wanglab/gogpt-training-data huggingface dataset:
Protein: Endothelial lipase (EC 3.1.1.3) (Endothelial-derived lipase) (EDL) (Phospholipase A1) (EC 3.1.1.32) (Q8VBX1)
Organism: Rattus norvegicus (Rat)
Function: Exerts both phospholipase and triglyceride lipase activities (By similarity). More active as a phospholipase than a triglyceride lipase (By similarity). Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity toward both types of substrates (By similarity). Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9Y5X9}.
Interaction partners:
- Gastric triacylglycerol lipase
- Patatin-like phospholipase domain-containing protein 2
- Acylglycerol transacylase
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Bile salt-activated lipase
- Pancreatic triacylglycerol lipase
- Hepatic triacylglycerol lipase
- Pancreatic lipase-related protein 2
- Lipoprotein lipase
Sequence:
MRDPVFLLGFWSLYCCFPAGSLTTLRPQGSLRDEHHKPTGVPVTITTKPSVTFNIRTSKDPEHEGCNLSLGDSKLLENCGFNMTAKTFFIIHGWTMSGMFESWLHKLVSALQTREKEANVVVVDWLPLAHQLYIDAVSNTRVVGRRVAGMLNWLQEKGEFSLGDVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGVDINRRLSPDDADFVDVLHTYTLSFGLSIGIRMPVGHIDIYPNGGDFQPGCGFNDVMGSFAYGTISEMVKCEHERAVHLFVDSLVNQDKPSFAFQCTDPNRFKRGICLSCRKNRCNNIGYNAKKMRKKRNSKMYLKTRAGMPFRVYHYQLKVHMFSYKNSGDIQPDLYITLYGSNADSQNLPLEIVEKIELNATNTFLVYTEEYLGDLFKIRLTWEGVSSSWYNLWNEFRSYLSQPSSPSRELHIRRIRVKSGETQRKVAFCVQDPMKNSISPGQELWFYKCQNDCRVKN
Protein: Uncharacterized protein C29A4.17c (O14020)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Autophagy-related protein 8
- MICOS complex subunit mic60
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Mitophagy receptor atg43
- Serine/threonine-protein kinase atg1
- Elongation factor Tu
- Casein kinase II subunit alpha
- Casein kinase II subunit beta-2
Sequence:
MNCLLLGRGFLHRFHPFRPVLCEDSASAATTITSQFKLNYRQIFIGSSLGLAAGFALGKLGRLFIVACSAVFATIAYINSKGLIRINWPQLQQQVIGPTEQYTGFHFPSSGRFNTQSTFPTIRNWICTNPNFKLSFFSAMYVGFVSS
Protein: Small ribosomal subunit protein uS5 (40S ribosomal protein S2) (Omnipotent suppressor protein SUP44) (RP12) (S4) (YS5) (P25443)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
- Large ribosomal subunit protein uL13A
- Large ribosomal subunit protein uL22A
- Small ribosomal subunit protein uS11A
- Small ribosomal subunit protein eS21B
- Small ribosomal subunit protein uS2B
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL8A
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein eS6A
- Small ribosomal subunit protein eS28A
Sequence:
MSAPEAQQQKRGGFGGRNRGRPNRRGPRNTEEKGWVPVTKLGRLVKAGKITTIEEIFLHSLPVKEFQIIDTLLPGLQDEVMNIKPVQKQTRAGQRTRFKAVVVVGDSNGHVGLGIKTAKEVAGAIRAGIIIAKLSVIPIRRGYWGTNLGQPHSLATKTTGKCGSVTVRLIPAPRGSGIVASPAVKKLLQLAGVEDVYTQSNGKTRTLENTLKAAFVAIGNTYGFLTPNLWAEQPLPVSPLDIYSDEASAQKKRF
Protein: Peroxidase 21 (Atperox P21) (EC 1.11.1.7) (ATP2a/ATP2b) (PRXR5) (Q42580)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Interaction partners:
Sequence:
MANAKPFCLLGFFCLLLQLFSIFHIGNGELEMNYYKESCPKAEEIIRQQVETLYYKHGNTAVSWLRNLFHDCVVKSCDASLLLETARGVESEQKSKRSFGMRNFKYVKIIKDALEKECPSTVSCADIVALSARDGIVMLKGPKIEMIKTGRRDSRGSYLGDVETLIPNHNDSLSSVISTFNSIGIDVEATVALLGAHSVGRVHCVNLVHRLYPTIDPTLDPSYALYLKKRCPSPTPDPNAVLYSRNDRETPMVVDNMYYKNIMAHKGLLVIDDELATDPRTAPFVAKMAADNNYFHEQFSRGVRLLSETNPLTGDQGEIRKDCRYVN
Protein: Odorant receptor coreceptor (Gustatory and odorant receptor 7) (Q178U6)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Plays a key role in preferred attraction of females for humans over non-human hosts for blood feeding. Human attraction plays a crucial role in the transmission of dengue and yellow fever by the mosquito. Also required for the response to the insect repellent IR3535; or to N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein.
Interaction partners:
- Odorant receptor
Sequence:
MNVQPTKYHGLVLDLMPNIRLMQGFGHFLFRYVNGPVLIRKLYSWWNLIMILLQYFAIMGNLVMNTGDVNELTANTITTLFFTHSVTKFIYVAVNSEHFYRTLGIWNQPNSHSLFAESDARYHSIALAKMRKLLVMVMVTTVLSVVAWITITFFGDSVKNVFDKETNETYTVEIPRLPIKAWYPWDAMSGVPYFFSFIYQAYFLLFSMCQANLADVMFCSWLLFTCEQLQHLKGIMRPLMELSATLDTYRPNSAALFRVASAGSKSELILNEEKDPDTKDFDLNGIYNSKADWGAQFRAPSTLQTFGDNGINGNPNGLTKKQELMVRSAIKYWVERHKHVVRLVSAIGETYGAALLLHMLTSTIKLTLLAYQATKIDALNVYGLTVIGYLVYALAQVFLFCIFGNRLIEESSSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMTISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK
Protein: tRNA-specific adenosine deaminase subunit TAD3 (tRNA-specific adenosine-34 deaminase subunit TAD3) (Q9URQ3)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Deaminates adenosine-34 to inosine in many tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Peroxisome {ECO:0000269|PubMed:36164978}.
Interaction partners:
- tRNA-specific adenosine deaminase subunit TAD2
- tRNA-specific adenosine deaminase 1
- Bifunctional protein RIB2
- Cytosine deaminase
- Cytidine deaminase
- tRNA
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Adenine deaminase
- tRNA
- tRNA
Sequence:
MVKKVNNPLKIDYQNGIIENRLLQIRNFKDVNTPKLINVWSIRIDPRDSKKVIELIRNDFQKNDPVSLRHLKRIRKDIETSTLEVVLCSKEYICDEGEINNKLKSIWVGTKKYELSDDIEVPEFAPSTKELNNAWSVKYWPLIWNGNPNDQILNDYKIDMQEVRNELSRASTLSVKMATAGKQFPMVSVFVDPSRKKDKVVAEDGRNCENSLPIDHSVMVGIRAVGERLREGVDEDANSYLCLDYDVYLTHEPCSMCSMALIHSRVRRVVFLTEMQRTGSLKLTSGDGYCMNDNKQLNSTYEAFQWIGEEYPVGQVDRDVCC
Protein: Glycosyltransferase (F4KHR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MARENPLMSFSFSFRYLCHFALLLSLLSFVSFLFRHNTSLCSCLYDHNTYVNTFDHQQNNETIDLLRFSSAWNHLTFPSKPKKTLKIAVVVKKWPRKSQAGGLERHALTLHLALANRGHELHVFTAASPSFPEYQLKNLMFHLSEPTAAGYLDQASVSQQLQTQNASGRPFDVIHTESVGLLHTRAKNLRNVVASWHGIAYETFHSDIIQELLRQADIAAATAAGTEEEQPPPSSPALTERAKRVVEEVKFFQRYAHHVATSDHCGDVLKRIYMIPEERVHIILNGVDENVFKPDVSKRESFREKFGVRSGKNKKSPLVLGIAGRLVRDKGHPLMFSALKRVFEENKEARENVVVLVAGDGPWGNRYKDLGSTNVIVLGPLDQEKLAGFYNAIDVFVNPTLRAQGLDHTLLEAMVSGKPVLATRLASITGSVVVGPHLGYTFSPNVESLTEAILRVVSDGTEELQRKGKEARERSLRLFTATKMADSYERFFLCISDQRFCTLQA
Protein: Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (Multisynthase complex auxiliary component p43) [Cleaved into: Endothelial monocyte-activating polypeptide 2 (EMAP-2) (Endothelial monocyte-activating polypeptide II) (EMAP-II) (Small inducible cytokine subfamily E member 1)] (Q12904)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation (By similarity). Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels (By similarity). Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum (By similarity). Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.
Subcellular location: Nucleus {ECO:0000269|PubMed:14500886}. Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Secreted {ECO:0000269|PubMed:10850427}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P31230}. Golgi apparatus {ECO:0000250|UniProtKB:P31230}. Note=Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (By similarity). Secreted in response to hypoxia (PubMed:10850427). Also secreted in response to both apoptotic and necrotic cell death. {ECO:0000250|UniProtKB:P31230, ECO:0000269|PubMed:10850427}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Bifunctional glutamate/proline--tRNA ligase
- Eukaryotic translation elongation factor 1 epsilon-1
- Methionine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Lysine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
Sequence:
MANNDAVLKRLEQKGAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIEELKQELIQAEIQNGVKQIPFPSGTPLHANSMVSENVIQSTAVTTVSSGTKEQIKGGTGDEKKAKEKIEKKGEKKEKKQQSIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCASSPEKIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKGKGVCRAQTMSNSGIK
Protein: Suppressor APC domain-containing protein 2 (Protein Ang) (Q9D818)
Organism: Mus musculus (Mouse)
Function: Plays a role in planar mitotic spindle orientation in retinal progenitor cells (RPCs) and promotes the production of symmetric terminal divisions. Negatively regulates the mitotic apical cortex localization of GPSM2 (By similarity). Involved also in positive regulation of cell proliferation and tumor cell growth (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86UD0}. Nucleus {ECO:0000250|UniProtKB:Q86UD0}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q86UD0}. Apical cell membrane {ECO:0000269|PubMed:26766442}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q86UD0}. Note=Localized at the apical membrane during the M phase (PubMed:26766442). In horizontally retinal progenitor dividing cells, localized at the pole cortical region from prophase to telophase cells (PubMed:26766442). In vertically retinal progenitor dividing cells, not detected at the pole cortical region at any stage of mitosis (PubMed:26766442). {ECO:0000269|PubMed:26766442}.
Interaction partners:
- Mitotic interactor and substrate of PLK1
- Proline and serine-rich protein 2
Sequence:
MAVAAMAERGRLSHAAPAPSTEGLPRAFLQSLRTLFDILDDRQRGYVHLREIESRWQGADARELPCGVLEGLRQVAPANGYLTFERFVAGLRTSLLKADGGQRDQARVAARPGDQSSLQQRLMFAPADEPRTVLERKPLPLSACPASGGPSGTSRNPELLCVPVEAASCPTETERPLSKALEQIPSADLGAAACKTLGKGTGEARQAPRARGERRRHTITNGVDCSLLKQMKELDQEQEVLLQGLEMMARGRDWYQQQLQRVQERQRRLSQSRAAADFGAEGSPRPLGRLLPKVQEVARCLGELLTAACSGRALPSSSLGPLGPPSPSTPVWQQQTILMLKEQNRLLTQEVTDKSERITQLEQEKSALIKQLFEARALSQQDSGPLDSTFI
Protein: Fgr38p (A0A1D8PCK2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MVIARPDVNLFHEVAKLPSEVVAIILGYLPNCMLPELLYFSPIKKIVASTILSNVHITEIFEKHEGSDVPGVGYSECDCNMFRITLENLKKGIDKWNIYPKTIKTEFTDSFEIGWDVFSKLLTKASSIYGFFVGTSNYPPEELFELLMDSNVKFESLHLMYFLTPVKLPPVATSVTLHQIKLDTYVIPGVKQLILRTKSINQERTNFTFSPDLEDLRIEAGSKMYVNLPPNLQELYISSTKTVNFRSEEMLKLKHLELQLPTIQSFEETGIRAPNLEKLVLSTCEELDCFDNLKQFQHLKHLVLNNCTYPTNLLKQKSFPMLESFQYSGTYFPNLDKMDIVTLTSPSTLKMLIVANHGFSHVFLDTLSLPATLTYLKLVNVVYNDDDGYFHLGENLQYVHIESFKLAFDRNFRIPHKVEFFLVEAFDLYFDSSDFMYHLPNSLIYLTLLAHEGGEMHLTNQRIKWPSMVDSIVLDGFNIDYRTLISLNFNESRLETIRICGGNIKKLDVDLFPVSVKDLALMDMGIQELPASFEKLENLHRLCLAKNRLKKVNSVKLPISSLRVLVLRKCDLRLISPFLVSMVEEENRDAKLKVEATGNSNINVIDVRKSLKAIKGLSLDINCVDEALNRISDNSTRFSCSSRLPDPYSEESGFSETEEVVVSDYDSDGLYNGSVFSPDEDDSDDDDDDDDDDDDDDNDDDDEDHKRRRIC
Protein: Astrotactin-1 (Neuronal migration protein GC14) (Q61137)
Organism: Mus musculus (Mouse)
Function: Neuronal adhesion molecule that is required for normal migration of young postmitotic neuroblasts along glial fibers, especially in the cerebellum. Required for normal rate of migration of granule cells during brain development and for normal cerebellum development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20573900, ECO:0000269|PubMed:8602532}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:20573900}. Endosome {ECO:0000269|PubMed:20573900}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305|PubMed:20573900}. Note=Detected close to the anterior pole and at the base of the leading process in migrating neurons. Is internalized from the membrane via clathrin-coated vesicles and endosomes, and recycled to the anterior pole of the migrating cell. {ECO:0000269|PubMed:20573900}.
Interaction partners:
Sequence:
MALAGLCALFACCWGPAAVLATAAGDVDPSKELECKLKSITVSALPFLRENDLSIMHSPSASEPKLLFSVRNDFPGEMVVVDDLENTELPYFVLEISGNTEDIPLVRWRQQWLENGTLLFHIHHQDGAPSLPGQDPTEEPQHESAEEELRILHISVMGGMIALLLSILCLVMILYTRRRWCKRRRVPQPQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDLRHHLQRECMNGGEDFASQVTRTLDSLQGCNEKSGMDLTPGSDNAKLSLMNKYKDNIIATSPVDSNHQQATLLSHTSSSQRKRINNKARAGSAFLNPEGDSSTEAENDPQLTFYTDPSRSRRRSRVGSPRSPVNKTTLTLISVTSCVIGLVCSSHVSCPLVVKITLHVPEHLIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWAMDLCARRLLDPCEHQCDPETGRREHRAAGECLCYEGYMKDPVHKHLCIRNEWGTNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELAINPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSKDNGGCSKNFRCISDRKLDSTGCVCPSGLSPMKDSSGCYDRHIGVDCSDGFNGGCEQLCLQQMAPFPEDPTLYNILMFCGCIEDYKLGVDGRSCQLVTETCPEGGDCGESREVPMNQTLFGEMFFGYNNQSKEVATGQVLKGTFRQNNFARGLDQQLPDGLVVASVPLENQCLEEISEPTPDPDFLTGMVNFSEVSGYPVLQHWKVRSVMYHIKLNQAAISQAFSNALHSLDGATSRADFVALLDQFGNHYIQEAVYGFEESCSIWYPNKQVQRRLWLEYEDISKGNSPSDESEERERDPKVLTFPEYIASLSDSGTKRMAAGVRMECQSKGRCPSSCPLCHVTSSPETPAEPVLLEVTRASPIYELVTNNQTQRLLQEATMSSLWCSGTGDVIEDWCRCDSTAFGADGLPTCAPLPQPVLRLSTVHEPSSNLVVLEWEHSEPPIGVQIVDYLIRQEKVTDRMDHSKVETETVLSFVDDIISGAKAPCAMPSQVPDKQLTTISLIIRCLEPDTIYMFTLWGVDNTGRRSRPSDVIVKTPCPVVDDVKAQEIADKIYNLFNGYTSGKEQQTAYNTLLDLGSPTLHRVLYHYNQHYESFGEFTWRCEDELGPRKAGLILSQLGDLSSWCNGLLQEPKISLRRGSLKYLGCRYSEIKPYGLDWSELSRDLRKTCEEQTLSVPYNDYGDSKDI
Protein: Atrochrysone carboxylic acid synthase (ACAS) (EC 2.3.1.-) (Endocrocin synthesis protein A) (Non-reducing polyketide synthase encA) (Q4W944)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA. The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA. The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC. The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself.
Interaction partners:
- Atrochrysone carboxyl ACP thioesterase
- Polyketide synthase, putative
- Anthrone oxygenase encC
Sequence:
MQGPSQLALFYFANGLPPDDIQDLFQRLRSQSKTESGWTLRAFVVQATNALREEIRQLPHHLRNPLTPLDNALDLAVVPDWRRGPLAGALEGVLLCLIEIGSLIAYYERTPDPFKFSARTACFTGIGTGLLAAAAAAASPTLADLPRLGAAAVRIALRMGVLVAETSQSVEAREPDAPADNWAAVVMDLDEDTVREELNLFNASTNNLGPSRLFISAGGTDNVTISGPPSKLRQVFRVSEKLRSARYAQLPVYGGLCHAPHLYNCHHWTWIMEPINGAAFNQNMVDTAPLFSAGDDVPFEASTPRQLFESVVCDLLMGMIRWNRAVDGVVELLGQTLPSECQVYAFRPCAVVTGMVASGQVKLPHCQFQTHDLLGWTCHDDTDNGPTCREDSSIAIVGMACRFPGGANDLNQFWDLLEQGADVHRRVPADRYDVESHTDTSGKSRNTSLTPFGCFIDQPGLFDAGFFDMSPREAMQTDPMHRLALMTAYEALEQAGFVPNRTESTHLKRIGTFYGQSCDDYREANAGQEVDTYYIPGGCRAFAPGRINYFFKFSGPSFDCDTACSSSLATIQMACTSLQHGDTNMAVAGGLNILTNSDGFAGLSRGHFLSKTGGCKTFDCNADGYCRADGIGSIVLKRLDDAQRDNDHIFGIILAAATNHSARAISITHPHAPSQAELYRDILTRAGVSPLDVDFIEMHGTGTQAGDSTEMESITSVFSPGVPKRSRPLYIGSVKANVGHGEAAAGVMSLIKVLLVLQRQAIPKHVGIKTALNPRFPNLDRLNVRIPHDQVPWPRSPTRKRYALVNNFSAAGGNTSLLIEEPPVRPEPKADPRAAFTVAVSAKSKASLKNNLRSFLAYLESQPSISLAHLSYTTTARRMHHNHRIAVHGSTLSSIMQELEPYLPAVDTHRPVPNTPPSIAFVFSGQGSFYTGIARQLYEHHPGFRLQITRLHNICLSHGFPSFRRAITGDLSNDGSEAEPIITHLTIVCVSIALCRLWETLGVKPCVVAGASLGEFAALYAAGVLSASDAIYLVGRRAQLLQELCTPNTHAMLAVRATVEQIRNVLAGQPYEVACINGSSDITLSCSVADIINLQLAIEQHGYKCTRLDVPFAFHSAQMDPLLGPFEHIARGVTFKAPNIPVMSPSLGDCVFDGKTINASYMCNVTRNPVKFVDALETARGMDLVDAKTVWVEIGPHASYSRFVGSAMPPGTATIASLNRNEDNWSTFARSMAQLHNLGVDLNWHEWHAPFESELRLLTDLPAYQWNMKNYWIQYNGDWMLRKDGKSSAAAASHPHQAIPPALRTSLVHRLVCESVQETRVEVIVESDILHPDFFEAMNGHRMNGCAVATTAIHADIAFTLAKYLYSSIMPNSTDAPAINVKNMQVQHGLVARKDRSRPQLIRIRGIADVTRGLVSLSWHLVDEQGRRVEESFATAVAEFGNHEAWLEEWSPMTHLVVSRIDVLQRLADDGTANRLSRDMVYMLFNNLVDYAEKYRGMQMVVLHGLEAMANVTLAAPEQSGGKWTVAPHYIDSVVHLAGFILNGGNGLDPRRNFYVTPGWKSMRFARPLVPGVRYQSYVKMMPIREQSGFYAGDVYILHEGQIVGLVGGITFRTFPRSLINTFFSPPDTMTHGGSQAGSVHQPACSERTLPVGPARQDSAARETLCQGHGLSRTVMDSSDSSPATTLTPPTLPSVAASTESPIVHRAMALIAAETAIELTELSDETAFSSIGVDSLLSLVLAEKFTAEFHLDFRSSLFLDCPTIGDLKAWLIDYC
Protein: Tyrosine-protein phosphatase (EC 3.1.3.48) (Q8IRJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
Interaction partners:
Sequence:
MPEACCFLHSSFILVMCFYLQIKRNILLGKLPCSSNTQCLLASYTVQSELGDFNALEHQPGYLSGMQLLCDQTTEAERKVGELHKLHRGQLPADAEYNYLEHAKRLELYGIDLHRATDSNGKELQLGVSAVGLLVFQHSLRVNTFSWSKMVKVSFKRKDFFIQLRREPSENYDTLLGFGMSSHKHAKALWKSCVEHHSFFRLKRPHRLSRFLNISLGSKFYYSGRTELQAVQESKQRGRIHKVFVRSPSKRLLGAAGGVGTSGSSGGTPMQQHSGSESANSHNNGKPAGAGTILTITKTSRPHDNKVTSKEADSMPRKAWEQQSDEYDIQLDVGFIEQCTRRFESASPSPMPPAYSSGQHSPILLPTTIADAVGHQQPESGSDLITIRLQADEQGRYGFNVKGGVDLSLPVQVSKVVPHTPADRCTPRVCEGDEVLMINGRDVHGLRHEQVVAMIRDCRHQASGELLLTVRPQRSAPLLLEEEPLYQYVPESDEIGSHSNLLDGDALFTQSLLLLSDGLASGALLAQYELMYRKNPDLAITEARKPANAPKNRYRDISPYDCTRVSLVNSLTGDYINANYVNMEIPGGAVNRYIATQGPLASTTTDFWRMVQQESSHLLVMLTTVMESGRQKCHQYWPVTGEELQLAEGFSVRCLSEKPDETGSFVFREFVLKDKHEQRHIHHMQYLAWPDHCVPSDPNLFLEFTERVRAARNRTLLQEIEESLKQVRLMDADADADENGGLMRERKCAASNGATPEDETPVSTSVHQCISAANPPVIVHCSAGIGRTGVLILMDTALALMEAREPVYPLDIVRTMRDQRACMVQNVSQYRFVCECICAAYMKISRSSAAINDDED
Protein: Egl-9 family hypoxia inducible factor 2 (M0R0Z6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRKWAEDGGDAPSPSKRPWARQ
Protein: Double-strand break repair protein MRE11 (EC 3.1.-.-) (Q9IAM7)
Organism: Gallus gallus (Chicken)
Function: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49959}. Chromosome {ECO:0000250|UniProtKB:P49959}. Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P49959}.
Interaction partners:
- Nibrin
- Zinc-hook domain-containing protein.
- Non-specific serine/threonine protein kinase.
- Uncharacterized protein.
- RB binding protein 8, endonuclease.
- Uncharacterized protein.
- ATR serine/threonine kinase
- X-ray repair cross-complementing protein 5
- Uncharacterized protein.
- X-ray repair cross-complementing protein 5
Sequence:
MSAVSLQDDEDTFKILIATDIHLGYLEKDAVRGNDTFVTFNEILEHAQKNEVDFILLGGDLFHENKPSRKTIHTCLESLRKYCMGDRPVSFEVLSDQAVNFQLSKFPWVNYQDENLNIFMPIFSIHGNHDDPTGVDALCALDILSCAGLLNHFGRSTSVEKIDISPILLRKGRTKIALYGLGAIPDERLYRMFVNKQVTMLRPKEDEDSWFNMFVIHQNRSKHGATNYIPEQFLDDFINLAVWGHEHECKITPAQNEQQHFYVTQPGSSVVTSLSPGEAVKKHIGLLRVKGKKMKMQRIALETVRTFYMEDVVLADHPELFNPDNPKVTQAIQAFCMEKVEMMLDNAERERLGNPRQPQKPLIILRVDYTGGFEPFIVHRFSQKYMDRVANPKDIIHFFRHREQKEKNDNDINFGKLLSRPASEEVTLRVEDLVKQYFQTAEKKVQLSLLTERRMGEAVQEFVDKEEKDAIEELVKFQLEKTQRFLKERHIDAEEEKIDEEVRKFRESRRKNTEEEDEEVREAMTRARAHRSEGVVLDSASSDEGLMDTGMKASGDSDDDIPTTLSRGRGRGRARGARGQNSAARGSSRRGRGNTSQGSSTSSRTYKSVPDKNSSIMDAFRSLKPEPSQSTSKFFSEDIIDDEMDLEESPISLSSKTNQRSSAMSSFSKRGSQSQMSRGVDFESDEDDPFKNTATSRRKK
Protein: Tail spike protein (TSP) (Endorhamnosidase) (EC 3.2.1.-) (Gene product 20) (gp20) (Q858F5)
Organism: Salmonella phage epsilon15
Function: Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.
Subcellular location: Virion {ECO:0000269|PubMed:16452981}.
Interaction partners:
Sequence:
MTVSTEVDHNDYTGNGVTTSFPYTFRIFKKSDLVVQVVDLNENITELILDTDYTVTGAGGYTCGDVVLSSPLANGYQISISRELPVTQETDLRNQGKFFAEVHENAFDKLTMLIQQVRSWLSLALRKPSFVANYYDALGNYIRNLRDPSRPQDAATKNYVDNLSEGNNSYADNLFSRTLRVPEKINTLPSSLDRANKIPAFDSNGNAIVIIPQSGSASDVLIELAKPSGSGLVGFSHSNNYNPGMVGEKLQNVVYPTDAPFYAPTDGTSDATTALQSAITHCEGKNAVLCINKSFSVSDSLSISSPLCVFAMNEQCGIVSSAPAGHAAVIFNGDNICWNGGFIRGLNQPSSSTIRQDGVLLNGNDCVLDNVSINGFFAKGLHTSNADGSGVGIRDYGTRNTISKCRVEYNKFGISLEGKDGWVLGNYVSNHYRMSSEAKPWDDTSNYWDGIVGGGEWLGVATGYLIDGNEFEDNGQSGIYAGGNGGIFAKNRITNNHIHGNWNRGIDFGVVQRLANSDVYENIITDNIVHNNRAANIWLAGVRDSIINNNNSWFTDDYRSMFAGNFDACVCLTLADGGEKAAPTGNQVNGNRCKTLESDDQISGFTLNITDTARGNQVRDNVLSPIGEAYIPNPELYAVNNIDIPTEFAFTPQLIGGSGVTLGNSSGKLTANGNVFSLSLSISAQSVSSPSGSLTIGYIPGLSGTSVRHHNVRTEFYNNLNTTMQRAQPYVNIGDSADQLRVYRLADGLSKDDLLEYFMSNSDLRMVGDIEIEPYNFSRSVTVVGHSFCTSDVMSTELNRLLGTDIYNFARGGASDVEVAMSQEAITRQYAPVGGSIPASGSVALTPTEVGIFWNGATGKCIFGGIDGTFSTTLVNAGTGETQLVFTRDSAGSAVSVSTTATFAMRPYTRFNTNTIPAGRKHSLHRDDIYIVWGGRNSTDYTRYVSELHTMVANMHTQRFVICPEFPYDTETTGTTGATNLAALNNNLKADFPDNYCQISGVDLLQNFKSKYNPAYAGDVTDIANGITPRSLREDNLHPSETLQPNGLYIGAKVNADFIAQFIKSKGWGG