wanglab/gogpt-training-data huggingface dataset:
Protein: Programmed cell death protein 4 (Protein MA-3) (Topoisomerase-inhibitor suppressed protein) (Q61823)
Organism: Mus musculus (Mouse)
Function: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:12894233}. Cytoplasm {ECO:0000269|PubMed:12894233}. Note=Shuttles between the nucleus and cytoplasm (PubMed:12894233). Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (By similarity). {ECO:0000250|UniProtKB:Q53EL6, ECO:0000269|PubMed:12894233}.
Interaction partners:
- Eukaryotic initiation factor 4A-I
- Eukaryotic initiation factor 4A-II
- Ribonuclease 3
- Eukaryotic translation initiation factor 4B
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Reversion-inducing cysteine-rich protein with Kazal motifs
- F-box/WD repeat-containing protein 1A
- Eukaryotic translation initiation factor 4E
- Ribosomal protein S6 kinase beta-1
- Protein argonaute-2
Sequence:
MDIENEQTLNVNPTDPDNLSDSLFSGDEENAGTEEIKNEINGNWISASTINEARINAKAKRRLRKNSSRDSGRGDSVSDNGSEAVRSGVAVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDETAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTNDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQPVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIVMVLESTGESAFKMILDLLKSLWKSSTITIDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY
Protein: Transcription factor-like 5 (basic helix-loop-helix) (E9Q5K1)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGPGPREPPPEAGATGGEAGPEGAGGGDAALGEPGLSFTTTDLSLVEMTEVEYTQLQHILYSHMEAADGELEARLGSALLAGPGAGSGAAGSLAPAPPVYPVLCPPLAADAPCLGHVDFQELRMMLLGEAGAAEKTPGGADGTRTRADGVAKEGAGGAGPDGAPEARAKPTVRVRLEDRFNSMPAEPPAPRGAEPAESGVALNKVLVTHALYWKLPSTRILDCLEHFLSVTSKRLSPPNRQEVVETKPCRSRFGLKWEKRYVNKQSIRGIGVESASWTQAWSEEPLERFRM
Protein: Alpha-2-macroglobulin receptor-associated protein (Alpha-2-MRAP) (Heparin-binding protein 44) (HBP-44) (Low density lipoprotein receptor-related protein-associated protein 1) (RAP) (P55302)
Organism: Mus musculus (Mouse)
Function: Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway.
Subcellular location: Rough endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P30533}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000250|UniProtKB:P30533}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P30533}. Golgi apparatus lumen {ECO:0000250|UniProtKB:P30533}. Endosome lumen {ECO:0000250|UniProtKB:P30533}. Cell surface {ECO:0000250|UniProtKB:P30533}. Note=May be associated with receptors at the cell surface. {ECO:0000250|UniProtKB:P30533}.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
- Low-density lipoprotein receptor-related protein 2
- Low-density lipoprotein receptor-related protein 8
- Sortilin-related receptor
Sequence:
MAPRRERVSTLPRLQLLVLLLLPLMLVPQPIAGHGGKYSREKNEPEMAAKRESGEEFRMEKLNQLWEKAKRLHLSPVRLAELHSDLKIQERDELNWKKLKVEGLDKDGEKEAKLIHNLNVILARYGLDGRKDAQMVHSNALNEDTQDELGDPRLEKLWHKAKTSGKFSSEELDKLWREFLHYKEKIQEYNVLLDTLSRAEEGYENLLSPSDMAHIKSDTLISKHSELKDRLRSINQGLDRLRKVSHQGYGSTTEFEEPRVIDLWDLAQSANFTEKELESFREELKHFEAKIEKHNHYQKQLEISHQKLKHVESIGDPEHISRNKEKYVLLEEKTKELGYKVKKHLQDLSSRVSRARHNEL
Protein: TMEM131 protein (Q0P631)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSLFASFSSDPKIKQPNGSKHKLTKAASLPGKNGNPTFAAVTAGYDKSPGGNGFAKVSSNKTGFSSSLGISHAPVDSDGSDSSGLWSPVSNPSSPDFTPLNSFSAFGNSFNLTGEVFSKLGLSRSCNQASQRSWNEFNSGPSYLWESPATDPSPSWPASSGSPTHTATSVLGNTSGLWSTTPFSSSIWSSNLSSALPFTTPANTLASIGLMGTENSPAPHAPSTSSPADDLGQTYNPWRIWSPTIGRRSSDPWSNSHFPHEN
Protein: Probable allantoicase (EC 3.5.3.4) (Allantoate amidinohydrolase) (Q09913)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Interaction partners:
- Ureidoglycolate lyase
- Urease
- Uricase
- Alpha-ketoglutarate-dependent xanthine dioxygenase xan1
- Dilute domain-containing protein SPAC25B8.08
- Uncharacterized urease accessory protein ureD-like
Sequence:
MSVENVERLSPEQADAFFGQSSVDLISRALGGQVLGCSDDFFASCENLINPADPIRKAGVFVETGAWYDGWETRRHNTAPCDWVIVKLGPSSGRVTGCEIDTTFFNGNHAPEVSVEAAFLPEGNPDAKTNWTPILPKLPCGPTQRHIYRFKEIPQQNFTHVRLCMYPDGGIARFRLYGNVVPVFPADLDARLDLAHMYLGGLVVQCSDQHFGKKDNLLLPGRGVNMGDGWETARSREKGHVDWVIVKLGARGYIDDALIDTNHFKGNYPKEVILEAIDSPDHIPGPDAQWVTILPARKLGPHMEHVFTNLQNNSTPMTHVRMIIIPDGGVKRLRIYGRRAAN
Protein: Cell division control protein 6 homolog (CDC6-related protein) (Cdc18-related protein) (HsCdc18) (p62(cdc6)) (HsCDC6) (Q99741)
Organism: Homo sapiens (Human)
Function: Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated.
Subcellular location: Nucleus {ECO:0000269|PubMed:26818844, ECO:0000269|PubMed:9566895}. Cytoplasm {ECO:0000269|PubMed:9566895}. Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells (PubMed:9566895). {ECO:0000269|PubMed:9566895}.
Interaction partners:
- DNA replication licensing factor MCM5
- Cyclin-dependent kinase 2
- DNA replication licensing factor MCM4
- Origin recognition complex subunit 1
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- Cyclin-A2
- Origin recognition complex subunit 4
- DNA replication licensing factor MCM7
- Origin recognition complex subunit 6
Sequence:
MPQTRSQAQATISFPKRKLSRALNKAKNSSDAKLEPTNVQTVTCSPRVKALPLSPRKRLGDDNLCNTPHLPPCSPPKQGKKENGPPHSHTLKGRRLVFDNQLTIKSPSKRELAKVHQNKILSSVRKSQEITTNSEQRCPLKKESACVRLFKQEGTCYQQAKLVLNTAVPDRLPAREREMDVIRNFLREHICGKKAGSLYLSGAPGTGKTACLSRILQDLKKELKGFKTIMLNCMSLRTAQAVFPAIAQEICQEEVSRPAGKDMMRKLEKHMTAEKGPMIVLVLDEMDQLDSKGQDVLYTLFEWPWLSNSHLVLIGIANTLDLTDRILPRLQAREKCKPQLLNFPPYTRNQIVTILQDRLNQVSRDQVLDNAAVQFCARKVSAVSGDVRKALDVCRRAIEIVESDVKSQTILKPLSECKSPSEPLIPKRVGLIHISQVISEVDGNRMTLSQEGAQDSFPLQQKILVCSLMLLIRQLKIKEVTLGKLYEAYSKVCRKQQVAAVDQSECLSLSGLLEARGILGLKRNKETRLTKVFFKIEEKEIEHALKDKALIGNILATGLP
Protein: Probable indole-3-pyruvate monooxygenase YUCCA3 (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA3) (O23024)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in auxin biosynthesis. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in roots.
Interaction partners:
- L-tryptophan--pyruvate aminotransferase 1
- Tryptophan aminotransferase-related protein 1
- Tryptophan aminotransferase-related protein 2
- Aromatic aminotransferase ISS1
- Amidase 1
- Auxin efflux carrier component 2
- Indole-3-acetaldehyde oxidase
- Auxin transporter protein 1
- Auxin efflux carrier component 7
- Tryptophan aminotransferase-related protein 3
Sequence:
MYGNNNKKSINITSMFQNLIPEGSDIFSRRCIWVNGPVIVGAGPSGLAVAAGLKREGVPFIILERANCIASLWQNRTYDRLKLHLPKQFCQLPNYPFPDEFPEYPTKFQFIQYLESYAANFDINPKFNETVQSAKYDETFGLWRVKTISNMGQLGSCEFEYICRWIVVATGENAEKVVPDFEGLEDFGGDVLHAGDYKSGGRYQGKKVLVVGCGNSGMEVSLDLYNHGANPSMVVRSAVHVLPREIFGKSTFELGVTMMKYMPVWLADKTILFLARIILGNTDKYGLKRPKIGPLELKNKEGKTPVLDIGALPKIRSGKIKIVPGIIKFGKGKVELIDGRVLEIDSVILATGYRSNVPSWLKDNDFFSDDGIPKNPFPNGWKGEAGLYAVGFTRKGLFGASLDAMSVAHDIANRWKEESKQQKKTAAARHRRCISHF
Protein: SWI/SNF complex component SNF12 homolog (Q9FMT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chromatin structure-remodeling complex protein BSH
- Actin-related protein 4
- SWI/SNF complex subunit SWI3C
- SWI/SNF complex subunit SWI3A
- SWI/SNF complex subunit SWI3B
- SWI/SNF complex subunit SWI3D
- Chaperone DnaJ-domain superfamily protein
- High mobility group B protein 10
- Armadillo repeat-containing protein LFR
- High mobility group B protein 9
Sequence:
MSGNNNNPQKPQGSAPLPFGNPGMASASVPGNQGFAQSHMAANFQAQFQFSQAQALAHAQAQSKVQAQLQAQLQAQGMTMNQAQGSPGIGGLGPSSPSLTTPGSLNMKRFQQKPPMRPPGAPASNNTISPMRTMELTPAARKKKQKLPEKSLQERVAAILPESALYTQLLEFESRVDAALTRKKVDIQEALKNPPCIQKTLRIYVFNSFANQNNTIPGNPNADPPTWTLKIIGRILEDGVDPDQPGFVQKANPLHPKFSSFFKRVTVSLDQRLYPENPLIIWENARSPAPQEGFEIKRKGNQEFAASIRLEMNYVPEKFKLSTALMDVLGIEVETRPRIIAAIWHYVKARKLQNPNDPSFFNCDAALQKVFGEEKLKFTMVSQKISHHLSPPPPIHLEHKIKLSGNNPAVSACYDVLVDVPFPIQRDLNNLLANAEKNKEIEACDEAICAAIRKIHEHRRRRAFFLGFSQSPVEFINALIESQSKDLKVVAGEASRNAERERRSDFFNQPWVEDAVIRYLNRRPAAGNDGPGSW
Protein: Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (P49591)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22353712, ECO:0000269|PubMed:28236339, ECO:0000269|PubMed:34570399, ECO:0000269|PubMed:36041817}. Nucleus {ECO:0000269|PubMed:22353712, ECO:0000269|PubMed:34570399, ECO:0000269|PubMed:36041817}. Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus. {ECO:0000269|PubMed:22353712, ECO:0000269|PubMed:34570399, ECO:0000269|PubMed:36041817}.
Interaction partners:
- L-seryl-tRNA
- Glycine--tRNA ligase
- O-phosphoseryl-tRNA
- Probable arginine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase 1, cytoplasmic
- Cysteine--tRNA ligase, cytoplasmic
Sequence:
MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEPSKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
Protein: Synaptic vesicle glycoprotein 2A (Synaptic vesicle protein 2) (Synaptic vesicle protein 2A) (Calcium regulator SV2A) (Q9JIS5)
Organism: Mus musculus (Mouse)
Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
Subcellular location: Presynapse {ECO:0000269|PubMed:12209837}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q02563, ECO:0000269|PubMed:12209837}.
Interaction partners:
- Synaptophysin
- Synaptotagmin-1
- Synaptic vesicle glycoprotein 2B
- Synaptic vesicle glycoprotein 2C
- Vesicle-associated membrane protein 2
- Synaptotagmin-2
- Laminin subunit alpha-5
- Laminin subunit alpha-1
- Synapsin-1
- Synaptosomal-associated protein 25
Sequence:
MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPAPADGYYRGEGAQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKDREELAQQYETILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFSPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYAARTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLVNSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVLSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ
Protein: Glutamate receptor ionotropic, delta-1 (GluD1) (GluR delta-1 subunit) (Q62640)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q61627}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEALTLWLLPWICQCVTVRADSIIHIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQSLTDAMHIPHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVRLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLDQASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEISDPEILDLVHSALGRMTVVRQIFPSAKDNQKCMRNNHRISSLLCDPQEGYLQMLQISNLYLYDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILGTTYSETFGKDMRKLATWDSEKGLNGSLQERPMGSRLQGLTLKVVTVLEEPFVMVAENILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGRYGHQLHNTSWNGMIGELISKRADLAISAITITPERESVVDFSKRYMDYSVGILIKKPEEKISIFSLFAPFDFAVWACIAAAIPVVGVLIFVLNRIQAVRSQSATQPRPSASATLHSAIWIVYGAFVQQGGESSVNSVAMRIVMGSWWLFTLIVCSSYTANLAAFLTVSRMDSPVRTFQDLSKQLEMSYGTVRDSAVYEYFRAKGTNPLEQDSTFAELWRTISKNGGADNCVSNPSEGIRKAKKGNYAFLWDVAVVEYAALTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWWPHTGRCDLTSHSSAQTDGKSLKLHSFAGVFCILAIGLLLACLVAALELWWNSNRCHQETPKEDKEVNLEQVHRRINSLMDEDIAHKQISPASIELSALEMGGLAPSQALEPTREYQNTQLSVSTFLPEQSSHGTSRTLSSGPSSNLPLPLSSSATMPSIQCKHRSPNGGLFRQSPVKTPIPMSFQPVPGGVLPEALDTSHGTSI
Protein: Glycosyl transferase, group 2 family protein (Q72DQ7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
Sequence:
MRPTITALVLTYNGERLLDRCLGSLAFCDRILVVDSFSTDATVAIAQAAGAEVLQRKWEGPGPQFAFALEKISDGWIVSLDQDEICSEELRDSILAATAADSGEAGYWIPRRSWYFDRFLKHSGWYPDHLLRLFRAGRMRVEVSGAHYSFHPDGETGTLTGDILHYPYESFRQHLDKVNDYAQKGADDLRAKGKRGGLCAGLCHGAGRFIRIYIIKRGFLDGRAGFINAIHGAFYAFLKHLRIEEGDWGRPFEHK
Protein: Sister chromatid cohesion 1 protein 2 (SCC1 homolog 2) (AtRAD21-1) (Q9FQ20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in sister chromatid cohesion during mitosis.
Subcellular location: Nucleus.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion protein SCC2
- Structural maintenance of chromosomes protein 4
- Protein GRAVITROPIC IN THE LIGHT 1
- Wings apart-like protein 1
- Sister-chromatid cohesion protein 3
- Wings apart-like protein 2
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6B
Sequence:
MFYSHCLVSRKGPLGAIWVAAYFFKKLKKSQVKATHIPSSVDQILQKELDALTYRVLAYLLLGVVRIYSKKVDFLFDDCNKALIGVKEFVAKERNREKTGVSLPASIECFSIALPERFELDAFDLGVLEDFHGGNVKPHEDITLKDGSQETERMDMYSMERFDMEEDLLFTFHETFSTNHNENKHESFAHDMELDAENVRDTTEEASVRVVEAEPLDSNEPSRDHQNASRHREDPESDDILLEPQMSEDIRIAQEEDTVRETICTIVQRLVDSHESSGDNLHRDGHTENLESEKTSKKTSCEEMQHDRSLPSECGIPEAIHGIEDQPSGATRINGEKEIPEMSTLEKPEPVSVTGSRDLQEGVEKCRDHNEAEMADFELFHGSHKEQSETSEVNLHGSEKGFLSDMTVSKDPSSEFNATDTPVTVTPKTPSRLKISEGGTSPQFSIIPTPAAKESSRVSRKRKCLIDDEVIIPNKVMKEMIEDSSKLLAKRRNVPHTDCPERRTKRFANPFRSFLEPLIQYGSSDLQSLFCQPIKLKNWATTGTPKDTKIARHKEKSSLDTVRSPGVILSSDQTENTQEIMETPQAAALAGLKVTAGNSNVVSVEMGASSTTSGTAHQTENAAETPVKPSVIAPETPVRTSEQTVIAPETPVVSEQVEIAPETPVRESMSKRFFKDPGTCYKKSRPASPFTSFEEHPSVYYVENRDLDTILMNDEQVNADERQDLQQETWSSRTRNVAKFLEKTFLEQREREEEEKVSLLQLCRGRTQKESARLFYETLVLKTKGYVEVKQNHPYSDVFLMRVSRPQKAC
Protein: Pinin, isoform B (A8JQW3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD23870p
- Histone deacetylase complex subunit SAP18
- Serine/arginine repetitive matrix protein 1
- Acinus, isoform A
- Uncharacterized protein, isoform B
- Eukaryotic initiation factor 4A-III
- RH42690p
- Protein mago nashi
- FI21285p1
- Serine/threonine-protein kinase PRP4 homolog
Sequence:
MVNDSGLSTVDDLEQKLNSAKQSLVILNENIRRIAGRVPKESLQRSEKFKYTQDGKKNEHNGDRPFPRNATPGGVFKDKRRMYESKNPISRFPIEENEGRPPRINSRVIREMPTKKEIVEAQGTDSESRARNRRMFGSLLGTLQKFCQEESRLKSKEDKKAEIDRKVEKQELQERAMLRKQRETLFLDRKKKQFEIRRLEYKMARMKDFKVWEATMLNAKNNIRTKTKPHLFFRPKVHSPRTEKLLSKSKSEADVFIEFRREELEVELKNLENMNFGKMEDDTAIDESFYEEPDDEEQLDKSLLYVK
Protein: Polyadenylate-binding protein (PABP) (Q19579)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
- Prion-like-
- Eukaryotic initiation factor 4A
- Eukaryotic peptide chain release factor GTP-binding subunit
- Ataxin-2 homolog
- Polyadenylate-binding protein
- PAN2-PAN3 deadenylation complex subunit PAN3
- MIF4G domain-containing protein
- PolyA-specific ribonuclease subunit panl-2
- Nuclear cap-binding protein subunit 2
- Large ribosomal subunit protein uL23B
Sequence:
MAQVPPPMTQVVTSAPPPTAAATVVAGAVAGQPQAVIQQGPPPTNIGYPPNATYSMASLYIGDLHPDVSEAMLFEKFSMAGPVLSIRVCRDNTSRLSLGYAYVNFQQPADAERALDTMNFEVIHGRPMRIMWSQRDPAARRAGNGNIFIKNLDRVIDNKSVYDTFSLFGNILSCKVATDDEGNSKGYGFVHFETEHSAQTAIEKVNGMLLSDKKVYVGKFQPRAQRMKELGESGLKYTNVFVKNFGEHLDQEKLSAMFSKFGEITSAVVMTDAQGKPKGFGFVAFADQDAAGQAVEKLNDSILEGTDCKLSVCRAQKKSERSAELKRKYEALKQERVQRYQGVNLYVKNIEEDLNDDGLRDHFSSFGTITSAKVMVDENGRSKGFGFVCFEKPEEATAAVTDMNSKMIGAKPLYVALAQRKEDRRAQLASQYMQRLATLRMGQQASGVPAMTQLYQPGQQGYFVPNPMNAQGRPGFQPQSAQIRGPPGQRVFQNQMFMQYPFNQRQVYPQQQGRPPMRTNDGRPQYGMAPRPAGAPRVGGPGVQMGGAPIRQQGPAPRGAPQKPFYQGPPRQQQPQQHSQQPAQQPGQQGQGQSGIVIHGQETLTSHMLAQAAPQEQKQLLGERIYALIEKMFPNHKEAGKITGMMLEIDNAELIMMLQDAELFRSKVEEAFGVLTNAQSAAASTSAPTAKN
Protein: Transcriptional regulator NRG1 (Q5A0E5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcriptional repressor that binds NRG1 response elements (NRE) of target promoters. Involved in regulation of chlamydospore formation, hyphal growth, virulence, and stress response. Plays a key role in regulating true hyphal growth, but does not regulate pseudohyphal growth in the same fashion. Directs transcriptional repression of a subset of filament-specific genes such as HWP1, HYR1, ALS8, HWP1, or ECE1; via the TUP1 pathway. Functions with UME6 in a negative feedback loop to control the level and duration of filament-specific gene expression in response to inducing conditions. Plays a key role in biofilm formation and dispersion. Also plays the role of a negative regulator of virulence in mice models. Required for the expression of the cell wall genes RBR1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcriptional repressor TUP1
- Enhanced filamentous growth protein 1
- Transcription activator TEC1
- Hyphal wall protein 1
- Transcriptional regulatory protein UME6
- Repressor of filamentous growth 1
- Biofilm regulator 1
- Transcription factor CPH1
- pH-response transcription factor pacC/RIM101
- Agglutinin-like protein 1
Sequence:
MLYQQSYPITNKLLNASAAGSTSTASIIDGGCTLSKPGSGKTKSTTSLPSFNELLTSIPLPNEFKPSTKNTNQAAAATATSPYNYYMGPPAQHRLPTPPPYPMSSPTTATAATPLSQQSPHLQPQQTLQQPQPYHQQYYNYQYAAPPYPHPSQVPPPASYQQRHQQPMYQNTNGVPIIIRPSPGLITPTSTTFDHAKIRSNSTGDLSANSLALSSNNNTQSKDPRRKHVCKVCSRSFTTSGHLARHNRIHTGERKHQCPWPTCEARFARQDNCNQHYKTHTNGKNKRNRQQHRTLEASHVGTKYNTKSLV
Protein: Ferric oxidoreductase domain-containing protein (Q8BV64)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGPSPRLYTEALQEKKQSGFLAQKFKQYKRFVENYRRHIVCVTIFSAICIGLFADRAYYYGFASPPTDIEETTYVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYIPFDAAVDFHRWIAMAAVVLAVLHSAGHAVNVYIFSVSPLSLMACVFPNVFVNDGYDRSPPAPGPGHHVRLRLPPLPPPQFPGLLADPPPLCCALCPGEYLPWAGVNLGGDTWDGKGR
Protein: Threonine synthase (TS) (EC 4.2.3.1) (P00934)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction.
Interaction partners:
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Homoserine kinase
- L-threonine dehydratase catabolic TdcB
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- L-threonine dehydratase biosynthetic IlvA
- Phosphoserine aminotransferase
- Low specificity L-threonine aldolase
- L-threonine 3-dehydrogenase
- 3-isopropylmalate dehydratase small subunit
- Aspartate-semialdehyde dehydrogenase
Sequence:
MKLYNLKDHNEQVSFAQAVTQGLGKNQGLFFPHDLPEFSLTEIDEMLKLDFVTRSAKILSAFIGDEIPQEILEERVRAAFAFPAPVANVESDVGCLELFHGPTLAFKDFGGRFMAQMLTHIAGDKPVTILTATSGDTGAAVAHAFYGLPNVKVVILYPRGKISPLQEKLFCTLGGNIETVAIDGDFDACQALVKQAFDDEELKVALGLNSANSINISRLLAQICYYFEAVAQLPQETRNQLVVSVPSGNFGDLTAGLLAKSLGLPVKRFIAATNVNDTVPRFLHDGQWSPKATQATLSNAMDVSQPNNWPRVEELFRRKIWQLKELGYAAVDDETTQQTMRELKELGYTSEPHAAVAYRALRDQLNPGEYGLFLGTAHPAKFKESVEAILGETLDLPKELAERADLPLLSHNLPADFAALRKLMMNHQ
Protein: Uncharacterized protein C1A4.11c (O74342)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase dbp2
Sequence:
MPEKDWIGEFGPSKFKSPIDKLNQLLPESNDPSILYETSQHLLSEFDKTLNDSLRVLNQQINQVSEVLPRLPTMISALDRESKRLFESCEKMDPEPSALMPLQELEKIRSNIQLTISQIDNLTP
Protein: Amelogenin, X isoform (Leucine-rich amelogenin peptide) (LRAP) (P63278)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99217}.
Interaction partners:
- Ameloblastin
- Enamelin
- Kallikrein-4
- Amelotin
- Matrix metallopeptidase 20
- Somatotropin
- Chymotrypsin like elastase 3B
- Somatoliberin
- Chondroadherin
- Neuropeptide Y receptor type 2
Sequence:
MGTWILFACLLGAAFAMPLPPHPGSPGYINLSYEKSHSQAINTDRTALVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATDKTKREEVD