wanglab/gogpt-training-data huggingface dataset:
Protein: Histone acetyltransferase type B subunit 2 (Q59RH5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-14' of histone H4 which is required for telomeric silencing.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Histone H4
- Tetratricopeptide SHNi-TPR domain-containing protein
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Chromatin modification-related protein EAF3
- Origin recognition complex subunit 6
- Origin recognition complex subunit 3
- Transcriptional regulatory protein SDS3
- Cac2p
Sequence:
MSEQPTEPLSIKEEYQLWRKNCRYMYEFVSETALMWPSLTIQWLPNYTTTNGLIDAKLLLGTHTSNQSANQLKVASTQLSADPNVKANSKIKTVQKLENNAEICRARYMPQDANIVATINGLGEVDLYNLDTETRYSHFAPHTKNGYGLSWNPKQKGLLVTGADDNFVCVTDTTTNKTTFKSDIQKDIVNDVKWHQFNGNLFASVSEDSHVYLFDARDNKVVSQYYAESSNGINSLAFSPFAENLVAIGNTSSNINLLDLRKLGENSGLLHTMMGHSEGITCMEFSPHHDGILATGSQDRRIIIWDLFKVGEEQQQEDAEDGCPELFMMHAGHTAGVSDLSWCPFKDWMIGSVADDNIVHLWEISKKLITNEEAEVDVSILE
Protein: Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (Lymphocyte Peyer patch adhesion molecules subunit alpha) (LPAM subunit alpha) (VLA-4 subunit alpha) (CD antigen CD49d) (Q00651)
Organism: Mus musculus (Mouse)
Function: Integrins alpha-4/beta-1 (VLA-4 or LPAM-2) and alpha-4/beta-7 (LPAM-1) are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Integrin beta-1
- Fibronectin
- Vascular cell adhesion protein 1
- Integrin beta-7
- Paxillin
- Mucosal addressin cell adhesion molecule 1
- Intercellular adhesion molecule 1
- Tetraspanin-8
- Integrin beta-2
- Integrin beta-3
Sequence:
MFSTKSAWLRNGGADQGPRGIALREAVMLLLYFGVPTGPSYNLDPENALLYQGPSGTLFGYSVVLHSHGSKRWLIVGAPTASWLSNASVVNPGAIYRCGIRKNPNQTCEQLQSGSPSGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYMKSDNKLPTGICYVMPSDLRTELSKRMAPCYKDYTRKFGENFASCQAGISSFYTQDLIVMGAPGSSYWTGTVFVYNITTNQYKAFVDRQNQVKFGSYLGYSVGAGHFRSPHTTEVVGGAPQHEQIGKAYIFSIDENELNIVYEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGMGAVMVEMERVLVGSDKYAARFGESIANLGDIDNDGFEDIAIGAPQEDDLRGAVYIYNGRVDGISSTYSQRIEGQQISKSLRMFGQSISGQIDADNNGYVDVAVGAFQSDSAVLLRTRPVVIVEASLSHPESVNRTKFDCTENGLPSVCMHLTLCFSYKGKEVPGYIVLFYNVSLDVHRKAESPSRFYFFSNGTSDVITGSIRVSSSGEKCRTHQAFMRKDVRDILTPIHVEATYHLGHHVITKRNTEEFPPLQPILQQKKEKDVIRKMINFARFCAYENCSADLQVSAKVGFLKPYENKTYLAVGSMKTIMLNVSLFNAGDDAYETTLNVQLPTGLYFIKILDLEEKQINCEVTESSGIVKLACSLGYIYVDRLSRIDISFLLDVSSLSRAHEDLSISVHASCENEGELDQVRDNRVTLTIPLRYEVMLTVHGLVNPTSFVYGSSEENEPETCMAEKLNLTFHVINTGISMAPNVSVKIMVPNSFLPQDDKLFNVLDVQTTTGQCHFKHYGRECTFAQQKGIAGTLTDIVKFLSKTDKRLLYCMKADQHCLDFLCNFGKMESGKEASVHIQLEGRPSILEMDETSSLKFEIKATAFPEPHPKVIELNKDENVAHVFLEGLHHQRPKRHFTIIIITISLLLGLIVLLLISCVMWKAGFFKRQYKSILQEENRRDSWSYVNSKSNDD
Protein: 18w protein (Q24591)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MPATSSIITIIAVAACLLLLVADAHAQQQCNWQYGLTTMDIRCSVRALESGTGSPLDLQVAEAAGRLDLQCSQELLHASELAPGLFRQLQKLSELRIDACKLQRVPPNAFEGLMSLKRLTLESHNAVWGPGKTLELHGQSFQGLKELSELHLGDNNIRQLPEGVWCSMPSLQLLNLTQNRIRSAEFLGFSEKLCAGSALSNANGAVSGGSELQTLDVSFNELRSLPDAWGASRLRRLQTLSLQHNNISTLAPNALAGLSSLRVLNISYNHLVSLPSEAFAGNKELRELHLQGNDLYELPKGLLHRLEQLLVLDLSGNQLTSHHVDNSTFAGLIRLIVLNLSNNALTRIGSKTFKELYFLQILDMRNNSIGHIEEGAFLPLYNLHTLNLAENRLHTLDNRIFNGLYVLTKLTLNNNLVSIVESQAFRNCSDLKELDLSSNQLTEVPEAVQDLSMLKTLDLGENQISEFKNNTFRNLNQLTGLRLIDNRIGNITVGMFQDLPRLSVLNLAKNRIQSIERGAFDKNTEIEAIRLDKNFLTDINGIFATLASLLWLNLSENHLVWFDYAFIPSNLKWLDIHGNYIEALGNYYKLQEEIRVTTLDASHNRITEIGAMSVPNSIELLFINNNIIGQIQANTFVDKTRLARVDLYANVLSKISLNALRVAPVSAEKPVPEFYLGGNPFECDCSMEWLQRINNLTTRQHPHVVDLGNIECLMPHSRSAPLRPLASLSASDFVCKYESHCPPTCHCCEYEQCECEVICPGNCSCFHDATWATNIVDCGRQDLAALPNRIPQDVSDLYLDGNNMPELEVGHLTGRRNLRALYLNASNLMTLQNGSLAQLVNLRVLHLENNKLTALEGTEFRSLGLLRELYLHNNMLTHISNATFEPLVSLEVLRLDNNRLSSLPHLQYRHSLQGLTLGRNAWSCRCQQLRELAQFVSDNAMVVRDAHDIYCLDAGIKRELELIGNLANGPDCSDLLDASASNISSSQDLAGAIGCPCWPAVLVLIFLVVVLIIVFVFRESVRMWLFAHYGVRVCEPRFEDAGKLYDAIILHSEKDYEFVCRNIAAELEHGRPPFRLCIQQRDLPPQASHLQLVEGARASRKIILVLTRNLLATEWNRIEFRNAFHESLRGLAQKLVIIEETSVSAEAEDVAELSPYLKSVPSNRLLTCDRYFWEKLRYAIPIELSPRGNNYTLDHHERFKQPVSPGMIFRQAPPPPAYYCTEEMEANYSSATTATPSPRPTRPGGAARIVDSMPMPMRPPSEHIYHSIESEYSAYDQHEALSMIPTGLMHQHQQQQLRLHQQQQQQQQQRLLQPQFRAMPQQAIPAPSAPVHLRSGSGLSQASTSTQSTAQASTSAAAAQQQQQQQQQQQQQQAAGSEAANKNGQAFLV
Protein: Envelope glycoprotein H (gH) (P03231)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. The heterodimer gH/gL targets also host EPHA2 to promote viral entry.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04033}.
Interaction partners:
Sequence:
MQLLCVFCLVLLWEVGAASLSEVKLHLDIEGHASHYTIPWTELMAKVPGLSPEALWREANVTEDLASMLNRYKLIYKTSGTLGIALAEPVDIPAVSEGSMQVDASKVHPGVISGLNSPACMLSAPLEKQLFYYIGTMLPNTRPHSYVFYQLRCHLSYVALSINGDKFQYTGAMTSKFLMGTYKRVTEKGDEHVLSLVFGKTKDLPDLRGPFSYPSLTSAQSGDYSLVIVTTFVHYANFHNYFVPNLKDMFSRAVTMTAASYARYVLQKLVLLEMKGGCREPELDTETLTTMFEVSVAFFKVGHAVGETGNGCVDLRWLAKSFFELTVLKDIIGICYGATVKGMQSYGLERLAAMLMATVKMEELGHLTTEKQEYALRLATVGYPKAGVYSGLIGGATSVLLSAYNRHPLFQPLHTVMRETLFIGSHVVLRELRLNVTTQGPNLALYQLLSTALCSALEIGEVLRGLALGTESGLFSPCYLSLRFDLTRDKLLSMAPQEATLDQAAVSNAVDGFLGRLSLEREDRDAWHLPAYKCVDRLDKVLMIIPLINVTFIISSDREVRGSALYEASTTYLSSSLFLSPVIMNKCSQGAVAGEPRQIPKIQNFTRTQKSCIFCGFALLSYDEKEGLETTTYITSQEVQNSILSSNYFDFDNLHVHYLLLTTNGTVMEIAGLYEERAHVVLAIILYFIAFALGIFLVHKIVMFFL
Protein: DNA polymerase theta (EC 2.7.7.7) (A0FLQ6)
Organism: Caenorhabditis elegans
Function: DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions. Required to prevent extensive loss of sequences near G-quadruplex (G4) DNA sites, which are prone to cause genome alterations, by generating deletions.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O18475}.
Interaction partners:
- DNA ligase IV
- DNA polymerase eta
- DNA polymerase kappa
- DNA polymerase
- Exonuclease 1
- ATP-dependent DNA helicase II subunit 2
- FANCD2
- Breast cancer type 1 susceptibility protein homolog
- Helicase ATP-binding domain-containing protein
- DNA repair endonuclease XPF
Sequence:
MDEASCRFPEWVSSKIIDYYAEQNIKALFDWQIDVLNEARQFEDQHLIFSAPTSAGKSIVAELLSWKVASTGRKVLFVLPYISVAREKLHQIQRCWRRDDISVCGFIGPQASNPNEWLGAVCTIEKAASLTNRALSEDWFEEIGMIVVDEMHMVFDSSRGAHIEHMLSKVLLWNQSALEKVRIIGMSATIPELYRIGKWLDGAKVFEARFRPIVLQNHIVIGSELRKSGDNKVLREFSEDPLILLTEESFRRNSQTLVMISSKLDAEKTALNIASRFHEINKTDSSLLEILKERANGLLFIKHGLERNGCKDRNVMSTLAWGVAYHHAGLTMEERECIELGFREKNIVILVATSTLASGVNLPAERVLIKAQPRGPSALTSLNYRQMVGRAGRTGHATRGETYLLIKKCDRDAVLKIIETPIDQGVLTRKRDAERTNLSRFILEGICTGLTTTRSQIHDLCKLLLFNSENLQLSDIAIEMLLRNSFISQDENDDQLSPTQLGRAAIASSLPPEASLAIFEDLNSASRAIALDTELHMLYLVTPINVSVWQECDWHHLFSIFSKLPSDHKRIAKLVGVSEKFILDQLQGRRNDKLLQIHIRFFSALALFDLISEMSIYEVSHKYRIPRGCLQTLQSQSATYAAMIVAFCLRLGWTYLKALLDGFATRLLFGVRSELSELVAIEGIDGQRARILHERGVTCLSHLSACDSSKLAHFLTLAVPYSSSNSNDGLGEWLFGEPRMRVDVAARTLKERARKVLIRRVQELGISVELPKFEENEENIQESCDSGLPDSCEGMEDELEEKENIVKMEEMTKSVTEMSLTDNTISFKSEDDLFKKEIKVEEDEVFIKKEIDEDEEEIVEETVIECLETSLLKLKASTDEVFLRRLSQTFSPIGRSRSILNNSLLEDSFDRPVPRSSIPILNFITPKRESPTPYFEDSFDRPIPGSLPISSSRRKSVLTNIANLDSSRRESINSNASDNNSFDVFVTPPTKSAKEEKRRIAVKHPRVGNIIYSPLTSSPVIKHPKLEINHFYLKDVCHDHNAWNLWTKSSTSTSSCSIRVSDDYTGIAIRTDAGNTFIPLLETFGGEPSPASKYFESFSKCIIPLNTRLEFLKTLAVTVEMYISSMEDAFLIFEKFGIKIFRLKVVRIAAYLNNVIDVEQEENSNFLPILMDRYSILDPEIRKTCSSSLHKAAVEVYSLKPIFEKMCCSGASLQLEMESCQTVLNIFYSGIVFDQALCNSFIYKIRKQIENLEENIWRLAYGKFNIHSSNEVANVLFYRLGLIYPETSGCKPKLRHLPTNKLILEQMNTQHPIVGKILEYRQIQHTLTQCLMPLAKFIGRIHCWFEMCTSTGRILTSVPNLQNVPKRISSDGMSARQLFIANSENLLIGADYKQLELRVLAHLSNDSNLVNLITSDRDLFEELSIQWNFPRDAVKQLCYGLIYGMGAKSLSELTRMSIEDAEKMLKAFFAMFPGVRSYINETKEKVCKEEPISTIIGRRTIIKASGIGEERARIERVAVNYTIQGSASEIFKTAIVDIESKIKEFGAQIVLTIHDEVLVECPEIHVAAASESIENCMQNALSHLLRVPMRVSMKTGRSWADLK
Protein: Abasic site processing protein YedK (EC 4.-.-.-) (Peptidase YedK) (EC 3.4.-.-) (P76318)
Organism: Escherichia coli (strain K12)
Function: Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue. May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Interaction partners:
- Uncharacterized N-acetyltransferase YedL
- Putative sulfur carrier protein YedF
Sequence:
MCGRFAQSQTREDYLALLAEDIERDIPYDPEPIGRYNVAPGTKVLLLSERDEHLHLDPVFWGYAPGWWDKPPLINARVETAATSRMFKPLWQHGRAICFADGWFEWKKEGDKKQPFFIYRADGQPIFMAAIGSTPFERGDEAEGFLIVTAAADQGLVDIHDRRPLVLSPEAAREWMRQEISGKEASEIAASGCVPANQFSWHPVSRAVGNVKNQGAELIQPV
Protein: Bonus (Q9U3Y7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDLEQLKNDFLPLIAGIKQEQLDAVPTDALPQMSTPNTASGAPTTSSLSSSSLSLSNPCDSAEKRSESNSSASAKFTLFKCVYCAQLLGSNDRPKLLECLHVACAQCVSTKFSELDRSLPPLIHCPVCDNASQQEFIVDNQFLIEQCTAGDSGDGVGLLGLTGEGQKSSAAASIQCSSCSDGAVATSWCVDCSEYICDSCVQAHQRLKITKDHTIKPKDEANNEQLAGAAGVDKLHMCQLHPQEKLSLFCETCDKLTCRDCQLSDHRDHKYKFAHEIATESRQALSTLVSEINYKRFLLSSATKVIDDRQQLIHDKKKDLIKEITAMAVKITNTVNTRGKQLIMRLNEVCDSKLKVLVEKKETLQLLSDNTDHCIDFMQNALEKGSDFAILSSKKSLVRHLQKLKCQRADIPNPEIPVRIQVQLNQVSDLQKVISQLGIIIVDGKPYPPTPSPNGTPQPQHPPRQPPSPNMAPPLRPGLPPGMPAGLSPNGPPVNFGPQNGPPLYSNAAQQQFNNLSMSRSFPGDGSGKVRFGGMPPVGMQRHGQPHVSSSTHPQNMDISLRGLLNNQAAQSPNAHMAFNGPPSYPGGPQGAPAPAHQPMGPQMRPHFMPGQQGFSQGGGPGGGPRDANFMNSNARFQSQYQRMANHAQQAAAAAAMAGAAGGGGGQIPSPGALQRPQMMSNPMQNVSAMQNSLGFHGSQAGFNTGPPQTSPQLGGGGMHSLAKWHIPQSAQQSNMCSQQGPLLPFANGRQTSENFKISLKSPNTLKNSTPPSLGGGGAGHQGHGNGSSSAQLNAAALGLGPAVSILSNVTSTIPKTPSPSTHENTKDFTEPIDKVRDDSINDLIATIAKLDSNGVQVLPEGRTKTTSPQVHSSTDLSNTQEVNNKNEQKDDPNEDWCAVCLDGGELMCCDKCPKVFHQNCHIPAISSLPDESESWQCLLCVNIKELTKTEGSEKSSSGELSALELRILQRICLELYCQYEQSLNFREPESPANTSYYEIVSSPMSLDVIRTRLDPSSPNHYKDIAGFVSDVRLIFSNTYLFYQEDTKTYSNAKYLENFFEEQLAKWLPQFEGTKPQGKRNTSNSPALLGVNATGSPSPIENGRKSCGSASLGDSDGACLPAKRARRSAHE
Protein: Aldehyde reductase YahK (EC 1.1.1.2) (Zinc-dependent alcohol dehydrogenase YahK) (P75691)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined.
Interaction partners:
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Probable alcohol dehydrogenase EutG
- Probable alcohol dehydrogenase
- Alcohol dehydrogenase, propanol-preferring
- Aldehyde reductase Ahr
- Aldehyde dehydrogenase B
- S-
- Glycerol dehydrogenase
- Glycerol kinase
- NADPH-dependent aldehyde reductase YqhD
Sequence:
MKIKAVGAYSAKQPLEPMDITRREPGPNDVKIEIAYCGVCHSDLHQVRSEWAGTVYPCVPGHEIVGRVVAVGDQVEKYAPGDLVGVGCIVDSCKHCEECEDGLENYCDHMTGTYNSPTPDEPGHTLGGYSQQIVVHERYVLRIRHPQEQLAAVAPLLCAGITTYSPLRHWQAGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSEAKREAAKALGADEVVNSRNADEMAAHLKSFDFILNTVAAPHNLDDFTTLLKRDGTMTLVGAPATPHKSPEVFNLIMKRRAIAGSMIGGIPETQEMLDFCAEHGIVADIEMIRADQINEAYERMLRGDVKYRFVIDNRTLTD
Protein: DnaJ homolog subfamily B member 1 (Q17438)
Organism: Caenorhabditis elegans
Function: Acts as a co-chaperone with Hsp70 required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). Acts by determining Hsp70's ATPase and polypeptide-binding activities (By similarity). Can also act as a chaperone that promotes maturation of potassium channel unc-103 by stabilizing nascent channel subunits and assembling them into tetramers.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Heat shock protein hsp-1
- Heat shock protein 70
- Heat shock 70 kDa protein C
- Mitochondrial-processing peptidase subunit beta
- Heat shock protein 110
- Heat shock 70 kDa protein 13
- Endoplasmic reticulum chaperone BiP homolog
- Signal peptidase complex catalytic subunit SEC11
- DnaJ homolog dnj-2
- Heat shock protein 70
Sequence:
MTADANKSESLLCMDKAREAIKSGDTDKARRMLLKAKKLDPGQNIEFLTKKIDDMTNNTSSSSQTSSSRASEERSYAHDDHYDDPNLRNRKARSPVKKNGKTEPEPKQRSASRTPKLGVDYTSEQKELVERIRHCKDYYEILKIDKKASDDDIRKEYRKLALKLHPDKCRAPHATEAFKALGNAYAVLSDTDKRRQYDQYGAEAANSHTPTTRRRGGGHGAFFEHDYAHGFEAEFTPEEIFNMFFGGGFPTEQVRRRARYAQQQQYHHYEQQQSPYGPLLQLLPLIAIMVIGLLAQLMVGEPAYSLHQTSKFTIKRLTADLRVPYFVRTDFETSYRGRIRQVEQQVEDDYIQNLRMNCYKEQNLKETKLYRARWMRDEAMMRDAERTPLPSCIRLNEIYSH
Protein: Cationic amino acid transporter 6, chloroplastic (Q9LZ20)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Permease involved in the transport of the cationic neutral or acidic amino acids.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Amino acid permease 5
- Amino acid permease 8
- Amino acid permease 1
- Amino acid transporter ANT1
- Lysine histidine transporter 1
- WAT1-related protein At2g39510
- Uncharacterized protein At4g36500
- WAT1-related protein At5g45370
- Amino acid permease 2
- Putative pectinesterase 63
Sequence:
MEVQSSSNNGGHSSFSSLRVYLNSLSATPSRLSRRAISVSTSSDEMSRVRAVSGEQMRRTLRWYDLIGLGIGGMVGAGVFVTTGRASRLDAGPSIVVSYAIAGLCALLSAFCYTEFAVHLPVAGGAFSYIRITFGEFPAFFTGANLVMDYVMSNAAVSRSFTAYLGTAFGISTSKWRFVVSGLPKGFNEIDPVAVLVVLVITVIICCSTRESSKVNMIMTAFHIAFIFFVIVMGFIKGDSKNLSSPANPEHPSGFFPFGAAGVFNGAAMVYLSYIGYDAVSTMAEEVENPVKDIPVGVSGSVAIVTVLYCLMAVSMSMLLPYDLIDPEAPFSAAFRGSNGWEWVTKVVGIGASFGILTSLLVAMLGQARYMCVIGRSRVVPFWFAKIHPKTSTPVNASTFLGIFTAALALFTDLNVLLNLVSIGTLFVFYMVANALIFRRYVPVGPTKPWPTLCFLTLFSITSLVFTLIWKLVPEGKPKAFMLGASAVVAIAIVLSFQCVVPQARKPELWGVPFMPWTPCVSIFLNIFLLGSLDAPSYVRFGFFSGLIVLVYLFYGVHASSDAEANGSFGVKDGQVMKELIEV
Protein: Suppressor of variegation 2-10, isoform L (A0A0B4JD33)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKTRSQTARTQAENAATSSSPGHQSTSSAPIAVNPFDSTKYKECEQMVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSEDNDENCMAKAKEDSVIDLLDSP
Protein: 60Kd inner membrane protein (Q38DZ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Pretranslocation protein, alpha subunit, putative
- Small ribosomal subunit protein uS5
Sequence:
MRKLVRSSTVQRAMPVFCTPILTSRCTVSSNERVTYFDYLDRIWNCHWFGVSDVGIAPSQEPAFITNMFVSFQEGLNLGAPEAILLLGVLCRVATLGFSLYGERASERMRKAICKLKTPHEAYQRVYHSEGATSLDIQLAATALKGERRRVFAEEKTSNAQCLSSILGSPIVLFGMFQAKSLCENPYLEFGTSPFLWCTSLTMPDPYGILPLAFCGLTLANFELSISKELKTGWMSNVVWGARLGCLCVLPVALQFRSGVCLYFLGMGLVGLLQPILLRSNKFRSFFNFPTEGKADTNKFSYTDDGFYTRMSVQFPYVSHLFDSVEEENISRPPQPPVAPVWFGGAQSAMGYGKKRISSPASVASEKRVSFGKGLNFAAPGWKAHRAEFREEDLIPDNSCFGDKSCKSGKDGALKDTGGTRVRS
Protein: IQ motif containing GTPase activating protein 3 (A2RRC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERRAAGPGWAAYERLTAEEMDEQRRQNVAYQYLCRLEEAKRWMEACLKEELPSPVELEESLRNGVLLAKLGHCFAPSVVPLKKIYDVEQLRYQATGLHFRHTDNINFWLSAIAHIGLPSTFFPETTDIYDKKNMPRVVYCIHALSLFLFRLGLAPQIHDLYGKVKFTAEELSNMASELAKYGLQLPAFSKIGGILANELSVDEAAVHAAVLAINEAVERGVVEDTLAALQNPSALLENLREPLAAVYQEMLAQAKMEKAANARNHDDRESQDIYDHYLTQAEIQGNINHVNAHGALEVVDDALERQSPEALLKALQDPALALRGVRRDFADWYLEQLNSDREQKAQELGLVELLEKEEVQAGVAAANTKGDQEQAMLHAVQRINKAIRRGVAADTVKELMCPEAQLPPVYPVASSMYQLELAVLQQQQGELGQEELFVAVEMLSAVVLINRALEARDASGFWSSLVNPATGLAEVEGENAQRYFDALLKLRQERGMGEDFLSWNDLQATVSQVNAQTQEETDRVLAVSLINEALDKGSPEKTLSALLLPAAGLDDVSLPVAPRYHLLLVAAKRQKAQVTGDPGAVLWLEEIRQGVVRANQDTNTAQRMALGVAAINQAIKEGKAAQTERVLRNPAVALRGVVPDCANGYQRALESAMAKKQCPADTAFWVQHDMKDGTAYYFHLQTFQGIWEQPPGCPLNTSHLTREEIQSAVTKVTAAYDRQQLWKANVGFVIQLQARLRGFLVRQKFAEHSHFLRTWLPAVIKIQAHWRGYRQRKIYLEWLQYFKANLDAIIKIQAWARMWAARRQYLRRLHYFQKNVNSIVKIQAFFRARKAQDDYRILVHAPHPPLSVVRRFAHLLNQSQQDFLAEAELLKLQEEVVRKIRSNQQLEQDLNIMDIKIGLLVKNRITLQEVVSHCKKLTKRNKEQLSDMMVLDKQKGLKSLSKEKRQKLEAYQHLFYLLQTQPIYLAKLIFQMPQNKTTKFMEAVIFSLYNYASSRREAYLLLQLFKTALQEEIKSKVEQPQDVVTGNPTVVRLVVRFYRNGRGQSALQEILGKVIQDVLEDKVLSVHTDPVHLYKNWINQTEAQTGQRSHLPYDVTPEQALSHPEVQRRLDIALRNLLAMTDKFLLAITSSVDQIPYGMRYVAKVLKATLAEKFPDATDSEVYKVVGNLLYYRFLNPAVVAPDAFDIVAMAAGGALAAPQRHALGAVAQLLQHAAAGKAFSGQSQHLRVLNDYLEETHLKFRKFIHRACQVPEPEERFAVDEYSDMVAVAKPMVYITVGELVNTHRLLLEHQDCIAPDHQDPLHELLEDLGELPTIPDLIGESIAADGHTDLSKLEVSLTLTNKFEGLEADADDSNTRSLLLSTKQLLADIIQFHPGDTLKEILSLSASREQEAAHKQLMSRRQACTAQTPEPLRRHRSLTAHSLLPLAEKQRRVLRNLRRLEALGLVSARNGYQGLVDELAKDIRNQHRHRHRRKAELVKLQATLQGLSTKTTFYEEQGDYYSQYIRACLDHLAPDSKSSGKGKKQPSLHYTAAQLLEKGVLVEIEDLPASHFRNVIFDITPGDEAGKFEVNAKFLGVDMERFQLHYQDLLQLQYEGVAVMKLFNKAKVNVNLLIFLLNKKFLRK
Protein: Polynucleotide kinase (PNK) (EC 2.7.1.78) (Deoxynucleotide 3'-phosphatase) (EC 3.1.3.34) (Polynucleotide 5'-hydroxyl-kinase) (P06855)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Acts as a 5'-hydroxyl kinase, a 3'-phosphatase and a 2',3'-cyclic phosphodiesterase. Catalyzes the transfer of the terminal phosphate of ATP to the 5'-hydroxyl termini of ribo- and deoxyribonucleotides. In the presence of ADP the enzyme also catalyzes an exchange reaction. In the exchange reaction, an excess ADP causes the enzyme to transfer the 5' terminal phosphate from phosphorylated DNA to ADP. Involved in countering a host defense mechanism which activates T4-induced anticodon nuclease and shuts off viral translation. The polynucleotide kinase modifies the ends of nicked tRNA generated by the antiviral response of the host bacteria and facilitates repair by T4 RNA ligase.
Interaction partners:
Sequence:
MKKIILTIGCPGSGKSTWAREFIAKNPGFYNINRDDYRQSIMAHEERDEYKYTKKKEGIVTGMQFDTAKSILYGGDSVKGVIISDTNLNPERRLAWETFAKEYGWKVEHKVFDVPWTELVKRNSKRGTKAVPIDVLRSMYKSMREYLGLPVYNGTPGKPKAVIFDVDGTLAKMNGRGPYDLEKCDTDVINPMVVELSKMYALMGYQIVVVSGRESGTKEDPTKYYRMTRKWVEDIAGVPLVMQCQREQGDTRKDDVVKEEIFWKHIAPHFDVKLAIDDRTQVVEMWRRIGVECWQVASGDF
Protein: Early E1A protein (Early E1A 32 kDa protein) (P03254)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interacts with host TBP protein; this interaction probably disrupts the TBP-TATA complex. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03255}.
Interaction partners:
Sequence:
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP
Protein: Protein SHORT INTERNODES 1 (OsSHI1) (Q652K4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Regulates tillering and panicle branching by modulating SPL14/IPA1 transcriptional activity on the downstream TB1 and DEP1 target genes. Binds directly to the 5'-T/GCTCTAC-3' DNA motif found in the promoter regions of both TB1 and DEP1. Represses the DNA binding activity of SPL14/IPA1 toward the promoters of both TB1 and DEP1. Exhibits weak transcriptional activation activity in yeast cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:30914468}.
Interaction partners:
Sequence:
MAGFPLGGGSHSRDNPAPPVPPVHPADAASFLYATRGGSFQLWQQQEQQPFYASNIIRFADDAPPAPSLAGASSSSSSRGMRSSGGGGGGGGGGISCQDCGNQAKKDCTHMRCRTCCKSRGFACATHVKSTWVPAAKRRERQQQLAALAASAAATAGGAGPSRDPTKRPRARPSATTPTTSSGDQQMVTVAERFPREVSSEAVFRCVRLGPVDQAEAEVAYQTAVSIGGHVFKGILHDVGPEALAVAGGGGASEYHFRLTGDGSSPSTAAAGEAGSGGGGNIIVSSAVVMDPYPTPGPYGAFPAGTPFFHGHPRP