wanglab/gogpt-training-data huggingface dataset:
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (F1RCS0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSSTGSSESGRRRGQRGPDDTVSTSKKKQKDRANQESKEAKRVATSTETKKDLFLDWKQNAYEVIVRLNCGGAGELRVEDIEYDFSNSACHIRLPDGREWSCHLHEEIEASCSKLNYKEKSNVLQLVMHKKIPLNTWPAYAKKSEPVNILQKNGSNNYQSSTGRSEKSSEAIEKTPPVSSAEQKRGKPDRGLKRGMKGKQVHVTKSTGEKTPEIKSSDKADSINEPSAKRTTRPSKNTKEPPLAPCLGNESKSKATVNGKTHTSEVNSGASSSSNAKDNRAQMQGKPQGCQALQKEKGIDRKPKSNAQVGSGESKSVSVCEPQVPQKDHSTPVKTCTDKIASDEPENRKEETKPQAEGHIPKMLPSHDLGSGEPASTDSKREESPQKSHTEEKRDKSKEEPQGASQEEDTEGPEPMVDLKFVKNDSYEKGTDLMVVNVYMKEICRQTSRVLFREQDFTLIFQTSDPNFLRLHSDCGPNTVFKWQVKLRNLIQPDQSNYAFTPSRIDITLKKRHSQRWGGLEAPATQGAVGGAKVAVASSPSTLEKSQPGSSQHALPAKEEPRVGEEKPKPPRAPEDSGLDAVSPRSVSEHVSLKQEPAVATPKPTCMVQPMTHTPPVGNERSEEVEEKKVCHPGFTGLVNLGNTCFMNSVIQSLSNTRELRDYFHDRGFESEINCNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRQDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPMCSKVSITFDPFLYLPVPLPQKQKVLTVFYFAKEPHKKPVKFLVSVSKESSSTAEVLESISRSVRIKPENLRLTEVVKGRFHRIFSPSQSLDTVSSSDLLFCFEMLSKDLIKERVVLLKVQQRPQIPSIPITKCAGCLKPPASDDEKLKRCTRCYRVGYCNQTCQKNHWPSHKTMCRSNVENIGQPFLISVPESRLSYTRLTQLLEGYSRYSVNVFQPPFQSGRTSPESSLSRVDLTSMASSVPECQEKDLPSAGDPENPAEQDESVTASQTESAADGGDTLSTHTTDSGCCELASSSHDSLLEKETSCEKAVKPEAVVTGYQQPSESASGGASQFYITILDSSQKEDKKLEEKGDAVLELPDECTLELVWKNNERQKEYVLVRSKDLEFDEDPGSATETSRAGHFTLEQCLNLFTKPEVLAPEEAWYCPKCQQHREASKQLLLWRLPNVLIIQLKRFSFRSFIWRDKINDMVDFPVRNLDLSKFCIGHKGDIQQPPIYDLYAVINHYGGMIGGHYTAYARLPSDKNSQLSDVGWRLFDDSTVTTVEESQVVTRYAYVLFYRRRNSPVERPSHLLGPLGAESSAATGGAASQASSQTLFGTDLDPDGPPQLSTEVTSDMFAHSGECAAPSYSSMEEVD
Protein: Ketose 3-epimerase (EC 5.1.3.-) (D-allulose 3-epimerase) (D-AE) (L-ribulose 3-epimerase) (A0A1L7NQ96)
Organism: Arthrobacter globiformis
Function: Catalyzes the reversible C-3 epimerization of several ketoses. Shows the highest enzymatic activity for the epimerization of L-ribulose to L-xylulose. Is also able to convert D-allulose (also known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose to L-sorbose, D-ribulose to D-xylulose, L-allulose to L-fructose and D-tagatose to D-sorbose.
Interaction partners:
Sequence:
MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH
Protein: Mitochondrial FAD-linked sulfhydryl oxidase ERV1 (EC 1.8.3.2) (14 kDa regulatory protein) (Essential for respiration and vegetative growth protein 1) (P27882)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:11493598, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984289}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit TIM10
- Cytochrome c oxidase copper chaperone
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM13
- Cytochrome c isoform 1
- Helper of Tim protein 13
- Mitochondrial import inner membrane translocase subunit TIM8
- Cytochrome c isoform 2
- Mitochondrial protein PET191
Sequence:
MKAIDKMTDNPPQEGLSGRKIIYDEDGKPCRSCNTLLDFQYVTGKISNGLKNLSSNGKLAGTGALTGEASELMPGSRTYRKVDPPDVEQLGRSSWTLLHSVAASYPAQPTDQQKGEMKQFLNIFSHIYPCNWCAKDFEKYIRENAPQVESREELGRWMCEAHNKVNKKLRKPKFDCNFWEKRWKDGWDE
Protein: DNA primase small subunit PriS (EC 2.7.7.-) (Q97Z83)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the activity, increasing the rate of DNA synthesis while decreasing the length of the DNA fragments, and conferring RNA synthesis capability. The DNA polymerase activity may enable DNA primase to also catalyze primer extension after primer synthesis. May also play a role in DNA repair. Possesses a template-independent 3'-terminal nucleotidyl transferase activity.
Interaction partners:
- DNA primase large subunit PriL
- DNA polymerase sliding clamp 2
- Primase X domain-containing protein
- DNA primase DnaG
- DNA polymerase 3
- Minichromosome maintenance protein MCM
- DNA polymerase 1
- Ribonuclease HII
- Replication factor C small subunit
- Ribosome biogenesis protein Nop10
Sequence:
MGTFTLHQGQTNLIKSFFRNYYLNAELELPKDMELREFALQPFGSDTYVRHLSFSSSEELRDYLVNRNLPLHLFYSSARYQLPSARNMEEKAWMGSDLLFDIDADHLCKLRSIRFCPVCGNAVVSEKCERDNVETLEYVEMTSECIKRGLEQTRNLVEILEDDFGLKPKVYFSGNRGFHVQVDCYGNCALLDSDERKEIAEYVMGIGVPGYPGGSENAPGWVGRKNRGINGVTIDEQVTIDVKRLIRIPNSLHGKSGLIVKRVPNLDDFEFNETLSPFTGYTIFLPYITIETEVLGSIIKLNRGIPIKIKSSIGIYLHLRNLGEVKAYVR
Protein: Homoserine O-succinyltransferase (HST) (EC 2.3.1.46) (Homoserine transsuccinylase) (HTS) (P07623)
Organism: Escherichia coli (strain K12)
Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-succinylhomoserine. Cannot use acetyl-CoA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305}.
Interaction partners:
- Cystathionine gamma-synthase
- 5,10-methylenetetrahydrofolate reductase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-lyase MetC
- Methionine import ATP-binding protein MetN
- HTH-type transcriptional regulator MetR
- S-adenosylmethionine synthase
- D-methionine transport system permease protein MetI
Sequence:
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLTRGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDAQTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYDLRHMNPTLD
Protein: ACC oxidase 2 (I1VCA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKNMKFPVVDLSKLNGEERDQTMALINEACENWGFFEIVNHGLPHDLMDKIEKMTKDHYKTCQEQKFNDMLKSKGLDNLETEVEDVDWESTFYVRHLPQSNLNDISDVSDEYRTAMKDFGKRLENLAEDLLDLLCENLGLEKGYLKKVFHGTKGPTFGTKVSNYPPCPKPEMIKGLRAHTDAGGIILLFQDDKVSGLQLLKDGDWIDVPPLNHSIVINLGDQLEVITNGKYKSVLHRVVTQQEGNRMSVASFYNPGSDAEISPATSLVEKDSEYPSFVFDDYMKLYAGVKFQPKEPRFAAMKNASAVTELSPTAAVETF
Protein: Apoptosis-enhancing nuclease (EC 3.1.-.-) (Interferon-stimulated 20 kDa exonuclease-like 1) (Q8WTP8)
Organism: Homo sapiens (Human)
Function: Exonuclease with activity against single- and double-stranded DNA and RNA. Mediates p53-induced apoptosis. When induced by p53 following DNA damage, digests double-stranded DNA to form single-stranded DNA and amplifies DNA damage signals, leading to enhancement of apoptosis.
Subcellular location: Nucleus. Nucleus, nucleolus. Note=Localized predomintly in the nucleolus. Translocates from the nucleolus to the nucleoplasm upon apoptosis induction.
Interaction partners:
- Angio-associated migratory cell protein
Sequence:
MVPREAPESAQCLCPSLTIPNAKDVLRKRHKRRSRQHQRFMARKALLQEQGLLSMPPEPGSSPLPTPFGAATATEAASSGKQCLRAGSGSAPCSRRPAPGKASGPLPSKCVAIDCEMVGTGPRGRVSELARCSIVSYHGNVLYDKYIRPEMPIADYRTRWSGITRQHMRKAVPFQVAQKEILKLLKGKVVVGHALHNDFQALKYVHPRSQTRDTTYVPNFLSEPGLHTRARVSLKDLALQLLHKKIQVGQHGHSSVEDATTAMELYRLVEVQWEQQEARSLWTCPEDREPDSSTDMEQYMEDQYWPDDLAHGSRGGAREAQDRRN
Protein: Tumor protein p63-regulated gene 1-like protein (Mossy fiber terminal-associated vertebrate-specific presynaptic protein) (A8WCF8)
Organism: Rattus norvegicus (Rat)
Function: Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17869247, ECO:0000269|PubMed:23723986, ECO:0000269|PubMed:26212709}; Peripheral membrane protein {ECO:0000269|PubMed:23723986, ECO:0000269|PubMed:26212709}. Presynaptic active zone {ECO:0000269|PubMed:17869247, ECO:0000269|PubMed:26212709}.
Interaction partners:
Sequence:
MLQLRDTVDSAGTSPTAVLAAGEDAGAGRQGAGTPLRQTLWPLNVHDPTRRARVKEYFVFRPGTIEQAVEEIRAVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTDQSLLICKYDFISLQCQQVVRVALSAVDTISCGEFQFPPKSLNKREGFGVRIQWDKQSRPSFINRWNPWSTNMPYATFIEHPMAGMDEKTASLCHLESFKALLIQAVKKAQKESPLPGQANNVLVLDRPLLIETYVGLMSFINNEAKLGYSMTRGKIGF
Protein: Cell division cycle protein 27 homolog (G5EA36)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGITQPNINDSLEITKLDSSIISEGKISTITPQIQAFNLQKAAAGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF
Protein: Protein FMP52, mitochondrial (Found in mitochondrial proteome protein 52) (P40008)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}; Peripheral membrane protein {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Bud site selection protein 22
- Cytochrome c1, heme protein, mitochondrial
- RNA polymerase I-specific transcription initiation factor RRN11
- Acyl carrier protein, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- UDP-N-acetylglucosamine transferase subunit ALG14
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
Sequence:
MNGLVLGATGLCGGGFLRHAQEAPQFSKVYAILRRELPFPATDKVVAIVERDNSKWSQLITNEMNPQVLFTALATTRAAAGGLDKQYKIDHDLNLQLAQAAKEKGCETIVLVSSAGAHPDSRFGYMKMKGEIERDVIALDFKHIIILRPGPLLGERTNSKQSGFGGNLTAALGTRVYRSRFQRLLGYPVYGDEVGKVGVHLALNTSGKDKVQFVSSKDILDISASLEKIAT
Protein: Beta sliding clamp (Beta clamp) (Sliding clamp) (Beta-clamp processivity factor) (DNA polymerase III beta sliding clamp subunit) (DNA polymerase III subunit beta) (O25242)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
Interaction partners:
- DNA polymerase III subunit gamma/tau
- DNA polymerase I
- Predicted 3'-5' exonuclease PolB-like domain-containing protein
- DNA polymerase III subunit alpha
- Protein HP_1247
- Chromosomal replication initiator protein DnaA
- DNA polymerase III epsilon subunit
- 5'-3' exonuclease domain-containing protein
- DNA polymerase III delta prime subunit
- Exodeoxyribonuclease
Sequence:
MKISVSKNDLENALRYLQAFLDKKDASSIASHIHLEVIKEKLFLKASDSDIGLKSYIFTQSSDKEGVGTINGKKFLDIISCLKDSNIILETKDDSLAIKQNKSSFKLPMFDADEFPEFPVIDPKVSIEVNAPFLVDAFKKIAPVIEQTSHKRELAGILMQFDQKHQTLSVVGTDTKRLSYTQLEKISIHSTEEDISCILPKRALLEILKLFYENFSFKSDGMLAVIENEMHTFFTKLIDGNYPDYQKILPKEYISSFTLGKEEFKESIKLCSSLSSTIKLTLEKNNALFESLDSEHSETAKTSVEIEKGLDIEKAFHLGVNAKFFLEALNALGTTQFVLRCNEPSSPFLIQESLDEKQSHLNAKISTLMMPITL
Protein: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II) (P0A7I7)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Interaction partners:
- Riboflavin biosynthesis protein RibD
- 6,7-dimethyl-8-ribityllumazine synthase
- Riboflavin synthase
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- GTP cyclohydrolase 1
- N-glycosidase YbiA
- GTP 3',8-cyclase
- Nucleoside diphosphate kinase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Bifunctional
Sequence:
MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK
Protein: Retinoic acid receptor responder protein 2 (Chemerin) (A0A8I6AUZ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKCLLISLALWLGTADIHGTELELSETQRRGLQVALEEFHRHPPVQWAFQEIGVDSADDLFFSAGTFVRLEFKLQQTSCLKKDWKKPECTIKPNGVSEGALVDGTGCQGRSWSPEKCCAHHWGLSAKKGGWRKGGNFSIRVGPPEEASLWSLSCILASSPKDFTVIGHPGGDTEAMDDLGLEVQHF
Protein: Immunoglobulin lambda constant 3 (Ig lambda chain C region DOT) (Ig lambda chain C region NEWM) (Ig lambda-3 chain C regions) (P0DOY3)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS
Protein: LD33361p (Simjang, isoform C) (Q960V1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKMEVDDVVDLSLGSGRDPALTITPAPPPAALSNRDLRALTANNAGLTITPSASPATNNGTTSNSSNTNSNSSSTTTTTNNNNNSSSNTNSSSANNNNNNNSINASDGVTGATSGSIGGGQDENKVQRRVLRPRTEPKSYAEAPDIVLLPARTNGRQQNGNIDSETDDEEMPPYVPIKELSHAELKEREKSLRKLRQDLRNEETKLMLLKKLKQSQQVMKENLVVTPTSVSPNNPLSAIPAALTSKGSLSVTPTSAVPLPAHSKGSRSSLSGSGGPAVSISATNSRTGSSSSAAAAASAIAAAAMSGQHRSGSNSILPPPRSSLPAGATLAAGTTITPATSSSHRSSNLPPRTNLPNLTITPSVTITPTSAPPSSLKPRNVPGTISNSVSITPALPLSQSHQNQHNDQKNDRSTPREDAQTPAQRQAAAKMALRKQLEKTLLQIPPPKPPPPEMHFIPNPSNTDFVYLLGLETVVDYLTVNKKANAVAAPFRCAQCKIDFTPVWKWEKQTNKDPKVICEQCVTSNVKKALKAEHTNRLKQAFVKALQQEQEIEQRLASQSSPSPVDNHGSSGGGNSLSVSAVSSNSSSSHMQREREQLQASHASAAAALVNLPPSVTVIPTKCQTPTPATPRPTPPPPQSQATPPPSSGGSRSSRAAATAAAAAIAAQQAGILSPGPSPAHHHEPTTSSRSSRNDRLDHHHQSQQQQQRDQRERDQQQRDQQSQQQAQNYDKYSAATLAAAAHLSALGGMGGLNINSLASLGNLGNLGNLSQLGNLAALGGLGNFGGASTGSANPAAGLSGSSPAATAAAMQAFQQQLFRGLGGNPQHMMQFAPLLYSYQMAMAQAAQVAAFNNNNKKSSSSSGSAKNSSSSNSMAEVQRAAELQRQYLLEMIPPQQQSGASGSRQNNWKA
Protein: Flotillin-1 (O61491)
Organism: Drosophila melanogaster (Fruit fly)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9573373}; Peripheral membrane protein {ECO:0000269|PubMed:9573373}. Membrane, caveola {ECO:0000269|PubMed:9573373}; Peripheral membrane protein {ECO:0000269|PubMed:9573373}. Note=Membrane-associated protein of caveolae.
Interaction partners:
- Flotillin-2
- Syntaxin-1A
- Tumor suppressor protein 101
- Kekkon 5, isoform A
Sequence:
MTWGFVTCGPNEALVVSGCCYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAAKLTGEVLSIVNKVPELVKNITGVDIARSVHAG
Protein: Heterogeneous nuclear ribonucleoprotein A3, isoform CRA_a (cDNA FLJ52659, highly similar to Heterogeneous nuclear ribonucleoprotein A3) (cDNA, FLJ79333, highly similar to Heterogeneous nuclear ribonucleoprotein A3) (B4DDB6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGHDPKEPEQLRKLFIGGLSFETTDDSLREHFEKWGTLTDCVVMRDPQTKRSRGFGFVTYSCVEEVDAAMCARPHKVDGRVVEPKRAVSREDSVKPGAHLTVKKIFVGGIKEDTEEYNLRDYFEKYGKIETIEVMEDRQSGKKRGFAFVTFDDHDTVDKIVVQKYHTINGHNCEVKKALSKQEMQSAGSQRGRGGGSGNFMGRGGNFGGGGGNFGRGGNFGGRGGYGGGGGGSRGSYGGGDGGYNGFGGDGGNYGGGPGYSSRGGYGGGGPGYGNQGGGYGGGGGYDGYNEGGNFGGGNYGGGGNYNDFGNYSGQQQSNYGPMKGGSFGGRSSGSPYGGGYGSGGGSGGYGSRRF
Protein: Envelope glycoprotein N (F5HHQ0)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Envelope glycoprotein necessary for proper maturation of gM and modulation of its membrane fusion activity. Also plays a critical role in virion morphogenesis.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}. Host membrane {ECO:0000255|HAMAP-Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}. Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04037}. Note=When coexpressed with gM, localizes in the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04037}.
Interaction partners:
Sequence:
MEWNTLVLGLLVLSVVASSNNTSTASTPRPSSSTHASTTVKATTVATTSTTTATSTSSTTSAKPGSTTHDPNVMRPHAHNDFYNAHCTSHMYELSLSSFAAWWTMLNALILMGAFCIVLRHCCFQNFTATTTKGY
Protein: Thiosulfate:glutathione sulfurtransferase (TST) (EC 2.8.1.3) (Q8NFU3)
Organism: Homo sapiens (Human)
Function: Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism. Provides the link between the first step in mammalian H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses GSS(-) as substrate. The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12817473}. Note=Localized around the nuclear membranes.
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Small ribosomal subunit protein mS29
- Endoribonuclease YbeY
- Catalase
- Molybdenum cofactor sulfurase
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein uL3m
Sequence:
MAGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLEKES
Protein: Guanylate kinase (EC 2.7.4.8) (GMP kinase) (P31006)
Organism: Sus scrofa (Pig)
Function: Catalyzes the phosphorylation of GMP to GDP. Essential enzyme for recycling GMP and indirectly, cyclic GMP (cGMP). Involved in the cGMP metabolism in photoreceptors.
Subcellular location: Photoreceptor inner segment {ECO:0000250|UniProtKB:Q64520}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q64520}. Note=Colocalizes with RD3 in photoreceptor inner segments and to a lesser extent in the outer plexiform layer. {ECO:0000250|UniProtKB:Q64520}.
Interaction partners:
- GMP synthase
- adenine phosphoribosyltransferase
Sequence:
MGSPRPVVLSGPSGAGKSTLLKKLLQEHSSIFGFSVSHTTRDPRPGEENGKDYYFVTREVMQRDIAAGDFIEHAEFSGNLYGTSKAAVRAVQAMNRICVLDVDLQGVRNIKKTDLQPIYIFVQPPSLDVLEQRLRQRNTETEESLAKRLAAAKADMESSKEPGLFDLIIINDSLDKAYWALKEALSEEIKKAQATGHS
Protein: Eukaryotic translation initiation factor 3 subunit B (eIF3b) (Eukaryotic translation initiation factor 3 subunit 9) (Q0E940)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit K
Sequence:
MAKKKSEEHSGTDANDSDYQEEPNFDDPPGFVDNISDEDLLGDMLAQRPSEADGVESVVVVDNIPKVEPVRLEKLKLVINKLFSNYGEIVNVVYPVDEEGKTKGYAFMEYKQARQAEEAVKKLNNHRLDKNHTFAVNLFTDFQKYENIPEKWEPPTVQTFKVQSDLYNFINDPDTYDQYCVAAETAPNCVQVGFWQNVLPEPFELETRERFTDTFVKWSPLGTYVVTFHKPGVAIWGGSSFQKIQKFPHPGTQFVEFSPCENYLVTYGPTPTGQKIIIWDIRTGAEKRSFVADGMSVLSMFRWSHDDKFVARMGENSIHIYETPSFYLLDLKSIKIPGIRGFSWSPTDNVIAYWVEEQNQIPARVTLMEIPKKREIRNKNLFHVADCKLHWQKSGDYLCVKVDRYSKLKKDKKDLDVKFLGMFYNFEIFHMREKEIPVDSVEIRELILAFAWEPVGNKFSIIHGETNSSNVSFYEVNKGVKPSLVKRLEKKSCTHLFWSPRGQFIVMANLTMGTFEFVDSTNDYIITASPDHFRASEVEWDPTGRYVVTGVSSWKVKEDTGFNMYTFQGRIIKRTILKNFVQFLWRPRPPTLLSEEKQKEIKKNLKKYYAAFEQKDRLRLTRASKELLEKRSQLRETFMEYRNKRIAEWAEQKSRRIMLRGHVDTDNLETDEVDEEIVEFLVKEEVTLLE
Protein: Recombination-associated protein RdgC (P36767)
Organism: Escherichia coli (strain K12)
Function: May be involved in recombination.
Subcellular location: Cytoplasm, nucleoid.
Interaction partners:
- Regulatory protein RecX
- DNA damage-inducible protein I
- DNA repair protein RecO
- Recombination protein RecR
- DNA replication and repair protein RecF
Sequence:
MLWFKNLMVYRLSREISLRAEEMEKQLASMAFTPCGSQDMAKMGWVPPMGSHSDALTHVANGQIVICARKEEKILPSPVIKQALEAKIAKLEAEQARKLKKTEKDSLKDEVLHSLLPRAFSRFSQTMMWIDTVNGLIMVDCASAKKAEDTLALLRKSLGSLPVVPLSMENPIELTLTEWVRSGSAAQGFQLLDEAELKSLLEDGGVIRAKKQDLTSEEITNHIEAGKVVTKLALDWQQRIQFVMCDDGSLKRLKFCDELRDQNEDIDREDFAQRFDADFILMTGELAALIQNLIEGLGGEAQR