wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 277 (Q9W1V7)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA binding protein which is involved in the positive regulation of both basal and inducible transcription. Mainly localizes to active promoter sites and interacts with components of various transcription and replication regulatory complexes, such as the ORC, SAGA, THO, TFIID and SWI/SNF complexes. It may therefore regulate transcription by promoting the association of these complexes to their binding sites.
Subcellular location: Nucleus {ECO:0000269|PubMed:30713769, ECO:0000269|PubMed:33456983}. Cytoplasm {ECO:0000269|PubMed:30713769}. Note=Predominantly localizes to the cell nucleus (PubMed:30713769). Associates with chromatin (PubMed:33456983). {ECO:0000269|PubMed:30713769, ECO:0000269|PubMed:33456983}.
Interaction partners:
- Origin recognition complex subunit 2
- GH25257p
- Origin recognition complex subunit 3
- Enhancer of yellow 2 transcription factor
- THO complex subunit 5
- histone acetyltransferase
Sequence:
MEHEVAVSGGDSSLEEITGSSKLKPSKNTAIKCLKCDKVYIFPSDKDDCLAHLYMEHRLVIADVEDIALLEDYLQYWEKEFHTHEFEQYCTTMFLDQLPDGKYAKNEKYYLLCDILPQDYELRRRLKEKRLSEALERHQFELTDRTFSKECLFCRAIIKGLRADYLDHLFDKHFLLVGKPEKLVYVDELLDHLEENLNRLMCLYCEKIFRDRPTLKEHMRKKGHKRINPNRREYDKYFLINYNRVPTAPTPRKQHLQKRRRETASVSTVADPETGSVDFDKHFARPDSDGEHDSDWSDWAADGEPSSIKCLFCHHLGDNFTALKKHMHEVHRLDFEKATSSLNFYQRVKVVNYLRRQMCLLRCVTCDLQFDEEELLVEHMAQESHHGIGDKESWDKPEFFFPYIENDGLLCVLDDSGGDDPDVDTVRIISEDSLAQINKDAERLSLENFKLL
Protein: Afadin, adherens junction formation factor (A8MQ02)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGEERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPPKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKDDRPFQGEDVENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAEALEKYGLEKENPKDYCIARVMLPPGAQHSDEKGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDHIPKKTKKHLEGKTPKGKERADGSGYGSTLPPEKLPYLVELSPGRRNHFAYYNYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKLDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVEGQRISETTMLQSGMKVQFGASHVFKFVDPSQDHALAKRSVDGGLMVKGPRHKPGIVQETTFDLGGDIHSGTALPTSKSTTRLDSDRVSSASSTAERGMVKPMIRVEQQPDYRRQESRTQDASGPELILPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSNQYRPDISPTERTHKVIAVVNKMVSMMEGVIQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYAPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVTVAENTADELARSDGREVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLIPHTRSPGTWTIYFEGADYESHLLRENTELAQPLRKEPEIITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSTQNGSPESPQLPWAEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSAYASGTTAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPPQNQWPNYEEKPHMHTDSNHSSIAIQRVTRSQEELREDKAYQLERHRIEAAMDRKSDSDMWINQSSSLDSSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAIPATPVAVSQPIRTDLPPPPPPPPVHYAGDFDGMSMDLPLPPPPSANQIGLPSAQVAAAERRKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPAPFSPLTAQQMKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITVSKEELSSGDSLSPDPWKRDAKEKLEKQQQMHIVDMLSKEIQELQSKPDRSAEESDRLRKLMLEWQFQKRLQESKQKDEDDEEEEDDDVDTMLIMQRLEAERRARDEERRRQQQLEEMRKREAEDRARQEEERRRQEEERTKRDAEEKRRQEEGYYSRLEAERRRQHDEAARRLLEPEAPGLCRPPLPRDYEPPSPSPAPGAPPPPPQRNASYLKTQVLSPDSLFTAKFVAYNEEEEEEDCSLAGPNSYPGSTGAAVGAHDACRDAKEKRSKSQDADSPGSSGAPENLTFKERQRLFSQGQDVSNKVKASRKLTELENELNTK
Protein: AE binding protein 2 (G5EA50)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRTMPQKRLKR
Protein: Ubiquinol oxidase 1c, mitochondrial (EC 1.10.3.11) (Alternative oxidase 1c) (OsAOX1C) (Q8W855)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Os04g0589400 protein
Sequence:
MGSRAAGSVLLRHLCPRVSSSTSAAAHAHAQRPPLAGAGGGGVALWARLLSTSAAAAKEETAASKENTGSTAAAKAEATKAAKEGPASATASPVASSYWGIEASKLASKDGVEWKWSCFRPWETYSPDTTIDLKKHHEPKVLLDKVAYWTVKALRVPTDIFFQRRYGCRAMMLETVAAVPGMVGGMLLHLRSLRRFEHSGGWIRALLEEAENERMHLMTFMEVAKPRWYERALVLAVQGVFFNAYFLGYLLSPKLAHRVVGYLEEEAIHSYTEYLKDIEAGKIENVPAPPIAIDYWRLPAGATLKDVVVVVRADEAHHRDVNHFASDVHFQGMDLKDIPAPLDYH
Protein: Integrin subunit alpha 6 (A0A8I6G9S4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MTGLLARLSTAFNLDTREDNVIRKSGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQKANRTGGLYSCDITSRGPCTRIVFDNDADPMSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETDHDESLVPVPANSYLGFSLDSGKGIVSKDDITFVSGAPRANHSGAVVLLKRDMKSAHLLLEYIFDGEGLASSFGYDVAVVDLNADGWQDIVIGAPQYFDRDGEVGGAVYVYINQQGRWSNVKPVRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSPTGIITKPTQVLEGTTPFFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINILKTITVTPSRIDLRQKSMCGSPSGICLKVKACFEYTAKPSGYNPPISILGILEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLNRQKQRACMEETLWLQENIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSNEAKTVQTDVHFLKEGCGDDNVCNSNLKLEYKFGTREGNQDKFSYLPIQKGIPELVLKDQKDIALEITVTNGPSDPRNPRKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSSVTFYLILSTTEVTFDTTDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLKNLGTATLNIQWPKEISNGKWLLYLMKVESKGLEQVVCEPHNEINFLKLKESHNSRKKRELPEKQIDDSRKFSLFSERKYQTLNCSVNVRCVNIRCPLRGLDSKASLVLRSRLWNSTFLEEYSKLNYLDILVRASIDVTAAAQNIKLPHAGTQVRVTVFPSKTVAQYSGIAWWIILLAVLAGILMLALLVFLLWKCGFFKRNKKDHYDATYHKAEIHTQPSDKERLTSDA
Protein: Adenomatous polyposis coli protein-related protein 1 (APC-related protein 1) (Q21227)
Organism: Caenorhabditis elegans
Function: Has a role in endoderm cell specification and pharyngeal development. Required for the migration of epithelial cells, organization of the anterior seam cells and ceh-13 expression during embryo morphogenesis. Prevents hyperactivation of the Wnt signaling pathway during endoderm development, probably by preventing hmp-2 nuclear translocation. During larval development, apr-1 is required for expression of lin-39 in P3-8.p. Shown to negatively regulate Wnt signaling in vulval precursor cells. Has a role in cell division by establishing the polarity of the mother cell which forms the asymmetries of the daughter nuclei. During the L4 larval stage, it is required for the asymmetric division and self-renewal of seam cells. Thought to regulate export of wrm-1 from the nucleus possibly as part of a complex involving pry-1.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}. Cytoplasm {ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}. Nucleus {ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}. Note=Found in clusters near the ends of microtubules that extend into regions of actively migrating plasma membranes. Shuttles between the cytoplasm and nucleus. {ECO:0000269|PubMed:10766743, ECO:0000269|PubMed:17276345}.
Interaction partners:
- Beta-catenin/armadillo-related protein 1
- Beta-catenin-like protein hmp-2
- Armadillo repeat-containing protein wrm-1
- Axin-like protein pry-1
- Protein pop-1
- Glycogen synthase kinase-3
- Protein kinase domain-containing protein
- Casein kinase I isoform alpha
- Beta-catenin homolog sys-1
- C-terminal-binding protein 1
Sequence:
MSSSSSDENETTIHRTGSNTGGSGIYSQPRAGSSKRTSNVRHDVSDVDDEEEHYARFREDTAIEVDDAITVLLSSLHFEHKRDIVPTDEDDNKLRELHEKIFALITSESDVNRKRRLKKALPASNCVREQVYYLRRKPSTPPASYYHRLNAALHTIVKESFGEEYRKVATVLGLVEALAEVLILEVHTFGINETNPGEHRNIRKLIANALTNLTYGQIHSKRRLCSYDGFIRCVVRIVIESPNITQVYAGLIRNLSWNADSGMSEALQPTVHALSIAAVHAHTHRFDVTATLSALWNLAGHSVENKRTICDTPNCLKVLASLLSPDARFTSLVDSATGILKYVSQYLANTSTHLELRSLLITRMLTLLKSASFTCVTNTLGAIANLIVKDPHMQQMIRQDMAAVQQLNVLRNSNRDDIRTAVKSVLNTLNQPCSHRYGDMSHSVGGGATGMQMLSEPQLQMQTSHHAYHGTASPRLLSLRATRASPGKYIQPQAQQQLIQTPQVDQRSSSLPRHFAVQRNGFVMAQSYNQQMDQHQQQQMIYQLQQQQQIMFQTEDQAQMEHHQQIMYLQQQQQQFHQIQQQQQMQKAQEADPVPPTDDDLDIPTSTVMGTRSNSERSLGSMNPGSVMTNWNSSLDTAANSSRALSPVSYNDIPASPTMCAQVFNLPKSTESEHHQLTSQQQNTTHYSSGSANTMTRSDGATTVPMDNIITPTYAILNPILVHEQTPNGTVPRKTSEELDSPDDVLPGPSLEEEEGDYAIIGGAAQKTDDELLTRSIQSEMPTSSSTPKMKVSPRLNGFFSPTQKTTSSPAWSHPDTSPIPKSSSHRTQPNRRQDASDADRLLMESIMSEMPKSRIISPRLAGTQQYLEPEPERRSHSKNEEADRRDAFTASHEPSDHNGIDVARGSDWSPQQQLHRMESLESQASSEDSFGLTAEEPNSSTSGAAANTMRFDDEIDASLPMDCVDDDDYDYTYDHFEDYEDEEDPDATQFDDGVDAQLTIDCSMISSGSGSSQRNETTTTSRDSKALATSTPKGSASSLPGVRQATRVSTNGKSRLPVPKTNGSLVDKNPKPIIASRRPRLPPKPTLLKDKHYPEEDSIENQTRDDTIYVNAPVVEAEQERIYMNALKQQKNIEQSPSIGNGSPIAKSAIVTPYNYQKPPFTGRNNGEMSNEKSVTPNPKQMLVTIV
Protein: KEOPS complex subunit Pcc1 (Q9V1Z9)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Pcc1 functions as a dimerization module for the complex.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- KEOPS complex subunit Bud32
- KEOPS complex subunit Cgi121
- DNA-directed RNA polymerase subunit Rpo12
- Probable Brix domain-containing ribosomal biogenesis protein
- Large ribosomal subunit protein eL43
Sequence:
MKPKRVQGKIVIEFPSEDIAEVVYTSVLYEHVSVPYRRSRVNFRREGRRIVLEIEANDSSAMRGTVNSYLRWIKVALDVLNI
Protein: DNA excision repair protein ERCC-8 (Cockayne syndrome WD repeat protein CSA homolog) (Q8CFD5)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair (By similarity). The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair (By similarity). It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes (By similarity). Plays a role in DNA single-strand and double-strand breaks (DSSBs) repair; involved in repair of DSSBs by non-homologous end joining (NHEJ) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13216}. Chromosome {ECO:0000250|UniProtKB:Q13216}. Nucleus matrix {ECO:0000250|UniProtKB:Q13216}. Note=Recruited to lesion-stalled RNA polymerase II (Pol II) sites by ERCC6/CSB. UV-induced translocation to the nuclear matrix is dependent on ERCC6/CSB. {ECO:0000250|UniProtKB:Q13216}.
Interaction partners:
- DNA damage-binding protein 1
- DNA excision repair protein ERCC-6
- Cullin-4A
- UV-stimulated scaffold protein A
- E3 ubiquitin-protein ligase RBX1
- DNA damage-binding protein 2
- DNA-directed RNA polymerase II subunit RPB1
- DNA repair endonuclease XPF
- DNA excision repair protein ERCC-5
- Cullin-4B
Sequence:
MLSFLSARQSGLEDPLRLRRAQSTRRVLGLELNKDRDVERIHGSGVNTLDIEPVEGRYMLSGGSDGVVVLYDLENASRQPHYTCKAVCSVGRSHPDVHKYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQAADVFNFEETVYSHHMSPAATKHCLVAVGTRGPKVQLCDLKSGSCSHILQGHRQEILAVSWSPRHDYILATASADSRVKLWDVRRASGCLLTLDQHNGKKSQAAESANTAHNGKVNGLCFTSDGLHLLTIGTDNRMRLWNSSSGDNTLVNYGKVCNDSRKGLQFAVSCGCSSEFVFVPHGSTIAVYAVHSGERLAMLKGHYKSVDCCVFQPNFQELYSGSRDCNILAWVPPSYEPVPDDDDEAPAKSQLNPAFADAWSSSDEDG
Protein: Proline-rich cell wall protein (Q39789)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MKVCNKNLFLSALLCIAVAGVLGQAPSNPPTSTPATPTPPASTPPPTTQAPPTPTATPPPVSTPPPTSSPPPVTASPPPVSTPPPSSPPPATPPPASPPPATPPPASPPPATPPPASPPPATPPPATPPPATPPPATPPPAPLASPPATVPAISPVQTPLTSPPAPPTEAPAPTLGAATPGPAGTDTSGANQMWTVQKMMGSLAMGWALLNLMV
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Q6FWL5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
Interaction partners:
- Superoxide dismutase 1 copper chaperone
- Superoxide dismutase
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
- Catalase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- orotate phosphoribosyltransferase
- Candida glabrata strain CBS138 chromosome E complete sequence
- Thioredoxin
Sequence:
MVKAVAVLRGSAGVSGVVTLEQASEQDPTTITYEIAGNDPNAERGFHIHEFGDVTNGCVSAGPHFNPFKKTHGAPQDENRHVGDLGNIKTDAQGVAKGVITDSLVKLIGPTSVVGRSVVVHAGTDDLGKGGNEESLKTGNAGPRPACGVIGLTN
Protein: UL37 immediate early glycoprotein (P16778)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Isoform vMIA sequesters proapoptotic BAX at the outer mitochondrial membrane and prevents cytochrome c release and subsequent initiation of the proapoptotic cascade. Also provoques a calcium efflux from host endoplasmic reticulum and F-actin cytoskeleton disruption. Participates in the increase of host mitochondrial biogenesis, thus promoting viral replication by efficient use of newly made mitochondria.
Subcellular location: [Isoform gpUL37]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane protein {ECO:0000255}. Host Golgi apparatus membrane {ECO:0000269|PubMed:8794367}; Single-pass membrane protein {ECO:0000255}. Host mitochondrion membrane {ECO:0000269|PubMed:20504938}; Single-pass membrane protein {ECO:0000255}. Note=The C-terminal fragment localizes to the endoplasmic reticulum while the N-terminal fragment is stable and traffics to mitochondria.; SUBCELLULAR LOCATION: [Isoform vMIA]: Host mitochondrion membrane {ECO:0000269|PubMed:15218184}; Single-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:15218184}; Single-pass membrane protein {ECO:0000255}. Host peroxisome {ECO:0000269|PubMed:27181750, ECO:0000269|PubMed:32726614}. Note=Transported from the endoplasmic reticulum (ER) through the mitochondrial associated membrane (MAMs) to the mitochondrial outer membrane. Associates with internal lipid rafts (LRs) in the MAM. {ECO:0000269|PubMed:15218184}.; SUBCELLULAR LOCATION: [Isoform pUL37m]: Host mitochondrion membrane {ECO:0000269|PubMed:15218184}; Single-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:15218184}; Single-pass membrane protein {ECO:0000255}. Note=Not cleaved or N-glycosylated. {ECO:0000269|PubMed:15218184}.
Interaction partners:
Sequence:
MSPVYVNLLGSVGLLAFWYFSYRWIQRKRLEDPLPPWLRKKKACALTRRSRHRLRRQHGVIDGENSETERSVDLVAALLAEAGEESVTEDTEREDTEEEREDEEEENEARTPEVNPIDAEGLSGLAREACEALKKALRRHRFLWQRRQRARMLQHNGPQQSHHAAVFCRVHGLRGFQVSVWLLLTLLWSTGHGVSVRCTYHGTDVNRTSNTTSMNCHLNCTRNHTQIYNGPCLGTEARLPLNVTFNQSRRKWHSVMLKFGFQYHLEGWFPLRVLNESREINVTEVHGEVACFRNDTNVTVGQLTLNFTGHSYVLRAIAHTSPFESYVRWEETNVTDNATSSENTTTVMSTLTKYAESDYIFLQDMCPRFLKRTVKLTRNKTKHNVTVTGNNMTTLPVWTPECKGWTYWTTLSVMWRNRRSALLRAKSRALGHWALLSICTVAAGSIALLSLFCILLIGLRRDLLEDFRYICRDEGSSSTKNDVHRIV
Protein: Interleukin-13 (IL-13) (P35225)
Organism: Homo sapiens (Human)
Function: Cytokine that plays important roles in allergic inflammation and immune response to parasite infection. Synergizes with IL2 in regulating interferon-gamma synthesis. Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells. Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1 (By similarity). Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B (By similarity). Functions also on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils. Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6. Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-13 receptor subunit alpha-1
- Interleukin-4 receptor subunit alpha
- Interleukin-13 receptor subunit alpha-2
- Interleukin-4
- Interleukin-5
- Signal transducer and activator of transcription 6
- Interferon gamma
- Tumor necrosis factor
- Interleukin-6
- Interleukin-1 beta
Sequence:
MHPLLNPLLLALGLMALLLTTVIALTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGQFN
Protein: Probable quinol monooxygenase YgiN (QuMo) (EC 1.-.-.-) (P0ADU2)
Organism: Escherichia coli (strain K12)
Function: Can oxidize menadiol to menadione. May work in concert with MdaB to form a quinone redox cycle.
Interaction partners:
- NADPH:quinone oxidoreductase MdaB
- ABC transporter ATP-binding protein ModF
- Putative monooxygenase YdhR
- Uncharacterized protein YpfG
Sequence:
MLTVIAEIRTRPGQHHRQAVLDQFAKIVPTVLKEEGCHGYAPMVDCAAGVSFQSMAPDSIVMIEQWESIAHLEAHLQTPHMKAYSEAVKGDVLEMNIRILQPGI
Protein: Sam51p (A0A1D8PN01)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SAM complex subunit
- Translocase of outer membrane 40 kDa subunit
- SAM complex subunit
- MICOS complex subunit MIC60
- Tom22p
- Mitochondrial distribution and morphology protein 10
- Mitochondrial import receptor subunit TOM20
Sequence:
MVELQVNTNPDLKSKLIEEQYLQESNNLPIYLTKIEVVGGESFSNQFFQNLLSPILQNGDLTFIQLVNKIKSSQSKLIETGIFDKVAIQILPDNFYSLSSNKIKSYNNEPSLLTKVLIDLSAINLSNNQGFFNFNNEEYLNLKLNHINHNFNGNGELISIGVDYNPYKPLDHLIANGKFISYLKNPKFKFLIDLQLNQENNEIWQDTKQEIIGGKLGLLYGNSTTNDLSVFTGFQLLKRNLINLDDGNFDSIKFFNGQFLKSSILNQLKYQKIEYLHDQSKNFPKNGYELLFNGEISSNQEQLNTNNLNEFIKTDLSINLYKSLFNEFFTTKFQAQLGGIYSFNNNNNDSNNNNKLTPIHPSDKFYLGGYNSFPGFSKNSVELQGGDQYYKLQTTLYSKIPTLLYAPPPPSASTIGLGNEQDLNPLRIYATGIIGNVVNSSKANLLEDENGAISYGFGLKYFNNWANFDIGYFFSKRLAFNNDTNSVNTAGIKDGLHFSISIGGSNNN
Protein: Guanylate cyclase activating protein 7 (Guanylate cyclase activator 1g) (Q5MAC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGQNQSDEEEEEVELTEIQPLYTRFMKVCPSGALHLHEFRRIFGVQSSSEEEALYMETIFKSFDTNRDNVIDFMEFVAAVHLVLRGNLEDRLKWSFKVYDRDENGKLDRQEVIHVIRILCKLKKNRINMTPVEICDRIFELLDENNDGQISLSEFLEGAEKDAWIMDLLKLDTNARVWFRDNLGKKT
Protein: Sideroflexin-1 (S4R2X2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
MSGELPPNINIKEPRWDQSTFIGRANHFFTVTDPRNILLTNEQLESARKIVHDYRQGIVPPGLTENELWRAKYIYDSAFHPDTGEKMILIGRMSAQVPMNMTITGCMMTFYRTTPAVLFWQWINQSFNAVVNYTNRSGDAPLTVNELGTAYVSATTGAVATALGLNALTKVLRFLFP
Protein: Inositol 1,4,5-trisphosphate receptor-interacting protein (Protein DANGER) (Q8IWB1)
Organism: Homo sapiens (Human)
Function: Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16990268}; Single-pass type I membrane protein. Nucleus outer membrane {ECO:0000250|UniProtKB:Q3TNL8}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
Sequence:
MAMGLFRVCLVVVTAIINHPLLFPRENATVPENEEEIIRKMQAHQEKLQLEQLRLEEEVARLAAEKEALEQVAEEGRQQNETRVAWDLWSTLCMILFLMIEVWRQDHQEGPSPECLGGEEDELPGLGGAPLQGLTLPNKATLGHFYERCIRGATADAARTREFLEGFVDDLLEALRSLCNRDTDMEVEDFIGVDSMYENWQVDRPLLCHLFVPFTPPEPYRFHPELWCSGRSVPLDRQGYGQIKVVRADGDTLSCICGKTKLGEDMLCLLHGRNSMAPPCGDMENLLCATDSLYLDTMQVMKWFQTALTRAWKGIAHKYEFDLAFGQLDSPGSLKIKFRSGKFMPFNLIPVIQCDDSDLYFVSHLPREPSEGTPASSTDWLLSFAVYERHFLRTTLKALPEGACHLSCLQIASFLLSKQSRLTGPSGLSSYHLKTALLHLLLLRQAADWKAGQLDARLHELLCFLEKSLLQKKLHHFFIGNRKVPEAMGLPEAVLRAEPLNLFRPFVLQRSLYRKTLDSFYEMLKNAPALISEYSLHVPSDQPTPKS
Protein: Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMP decarboxylase) (OMPDCase) (OMPdecase) (P08244)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Interaction partners:
- Orotate phosphoribosyltransferase
- Dihydroorotate dehydrogenase
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Uracil phosphoribosyltransferase
- Uridylate kinase
- Uridine kinase
- Carbamoyl phosphate synthase small chain
- 5'/3'-nucleotidase SurE
- Dihydroorotase
Sequence:
MTLTASSSSRAVTNSPVVVALDYHNRDDALAFVDKIDPRDCRLKVGKEMFTLFGPQFVRELQQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAREALVPFGKDAPLLIAVTVLTSMEASDLVDLGMTLSPADYAERLAALTQKCGLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSEAGDQRRIMTPEQALSAGVDYMVIGRPVTQSVDPAQTLKAINASLQRSA
Protein: Alkylglycerone-phosphate synthase (Alkyl-DHAP synthase) (EC 2.5.1.26) (Alkyldihydroxyacetonephosphate synthase) (Q9V778)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Subcellular location: Peroxisome {ECO:0000255|RuleBase:RU363113}.
Interaction partners:
- Peroxin-7
- Dihydroxyacetone phosphate acyltransferase
- Sterol carrier protein 2
- RING-type E3 ubiquitin transferase
- Peroxisome assembly protein 12
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX13
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- Peroxisomal membrane protein PEX14
Sequence:
MAAKRNAVTTEAPESSAPGEGTALALDSRLSKRVESVIPKKRHEALKWFGWGYNDSQFYGKDGIICFRGEKYPLGGCELPSFTKWVEKKFDLRVDTTKQYPQLPRTYPRPVENAPFLHELKGTTQVDYSAEGIDRLVRCHGQTLNDIYSLWHHKFRRIPDLVVWPRCHDEVVQLVRLANKHNVMLVPFGGGTSVSGAITCPQNESRMICALDTSQMNRLLWLNRENLTVCFESGIVGQDLERVLRSEGLTVGHEPDSYEFSTLGGWVATRASGMKKNVYGNIEDLVVRVRMVTPSGTLERECSAPRVSCGPDFNHVILGSEGTLGVITEVVLKVRPLPSLRRYGSLAFPNFEQGVLFMREVARRRCQPASVRLMDNEQFMFGQALKPEKSWWASVVDAMKQRYVTSWKGIDLNQICAATLLFEGDLKDVQRQEALIYEIAEKFQGFPAGGQNGERGYILTFVIAYIRDFGLHQGIVAESFETSVPWDRCSLLCRSVKQRVVSECSKRSINYYTISCRVTQTYDAGACIYFYFGFRSTDVADPVELFEAIEHSARDEILSCGGSLSHHHGVGKIRSHWYRNAVTETGSSLYSAAKRHLDPKNIFALGNLLPLEEAQASPPPPTSSTPPKAKL
Protein: Nucleoside diphosphate kinase-like domain-containing protein (Q57VY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Tubulin alpha chain
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S14
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S5, putative
- peptide-methionine
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS2
- thioredoxin-dependent peroxiredoxin
Sequence:
MFKKTRKAQATQVAEHTFLLCKPDAEQYHRNILQIVADEGFRVIAKSFIITPKQAEMIVKMFPSVRRSRYAEHRVDKVFPDRKAGNISQNQSSSDKQLESTPLRAMDNAERGSSGNSNDGESDSKQGSSQPERSQVIIAEIMQLTKLRCEGGDAVNAGLTKTADDGETSEGSVNGCDKKSLFPPAESIDVQQGCDNAETRYSSAAVLRNRMLENLPYQELLQKHTQHLAFGGTCLAVELVGENAVERLLALVGPENPVDACCNSPNSIRARFGHDLVRNAVHAASNLVEAGECIAAIFGFAPHHATAEVGDQGVSSESPGCTGLSGYMDHGEIAGVVTVRPHCELVFPGLRAPTRGPTTLEATVTVKNANMQAHISYYTGETPLGSKRKGVKGRPGSVTANRELNARDWQQKAKELEHQLAQQQRELAANAKLLRARELDLLLREHELESAVQAIFPPLQSQQGQLQQEHGEGERELLQSDATAAVPLPSVGEGHTGERYLLPFASGRDCGTGADLSFRHSGYISNSVLSRVAPKFATPQPMYDIPPTIEVDDVSLLLSHPVRLRALFMALERSTPCGKVMWEDMEGLYNRSPAVHLLWFEDHRAHFRNYLVKNTLEPLSFHTFVSVIMFLFKQ