wanglab/gogpt-training-data huggingface dataset:
Protein: 1,3-beta-glucan synthase component bgs3 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (Q9P377)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex (By similarity). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall (By similarity). Required for cell wall biosynthesis and cell elongation.
Subcellular location: Membrane {ECO:0000269|PubMed:12582133}; Multi-pass membrane protein {ECO:0000269|PubMed:12582133}. Note=Found at the growing tips during interphase and at the septum prior to cytokinesis.
Interaction partners:
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Glucan 1,3-beta-glucosidase 1
- Glucan 1,3-beta-glucosidase 2
- Glucan 1,3-beta-glucosidase
- Cell wall alpha-1,3-glucan synthase ags1
- Uncharacterized oxidoreductase pbr1
- 1,3-beta-glucan synthase component bgs4
- 1,3-beta-glucan synthase component bgs1
- 1,3-beta-glucan synthase component bgs2
Sequence:
MDYKKGEHSPSSSIQILSDDATINSNYAYGEQLQSNDQYNNIQHPAPSFANPFIHEQDDSYSDILEEEPDEDAYDSPERPSSTEEFISQDESNISAGSSFMFPYNRGHPLSKRHDSIMVDEFGHEYIVEGDSIASADEAIDYDALYASWTAETKAPILAIDIENIYIELAMKFGFQWDNMRNMFDYLMVMLDSRASRMTPQEALLTLHADYIGGPQSNFKKWYFACKMDQFDLKSGVLSFISRDPSTQVPYKDMSSCEALWISRMDELSNYERIEQLALYLLCWGEANNVRFMPECLCFIYKVAYDYLISPSFKEQKNPAPKDYFLDNCITPLYNLMHDQQYEIRDQKYVRKEKDHASIIGYDDINQMFWYSKGLKALLLSDGSRIMDADVASRYFLLADIQWQRVCYKSFRESRTWLHFLHNFSRIWILHISVFWYFTVYNSPTIYTPNFHYLEGTQPARAAKWCAPALAGAVASFISFLALILEAYFVPRNNPGAQPVIPRLIFVSILIALNIVPAAFIFGFSNATQQHYRSREIVGYVHFFFSIGCVAYQSFIPLPFLLGPRFKFRSSSRKYLANSYFTNDIASLPWGRTLLSAALWITVFIAKFVESYYFLTLSVRDPIRFLQRMKPYDCYDFMIGASLCSHQPKFLLSLVYLTDLVLFFLDTYLWYMLISTMFSIAYSFYMGSAIWTPWRVIFSNLPRRIYFTLLAYKDLSTEFKPKIYVGQIWNSIMISMYREHLLSLEHLKGLLYQQVGSEYFGKQTFQSPKFFMEAAKGLNKWDAFFRRNSEAERRISFFAQSLGGKIPDAVPVPKMPSFTVLIPHYGEKILLSLREIIREQDPMSRITLLEYLKQLYPNDWDNFVQDTKLMAGDVGVEETKSDVKSEKGKKQGTVKEDLPFYCIGFKSTAPEYTLRTRIWASLRSQTLYRTASGMMNYSRALKLLYRVEQPNLLDDCDGNFERLEHQLEQMAYRKFRLCISMQRYAKFNRDEYENAEFLLRAHPELQIAYLDQDPSEDGEEPKVYATLINGFCPFENGRRLPKYRIRLSGNPILGDGKADNQNMALPFVRGEYLQLIDANQDNYIEECMKIRNVLSEFEEMDCATLTPYTKKGNARHPVAMLGAREYVFSENSGILGDVAAGKEQTFGTLFSRSLALIGGKLHYGHPDFLNTIFMTTRGGVSKAQKGLHVNEDIYAGMTALQRGGRIKHCDYFQCGKGRDLGFGTIINFTTKIGTGMGEQSLSREYFYLGTQLPFFRMLSFYYAHAGFHLNNVFIMISMQLLMLVFVNLGAMYHTVEICDYQAGAAINASLYPPGCYMLKPVLDWIRRCIISIFIVFFISFLPLVVHDLLEKGVIRAVARLCKQIFSLSPMFEVFVTQNYANSIFTNLTYGGARYIATGRGLATTRVPFSVLYSLYTGSSIYLGSRLIMMLLFGTMTVWTTHYVYFWVTMFALVICPFIYNPHQFSFVDFFVDYREFLRWLSRGNTKGHAHSWIGFCRLARTRITGVNRKVKGSPSNKLTMDMPRAGLRNVIFTEVFLPACFAFFTICAYTFMNSQPGLEDKSRAVNGFIRIWIMAALPIAISTAALLILLMFSCMLGPLLRKCSKRYGAVLAALAHAVSVFGLVFTFEALWFLEAWSFSKTVLGCIVIFAIHRLVFKLVVVFLLPREVASGENNYSWWDGHWFGRKGIPYMPIQFIREFMCKVVEMNLFAMDFILSHCILFSLTPILCIPFIDIPHSVLLFWLHPSRQIRPPIYTRKQNQLRRRTFYRYSLLFFALLCTFVAMIVVPLVLDQKLSYQFKFENSVKFFRLMQPSLGVLPNTNKNTSE
Protein: Large ribosomal subunit protein eL13 (60S ribosomal protein L13) (Q90Z10)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
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. As part of the LSU, it is probably required for its formation and the maturation of rRNAs.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P26373}.
Interaction partners:
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS12
- Ribosomal protein S10
- Large ribosomal subunit protein uL16
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein uL23
Sequence:
MAPSRNGMILNPHFHKDWQKRVRTWFNQPARKIRRRKARQAKARRIAPRPVSGPLRPVVRCPTIRYHTKVRAGRGFTLEELKAAGINKKVARTIGISVDSRRRNRSTESLQANVQRLKEYRTKLIIFPRKAAKPKKGDSTEEELKMATQLTGPVMPIKKVHKKEKARVISEDEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK
Protein: Transforming acidic coiled-coil protein, isoform K (A0A0B4JD97)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Protein mini spindles
- Aurora kinase
- Centrosomin
- Protein claret segregational
- Alkaline phosphatase
Sequence:
MDFLANIIKRPKSIATTGISTNQPTTMEALEAASPADECSTPRDKGGVTLVSAHLDSLLESASEELQRLEGKHCELFMESISNPLPAPEDSTDSREEIQKFLSEINFNLNQVSANEMEHLQAMSGELSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEDRHLMQTHILSVTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKIIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFDSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVVQPTKEEEEAKSRRTFCMENENPRRTFCMQQNASPAVEATEDTGADEVMDVDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEQTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNLILNSSDFDYLYTKGSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: Serpentine receptor class alpha-10 (Protein sra-10) (Q20405)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGPITANSSKCATEDQMILQTSLLLRINVIIMTIVAIITFILTYKALFILKIRPIFHSSTKILLYTSLLFVNVHAVIFMVIQNTALIRSFTLSDKPCEIMRTTLECRFQNHVLIFGIAGVNFNQFGLTVDRLLATIIPQSYSHMGALPGVILSVLVVACSIAAPLIIAIGDPYDDIVPNCFFFPEHSAPRANIFLVTLSTLVITSIFLNFIIIYANKKLEKGCRTRFYVTQRYQKREALISTRIISYIAASQFLGLTLYSTMVLTLRLHKSMIPISIYHNMVWWAYTVPFAAVSLPALLIYRINQVGSNRKRVINRITAKVETQEEHMKSLKELWA
Protein: Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 7) (mTTLL7) (A4Q9F0)
Organism: Mus musculus (Mouse)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cell projection, dendrite {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Perikaryon {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}.
Interaction partners:
Sequence:
MPSLPQDGVIQGSSPVDLGTELPYQCTMKRKVRKKKKKGIITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDAAVQQEKITDLQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKVPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQANQHDVTKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRKNLAKQKAEAQRRLYGQNPVRRLSPGSSDWEQQRHQLERRKEELKERLLQVRKQVSQEEHENRHMGNYRRIYPPEDKALLEKYEGLLAVAFQTFLSGRAASFQREMNNPLKKMREEDLLDLLEQCEIDDEKLMGKTGRVRGPKPLCCMPECAEVTKKQKYYGSSDSSYDSSSSSSNSELDENEKELCQKRLDQVPYSLKHTSHCKIIQQPSGSHNLIYSESPVYLTTLVFLSEFPDSMRRSVSCPRSISAHLPSRGDVRPFSSQQVIPLARPTSASRSHSLNRASSYARHLPHGSDTGSTNTLNESLRQLKTKEQEDDLTSQTLFVLKDMRIRFPGKSDAESELLIEDIMDNWKHYKTKVASYWLIKLDSVKQRKVLDIVKSSIRTVLPRIWRVPDAEELSLYRIFNRVFNRLLWSHGQGLWSCFCDSGSSWESIFSKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYTTETRGPISGIGPDWGNSRYLLPGSTQFLMRSPLYNMKYNSPGMTRSNVLFTSRYGRL
Protein: Lipopolysaccharide heptosyltransferase 2 (EC 2.4.99.24) (ADP-heptose:lipopolysaccharide heptosyltransferase II) (ADP-heptose:LPS heptosyltransferase II) (Heptosyltransferase II) (P37421)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- ADP-L-glycero-D-manno-heptose-6-epimerase
- Lipopolysaccharide heptosyltransferase 1
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Bifunctional protein HldE
- Glucosyltransferase I
- O-antigen ligase
- Phosphoheptose isomerase
- Lipopolysaccharide core heptose
- NADH-quinone oxidoreductase subunit C/D
- Lipopolysaccharide 1,3-galactosyltransferase
Sequence:
MKILVIGPSWVGDMMMSQSLYRTLKARYPQAIIDVMAPAWCRPLLSRMPEVNEAIPMPLGHGALEIGERRRLGHSLREKRYDRAWVLPNSFKSALIPFFANIPHRTGWRGEMRYGLLNDARVLDKDAWPLMVERYVALAYDKGVMRAAKDLPQPLLWPQLQVSEGEKSLMCSDFSLSSERPLIGFCPGAEFGPAKRWPHYHYAELAKQLINEGYQVVLFGSAKDHEAGNEILAALNSEQQAWCRNLAGETQLEQAVILIAACKAIVTNDSGLMHVAAALDRPLVALYGPSSPDFTPPLSHKARVIRLITGYHKVRKGDTAQGYHQSLIDITPQRVLEELHSLLSEEGV
Protein: Probable ribonuclease ZC3H12D (EC 3.1.-.-) (MCP-induced protein 4) (Transformed follicular lymphoma homolog) (Zinc finger CCCH domain-containing protein 12D) (Q8BIY3)
Organism: Mus musculus (Mouse)
Function: May regulate cell growth likely by suppressing RB1 phosphorylation (By similarity). May function as RNase and regulate the levels of target RNA species (Potential). In association with ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in activated macrophages. Serve as a tumor suppressor in certain leukemia cells (By similarity). Overexpression inhibits the G1 to S phase progression through suppression of RB1 phosphorylation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A2A288}. Cytoplasm, P-body {ECO:0000250|UniProtKB:A2A288}. Note=Colocalizes with ZC3H12A in GW bodies (GWBs). {ECO:0000250|UniProtKB:A2A288}.
Interaction partners:
Sequence:
MEHRSKMEFFQKLGYSQEDVVRVLGKLGDSALVNDVLQELIQTGSRPRAQEDPASGTGVVLIPRGCCGVQDSAQQGPGTRPRRGWRRSSPLLRPIVIDGSNVAMSHGNKEAFSCRGIRLAVDWFTDRGHTYIKVFVPSWRKEPSRSDTPIREQHVLEELERQAVLVYTPSRKVNGKRVVCYDDRYIVKVAYEKDGIIVSNDNYRDLQNENPEWKWFIEQRLLMFSFVNDRFMPPDDPLGRRGPTLSNFLSKKPRPPEPSWQHCPYGKKCTYGVKCRFYHPERPHHGQLSVADELRAKTRAWLGGGAEEPRTPSARSRPTTARLLPQEPGEHDLPPAPQPAVLAALNRSFARLTFSDTAASGVVSQSRGPDWMPTGVPTSWAPPSLRAGSAATIGLPGMRSLRTPNNPLSPGDLGSPICPQARLSERHRSRDMHSDLPPQRRPLEDPWALLPSSYCYLNHSVWSESAWGEDIFRGPSESAQPVANGGGTRPVHCSFFPPDQDHPVMASGPPLSDMALLTLLQRSQKTGAPLGDP
Protein: Ankyrin repeat and SOCS box protein 1 (ASB-1) (Q9WV74)
Organism: Mus musculus (Mouse)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Mediates Notch-induced ubiquitination and degradation of TCF3/E2A and JAK2 (By similarity). May play a role in testis development.
Interaction partners:
- Cullin-5
- RING-box protein 2
- Elongin-B
- Elongin-C
Sequence:
MAEGGTGPDGRAGPGPAGPNLKEWLREQFCDHPLEHCDDTRLHDAAYVGDLQTLRNLLQEESYRSRINEKSVWCCGWLPCTPLRIAATAGHGNCVDFLIRKGAEVDLVDVKGQTALYVAVVNGHLESTEILLEAGADPNGSRHHRSTPVYHASRVGRDDILKALIRYGADVDVNHHLTPDTRPPFSRRLTSLVVCPLYISAAYHNLQCFRLLLQAGANPDFNCNGPVNTQEFYRGSPGCVMDAVLRHGCEAAFVSLLVEFGANLNLVKWESLGPEARGRRKMDPEALQVFKEARSIPRTLLSLCRVAVRRALGKYRLHLVPSLPLPDPIKKFLLYE
Protein: Receptor-binding cancer antigen expressed on SiSo cells (Cancer-associated surface antigen RCAS1) (Estrogen receptor-binding fragment-associated gene 9 protein) (Q9D0V7)
Organism: Mus musculus (Mouse)
Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Predominantly located in the Golgi. {ECO:0000250}.
Interaction partners:
- Estrogen receptor
Sequence:
MAITQFRLFKVCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGVPDGSTGFSSRLAATQDMPFIHQSSELGDLDTWQENSNAWEEEEDAAWQAEEVLRQQKIADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS
Protein: DNA primase (EC 2.7.7.-) (F5HIN0)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}. Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
Interaction partners:
Sequence:
METTYRREALTVRVIFCTSGDSAETIADVLTGAPTSASFFSVLHDLFYSQILAPRVTLKLCLPARRPGNGTRCSPVLVLRTDASVASGFLGGRPLEASDIKYMLLSDQTAGLFKPLLEIIGGARAPPNQDACTFQSQVAWLRTKFVTALRKLYKMTPSPYWMLSAFGAQEAQFVLTSSFYFFEHTVVCTTETVSHLSRLFSPQQGQTLVSVTSHEELGQLYGTSPFRRRVPAFVAYVKEKLARDSLETEAIDRTIDQIRGKLMLSNQDLVHFIYISFYQCLNKRAFLRYSRQTSSSSALRELGEDPQLCGALHGEFRDHVQSYYHKKTYLSTYIDIRYVGGVLPDGYFGGSLVGERCVYWCGQSKDTASLLATISQQVPHLRLQNEFAGMLDVAALRGSDDGQFKEGLFSHSQALPLYRCEFLGKQFFTMLQEDGLERYWEQSVIFPGDQDWDMLSDKDLTYRIFYHDLSLSLPTLKEQLLVSRHEYFNPRLPVYRWVLDFDLPVCRDIDRTFEEVHSLCCSLREAILDIIQLLGPVDPRTHPVYFFKSACPPDEWRGEDVASTSFCRCHDKLGMRIIVPFPEGVCVVGSEPMVALTGILNRTIKLDPELVHRFPSIQKKGGPFDCGIYGRGRSVRLPHCYKVGLVGELCRLLKILVCHPAPNGKAQYVRRAFTLRELLHHSPGHSAGHVGRIIYSIMDRNENFLENKTISYLPAKIPHIFQRIETLSGRSIEDWLHSAVWDKAYDTICKFFPDEKAQQFSHVAFTQQGENIIQLRPRQGRHFLCINHNHKNKSKTVRVFLTLHSIRVSEVTVTLMSQCFASKCNNNVPTAHFSFVVPVGLAS
Protein: Replicative helicase loader DnaI (EC 3.6.4.-) (Primosomal protein DnaI) (P06567)
Organism: Bacillus subtilis (strain 168)
Function: Probably involved in DNA replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10844689}. Note=Forms foci near both cell poles and in the middle of cells (PubMed:10844689). {ECO:0000269|PubMed:10844689}.
Interaction partners:
- Replicative DNA helicase DnaC
- Replicative helicase loading/DNA remodeling protein DnaB
- Replicative helicase loading/DNA remodeling protein DnaD
- Chromosomal replication initiator protein DnaA
- Beta sliding clamp
- DNA polymerase III PolC-type
- TVP38/TMEM64 family membrane protein YtxB
- DNA primase
- DNA polymerase III subunit tau
- Uncharacterized protein YtxC
Sequence:
MEPIGRSLQGVTGRPDFQKRLEQMKEKVMKDQDVQAFLKENEEVIDQKMIEKSLNKLYEYIEQSKNCSYCSEDENCNNLLEGYHPKLVVNGRSIDIEYYECPVKRKLDQQKKQQSLMKSMYIQQDLLGATFQQVDISDPSRLAMFQHVTDFLKSYNETGKGKGLYLYGKFGVGKTFMLAAIANELAEKEYSSMIVYVPEFVRELKNSLQDQTLEEKLNMVKTTPVLMLDDIGAESMTSWVRDEVIGTVLQHRMSQQLPTFFSSNFSPDELKHHFTYSQRGEKEEVKAARLMERILYLAAPIRLDGENRRHP
Protein: Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] (P18155)
Organism: Mus musculus (Mouse)
Function: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency.
Subcellular location: Mitochondrion.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Bifunctional purine biosynthesis protein ATIC
- Aminomethyltransferase, mitochondrial
- Methionyl-tRNA formyltransferase, mitochondrial
- Thymidylate synthase
- Methylenetetrahydrofolate reductase
- Mitochondrial 10-formyltetrahydrofolate dehydrogenase
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Sequence:
MASVSLLSALAVRLLRPTHGCHPRLQPFHLAAVRNEAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRPEELEVFKSKQRGVATN
Protein: GH20156p (Q95TZ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVYNTESSANSAMQHYDCGISAQINMDSPANIGSAIAHGPQEISATSNVHMHQPHRQFSDCSMQNQPVTTPMHMSIQNSHMQQQNNLNLNLAPEGSSNINLLSNPQHQHQSRKLNAQADIAVSSPTPSHRATTPKQIRSGNTQQRDAKNAAPPTTTTNTHHQIPQGGAAANISKSHHDSLHNLQFSQHGHQQNMQPIYYVPIPQISQNFSANPSNYDIVGMPAVIQQRMSLNGSVHSLANSHQRIEQPSSACAVNNFYLQNNMPAAENAPRVPVSSSLGGPPTAGNNDQRQAGQDSITTANSSGATASLAGNLCSLSKLQQLTNCLESQPCNTSPGAQVNLAPSPHHPIPPNSTPPPHLLMQNRNISTPPNMLQTQVTPLQYKYYPGNMNIPPITSAQNTSRNTRNTPSAPVQHTSTPMGSGNNRTANVHISPNLMAPYGAINSYRMSPQQSPPTGSYSSGGDYPNSQIPMQMMNMQSQYQDACVLQRGTPSNPMYPTYSPYLPLNGSIRR
Protein: Immunogenic protein MPT70 (P9WNF5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Secreted.
Interaction partners:
- Protein DipZ
- ECF RNA polymerase sigma factor SigK
- NADH-quinone oxidoreductase subunit D
- Immunogenic protein MPT64
- Anti-sigma-K factor RskA
Sequence:
MKVKNTIAATSFAAAGLAALAVAVSPPAAAGDLVGPGCAEYAAANPTGPASVQGMSQDPVAVAASNNPELTTLTAALSGQLNPQVNLVDTLNSGQYTVFAPTNAAFSKLPASTIDELKTNSSLLTSILTYHVVAGQTSPANVVGTRQTLQGASVTVTGQGNSLKVGNADVVCGGVSTANATVYMIDSVLMPPA
Protein: UPF0060 membrane protein Rv2639c (P9WFN9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00010}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00010}.
Interaction partners:
Sequence:
MVVRSILLFVLAAVAEIGGAWLVWQGVREQRGWLWAGLGVIALGVYGFFATLQPDAHFGRVLAAYGGVFVAGSLAWGMALDGFRPDRWDVIGALGCMAGVAVIMYAPRGH
Protein: NADH-cytochrome b5 reductase 1 (EC 1.6.2.2) (Microsomal cytochrome b reductase) (P35) (P38626)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NADH-dependent reductase for KTI11/DPH3 and cytochrome b5. Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1. By reducing KTI11/DPH3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Cytochrome b5
- 2-
- Diphthamide biosynthesis protein 3
- 2-
- NADPH--cytochrome P450 reductase
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Protein KTI13
Sequence:
MAIDAQKLVVVIVIVVVPLLFKFIIGPKTKPVLDPKRNDFQSFPLVEKTILTHNTSMYKFGLPHADDVLGLPIGQHIVIKANINGKDITRSYTPTSLDGDTKGNFELLVKSYPTGNVSKMIGELKIGDSIQIKGPRGNYHYERNCRSHLGMIAGGTGIAPMYQIMKAIAMDPHDTTKVSLVFGNVHEEDILLKKELEALVAMKPSQFKIVYYLDSPDREDWTGGVGYITKDVIKEHLPAATMDNVQILICGPPAMVASVRRSTVDLGFRRSKPLSKMEDQVFVF
Protein: GDP-mannose pyrophosphorylase (A6MUT4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MGISDEKVVAVIMVGGPTKGTRFRPLSLNIPKPLFPLAGQPMVHHPISACKRIPNLAQIYLVGFYEEREFAMYVSSISTELRVPVRYLREDKPHGSAGGLYNFRDLIMEDNPSHIFLLNCDVCCSFPLPEMLEAHKRYGGMGTILVIKVSAESASEFGELVADPITNELLHYTEKPETFVSDRINCGVYVFTPDIFTAIQGVSSQRKDRANLRRLSSFEALQSATRNPPSDFVRLDQDILTPFAGKKKLYTYETMDFWEQIKTPGKSLKCSGLYLAQFRFTSPNLLASGDG
Protein: Magnesium transporter NIPA2 (A3KFD2)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASVASSSQVILPVAADSSSIGSVNTMDEVHYASTDFYIGLGLAVSSSLFIGSSFIIKKKALLKLASGDTSQRASEGGYGYLREWMWWMGVITMGIGEACNFAAYAFAPASLVTPLGALSVIVTAILSSRMLNERLNLLGSIGCALCLLGSTVIVIHSPKEEEVGSMADLALKMKDAGFLIYVILIILATGFIVVYVAPRYGHSNILVYISVCSLIGSLSVLSVKGLGLAIKETLAGNQQFTNWLTYFWLASVAMCVSVQLIYLNKALDIFNTSMVTPIYYVFFTTFVILASSILYKEWSCLGASDVIGNFVGFLTTIIGIFQMQLFRDVNISLYQVQRLVSRPSATLANADFSSSSTNLVDDYCMRQSNSNRRMVYT
Protein: G/U mismatch-specific DNA glycosylase (EC 3.2.2.28) (Double-strand-specific uracil glycosylase) (Mismatch-specific uracil DNA-glycosylase) (MUG) (P0A9H1)
Organism: Escherichia coli (strain K12)
Function: Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Exodeoxyribonuclease III
- Endonuclease III lyase)
Sequence:
MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQLKPQEAQHLLDYRCGVTKLVDRPTVQANEVSKQELHAGGRKLIEKIEDYQPQALAILGKQAYEQGFSQRGAQWGKQTLTIGSTQIWVLPNPSGLSRVSLEKLVEAYRELDQALVVRGR
Protein: Expansin-like protein 3 (Ddexpl3) (Q7KWS2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May serve to lubricate the movement of the cellulose microfibrils during cell growth and wall extension and/or may serve to maintain the fluid state of the slug cell wall.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Expansin-like protein 8
Sequence:
MKFNTIFLVLSIVKFILISAQSCPFSQSIINGASATFYTAIDAGNCGFEKLNGPLGPGNYMIAALGSKLYQNGAQCGQCFKISNSKNASVTVMATDSCHDAGYCQRDNHFDLSPAAFSILGPQSQGVLDGLSYVKVPCEVSGNVKIMMKDGSNDFWTSFFVFNSKVIIKQVSIKLSNSNQFVPLSQTTYNYWPTSITGGQFHVRIESIGGEFIYVTIPKVESRKVYETSGQFSTSCSNLNENNPINYKPQTFNSQQTSNNQNSNTQTPTKQPSPNSQNFIPSYCQQYIQKPNYIFAKESKEMLVLNENENIESNSLKLLPNFLLLILIILLNINF
Protein: Serine/threonine-protein phosphatase with EF-hands pef-1 (CePPEF) (EC 3.1.3.16) (Phosphatase with EF hands 1) (G5EBX9)
Organism: Caenorhabditis elegans
Function: Probably acts as a protein phosphatase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11312268}; Lipid-anchor {ECO:0000269|PubMed:11312268}. Perikaryon {ECO:0000269|PubMed:11312268}. Cell projection, dendrite {ECO:0000269|PubMed:11312268}. Cell projection, axon {ECO:0000269|PubMed:11312268}. Cell projection, cilium {ECO:0000269|PubMed:11312268}.
Interaction partners:
- BTB domain-containing protein
Sequence:
MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLTIKSAILIQKWYRRCEARLEARRRATWQIFTALEYAGEQDQLKLYDFFADVIRAMAEENGKGGVENGRNSPLMSALSHYAKPSLMDSEGETVKKMLEDTSPTNVDIDRNYKGPTLSLPLDKPQVAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASKTHRKSTLRERLGVVEESAVKELKEKLSSFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGLNLPWIALAPKVATLSEDGKYVMYKEDRRIAQVGGTHAQEKDIVESLYRHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKYTKRPLQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRPLLR