAGVLQSLVTVAKEGGLITEGVTWAGRLVEVVGAEKEGVKFCSLQAQVLGLKLKAPERFWGAEEDAELKKVMECIMGPLRGDTAELDELLGCVCGLRKGAMQVLLAAMRDNNNSGSEEAEYKPSPETRQLLESFVLQCPRFCLRWLGKPPGSRGNTKDYLRYDQRRQLLTQYLPHVLDSSLLLIKTLLDHGTPAWEQIDAILSDCSTLLEYTPLPDSSSPSSYYVKISHFHYLHFISLRQRSSNPQDVGPLRALRKAVDVVKHRSKPEKSAAKLTLKLERLADLCRSLGRIDEALSALQALRSSLVEDGVLRKIARRLQTESPVVVWNRDEGALPLGRCLVGIGRLETVWVDWTVELEEEQERGAVLEWWVRVGVLGRGEEVGLGHAVVERLLGVYIPTKYPVRRLRVLLLVLCAVLGDGKTAGEVLALAREASRVASGDDLGEDKGLASFLPHLKTLCASLEAAVDEYRDIRAVEQCLTSWRGIVSSCEDKNTLEQSIDDVPGLLEHLQAVADFHRMKGRETILISVLELMADISRLAEGPRAEDVIVHGSTFGLQLTNLGRAAKAEEVFRKMGEYLASLQPQDSSDNAAVGEGAVNYHLAMAEHFVALGQIRQAEEHLALAHNAASEEGAVQKYGKVERRRLVARACYLYSVVALERGDSHLALVYARESVRNLFSEWARLEAKMSSSSSSSSSPTETRQEQQHQDDPDAMDIDAAPPALESTRTPKRDAQHTAAGPEFWRLFCSLHRNISWLSAVYAHLGLFNETMYYAEQALRMANLIGSEFYSAQAAAWIASVAWRAADVQKAGEMLRQVMAGLLEKDGGCEYARAVLACRVSETALAQGDLESARRLLEWAEGVVRGIAMGGQKEVVTVEVAEEYEGRKAPIRATRTRKATTRAQSTTRKGAMRSAKGKSASTTTTPSNSRPGTPEVKEEDALLAKLKAYILVQKASMMLRQRDWAAAQQVLSEVPAPAVQSKSSSFLPARHLAMAACLLGMSMDQMAHDPVFSVIQDSTISFPALSGSGSVLLAGKGSPVKAAASPVVTSPRKPDLPTTTKTTTTTTETDPRVYVEHLKSAHDYLLEAHAVAALSGDASLVHRISGMLQNVGLILTATSTKIRPAAVPSAQTAYSVELARNLTWRRERKALLQEKKGLVNGNGTEMTSVQFPPPPNLAASAPRRSSLGFTLDLHRIQRDYIDLVPKHWHVISLSLSDGGHDLCITRLQAGQAPFVLRLPLERASSRDSSVDETDVFDFHTGRAELLEIIKEINRTCHDSRDMAAKGEREKWWAEREALDQRLKELLMNIEHVWLGGFRGVFSQHGRRPELLEKFRAMFEGVLDKHLPSRRQVGRGKKGKGVAGQTKVVLDGNVLELFIGLGDATKSGADFDEELTDLLYFVVDILQFHGERNAYDEIDFDSMVVETMDALMAYHAEANAAPESDSHAHTILVLDKQLHVFPWESLPCLQGLAVSRIPSLACLRKLLLDRRRSSSQIQGEDSEEEDPRSAGHHAPLSGGTYILNPSSDLLSTQKTFESLFSTHLHSPNSWTRIISRPPTEPEFLSALTHSPILLYFGHGSGAQYIRSRNIRHLDHCRATVLLMGCSSAALTAKGEFEPSGPVWNYMLAGAPAVVGTLWDVTDRDIDRFAGGVLEGWGVLPEGCMGEKNGKKKAGRNGLSLVQAVAKARDRCRFRYVTAAAAVVYGIPVYVDVDGKSKD
Protein: Double parked, isoform A (Double parked, isoform B) (LD35784p) (Replication protein double parked) (Q7JVY2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Geminin
- Origin recognition complex subunit 2
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm2
- Origin recognition complex subunit 5
- Cell division control protein
- DNA replication licensing factor Mcm6
- DNA replication licensing factor Mcm7
- Origin recognition complex subunit 4
Sequence:
MAQPSVAAFFTNRKRAALDDAISIKNRRLVEPAETVSPASAPSQLPAGDQDADLDTLKAAATGMRTRSGRTARLIVTAAQESKKKTPAAAKMEPHIKQPKLVQFIKKGTLSPRKQAQSSKLDEEELQQSSAISEHTPKVNFTITSQQNADNVQRGLRTPTKQILKDASPIKADLRRQLTFDEVKTKVSRSAKLQELKAVLALKAALEQKRKEQEERNRKLRDAGPSPSKSKMSVQLKEFDTIELEVLISPLKTFKTPTKIPPPTPDKHELMSPRHTDVSKRLLFSPAKNGSPVKLVEVPAYKRYASLVESSRAGQLPLPYKYRHLLDVFKGLDSVVAMFHNRKETITFKKLKPAVQRMLRKNFTETHLAQIKHIYPDAFIFSQVKTRNFGSVSKADYFQLIIAPNVEPLPEQQQSEKPQHFTKINEDDVLASAQSTSMNPHVMTARMQRFQSLLLDRAMRAHDQFLRSQDPPIIIEKALTRWHPQFDLESCPEVELSPLPQPPNVEKYSSAKDILSTARNLFNCATPMERAMDRYEAKLESEKQQAAESNKKTEEQQAGEVTRTSTAIQTSQEVPGISGSSKNPTVPETTNQTETAKPTVKDCTVPDASSNLLKGLPKSLIEKIRAKQAAKALEAMTRRPSQDQEATKYSRLPELARHLRNVFVTERKGVLTLEVIIKKIQNSFRANLTPQEIEAHLKLLAKELPSWASFHEVRKTMYLKVAKDMDMNKIIEKLESVANAKSN
Protein: Xenotropic and polytropic retrovirus receptor 1 homolog (A8DZH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:23791524}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- NLR family CARD domain-containing protein 3 isoform X1
- Glycerophosphocholine phosphodiesterase 1
- Phosphate transporter
Sequence:
MKFTEHLSAHITPEWRKQYIQYEAFKEMLYSAQDQAPSIEVTDEDTVKRYYAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQRESSRAAGLRHRRTVFHLSQQERCKHRNIKDLQLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKIFETSRGADWRVAHVEVAPFYTCKKITQLISETETLVTTELEGGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLYCGVFVALTVTVIIAGVVKLVEHFGDNTDVWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRNNLSHQHLFEIAGFLGVLWCVSILSCLFAENTLIPIHMNPLALYGFFFLFLINPLKTCYYKSRFWLLKLLFRVVTAPFHRVGFADFWLADQLNSLVVVLMDLEYMICFYSLELNWTMSEGELWIKEGERICYSYSYGVRAVIKCLPAWFRFVQCLRRYRDTKRAFPHLVNAGKYSTTFFVVIFEALFKTHSGDERFVFLYIMIACRIVNSCYTLLWDLKMDWGLFDRNAGENTLLREEIVYPQKAYYYCAIVEDVILRFAWTIPLSLEVVYDRPVISNILGTVLPPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQEDGVRNRLGKKNWKRSYSMSLRRPRLSSQSKVRDTKVLIEDTDDDT
Protein: Protein IscX (P0C0L9)
Organism: Escherichia coli (strain K12)
Function: May function as iron donor in the assembly of iron-sulfur clusters.
Interaction partners:
- 2Fe-2S ferredoxin
- Co-chaperone protein HscB
- Chaperone protein HscA
- Iron-sulfur cluster assembly scaffold protein IscU
- Cysteine desulfurase IscS
- Iron-binding protein IscA
- HTH-type transcriptional regulator IscR
- Iron-sulfur cluster assembly protein CyaY
- Peptidase B
- Protein SseB
Sequence:
MGLKWTDSREIGEALYDAYPDLDPKTVRFTDMHQWICDLEDFDDDPQASNEKILEAILLVWLDEAE
Protein: E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (Putative transcription factor XPRF) (RING finger protein 59) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18) (O15344)
Organism: Homo sapiens (Human)
Function: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10077590}. Note=Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interphase and with the mitotic spindle and midbodies during mitosis and cytokinesis.
Interaction partners:
- Immunoglobulin-binding protein 1
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Probable E3 ubiquitin-protein ligase MID2
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin-conjugating enzyme E2 D2
- Gamma-butyrobetaine dioxygenase
- Elongation factor 1-alpha 1
- Mid1-interacting protein 1
Sequence:
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNSQPFKLDPKSAHRKLKVSHDNLTVERDESSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGLAYKSAPKHEWIGKNSASWALCRCNNNWVVRHNSKEIPIEPAPHLRRVGILLDYDNGSIAFYDALNSIHLYTFDVAFAQPVCPTFTVWNKCLTIITGLPIPDHLDCTEQLP
Protein: Probable desiccation-related protein LEA14 (O03983)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Low-temperature-induced 78 kDa protein
- Dehydrin ERD10
- Dehydrin COR47
- Late embryogenis abundant protein 2
- Late embryogenesis abundant protein 29
- Dehydrin Xero 1
- Dehydrin Xero 2
- Protein COLD-REGULATED 15A, chloroplastic
- Late embryogenesis abundant protein 7
- Protein SENESCENCE-ASSOCIATED GENE 21, mitochondrial
Sequence:
MASLLDKAKDFVADKLTAIPKPEGSVTDVDLKDVNRDSVEYLAKVSVTNPYSHSIPICEISFTFHSAGREIGKGKIPDPGSLKAKDMTALDIPVVVPYSILFNLARDVGVDWDIDYELQIGLTIDLPVVGEFTIPISSKGEIKLPTFKDFF
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (A0A8I6GLU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MATGLGEPIYGLSEEEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSEQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRSTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEASEGGGEGPEPWETISEEVNMAGDSLSLALPPPPASPVSRTSPQELSEELSRRLQITPDSNGEQFSALIQREPSSRLRSCSVTDTVAEQAHLPPPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEGAKDSPIRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKASLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
Protein: Transmembrane protein 184A (Sexually dimorphic expressed in male gonads 1) (Q3UFJ6)
Organism: Mus musculus (Mouse)
Function: Acts as a heparin receptor in vascular cells (By similarity). May be involved in vesicle transport in exocrine cells and Sertoli cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q1RMW2}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q1RMW2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:18321981}; Multi-pass membrane protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:18321981, ECO:0000269|PubMed:19097053}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19097053}. Note=Colocalizes with the secretory granule marker VAMP2 in pancreatic acinar cells (PubMed:19097053). {ECO:0000269|PubMed:19097053}.
Interaction partners:
Sequence:
MRNASGFLKTAGAPLVSATWLPPSPPPAMPTVAAGPQMERVDNGSQGAPQLFLTSALARGVSGVFVWTALLLTGHQIYSHLRSYTAPREQRFVIRLLFIVPIYAFDSWLSLLLLGGHPYYVYFDSVRDCYEAFVIYSFLTLCFQYLGGESAIMAEIRGKPIRSSCFYGTCCLRGMSYSITFLRFCKQATLQFCIVKPVMALITIILQAFDKYHDGDFNIHSGYLYVTLVYNASVSLALYALFLFYFATRDLLRPFEPVLKFLTIKAIIFLSFWQGMLLAILERCGVIPEVQAVDGTRVGAGTLAAGYQNFLICVEMLFASLALRYAFPSQVYSEKKNSPVPPAPMQSISSGLKETISPQDIVQDAIHNFSPAYQQYTQQSTHEAPGPGQGGHPAPSTHPGPASGSGGGKKSRNIEKRMLIPSEDL
Protein: Cytochrome oxidase assembly factor 4 (Cx9C motif-containing protein 3) (Q05809)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cytochrome c oxidase assembly or stability.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20624914}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20624914}; Intermembrane side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19703468, ECO:0000269|PubMed:20624914}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1 machinery.
Interaction partners:
- Cytochrome c oxidase assembly factor 6
- Mitochondrial intermembrane space import and assembly protein 40
- COX assembly mitochondrial protein 2
- Cytochrome c oxidase copper chaperone
- mRNA-binding protein PUF3
- Cytochrome oxidase assembly protein SHY1
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
Sequence:
MSETGETSEYYKQALEEYKEVQEDEDPDVWDTRISKTGCYVENLALQLCHAETGDWRQCFNEMALFRKCWEKNGNRERVSTVDVDGTTSKDSEKKK
Protein: Histone-lysine N-methyltransferase (EC 2.1.1.355) (A0A8I6A0U8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009343}.
Interaction partners:
Sequence:
VSRNCHFLLQRILALSKTCDYIFLWVFGLLIPGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCVRILKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYNLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
Protein: Testin (Xtes) (Q7ZXE9)
Organism: Xenopus laevis (African clawed frog)
Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. May inhibit cell growth (By similarity). Regulates cranial neural crest migration. Acts together with prickle1 to control axial elongation.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:16554046}. Cell junction, focal adhesion {ECO:0000250}. Note=Detected along actin stress fibers. {ECO:0000250}.
Interaction partners:
Sequence:
MELENKFKKVTLGHEEGSGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHSVLSNNEDDRKVGKLFEDTKYTALIAKLKTDGIPTYKRNVMILTSPVAAKKDVSINTVTYEWAPPVQNQALARRYMELIPKDKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPNEVKQMEQFVKKYKNEVLGVGDVKLPKEVEAQASGAGRSTNGSLSTLTTVKSTDDKVAAQKGSTYYCFRCKENMREGDPAVYAERAGYDKLWHPSCFVCFTCNELLVDMIYFWKNGKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAEGLNWHLKHFCCFDCDIVLAGEIYVMVNDKAVCKPCYVKNHAVSCQGCHNAIDPEVQRVSYNGFHWHAAPECFICSCCSKCLIGQKFMPIEGMVFCSVECKKKMSS
Protein: Large ribosomal subunit protein uL18 (60S ribosomal protein L5) (L1) (L1a) (Ribosomal 5S RNA-binding protein) (YL3) (P26321)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}.
Interaction partners:
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS1A
- Large ribosomal subunit protein uL6A
- Large ribosomal subunit protein eL24B
- Small ribosomal subunit protein eS10A
- Large ribosomal subunit protein uL6B
- Large ribosomal subunit protein eL19A
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL4B
Sequence:
MAFQKDAKSSAYSSRFQTPFRRRREGKTDYYQRKRLVTQHKAKYNTPKYRLVVRFTNKDIICQIISSTITGDVVLAAAYSHELPRYGITHGLTNWAAAYATGLLIARRTLQKLGLDETYKGVEEVEGEYELTEAVEDGPRPFKVFLDIGLQRTTTGARVFGALKGASDGGLYVPHSENRFPGWDFETEEIDPELLRSYIFGGHVSQYMEELADDDEERFSELFKGYLADDIDADSLEDIYTSAHEAIRADPAFKPTEKKFTKEQYAAESKKYRQTKLSKEERAARVAAKIAALAGQQ
Protein: Evasin P1183 (A0A023G9N9)
Organism: Amblyomma triste (Neotropical tick)
Function: Salivary chemokine-binding protein which binds to host chemokine CCL2.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MTRNWSFRVIFVSAMWCALLKFATLEAPKDDFEYDGGCPFVVLDNGTHVKPAGCSHLCNGAPETLDNIECYNVTEEVAKRMTPGIPYACWLGWCSKGECKRDNRTEVCYRGSEEE
Protein: Probable G-protein coupled receptor 173 (Super conserved receptor expressed in brain 3) (Q6PI62)
Organism: Mus musculus (Mouse)
Function: Is a receptor for the SMIM20 derived peptides Phoenixin-14 and Phoenixin-20. It mediates the Phoenixin-14 and Phoenixin-20 augmentation of gonadotropin-releasing hormone (GNRH) signaling in the hypothalamus and pituitary gland. In the ovary, it mediates the effects of Phoenixin-14 and Phoenixin-20 induced granulosa cell proliferation during follicular growth.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Small integral membrane protein 20
Sequence:
MANTTGEPEEVSGALSLPSASAYVKLVLLGLIMCVSLAGNAILSLLVLKERALHKAPYYFLLDLCLADGIRSAICFPFVLASVRHGSSWTFSALSCKIVAFMAVLFCFHAAFMLFCISVTRYMAIAHHRFYAKRMTLWTCAAVICMAWTLSVAMAFPPVFDVGTYKFIREEDQCIFEHRYFKANDTLGFMLMLAVLMAATHAVYGKLLLFEYRHRKMKPVQMVPAISQNWTFHGPGATGQAAANWIAGFGRGPMPPTLLGIRQNGHAASRRLLGMDEVKGEKQLGRMFYAITLLFLLLWSPYIVACYWRVFVKACAVPHRYLATAVWMSFAQAAVNPIVCFLLNKDLKKCLRTHAPCWGTGGAPAPREPYCVM
Protein: Peptidase S1 domain-containing protein (Q9VEM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trypsin zeta
- Peptidase S1 domain-containing protein
- Peptidase S1 domain-containing protein
- Uncharacterized protein, isoform A
- Serine protease K12H4.7
- Peptidase S1 domain-containing protein
- Metalloendopeptidase
- FI02848p
- Trypsin iota
- RE36938p)
Sequence:
MKLLRLSLLILLAVKPPNPCESKRIVGPFPAGQSGRIKGGEEAEIGFAPYQVSLQPIVGSHNCGGAILNENWIITAGHCVENFIPALVNVITGTNKWAEPGAIYYTAEIHKHCMYDQPYMHNDIALVKLTENITFNELTQPIALPTRPVQLGEEIVLTGWGSDVAYGSSMEDLHKLTVGLVPLDECYETFNRTSSMGVGHICTFSREGEGACHGDSGGPLVSNGQLVGVVNWGRPCGVGLPDVQANVYYYLDWIRSKLSGNNKCYY
Protein: Transcription initiation factor TFIID subunit 4 (TBP-associated transcription factor family member taf-4) (O61707)
Organism: Caenorhabditis elegans
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-4 (By similarity). Essential for early embryonic development, probably acting via activating transcription initiation by RNA polymerase II, as part of the TFIID complex. In early embryos, but not oocytes, remains, presumably inactive, in the cytoplasm as a result of binding to oma-1. Upon degradation of oma-1, taf-4 is released and bound by taf-12, and the taf-4/12 heterodimer translocates to the nucleus and transcriptional repression is relieved. Involved in lifespan extension in a manner dependent upon mitochondrial function. Plays a role in modulating polyribosome formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440, ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:18854162}. Cytoplasm {ECO:0000269|PubMed:18854162}. Note=Localization is ubiquitous in one-cell and early two-cell embryos, then enriched in nucleus in all subsequent embryo stages (PubMed:18854162). Localization to the nucleus is prevented by interaction with oma-1 and is sequestered in the cytoplasm, following fertilization, and thus allows for transcriptional suppression in early embryos, but not in oocytes (PubMed:18854162). Localized to the nucleus in a taf-12-dependent manner (PubMed:18854162). {ECO:0000269|PubMed:18854162}.
Interaction partners:
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 13
- PHD-type domain-containing protein
- Transcription initiation factor TFIID subunit 8
Sequence:
MSLPRFRLVQGKAIGERSTPGVSTPEPAPPQIKQEVDYQDAHQMAPEPVEAPQAQNHQMQPPRQPIQQQMQHFQSPSPMAPQGPPGTPQNSAAAAAAASDDKNVTKCVRFLKTLINLSNNDDPEMPDKAARVKELIRGVIYLETTAEEFTRNLQQVLKSQAQPHLLPFLQNTLPALRNAVRNGTASVEGVNPPPGYVFNNGRTPGPPQPPPPQQQSQQQPPLEMRQIPNPNQIPPQMVQGGPHMVSVGARPMIRPMGPGGPSPMGLQGPVRGPMGHQMVQMHPPPPPQQIQQQHPAPPVEMEVEENLQPTAAATATRQYPEGSLKSSILKPDEVLNRITKRMMSSCSVEEEALVAISDAVESHLRELITLMAGVAEHRVESLRIPENYVAIDDVKRQLRFLEDLDRQEEELRESREKESLIRMSKNKNSGKETIEKAKEMQRQDAEAKRNRDANAAAIAALSSNKTVKNKWENTGAATTAPRPRTVRVTTRDLHLLVNQDSRFTGTFIREKMSYGGPAVDTTI
Protein: Golgin A2 (H0Y7B8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWPQPRLPPRPAMSEETRQSKLAAAKKKLREYQQRNSPGVPTGAKKKKKIKNGSNPETTTSGGCHSPEDIQDILKVLVSDLNRSNGVALPPLDKWKTPKDNAATLQPSDDTVLPGGVPSPGASLTSMAASQNHDADNVPNLMDETKTFSSTESLRQLSQQLNGLVCESATCVNGEGPASSANLKDLESRYQQLAVALDSSYVTNKQLNITIEKLNQEITDQLEEEKKECHQKQGALREQLQ
Protein: N-terminal acetyltransferase A complex subunit NAT1 (NatA complex subunit NAT1) (Amino-terminal, alpha-amino, acetyltransferase 1) (P12945)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- N-terminal acetyltransferase B complex catalytic subunit NAT3
- N-terminal acetyltransferase A complex catalytic subunit ARD1
- N-alpha-acetyltransferase NAT5
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase B complex subunit MDM20
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Large ribosomal subunit protein uL4A
- Large ribosomal subunit protein eL31A
- Large ribosomal subunit protein uL23
Sequence:
MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALKGLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNNGSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAINTLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDKFGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGKLEQFYPRCEPPKFIPLTFLQDKEELSKKLREYVLPQLERGVPATFSNVKPLYQRRKSKVSPLLEKIVLDYLSGLDPTQDPIPFIWTNYYLSQHFLFLKDFPKAQEYIDAALDHTPTLVEFYILKARILKHLGLMDTAAGILEEGRQLDLQDRFINCKTVKYFLRANNIDKAVEVASLFTKNDDSVNGIKDLHLVEASWFIVEQAEAYYRLYLDRKKKLDDLASLKKEVESDKSEQIANDIKENQWLVRKYKGLALKRFNAIPKFYKQFEDDQLDFHSYCMRKGTPRAYLEMLEWGKALYTKPMYVRAMKEASKLYFQMHDDRLKRKSDSLDENSDEIQNNGQNSSSQKKKAKKEAAAMNKRKETEAKSVAAYPSDQDNDVFGEKLIETSTPMEDFATEFYNNYSMQVREDERDYILDFEFNYRIGKLALCFASLNKFAKRFGTTSGLFGSMAIVLLHATRNDTPFDPILKKVVTKSLEKEYSENFPLNEISNNSFDWLNFYQEKFGKNDINGLLFLYRYRDDVPIGSSNLKEMIISSLSPLEPHSQNEILQYYL
Protein: Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a [Includes: Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (Q39659)
Organism: Cucumis sativus (Cucumber)
Subcellular location: Glyoxysome {ECO:0000269|PubMed:8051146}.
Interaction partners:
Sequence:
MGSNAKGRTVMEVGTDGVAIITIINPPVNSLSFDVLFSLRDSYEQALRRDDVKAIVVTGAKGKFSGGFDITAFGVLQGGKGEQPNVRNISIEMITDIFEAARKPAVAAIDGLALGGGLEVAMACHARISTPTAQLGLPELQLGIIPGFGGTQRLPRLVGLSKALEMMLTSKPIKGQEAHSLGLVDAIVPPEELINTARRWALEILERRRPWVHSLHRTDKLESLAEARKIFNLARAQAKKQYPNLKHTIACIDAVETGVVSGPRAGLWKEAEEFQGLLHSDTCKSLIHIFFAQRSTTKVPGVTDLGLVPRQIKKVAIVGGGLMGSGIATALILSNYHVVLKEVNDKFLQAGIDRVRANLQSRVKKGNMTNEKFEKSISLLKGVLNYESFKDVDMVIEAVIENVSLKQQIFSDLEKYCPPHCMLATNTSTIDLELIGERIKSRDRIIGAHFFSPAHIMPLLEIVRTKHTAAQVIVDLLDVGKNIKKTPVVVGNCTGFAVNRMFFPYSQAAILLAEHGVDPYQIDRAISKFGMPMGPFRLCDLVGFGVAAATASQFVQAFPERTYKSMLIPLMQEDKNAGESTRKGFYVYDKNRKAGPNPELKKYIEKARNSSGVSVDPKLTKLPEKDIVEMIFFPVVNEACRVLAEGIAVKAADLDIAGVMGMGFPSYRGGLMFWADSLGSNYIYSRLEEWSKQYGGFFKPCGYLAERAVQGATLSAPGGHAKPRM