wanglab/gogpt-training-data huggingface dataset:
Protein: Type I restriction enzyme EcoKI specificity subunit (S protein) (Type I specificity subunit S.EcoKI) (S.EcoKI) (Type-1 restriction enzyme EcoKI specificity subunit) (P05719)
Organism: Escherichia coli (strain K12)
Function: The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. The M and S subunits together form a methyltransferase (MTase) that methylates A-2 on the top and A-3 on the bottom strand of the sequence 5'-AACN(6)GTGC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
Interaction partners:
- Type I restriction enzyme EcoKI methylase subunit
- Type I restriction enzyme EcoKI endonuclease subunit
- Type IV methyl-directed restriction enzyme EcoKMcrB subunit
- Type IV methyl-directed restriction enzyme EcoKMrr
- Protease 7
- Gamma-glutamyl phosphate reductase
- Type IV methyl-directed restriction enzyme EcoKMcrA
- Type IV methyl-directed restriction enzyme EcoKMcrBC
- Uncharacterized protein YbjD
- Small ribosomal subunit protein uS12
Sequence:
MSAGKLPEGWVIAPVSTVTTLIRGVTYKKEQAINYLKDDYLPLIRANNIQNGKFDTTDLVFVPKNLVKESQKISPEDIVIAMSSGSKSVVGKSAHQHLPFECSFGAFCGVLRPEKLIFSGFIAHFTKSSLYRNKISSLSAGANINNIKPASFDLINIPIPPLAEQKIIAEKLDTLLAQVDSTKARFEQIPQILKRFRQAVLGGAVNGKLTEKWRNFEPQHSVFKKLNFESILTELRNGLSSKPNESGVGHPILRISSVRAGHVDQNDIRFLECSESELNRHKLQDGDLLFTRYNGSLEFVGVCGLLKKLQHQNLLYPDKLIRARLTKDALPEYIEIFFSSPSARNAMMNCVKTTSGQKGISGKDIKSQVVLLPPVKEQAEIVRRVEQLFAYADTIEKQVNNALARVNNLTQSILAKAFRGELTAQWRAENPDLISGENSAAALLEKIKAERAASGGKKASRKKS
Protein: Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) (Synthetic lethal of unknown function protein 1) (P38324)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:12832395}.
Interaction partners:
- Structure-specific endonuclease subunit SLX4
- Crossover junction endonuclease MUS81
- ATP-dependent helicase SGS1
- Actin-related protein 2/3 complex subunit 4
- RecQ-mediated genome instability protein 1
- Regulator of Ty1 transposition protein 107
- Holliday junction resolvase YEN1
- Asparagine--tRNA ligase, cytoplasmic
- DNA topoisomerase 3
- Crossover junction endonuclease MMS4
Sequence:
MSQKIQQHQFPDFYCCYLLQSINKRQSFYVGSTPNPVRRLRQHNGKLAVGGAYRTKRDGSRPWEMIMIVRGFPSKIAALQFEHAWQHGYQTHYIAEKDRVVKHKAGGRTLHHKVALMKLLLKHEFFQRMNLIVEVFNIKAWEVWKQDKFFIERDRFPINIQINENALEEPKEKTVDVLMDHSDENLKVVEAVYTKVIENERNIFETFEKKLTTGVVRCEICEKEIDYTSEEQNLKPFVALCNNKDCGCVNHLKCLHRYFLDDEQLMVGRRNLIPRGGKCPKCDMFCDWTTLVKFSTRMKLAHGK
Protein: Tabersonine synthase (EC 4.-.-.-) (Hydrolase 2) (CrHL2) (A0A2P1GIW3)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Component of iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. tabersonine and catharanthine) biosynthesis pathway from 19E-geissoschizine. Catalyzes the conversion of O-acetylstemmadenine (OAS) to tabersonine, a precursor of vindoline.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}.
Interaction partners:
Sequence:
MGSSDETIFDLPPYIKVFKDGRVERLHSSPYVPPSLNDPETGGVSWKDVPISSVVSARIYLPKINNHDEKLPIIVYFHGAGFCLESAFKSFFHTYVKHFVAEAKAIAVSVEFRLAPENHLPAAYEDCWEALQWVASHVGLDISSLKTCIDKDPWIINYADFDRLYLWGDSTGANIVHNTLIRSGKEKLNGGKVKILGAILYYPYFLIRTSSKQSDYMENEYRSYWKLAYPDAPGGNDNPMINPTAENAPDLAGYGCSRLLISMVADEARDITLLYIDALEKSGWKGELDVADFDKQYFELFEMETEVAKNMLRRLASFIK
Protein: Large ribosomal subunit protein eL28 (60S ribosomal protein L28) (Q9GS21)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL15
Sequence:
MSQDLVWSIIKKNNAFLKSSHGLTLSAEPGNLRNKNSLKYSGLARRTTIDVAAVNGKVVVSSKIVKKAAFPAQSKKTTTFSTVNTRKTARFVKTLATQYAPELRAAALGRLHRVQSALRSAKKAAARKAKKN
Protein: RT03039p (Seminal fluid protein 65A) (B4ZJA2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seminal fluid protein 24F
- GEO08953p1
- trypsin
- SCP domain-containing protein
- RE43153p
- FI01450p
- GEO10376p1
- Uncharacterized protein, isoform C
Sequence:
MVWILRLLSILCASVLAYQKDDSANSIILNDGAITVNTSTSGLTEAEGNTYVPGPGFFQETFLGKKTIGSSPRLPDLGNNIVVMSESKQLKAGEKNIVNSKVQTVTRKPKMSKADIFHGIKLFQGPIHEQFENDLHDHHHD
Protein: Fms related receptor tyrosine kinase 3 ligand (A0A1W2Q6J3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Ubiquitin-like protein FUBI
- Receptor-type tyrosine-protein kinase FLT3
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein bL17m
Sequence:
MTVLAPAWSPNSSLLLLLLLLSPCLRGTPDCYFSHSPISSNFHMRISELTDYLLKDYPVTVAINLQDEKHCKALWSLFLAHRWIEQLKTVAGSKMQKLLEDVNTEIHFVTSCTFQPLPECLRFVQTNISHLLQDTCSQLLALKPCIGKACQNFSRCLEVQCQPDSSTLLPPESPGALGATELPKPQPRQLWLLLLLPLTVVLLAAAWCLRWQRTRRRVELRPGVPLPSHP
Protein: Ubiquitin-like-specific protease 2 (EC 3.4.22.-) (O13769)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ubiquitin-like protein pmt3/smt3
- SUMO-conjugating enzyme ubc9
- Ubiquitin-activating enzyme E1-like
- Ubiquitin-like-specific protease 1
- Monopolin complex subunit pcs1
- E3 SUMO-protein ligase pli1
Sequence:
MRDSKDALDDKSGSFTSLLPPFGKQRGTSPNDAIPIKSPLERLANSVTSPEKPTVRTAIQKDSPRRKQIDDDQTPPKHLKRSFQNVTVVSPRKKKTIDVVELPFTKGGYGGFYDPRPGCLKFTTHEINVSYTDTSIPVIHIPVQLLKRCCWLQGWRDNLVESPVHAIHLTLKNRDMKRITIGDSASLLFLYNPLHVESARAGLDLLDQSDFSLTSPSSAKEFKQLLTLKQSTIIPRTPQKTVRSIVKQTSSPHSSKMPKHSLPSSPTPFNSNSGDSLLSRIKNSNQSSSERPTANNGAQEQNQSSSSAGNTSNDFSTLCSQGSDKTLLSDASCTTILVYPFSGTNSIAITNTDLTRLNEGEFLNDTIVDFYLRYLYCKLQTQNPSLANDTHIFNTFFYNRLTSKDKDGKRLGHRGVRKWTQKVDLFHKKYIIVPINETFHWYLAIICNIDRLMPVDTKLEEQDEIVMSSVEQPSASKTRQAELTSNSPAILIFDSLANLHKGALNYLREYLLEEAFERKNVHLKSTDIRGFHAKVPQQSNFSDCGIYALHFVELFLETPEQVIANTLDKSLRRTDAKNFDQQWNLQKINTMRCDLKGLIRRLSTEWSSNNERQSLSSGSNDEEDKENDDDLAILPITN
Protein: P2X receptor D (P2XD) (Q54J33)
Organism: Dictyostelium discoideum (Social amoeba)
Function: P2X receptors are ligand-gated ion channels that play a role in intracellular calcium signaling. ATP does not evoke inward currents in p2xD. Not essential for osmoregulation.
Subcellular location: Contractile vacuole membrane {ECO:0000269|PubMed:19833731}. Note=Ligand binding domain within the lumen of the vacuole.
Interaction partners:
Sequence:
MDWDNIFSYNTAKIVTIKDRRLGGLHIIFMVLIIVYIVIYSTIYKKGYLLTETPVGSIRASLLAPNEFKDDSNFKYCDDNLIEYNFTKLECDYYDEAFVSFPVGDDVSFAVTTRVKTLDQVLNCSSKNPKCKYTTVSTRNVYVSDIEDFTILIDHTMFAPSSLIQYNSKQLKGYILDNDNNEIQINETINTVGIPGKPDILTIGKLLQLANIDLDGASSVNSTNSVRYDGVVALVFITYSNTFSYNTNNFKYVYSIQKVEDTEYGVPEAVILDNVSSRMYYNRHGIRLIFIQNGEIGSFNFQALLLTFVSGLGLLAISTVLVDQLAIRFLPERKTYSSHKFQITHGFSESRNKLRISQNEKDPLLLVETTKNNENNNNNDDYNDDDNEIFDDNNNGYQNIQNNNIIL
Protein: Histone deacetylase (EC 3.5.1.98) (A0A8I6AAJ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MNSPNESADGMSGREPSLEILPRTPLHSIPVAVEVKPVLPAAMPSSMGGGGGGSPSPVELRGALAGPMDPALREQQLQQELLVLKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLLGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGTGPGVSSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGSTLTGKFMSTSSIPGCLLGVALEGDTSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQMQLGKILTKTGELSRQPTTHPEETEEELTEQQEALLGEGALTMPREGSTESESTQEDLEEEEDEEEDEEDCIQVKDEDGESGPDEGADLEESSAGYKKLFADAQQLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGSMKSPTDHPTVVKHLFTTGPISQKMYAMLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLVELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLSVGKVLIVDWDIHHGNGTQQAFYDDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPSINAVATLEKVIEIQSKHWSCVQRFATGLGCSLREAQTGEKEEAETVSAMALLSMGAEQAQAAATQEHSPRPAEEPMEQEPAL
Protein: ARNT2 protein (Q86TN1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATPAAVNPPEMASDIPGSVTLPVAPMAATGQVRMAGAMPARGGKRRSGMDFDDEDGEGPSKFSRENHSEIERRRRNKMTQYITELSDMVPTCSALARKPDKLTILRMAVSHMKSMRGTGNKSTDGAYKPSFLTEQELKHLILEAADGFLFVVAAETGRVIYVSDSVTPVLNQPQSEWFGSTLYEQVHPDDVEKLREQLCTSENSMTGQWSSLYEAV
Protein: Protein FAM72C (H0Y354)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein FAM72B
Sequence:
MSTNICSFKDRCVSILCCKFCKQVLSSRGMKAVLLADTEIDLFSTDIPPTNAVDFTGRCYFTKICKCKLKDIACLKCGNIVVYHVIVPCSSCLLSCNNRHFWMFHSQAVYDINRLDSTGVNVLLRGNLPEIEESTDEDVLNISAEECIR
Protein: BHLHB2 protein (Basic helix-loop-helix domain containing, class B, 2, isoform CRA_a) (Basic helix-loop-helix domain-containing) (cDNA, FLJ92873, Homo sapiens basic helix-loop-helix domain containing, class B, 2(BHLHB2), mRNA) (Q6IB83)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
Protein: V-type proton ATPase subunit C (V-ATPase subunit C) (Vacuolar proton pump subunit C) (Q9HDW6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity). Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250|UniProtKB:P31412}; Peripheral membrane protein {ECO:0000250|UniProtKB:P31412}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d
- V-type proton ATPase subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase subunit D
- V-type proton ATPase subunit a
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c
- Probable V-type proton ATPase 20 kDa proteolipid subunit
- V-type proton ATPase subunit G
Sequence:
MSKSDFWILSVPSRGGSNADLCDDIERLLVSGSTSLISTVAPFDVPPFKVESLDVLISQSEQLTKQDAQCASAISKISDIIKNTVSSSSGDLKDYFMVQDKSPLEYVSSFAWNSSRFHMNKTISEISDRITSEIISFENDIRTRQTSFQQASSAFQNMQKKQSGNLSQKSLANIVHEEDVVHGSDYLTNVFIAVPLNLEKQFLNSYETLTDLVIPRSAKKLDQDSEFVLYTVVVFKKTADSFITKAREAKYTIREFTFEQGLRETEQSEFDDAAVKEKRMLSSLLRYASIAFSESFQGWIHLKCLCVYVESILRYGLPPDFSSVIFQPMAKSEVKIKNILLSKYAYLAQNPVGNNKVKNVDSSAGLDESMADLNLDEEYLPFVLFTVPSKVFNY
Protein: Suppressor of variegation 2-10, isoform C (A1Z7P9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPFPSLQECEQMVQMLRVVELQKILSFLNISFAGRKTDLQSRILSFLRTNLELLAPKVQEVYAQSVQEQNATLQYIDPTRMYSHIQLPPTVQPNPVGLVGSGQGVQVPGGQMNVVGGAPFLHTHSINSQLPIHPDVRLKKLAFYDVLGTLIKPSTLVPRNTQRVQEVPFYFTLTPQQATEIASNRDIRNSSKVEHAIQVQLRFCLVETSCDQEDCFPPNVNVKVNNKLCQLPNVIPTNRPNVEPKRPPRPVNVTSNVKLSPTVTNTITVQWCPDYTRSYCLAVYLVKKLTSTQLLQRMKTKGVKPADYTRGLIKEKLTEDADCEIATTMLKVSLNCPLGKMKMLLPCRASTCSHLQCFDASLYLQMNERKPTWNCPVCDKPAIYDNLVIDGYFQEVLGSSLLKSDDTEIQLHQDGSWSTPGLRSETQILDTPSKPAQKVEVISDDIELISDDAKPVKRDLSPAQDEQPTSTSNSETVDLTLSDSDDDMPLAKRRPPAKQAVASSTSNGSGGGQRAYTPAQQPQQSGGNVFKKPQKAEELYKRVHLGVWLRPRKPKPESSRRPNVG
Protein: Synaptojanin-2-binding protein (Mitochondrial outer membrane protein 25) (NPW16) (Q9WVJ4)
Organism: Rattus norvegicus (Rat)
Function: Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:10357812}.
Interaction partners:
- Ribosome-binding protein 1
- Synaptojanin-2
Sequence:
MNGRVDYLVSEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIYVSRIKEDGAAARDGRLQEGDKILSVNGQDLKNLLHQDAVDLFRNAGYAVSLRVQHRLPVQNGPIVHRGDGEPSGVPVAVVLLPVFALTLVAVWAFVRYRKQL
Protein: Hybrid signal transduction histidine kinase A (EC 2.7.13.3) (Q54U87)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a receptor histidine kinase for the cytokinin SDF-2 in a signal transduction pathway that regulates prestalk gene expression and controls terminal differentiation of prespore cells. Binding of SDF-2 to this protein inhibits phosphorelay and induces rapid sporulation. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Acyl-CoA-binding protein
- Serine protease/ABC transporter B family protein tagC
Sequence:
MELKTFKDLNDDIIGDTSPVINTGDQPNPLRTQQQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHHIPQQLYQKQQQQQHSHSYGNHSFIHNVSPTSPSYDINNNNNNNNNNNNNNNNNNNNNNNSNNNNNNNNNNKNNYNNNYYYSPIENSNISKSLEESVLNQFPHNFNLNSSNNNYLNNSSSLHNINQSVNSLSNNNNNQTNQQPINNNNNNNNNNNNNNSNNSNNSNNNNNGNNNNNITDSPTKSKRHSTYETNIGSHQRRKSIQSLIANSAIHSFSKLKNKPLSSSTPSTVNTCGAVNNNSNNNNNNNNNSTGSLGAIPMDRSFDGNINTITEESTGGNNSPRSNCGSNCGSNGGIPLSPRNLSSLNSGVNVSPRNIHLNNLNNNSSNLPPLSPRHINFHINVSNLNNNNNNNINPNNNPNNSNNSNNNVSPRNNNHNISPRGSNISPRSNNGGSTTISPRNISNNNNIINNINNNNILTPPRNSPRLENVNPTNSPRLLATSLNSTLPIVSSLTSSNNNNQSNNNTNPSINNNNGRNGHCIQTISEEILGNKPVVYNNGNNNNNNNTNNSTTSNNNITTNNNNNNNNNINNNVLSTPRKRTKGNHSKTNSLQDFETSSMNGGDDSISGAGSGGSLRRRNKDDNDENDGNSNNTNSNNSNNNNNNNNNSSNNNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNYHNGATMMMSHNHQSIGMSSSPKKNNFKPFSRNCSLMGMGRRAWAIILGLFIVGSSISILATLVLRYSEENSIADDFARVARDRFTMLRIEFNNRLYITQTLSLLLSVFPSTSEDQFVPFSKLWSDNAEGLEGIMWAPRVSNLDRYTWEIEHSVKIREIVTNPNNSSDMRDVPAAAASDYYPILFSEPQSSNDHFKGYNIYSDMWRRPSLNKTRDTGEKVSVASPYINKLANVPKNSRSNVLLYIYQAVYTYGKVLSTVEDRRHEVIGFASCRFFISRMVSASLQRLTEEDSLDLYVFDLDSTPIGELIYYRASNAGNDDGSSPTNIMNGKMLEDRSDMIYYNTMNVGGRNWMIALRPSRKFTNKHYTFYPYAIGGVCMLLSALVSFWFAVNTKHNIKLSATNEDLHKEIYNRKLAEKALAESQERLELAMEGSEDAVWDWKVNTGELHISSRWFQILKAHDTSYQSRTLYEELKSSSTNNLNFKGDSKNGGSNNGTFNLFKNGKVDSSSPQSITNVNTTNGGGGGELRKSNSGYLYNDELFSPIILEEMVSSPNTHQLAIWNMKFLAELIHPDDKQKFISEIKKTITRETSIMEIECRMRKKYGGYLYIIMRGKVVSNETSFKDNSLRMAGTLRDMTSRKDMQRLILEKEAAEEANKAKSAFVATVSHEVRTPLSGVIGVSDLLLETNLSEEQRDYVQTIQKSSQALLTIINDILDYSKLESRQLKMETLPFSIIETCQAVIHMLSVAANDDVDILLRVPPNVPRIIFGDAMRMRQVLLNLLSNAIKFTSRGHVLTDISVDDSIPPTNTEEEIIHLCITIEDTGIGIPQSLFDSIFEPFSQADNSTTRKYGGTGLGLSITKRLIEEVMGGTIQVSSIVGQGSKFKCIIPFLLPNTSPSDLNLISPSSLPKPFINRSPKSTYSFTDKKNSVPSTPIPSGDILINKVCLLICRDTVTELVFKEQLEWLGMIVKQVPRNVIDSIKNTILNNNNNNNNNNNNNNNNSNNSSSIISPSSLDYSDENEHLDLVLIDLEILTEHLKIPSNVPIIFITPTKFNISKHNGILNKWITKSPNQRVELIRRPAITDKLIPIISKCIKSQVQFTSGSSQLQSQQANLQQQLLHQQLCNNGQTLNNNYNSGGIGGGGGGGGSNTMNGSSGNLSNNNNFGQTPLSSGLVLLVHTGRTPPLFNNNGNSIIPPLELAVDHHGNQQQQLYQQQQQQQNNSSGNFQQFYQQQNNNSNNSFTPTLPNENSNNSIMNNSLNNNNTTPSNVTPTLFTSSPLDLQGRDTPVLQPPAYRKKALIVEDNELNRKVLAQLFKKIDWTISFAENGREALKEITGERCFDIVFMDCQMPVLDGFQTTKIIRSKERENNWKRMNIVALSAGSSSSFVQDCLDSGMDSFMGKPITLATLKDALAKWGGYNN
Protein: CTP synthase (EC 6.3.4.2) (CTP synthetase) (UTP--ammonia ligase) (O42644)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Interaction partners:
- Nucleoside diphosphate kinase
- Inosine-5'-monophosphate dehydrogenase
- GMP synthase
- Glutamate synthase
- Golgi apyrase
- Glutamine synthetase
- Amidophosphoribosyltransferase
- Probable arginine--tRNA ligase, cytoplasmic
- 25S rRNA adenine-N
- Asparagine synthetase domain-containing protein C4F6.11c
Sequence:
MKYVLVSGGVISGIGKGVIASSTGLLLKTLGLKVTSIKIDPYMNIDAGTMSPLEHGEVFVLNDGGEVDLDLGNYERYLNVTLTHDNNITTGKVYSNVIQKERRGDYLGKTVQIVPHVTNEIQDWVERVARIPVDQSGEEPDVCIVELGGTVGDIESAAFVEAMRQFQFRVGHENFVSIHVSLVPVINGEQKTKPTQQAIRDLRSLGITPDLIACRCKQPLEKSVIDKISLFCHVGPEQVLAVHDVSSTYHVPQLLEDKLLEYLKIRFALDKISVSRELALAGENMWSSWKHLTQGYDHLFKKVTIVLVGKYTHLQDSYISVIKALEHSAMRCGRKLDLQWVEASHLEASTNTSDPLSYHKAWHLVCSANGILVPGGFGSRGVEGMIAAAKWARENNTPYLGICLGMQVAVIEFARSVCGIEGAFSEEFDKECENNVVVYMPEIDKDKLGGTMRLGLRPTFFQPNSEWSKLRKLHKMVDEVLERHRHRYEINPAFVSRLEQGGISFIGKDERGERMEIIEKRDHPYFVGVQYHPEYLSKPLKPSPPIFGLVAASAGLLDEFIQSGEEVEWSNFSHFNAESALADMNDSVEVTEEATVVTIS
Protein: Protein cornichon homolog 3 (CNIH-3) (Cornichon family AMPA receptor auxiliary protein 3) (Q8TBE1)
Organism: Homo sapiens (Human)
Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization.
Subcellular location: Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). {ECO:0000250}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Glutamate receptor 3
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-8 subunit
- Protein shisa-9
- Voltage-dependent calcium channel gamma-2 subunit
- Cytosolic 5'-nucleotidase 1A
- Voltage-dependent calcium channel gamma-3 subunit
- Glutamate receptor ionotropic, NMDA 3A
Sequence:
MAFTFAAFCYMLSLVLCAALIFFAIWHIIAFDELRTDFKSPIDQCNPVHARERLRNIERICFLLRKLVLPEYSIHSLFCIMFLCAQEWLTLGLNVPLLFYHFWRYFHCPADSSELAYDPPVVMNADTLSYCQKEAWCKLAFYLLSFFYYLYCMIYTLVSS
Protein: Chromosome transmission fidelity protein 8 homolog (hCTF8) (P0CG13)
Organism: Homo sapiens (Human)
Function: Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DSCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single-stranded and primed DNAs and has weak ATPase activity that is stimulated the presence of primed DNA, replication protein A (RPA) and proliferating cell nuclear antigen (PCNA). The CTF18-RFC complex catalyzes the ATP-dependent loading of PCNA onto primed and gapped DNA. It also interacts with and stimulates POLH, which is suggestive of a protein network that coordinates DNA repair, recombination and chromosome cohesion reactions with replication fork progression.
Subcellular location: Nucleus {ECO:0000269|PubMed:12766176}. Note=Associates with chromatin during S phase. {ECO:0000269|PubMed:12766176}.
Interaction partners:
- Replication factor C subunit 5
- Chromosome transmission fidelity protein 18 homolog
- Replication factor C subunit 2
- Sister chromatid cohesion protein DCC1
- Replication factor C subunit 3
- Replication factor C subunit 4
- Structural maintenance of chromosomes protein 3
- N-acetyltransferase ESCO1
- WD repeat and HMG-box DNA-binding protein 1
- N-acetyltransferase ESCO2
Sequence:
MVQIVISSARAGGLAEWVLMELQGEIEARYSTGLAGNLLGDLHYTTEGIPVLIVGHHILYGKIIHLEKPFAVLVKHTPGDQDCDELGRETGTRYLVTALIKDKILFKTRPKPIITSVPKKV
Protein: Dihydropyrimidinase-related protein 2 (DRP-2) (Collapsin response mediator protein 2) (CRMP-2) (Turned on after division 64 kDa protein) (TOAD-64) (P47942)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but noncovalently associated with membranes. {ECO:0000269|PubMed:7472434}.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Protein numb homolog
- Cyclin-dependent kinase 5
- Dihydropyrimidinase-related protein 5
- Tyrosine-protein kinase
- Dihydropyrimidinase-related protein 3
- Plexin-A1
- Semaphorin-3A
- Glutamate receptor ionotropic, NMDA 2A
- Numb-like protein
Sequence:
MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
Protein: RH61354p (Q8MT16)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPSVDELDTKFAELVEELDLTAPNKEAMLSLPAQKKWQIYCSRKLPLDAADGPDAAAVTQPPTAEHYIERLKELVVHISLSPEDSPSHELGNRLDGHAAFVDALKTALRTSTHSFVLRFVELDGLPALLDLLLQLDIRVANSPLHTSLIGCIKALMNNSMGRAHVLAHPTAIDTIARSLAADNIRTKIAALEILGAVCLVPGGHRKVLQAMLHFQVFATERTRFQSIVNDLDRSTYAYRDNVNLKTALMSFVNAVHNYGPGQENLEFRLHLRYEFLMLGIQPVIDKLRTHENETLDRHLDFFEMVRAEDEKEFARRFKEEHVDTKSAGSMFELLRRKLSHSPAYPHMLSLLQHMLLLPYTGHCTEHWLLIDRVVQQIVLQVEQRPNSDLIVDPDDPEKQLKLAAESPVHDPDVAPLQIDVAKLVRLLVKEEQLTQARKRADELERENFDVQSRLAKKEQELDLRMQEKEDLETGLARMRERLEKESAQHSQAVQRAQTAEMRAEDLQHRLISEQQERARLERLVTEGSIPDDQKVAGLTGCNGAVSPPPAPPMLKAIPPPPPPMAPSMMPPPPPPCPGAPPPPPSMAQTMAPAPPKVDLPKKNVPQPTNPLKSFNWSKLPDAKLQGSVWSELDESKLYNNMELESIDKLFSAYQKNGVSATDGSYEDLRVTGKAAKQKVLSVIDGRRAQNCTILLSKLKMSDMEISKAILSMDSNEQLQLDMVEQLLKFTPSAEERALLDEHSEDIESLARADRFLYEISKIPHYEQRLKSLHYKKRFMLTINDLVPRITSVMEASREVARSRRLRKLLELVLALGNYMNRGARGNASGFRLASLNRLADTKSSAAKGTTLLHYLVQVIERKFKDLLKLEDDIPHVREASKVSLGEMDKDIQMLRTGLADVAREIEFHRSSGPAQQGDRFLPVMREFHAQASVRFAELEDKFQDMKTRFDRAVRLFGEDGSVLQPVEFFGIFDSFLAAFAEARHDNESFRRRQEEEEKRAKQEAELKKRTIERKNKTGLMTSVARNLGLKSGSSNGDPDSPAKGGDNKGEFDDLVSALRTGDVFGEDMAKFKRSRKARVLNGGGSSTGHTSPPRHGSLQREESGRERERTVRRQ