wanglab/gogpt-training-data huggingface dataset:
Protein: Non-structural maintenance of chromosome element 4 (Non-SMC element 4) (DNA repair protein rad62) (Q6BDR8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15485909}.
Interaction partners:
- Non-structural maintenance of chromosomes element 1
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- E3 SUMO-protein ligase nse2
- Non-structural maintenance of chromosome element 3
- Non-structural maintenance of chromosome element 5
- Non-structural maintenance of chromosome element 6
- Structural maintenance of chromosomes protein 3
- BRCT-containing protein 1
- Nucleolar protein dnt1
Sequence:
MSSIDKRDLRKRYRNLINKVQESRLELVDEENNNLYETITTANDLFSSVDAPTEATLDALLLTKTVDLASIKARQLHIGRPKFNIELFTKNIKQFLNYPTSHSNVTRIQEIDTAWSRLGKLASNCEKQPASLNLMVGPLSFRKKERNIQRRERLQKAPNVLTQPTMLNERNITTQENNTTKNVLHISRLLQAHQPVNFLKFITNPQSYPQTVENLFYVSFLFKEGKAALVENESGILMLETRIPPTDDQVVAGEIRNIQLVLDMTMDLYENIIKEYNIKESIIPTRAPVETSTNSNTWYG
Protein: Tsc2p (A0A1D8PMB6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- GTPase
- Uncharacterized protein
- GTP-binding protein
- Heat shock protein 90 homolog
- Flavin reductase like domain-containing protein
- Serine/threonine-protein kinase TOR
- Ubiquitin-binding TORC1 subunit
- 14-3-3 protein homolog
- GTP-binding protein
- Target of rapamycin complex subunit LST8
Sequence:
MSTYHPSFGSSGGGIGSVFKSITKSFKQSSSTKRVPVTINPTVVGGGQDLQNLIDQLQTSSSSSVKLQAIKKLIESIQNYSISSVPEIWYVARNNCDIKIIKHSRDLRRATLELLNACIEKDDLTSVGTRIRYFNDIFKNCMFQDNNNNNKFDPDFDLFLKALLVLTGEGRDIHDFIIYEDRNNLYIFLENCLTAAVELSALYKFQTDTKDIEIKENDKKFANIYGVIEFTRNCIKFNYTVFSEGMMIWIINKIIETKSDNKLILLAIIDIINSLSIYGQAPKQCIPQMIKFLATIYGSSLDNSLSLSVWNCVKNLCHDHNYRDIINSLCDNIHSSDINLYKIDVVEGIKPVYACTGSIKLIRNFQVQSGLSRNENIFEISQVQILNSFKMALNFGINIINSVFLDCIDRLLAKDSYLDNFGVSFNDSIDKIFPFQLWYSSSNSMYDIFNLLKVETEQDKSCFQSICISLQSLYESQELFTPKDKLINFFTNYIEYLPLNTVIFVLQYYSDSKMCSLLNPFWRENSMKLLNHFYLPSDIDVTVKMRCIQVILDAYNTSVAIFNDNDIKYEIILEIAKRSLRETNEELLRYLINNLFGVVFLKCPNPVFIQLMTVFLPLFQPQIPPPPKSSHSVFEGSITSSFVTSTRVSGTVQEHGSIEFTEAITKLLCTTFIKATPERAQECYNFLIQIANLSKHNCNILLIIAKCLVRIRTTTENYIYFTQPSDMAGLALAFRRDNSTTCSGNTNVSWVYPETVDYLPEELFDSPNRSLLLSRVDNGNVDDLGSDKYYIDIQKWLQLVLFIMDQYIDWEIYSYVWAHFVSQLSNTQLFYDCDLEINELRKIICYQLTLNLPTNIKLPHKTTPTTTTTTTTAATTNVNIEVTKADLQVVFVRSLSSLTGYFNKFTKPDQDQIVNSLIFGLGSWDKTAVPCINILTVCCYEIPLSIKKYLNSILTKLQTRITSANAAAHSLEFLISLSQLPNLTTNFTIEDFKQGFGIAFKYIQYAIDLEKRSHQQQQQQQQGHSQSAQIIQQHGVDADVEETPSTQQQTITPILSEYILMLSYHIIASWFVTLRMSDRVELQQFIIKNLKLCSEINENLQDQTIGFLDFIKKFTSSDLPLEMRLPGNNNNKRSSSSTTTTNTSICNRWMVDNLVVSIETEPFSGDTELIIRKPTGISKFNITLDHPSSLNNTSPMVLPNYFLSQLVESNTDPILIPDDVNTNRAISVLDRIPSVEFHKIGIIYIGKNQITENEVLNNKIGSIDYQKFLSNIGDLIKLQGCKRIYTGGLDTENNIDGEFTRYWRGKYIQIIFHVATMMNNNEQILGENQNDELSDMDIQRMIDLKKRHIGNNHVNIFFDESGHEFNFNLIKSQFNFLSIVITPHTYFQDYYNNNLPVSSTEDKKQQLSEKYFKVKMYRRGGVPSFCGISHFKLISEKELPVFIRSTSLLASIFANVWHGSKNVWSQRVKQLKLISSYTLPQSNSTTAGAV
Protein: Uncharacterized protein (A8J3B6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Dynein light chain roadblock
- Dynein-1, subspecies f
- Dynein-1, subspecies f
- Axonemal inner arm dynein I1/f subunit
- AAA+ ATPase domain-containing protein
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein axonemal intermediate chain 4
- Uncharacterized protein
- Uncharacterized protein
- Inner arm dynein light chain
Sequence:
MEDASAGPPPVDDGEVPAAPADSSPLDDAPASSGAEPGDGGYDEGEPLDNEQAGPADVEGLDDAGEPGAAPEDGEEGTGGEGEAGAGAEAPGDGESPEAAAEAEAAAAAPPPPVELEPLPEDYVPVRDLPPIPEPFARNEEGKPVPLDGVESLFLTGTTIELVGLKELGAANVMGEVSRDELLKDIQFRGAISDFHAYKAKIQAADYEPLLVRFNEDDVYGDGNNFELAVTAAAAAVWRGIGEEVARRAALLELEAAHAAAEKAKPRSKRVRKVKPWQSMGSEVDIEEASVRPRRDPIRLVVQRRRREFNQPNAKLADKDAHELWNSSQMECRPFKDPNFDMRRMEQDVAVQAVAPLRDAATQSTGTVPPRPAVTQTEPLDLPPEAKQDLVRRPRNAPGSVADFLERVRDQCEVALVQNEITNIFRDDLSSLNDEADGGGGGSRKETLVSEAQSFTHLTYSKNKVVSAIQWLPHRKGVVAVACTEAQSHAERVARMGRTAPAHILLWNFRDPIHPELVLQSPWEVFSFQFNPLQPDLLTGGCYNGQVVLWDLSSEADRLSRRAGGGAGAGAAKSSDGAAAGAGGKGADSTPPSTALPGGGGGGGGVDSTSGSSADGDAHIPVIKHRFMTDTQFSHHQVVTDLQWLPGVEISHRGKVTKLGEGSKECNFFATIAADGKVLFWDVRVEKLLKKGKKADELLDLVWKPIHSVHLISLIGMDLGGTKLAFDFRKLEQGMFYAGSFDGELVYADFVKPEGEENPDYAKSCLQAHVGPVIALERSPFFDDIVLTCGDWQWQIWQEGQSTPLFQSGYAQDYYTAACWSPTRPAVLYLADQSGSLEVWDLLDRSHEPSIRVTLAATPIMSLSFNPMPTSASAAQQAAQQLLAVGDATGVLRIMELPRNLRRPVHNEKKLMGTWLERQQARLADVGARQPVRTSARKEAEERKKEAESAALAEAAAKEAAAKDAAAAAAAGMPLPTANERKKDKGPPPPEFDEKAEQEYLKLEARFKAQLGLMPAEANGGPGH
Protein: Urocortin-2 (Stresscopin-related peptide) (Urocortin II) (Ucn II) (Urocortin-related peptide) (Q96RP3)
Organism: Homo sapiens (Human)
Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress.
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 2
- Urocortin-3
- Corticotropin-releasing factor receptor 1
- Urocortin
- Corticoliberin
- Corticotropin-releasing factor-binding protein
- Pro-opiomelanocortin
Sequence:
MTRCALLLLMVLMLGRVLVVPVTPIPTFQLRPQNSPQTTPRPAASESPSAAPTWPWAAQSHCSPTRHPGSRIVLSLDVPIGLLQILLEQARARAAREQATTNARILARVGHC
Protein: Alanine--glyoxylate aminotransferase (EC 2.6.1.44) (Q94055)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein R102.4
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Bifunctional glyoxylate cycle protein
- Phosphoserine phosphatase
- Aminomethyltransferase
- FMN hydroxy acid dehydrogenase domain-containing protein
- Glycine cleavage system P protein
- Glycine cleavage system H protein
- Putative sarcosine oxidase
Sequence:
MISTRFLRPSVSIFGFGIKSSMSSRAPPKALLQDMVVPPRQLFGPGPSNMADSIAETQSRNLLGHLHPEFVQIMADVRLGLQYVFKTDNKYTFAVSGTGHSGMECAMVNLLEPGDKFLVVEIGLWGQRAADLANRMGIEVKKITAPQGQAVPVEDIRKAIADYKPNLVFVCQGDSSTGVAQPLETIGDACREHGALFLVDTVASLGGTPFAADDLKVDCVYSATQKVLNAPPGLAPISFSDRAMEKIRNRKQRVASFYFDAIELGNYWGCDGELKRYHHTAPISTVYALRAALSAIAKEGIDESIQRHKDNAQVLYATLKKHGLEPFVVDEKLRLPCLTTVKVPEGVDWKDVAGKMMTNGTEIAGGLGATVGKIWRIGTFGINSNSTKIENVVELLSKSIGEKSK
Protein: Mcl-1a (Induced myeloid leukemia cell differentiation protein Mcl-1a) (Q9I9N3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALSLDFRRTATMSFFAQGVQTPTLKTCVEDELDGYTEEEEAPLKRLRPGTNGLKGLQLDGRFVSATDGSLPTTPDPEELDYAELERDTRQLLLDFYRTHTGMCPVDRKLHHAIPTMKRVVDNILVKHQIAYKGMIQRLQLDSQPASLDFIRCIASTMFKDGVTNWGRIASLVAFGAVVCSRLKELQQDQCVERVAEQISSYLTSEQQDWILKNKSWHGFVEFFHQEDVESVVRHGLLALVGCAGIGAGLAFLIR
Protein: Tumor necrosis factor receptor type 1-associated DEATH domain protein (TNFR1-associated DEATH domain protein) (TNFRSF1A-associated via death domain) (Q15628)
Organism: Homo sapiens (Human)
Function: Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B. The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3U0V2}. Cytoplasm {ECO:0000269|PubMed:11684708}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11684708}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q3U0V2}.
Interaction partners:
- TNF receptor-associated factor 5
- Receptor-interacting serine/threonine-protein kinase 3
- Baculoviral IAP repeat-containing protein 2
- Caspase-8
- TNF receptor-associated factor 1
- TNF receptor-associated factor 2
- TNF receptor-associated factor 3
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor
- CASP8 and FADD-like apoptosis regulator
Sequence:
MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQMLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRAGAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGARGGDGEVASAPLQPPVPSLSEVKPPPPPPPAQTFLFQGQPVVNRPLSLKDQQTFARSVGLKWRKVGRSLQRGCRALRDPALDSLAYEYEREGLYEQAFQLLRRFVQAEGRRATLQRLVEALEENELTSLAEDLLGLTDPNGGLA
Protein: V-type proton ATPase subunit c (V-ATPase subunit c) (V-type proton ATPase 16 kDa proteolipid subunit) (V-ATPase 16 kDa proteolipid subunit) (Vacuolar proton pump c subunit) (P50515)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P25515}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d
- V-type proton ATPase subunit a
- V-type proton ATPase subunit H
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit D
- V-type proton ATPase subunit G
- V-type proton ATPase subunit C
Sequence:
MSTDLCPVYAPFFGVMGCTAAIVFASFGAAYGTAKAGVGISAMGVLRPDLIVKNTIPVVMAGIIAIYGLVVSVLISGNLKQILSLYSGFIQLGAGLSVGLAGLAAGFAIGIVGDAGVRGTAQQPRLFVAMILILIFAEVLGLYGLIVALLLNTRATDNVTC
Protein: C2H2-type domain-containing protein (B2MZC6)
Organism: Caenorhabditis elegans
Interaction partners:
- Sun domain-containing protein 1
- Zygote defective protein 12
- HORMA domain-containing protein
- HORMA domain-containing protein
- Serine/threonine-protein kinase chk-2
- HORMA domain-containing protein
- Meiotic recombination protein spo-11
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- DNA repair protein RAD51 homolog
- Coiled-coil domain-containing protein
Sequence:
MTCDDWNSYIQVNIYGKTIEGLQQQGVVLESLLNNVGCSKVWIMEGSVCTNPRPESSTHSEESTIEPVVPLSTTLATNKLPRFSTPAIGHSNNNSSKNFTLNLAEKLSEILSDDDKTDEFLENSHQSETSKDDVIKDLLEEMVQTVANSNKPPILLSTTLANVGVPRFSTPIKPQHALNRDFTMNMTEMISEIDSNYEGYELFDDSSNDCTTLTPNCQEVESSFYRALSEAASSIVPYQEGKRRSSRRLSTLSSLKETVKVEPAVSKLTKRRRLTPVECSSETMIPHSQPIPLDTCSDQPIFPNSTHNAIQSDGFSYEQPICEFGDSQLFLSAKSLCTEPNSSIAEDVKPVLTVSDSDITASNRNNIDDHNRVIELSTEHKTMGEFQYNFDDEDTVLIGNYEEVGTEIDEADEQHNEENSEDDEEDESPIPSKKRVSFAVPLVQSRSKQKDEMNKVHIIKCHFDKCNKSYNWRKKYGKLRLVDHAFTHVPHLKMKCNFCDYMCKGIRNIRLHHKKSHPDEQLTGFGIKSVVRTSKKGKDLAKVWDECFKKNRVLQHGSGTDSNLLHFSRQDKGSKRSQKSMDSGAKQKLDEARDEDVKPFYFFRIR
Protein: Chordin-like protein 2 (Breast tumor novel factor 1) (BNF-1) (Chordin-related protein 2) (Q6WN34)
Organism: Homo sapiens (Human)
Function: May inhibit BMPs activity by blocking their interaction with their receptors. Has a negative regulator effect on the cartilage formation/regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation (By similarity). Implicated in tumor angiogenesis. May play a role during myoblast and osteoblast differentiation, and maturation.
Subcellular location: [Isoform 1]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Twisted gastrulation protein homolog 1
- Aminopeptidase Q
- Growth/differentiation factor 5
- Bone morphogenetic protein 7
Sequence:
MVPEVRVLSSLLGLALLWFPLDSHARARPDMFCLFHGKRYSPGESWHPYLEPQGLMYCLRCTCSEGAHVSCYRLHCPPVHCPQPVTEPQQCCPKCVEPHTPSGLRAPPKSCQHNGTMYQHGEIFSAHELFPSRLPNQCVLCSCTEGQIYCGLTTCPEPGCPAPLPLPDSCCQACKDEASEQSDEEDSVQSLHGVRHPQDPCSSDAGRKRGPGTPAPTGLSAPLSFIPRHFRPKGAGSTTVKIVLKEKHKKACVHGGKTYSHGEVWHPAFRAFGPLPCILCTCEDGRQDCQRVTCPTEYPCRHPEKVAGKCCKICPEDKADPGHSEISSTRCPKAPGRVLVHTSVSPSPDNLRRFALEHEASDLVEIYLWKLVKGIFHLTQIKKVRKQDFQKEAQHFRLLAGPHEGHWNVFLAQTLELKVTASPDKVTKT
Protein: Anoctamin (A0A0G2JXB5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-2
- Receptor
- Bestrophin
- Cyclic nucleotide-gated channel alpha-4
Sequence:
MAAPGLQDIPLLPGSPRRLSSRTMARGSQGPRHGQQYLKVPGPRLPGQRDNSSLHPSQVSRRESSRDRSVINNYLDANEPASSEARLSRMHFHDNQRKVDYVLAYHYRKRGAHLGHGSPGHSLAVISNGETGKERHGGGPGDIELGPLDALEEERREQRDEFEHNLMAAGLELEKDLESKSQGSVFVRIHAPWQVLAREAEFLKIKVPTKKMYEIKAGGSIAKKFSAILQTLSSPLQPRVPEHSNNRMKNLSYPFSREKMYLYNIQEKDAFFDNATRSRIVHEILKRTACSRANNTMGINSLIANNIYEAAYPLHDGEYDSPGDDMNDRKLLYQEWARYGVFYKFQPIDLIRKYFGEKIGLYFAWLGLYTSFLIPSSVIGVIVFLYGCATIEEDIPSKEMCDHQNAFTMCPLCDKSCDYWNLSSACGTARASHLFDNPATVFFSIFMALWATMFLENWKRLQMRLGYFWDLTGIEEEEERSQEHSRPEYETKVREKLLKESGKSAVQKLEANSPEDDEDDEDKLTWKDRFPGYLMNSVSILFMIALTFSIVFGVIVYRITTAAALSLNKATRSNVRVTVTATAVIINLVVILILDEIYGAVAKWLTKIEVPKTEQTFEERLILKAFLLKFVNAYSPIFYVAFFKGRFVGRPGSYVYVFDGYRMEECAPGGCLMELCIQLSIIMLGKQLIQNNIFEIGVPKLKKLFRKLKDETEPGESDPDHSKRPEQWDLDYSLEPYTGLTPEYMEMIIQFGFVTLFVASFPLAPVFALLNNVIEVRLDAKKFVTELRRPDAVRTKDIGIWFDILSGIGKFSVIINAFVIAVTSDFIPRLVYQYSYSHNGTLHGFVNHTLSFFNVSQLKEGTQPENSQFDQEVQFCRFKDYREPPWAPNPYEFSKQYWSVLSARLAFVIIFQNLVMFLSVLVDWMIPDIPTDISDQIKKEKSLLVDFFLKEEHEKVKLADEPAQRSQGGGNRSRRSRAASSAPSGRSQPGSIASSGSQHTNV
Protein: SWI/SNF chromatin-remodeling complex subunit SWI1 (Regulatory protein GAM3) (SWI/SNF complex subunit SWI1) (Transcription regulatory protein ADR6) (Transcription regulatory protein SWI1) (P09547)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:18362884}. Note=While the soluble protein is nuclear, [SWI+] aggregates appear to be cytoplasmic.
Interaction partners:
- SWI/SNF complex subunit SWI3
- Transcription regulatory protein SNF2
- Actin-like protein ARP9
- Transcription regulatory protein SNF12
- Transcription regulatory protein SNF6
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Actin-related protein 7
- SWI/SNF global transcription activator complex subunit SWP82
- Regulator of Ty1 transposition protein 102
- Transcription initiation factor TFIID subunit 14
Sequence:
MDFFNLNNNNNNNNTTTTTTTTNNNNTNNNNTNNNNNPANNTNNNNSTGHSSNTNNNTNNNNTNTGASGVDDFQNFFDPKPFDQNLDSNNNNSNSNNNDNNNSNTVASSTNFTSPTAVVNNAAPANVTGGKAANFIQNQSPQFNSPYDSNNSNTNLNSLSPQAILAKNSIIDSSNLPLQAQQQLYGGNNNNNSTGIANDNVITPHFITNVQSISQNSSSSTPNTNSNSTPNANQQFLPFNNSASNNGNLTSNQLISNYAASNSMDRSSSASNEFVPNTSDNNNNSNNHNMRNNSNNKTSNNNNVTAVPAATPANTNNSTSNANTVFSERAAMFAALQQKQQQRFQALQQQQQQQQNQQQQNQQPQQQQQQQQNPKFLQSQRQQQQRSILQSLNPALQEKISTELNNKQYELFMKSLIENCKKRNMPLQSIPEIGNRKINLFYLYMLVQKFGGADQVTRTQQWSMVAQRLQISDYQQLESIYFRILLPYERHMISQEGIKETQAKRIFLQQFLQELLKKVQQQQQAAALANANNNINSASSAPTPAAPGASVPATAAPGTEAGIVPVSANTPKSLNSNININVNNNNIGQQQVKKPRKQRVKKKTKKELELERKEREDFQKRQQKLLEDQQRQQKLLLETKLRQQYEIELKKLPKVYKRSIVRNYKPLINRLKHYNGYDINYISKIGEKIDSNKPIFLFAPELGAINLHALSMSLQSKNLGEINTALNTLLVTSADSNLKISLVKYPELLDSLAILGMNLLSNLSQNVVPYHRNTSDYYYEDAGSNQYYVTQHDKMVDKIFEKVNNNATLTPNDSNDEKVTILVDSLTGNQLPTPTPTEMEPDLDTECFISMQSTSPAVKQWDLLPEPIRFLPNQFPLKIHRTPYLTSLKKIKDEIDDPFTKINTRGAEDPKVLINDQLSTISMILRNISFSDNNSRIMSRNFYLKRFISDLLWLVLIHPENFTCNRKILNFKKDLVIVLSNISHLLEIASSIDCLLILILVISFGQPKLNPMASSSSFGSESLTFNEFQLQWGKYQTFGVDILAKLFSLEKPNLNYFKSILLNKNTGNNLYDRNSNNNHKDKKLLRRLLNLYNDNNKNNNNRHNLLNDVVSFLFSAIPLQQVLSQSADPSLLIDQFSPVISQSLTSILVIVQKILPLSNEVFEISENNSDSNSNNNGNKDSSFNFNKNLPFVWLSSEENIGSGLLKLSEIILNINNSTSKNTLLQQQNYSKVLLPSINISCVQLIKCLVEKSICFENCLNNDPEILKKIASIPNLFPTDLEIFQLFTNPSVDIQIINQYQLLYNLKNDILTNLE
Protein: Uncharacterized protein (Q57ZD0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRTTTHGSLYWRQLAFLPGHLNTRLASHGSCGTGSTRNYSFIMGSHRIIGGDMITSAAFVTPTFSTRCRLHSAVGGGTNTDLHQHCEQHSFEGGASVGTKPTNSASAKSTEQEEAVNNLLEEVQALLSRPVPIGSLFRALSADSKKTLVKNKVPLEQLLLQYPRNFALYQQGALRNRTIFCSPPHLVPANARPMVLENTSHISASTYAAGVRSSSSPSSPEAPASSPLKPDDINARVLQHDPLSEKQQRLNTVLQYIPNEWSPFTELGIPEEVRVRCMGKPGLKAMQFFERYPQYFEVRQQGRGEHTFHVRRSMALQRSQEPQHTQ
Protein: Dynamin-type G domain-containing protein (Receptor-mediated endocytosis 1 isoform I) (G5EEU7)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004159}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004159}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004159}.
Interaction partners:
Sequence:
MYNFFRTVPRANRNEITFYPDYEEEGQKKKKTRSMFSWLGGDSSKKKNKEVLETVSEGLRKIYKQKLLPLEEFHKFHDFHSPALDDPDFDAKPMILLVGQYSTGKTTFIRYLLESDFPGIRIGPEPTTDRFIAVMHGDEEGSIPGNALVVDAKKQFRALSGFGNAFLNRFQCSTLPNQVLESVTIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFKRCIEALAGNEDKIRIVLNKSDMVDHQQLMRVYGALMWSLGKVFKTPEVSRVYLGSFWDHPLHYDLNRRLFQDEQHDLFQDLQALPRNAALRKLNDLIKRARLAKVHAYIIAELRKQMPSMIGKDKKKKDLIQNLDKIYEQLQREHNISPGDFPDVNKMREKLQTQDFSKFNPLKPKLLEVVDGMLATDIARLMAQIPKEEAAAPAGSNGSADPTVRGGAFSQTTEAETPFGFGRGEGFDKGADEAEWVVSRERTTADSTFESLGPVNGYLSGRAAKEHMVKSKLPNSVLGKVWKLADIDKDGQLDADEFALANYLINLKLEGHEIPSELPKHLIPPSKRGEQDPVYPSLNDNDE
Protein: Listeria nuclear targeted protein A (Q8Y9T5)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Relieves the repression of host cell immune response genes (interferon-stimulated genes) by blocking the recruitment of host BAHD1 to these genes. May modulate interferon-mediated immune response to control bacterial colonization of the host.
Subcellular location: Secreted {ECO:0000269|PubMed:21252314}. Host nucleus {ECO:0000269|PubMed:21252314}.
Interaction partners:
Sequence:
MKKLVAWFNGLSKMWKVVVIIGAVFVVIIALTTGEDEGEQTKTKKDSNKVVKTASRPKLSTKDLALIKADLAEFEARELSSEKILKDTIKEESWSDLDFANDNINQMIGTMKRYQQEILSIDAIKRSSEASADTEAFKKIFKEWSEFKIERIQVTIDLLNGKKDSEAVFKKTYPNQIIFKKVRTNKLQTALNNLKVGYELLDSQK
Protein: Phospholipid scramblase 3 (PL scramblase 3) (Ca(2+)-dependent phospholipid scramblase 3) (Q9JIZ9)
Organism: Mus musculus (Mouse)
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of the phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer membrane of the mitochondria (By similarity). Plays an important role in mitochondrial respiratory function, morphology, and apoptotic response (By similarity). Mediates the translocation of cardiolipin from the mitochondrial inner membrane to outer membrane enhancing t-Bid induced cytochrome c release and apoptosis (Probable). Enhances TNFSF10-induced apoptosis by regulating the distribution of cardiolipin in the mitochondrial membrane resulting in increased release of apoptogenic factors and consequent amplification of the activity of caspases (By similarity). Regulates cardiolipin de novo biosynthesis and its resynthesis (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:21785166}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6QBQ4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Nucleus {ECO:0000269|PubMed:21785166}. Note=Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000269|PubMed:21785166}.
Interaction partners:
Sequence:
MAGYLPPKGYAPSPPPPYPVPSGYPEPVALHPGPGQAPVPTQVPAPAPGFALFPSPGPVAPGPPAPFVPLPGVPPGLEFLVQIDQILIHQKAERVETFLGWETCNMYELRSGTGQQLGQAAEESNCCARLCCGARRPFRIRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFLPKFSILDADRQPVLRVVGPCWTCGCGTDTNFEVKTKDESRSVGRISKQWGGLLREALTDADDFGLQFPVDLDVKVKAVLLGATFLIDYMFFEKRGGAGPSAITS
Protein: Phloretin 2'-O-glucosyltransferase (EC 2.4.1.-) (UDP-glucose:phloretin 2'-O-glucosyltransferase) (UDP-glycosyltransferase 88F2) (D3UAG3)
Organism: Pyrus communis (Pear) (Pyrus domestica)
Function: Glycosyltransferase that possesses phloretin 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Is specific for phloretin and does not possess glycosyltransferase activity toward naringenin, naringenin chalcone, eriodictyol, eriodictyol chalcone, apigenin, luteolin, kaempferol, quercetin, isoliquiritigenin, butein, caffeic acid, 2-coumaric acid, 3-coumaric acid, 3-hydroxybenzoic acid, 3,4-dihydroxybenzoic acid and 3,4-dihydroxyhydrocinnamic acid (Ref.1). Can glycosylate phloretin in the presence of UDP-glucose, UDP-xylose and UDP-galactose (By similarity).
Interaction partners:
Sequence:
MGDVIVLYASPGMGHIVAMVELGKFIVHRYGPHKFSITILYTCGSIVDTASIPVYIRRISHSHPFISFRQFPRVTNNITRNISVPAITFDFIRQNDPHVRSALQEISKSATVRAFIIDLFCTSALPIGKEFNIPTYYFHTSGAAVLAAFLYLPKIDEQTKTTESFKDLRDTVFEFPGWKSPLKATHMVQLVLDRNDPAYSDMIYFCSHLPKSNGIIVNTFEELEPPSVLQAIAGGLCVPDGPTPPVYYVGPLIEEEKELSKDADAAEKEDCLSWLDKQPSRSVLFLCFGSMGSFPAAQLKEIANGLEASGQRFLWVVKKPPVEEKSKQVHGVDDFDLKGVLPEGFLERTADRGMVVKSWAPQVVVLKKESVGGFVTHCGWNSVLEAVVAGVPMIAWPLYAEQHMNRNVLVTDMEIAIGVEQRDEEGGFVSGEEVERRVRELMESEGGRALRERCKKLGEMASAALGETGSSTRNLVNFVSSIT
Protein: SERPINE1 mRNA-binding protein 1 (PAI1 RNA-binding protein 1) (PAI-RBP1) (Plasminogen activator inhibitor 1 RNA-binding protein) (RDA288) (Q6AXS5)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8NC51}. Nucleus {ECO:0000250|UniProtKB:Q8NC51}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8NC51}.
Interaction partners:
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL15
- Ribosomal protein L15
Sequence:
MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVADKKEETQPPVALKKEGIRRVGRRPDQQLQGDGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIERPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNCSDLEQSNVTEETPEGEEHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA