wanglab/gogpt-training-data huggingface dataset:
Protein: Protein kinase C-binding protein NELL2 (MEL91 protein) (NEL-like protein 2) (Q61220)
Organism: Mus musculus (Mouse)
Function: Required for neuron survival through the modulation of MAPK pathways (By similarity). Involved in the regulation of hypothalamic GNRH secretion and the control of puberty (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:32499443}. Note=Detected in the epididymal lumen. {ECO:0000269|PubMed:32499443}.
Interaction partners:
- Roundabout homolog 3
Sequence:
MHAMESRVLLRTFCVILGLGAVWGLGVDPSLQIDVLTELELGESTDGVRQVPGLHNGTKAFLFQESPRSIKASTATAERFFQKLRNKHEFTILVTLKQIHLNSGVILSIHHLDHRYLELESSGHRNEIRLHYRSGTHRPHTEVFPYILADAKWHKLSLAFSASHLILHIDCNKIYERVVEMPSTDLPLGTTFWLGQRNNAHGYFKGIMQDVHVLVMPQGFIAQCPDLNRTCPTCNDFHGLVQKIMELQDILSKTSAKLSRAEQRMNRLDQCYCERTCTVKGTTYRESESWTDGCKNCTCLNGTIQCETLVCPAPDCPPKSAPAYVDGKCCKECKSTCQFQGRSYFEGERNTVYSSSGMCVLYECKDQTMKLVENIGCPPLDCPESHQIALSHSCCKVCKGYDFCSEKHTCMENSVCRNLNDRAVCSCRDGFRALREDNAYCEDIDECAEGRHYCRENTMCVNTPGSFMCICKTGYIRIDDYSCTEHDECLTNQHNCDENALCFNTVGGHNCVCKPGYTGNGTTCKAFCKDGCRNGGACIAANVCACPQGFTGPSCETDIDECSEGFVQCDSRANCINLPGWYHCECRDGYHDNGMFAPGGESCEDIDECGTGRHSCTNDTICFNLDGGYDCRCPHGKNCTGDCVHEGKVKHTGQIWVLENDRCSVCSCQTGFVMCRRMVCDCENPTVDLSCCPECDPRLSSQCLHQNGETVYNSGDTWVQDCRQCRCLQGEVDCWPLACPEVECEFSVLPENECCPRCVTDPCQADTIRNDITKTCLDEMNVVRFTGSSWIKHGTECTLCQCKNGHLCCSVDPQCLQEL
Protein: 5'-3' exoribonuclease (EC 3.1.13.-) (A0A8I5ZUU8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFNIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCALCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFPFDVERSIDDWVFMCFFVGNDFLPHLPSLEIREGAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDERDQPAFTPSGILTPYALGSRNSPGCQVASNPRQAAYEMRMQSNSSPSISPNTSFASDGSPSPLGGLKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMPSEFEKGTKPFKPLEQLMGVFPAASGNFLPPTWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEENRRNSLGSDVLFVGKVHPLHDFILELYQTGSTEPVDVPPELCHGIQGKFSLDEEAILPDQTVCSPVPMLRDLTQNTAISINFKDPQFAEDYVFKAIMLPGARKPAAVLKPGDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVIPRGSGTGVYSNTAPPPANYQGNVYRPLLRGQAQIPKLMSNMRPQDNWRGPPPLFQQQRFDRSVGAEPLLPWNRMLQTQNAAFQPNQYQMLAGPGGYPPRRDDHRGGRQGYPREGRKYPLPPPSGRYSWN
Protein: Ribose-phosphate pyrophosphokinase 5, chloroplastic (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 5) (O64888)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Amidophosphoribosyltransferase 2, chloroplastic
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- ATP phosphoribosyltransferase 2, chloroplastic
- Probable ribose-5-phosphate isomerase 4, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Probable ribose-5-phosphate isomerase 2
- Probable ribose-5-phosphate isomerase 1
- Ribokinase
- ATP phosphoribosyltransferase 1, chloroplastic
Sequence:
MASIVQPSPTFPALNLRRSSLIRPPSSVRFPLKCNAADPYKFDGGNSAGFHLLTGDTVPASFSRTRLEDSIYQNTTRLRIFSGTANPILAQEISCYLGLDLGKIKIKRFADGEIYVQLQESVRGCDVFLVQPTCPPANENLMELLVMIDACRRASAKTITAVIPYFGYARADRKTQGRESIAAKLVANLITQSGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASKAISSEDLVVVSPDVGGVARARAFAKKLSDAPLAIVDKRRHGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTISKGAALLHQEGAREVYACTTHAVFSPPAISRLSSGLFQEVIITNTIPLSEKNYFPQLTVLSVANLLGETIWRVHDDCSGAIEPFSTLGID
Protein: ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1) (P01096)
Organism: Bos taurus (Bovine)
Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:7397110}.
Interaction partners:
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
Sequence:
MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD
Protein: Enhancer of split malpha protein (E(spl)malpha) (O97178)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the Notch signaling pathway.
Interaction partners:
- Enhancer of split m7 protein
- Enhancer of split mbeta protein
- Enhancer of split M2 protein
- Enhancer of split m3 protein
- Enhancer of split mdelta protein
- Enhancer of split mgamma protein
- Enhancer of split m8 protein
- Bearded
Sequence:
MCQQVVVVANTNNKMKTSYSIKQVLKTLFKKQQKQQQKPQGSLESLESVDNLRNAQVEEAYYAEIDENAANEKLAQLAHSQEFEIVEEQEDEEDVYVPVRFARTTAGTFFWTTNLQPVASVEPAMCYSMQFQDRWAQA
Protein: Small ribosomal subunit protein uS17 (C3SQY7)
Organism: Escherichia coli
Interaction partners:
- Elongation factor Tu
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS10
- Alternative ribosome-rescue factor A
- GTP pyrophosphokinase
- 50S ribosomal protein L11
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS11
Sequence:
MTDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL
Protein: LIM zinc-binding domain-containing protein (G5EEF6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVRITTTPRPWQPSGAATRIWRPEVTENTGPGQDQTPYRVNLQHSSDTRPPQGFNNSALPFETDQRVKHMQYNSPLGIYSDKSAAEQYVQQTQGLGDNSGARAAAQRQDEPAYLRSETLRLLKEQEHGSAGGAGTTLSNHPNPSGLPVCFMCTRPILGVMARAAGKNLHGDCLSCATCGNSLRNVGHHFIEDKFYCDIHGTQRKHGGRPGMDPNIFVKSSPTAAQPVHIQDSPRAAYHPQVNTARPVSVSPAPSAGSKTVTTHYHTPKTQGILSPGQRGVPTAAFGADLSKSVTYGGGVGPGGTHYDSNRLSPAPSQYSTQSRNQSQQHYQQHVVQAPPPVPSNPPPSNGLREMEDDDRVRAIECIARHQSELEQTQTQLSTLLESAIVYLQNLRPELELTEPIDNDAKSLETVKFEPTRAEQRVNEIRKKVLEDLEHLPILGDGMDSVPPPPPERKVFPFQSYQPIAPQFPVPAAESPVTQSLHDVLDEFYSLRKPTPTQNVAQSSDTTAEDSRNFLASRLGQVMIDENKKAGGSNGSSQHHNQQGSSYTKTSFERTTTETRPQQNTGAPRAGDFRGTGHLTTTTTTQQNGGRAPFCESCKQQIRGAFVLATGKSWCPEHFVCANSSCRRRLLECGFVEEDGQKFCESCFEQHIAPRCNKCSKPIISDCLNALQKKWHPTCFTCAHCQKPFGNSAFYLEQGLPYCEQDWNALFTTKCVSCRYPIEAGDRWVEALGNAFHSNCFTCARCNHNLEGESFFAKNGQPFCRLHA
Protein: Holliday junction branch migration complex subunit RuvA (Q9AE10)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00031}.
Interaction partners:
- Crossover junction endodeoxyribonuclease RuvC
- Holliday junction branch migration complex subunit RuvB
- UvrABC system protein C
- DNA repair protein RecN
- Probable transcriptional regulatory protein Cgl1663/cg1872
- DNA polymerase I
- Protein RecA
- UvrABC system protein B
- Single-stranded DNA-specific exonuclease
- DNA replication and repair protein RecF
Sequence:
MIASLRGTVINIGLSSAVIECNGVGYEVVTTPNTLSQLVRGEEALVLTTMVVREDAMKLYGFIDNESREMFSVLQTVSGLGPRLALACESVLSPLEISQAITNADAKTLQRVPGVGKRMADRLIVELKGKVAAFAAGVVDEGGEQISLPNANIASEVVVEQVSQALVGLGFSEKQSDDAVSFVLAADPSLDTSGALRAALAKLSGK
Protein: Ponticulin-like protein C3 (Q54LC0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- CMP/dCMP-type deaminase domain-containing protein
- PhoPQ-activated pathogenicity-related protein
- Probable phosphoglycerate mutase
- Secreted protein A
Sequence:
MKFTKSLLLLIVAVFASSNAAETFSNFQVTNSDANSPCVTTPVELKVNTCQSACGSILNVLPVTGSTSKFTFNQFGAQDTKCAATPTSSNEFTCVDGKSKVAIGSTTYSVVCVPDKTNSSESDSSDSTRIGASFALFALALLSMLAL
Protein: Recoverin 3 (Q1LUD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Rhodopsin kinase grk7a
- G protein-coupled receptor kinase
- Rhodopsin kinase grk7-b
- G protein-coupled receptor kinase
- Green-sensitive opsin-2
- Rhodopsin
- Green-sensitive opsin-1
- Rhodopsin
- Green-sensitive opsin-3
- Green-sensitive opsin-4
Sequence:
MGNAQSGGIPREILDDLKLTTRFSESEITQWYENFQKQCPTGRITLQQFEEIYGKFFPDSDATTYAQHVFRSFDANDDGTLDFKEYVVALHMTSSGKSTLKLEWAFSLFDVDKNGYVTKPEVIELSQAIFKLIPKDKQTSLPNDESTPEKRAEKLWAIFDKKDNERVAEGEFIEAIQSSDDGLRLIQYDHK
Protein: Sperm-specific class P protein 19 (O01829)
Organism: Caenorhabditis elegans
Interaction partners:
- MS Related Protein
- SH2 domain-containing protein
- Sperm-Specific family, class S
- Sperm-Specific family, class Q
- SH2 domain-containing protein
- PARP catalytic domain-containing protein
- YDG domain-containing protein
- Sperm-Specific family, class Q
- Sperm-specific class P protein 16
- SPerm CHromatin enriched
Sequence:
MSLTADPPACTVPAAGVSSTHKLVNGGAEKIVFKIKSSNNNEYRIAPVFGFVDPSGSKDVVITRTAGAPKEDKLVVHFASAPADATDAQAAFVAVAPAGTVTIPMSATA
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 (Cell adhesion protein SQM1) (Complex I-B18) (CI-B18) (NADH-ubiquinone oxidoreductase B18 subunit) (P17568)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:21310150}; Peripheral membrane protein {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space {ECO:0000269|PubMed:21310150}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
Sequence:
MGAHLVRRYLGDASVEPDPLQMPTFPPDYGFPERKEREMVATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEFERERRLLQRKKRREKKAAELAKGQGPGEVDPKVAL
Protein: Cell cycle regulator CcrZ (EC 2.7.1.15) (EC 2.7.1.229) (Cell cycle regulator protein interacting with FtsZ) (C0SPC1)
Organism: Bacillus subtilis (strain 168)
Function: Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (By similarity). May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0A0H2ZQL5}.
Interaction partners:
Sequence:
MNIDMNWLGQLLGSDWEIFPAGGATGDAYYAKHNGQQLFLKRNSSPFLAVLSAEGIVPKLVWTKRMENGDVITAQHWMTGRELKPKDMSGRPVAELLRKIHTSKALLDMLKRLGKEPLNPGALLSQLKQAVFAVQQSSPLIQEGIKYLEEHLHEVHFGEKVVCHCDVNHNNWLLSEDNQLYLIDWDGAMIADPAMDLGPLLYHYVEKPAWESWLSMYGIELTESLRLRMAWYVLSETITFIAWHKAKGNDKEFHDAMEELHILMKRIVD
Protein: Dyschronic, isoform E (B7Z048)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MRLGGSGIPYDGDPLTMSAAGNDYAELCDLGPSRWSARPYGYNATAAAAASFGLGPSMGGTQSSSSVPTGGSAGLSGHHLRSSGAPGPSSFEAEDIGMAFGMISPPPGSGPYVGSSAAAGGSRVGNSTSSLRGAGGRSGLYYSPPGTSYTIVERPHSPHYYFNSAGVPTKGGSLPGRGSAYLSSSPASHMAAGTAGTLPTSTAASGRSMGQHASSNGNKKRPISPEQVLRMFGATQSSSVPTSSYHYSNGGTRDRDRTGRRSPASSPPSTTHQIYRDRERERDRSVPNIHELTTRTVSMSRDQQIDHGFGICVKGGKDSGLGVYISRIEENSVAERAGLRPGDTILEVNGTPFTSINHEEALKRCVQILKSSRQISMTVRAPPTLNSTAPLHGFGPPSRDPMYASMAPPLHPQNQAAAAAAAAAASGAGLPFRQTCSWMDRHGRPASPPMEYGGRRSERRDRIRRVELLIEPGQSLGLMIRGGVEYGLGIFVTGVDKDSVADRSGLMIGDEILEVNGQSFLDVTHDEAVGQLKYHKRMSLVIRDVGKVPHSCTSIEMEPWDAYSPTGTRARRKGQIATMVEEKARSLLPRHHFASLSYYIAEYSAKAMTIDAFVAVLLEMLDTYEKHTLVTEIRELVFPEDRTRYDELVYRRERDPYSVDRHRRKGDPARDLPEYGCDEHRTRRGSETLLPEYEPDAEQELATKLSRSFDMKEEGGTLLGDKGVRRHQSMQRLSAEQNGGSTTEQTHEHNPNVVPDHRGNLHITVKKTKPILGIAIEGGANTKHPLPRIINIHENGAAFEAGGLEVGQLILEVDGTKVEGLHHQEVARLIAECFANREKAEITFLVVEAKKSNLEPKPTALIFLEA
Protein: Calcium-transporting ATPase 10, plasma membrane-type (EC 7.2.2.10) (Ca(2+)-ATPase isoform 10) (Q9SZR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Protein BONZAI 1
- Alpha carbonic anhydrase 8
- Vacuolar cation/proton exchanger 3
Sequence:
MSGQFNNSPRGEDKDVEAGTSSFTEYEDSPFDIASTKNAPVERLRRWRQAALVLNASRRFRYTLDLKREEDKKQMLRKMRAHAQAIRAAHLFKAAASRVTGIASPLPTPGGGDFGIGQEQIVSISRDQNIGALQELGGVRGLSDLLKTNLEKGIHGDDDDILKRKSAFGSNTYPQKKGRSFWRFVWEASQDLTLIILIVAAVASLALGIKTEGIEKGWYDGISIAFAVLLVIVVTATSDYRQSLQFQNLNEEKRNIRLEVTRDGRRVEISIYDIVVGDVIPLNIGDQVPADGVLVAGHSLAVDESSMTGESKIVQKNSTKHPFLMSGCKVADGNGTMLVTGVGVNTEWGLLMASVSEDNGGETPLQVRLNGVATFIGIVGLTVAGVVLFVLVVRYFTGHTKNEQGGPQFIGGKTKFEHVLDDLVEIFTVAVTIVVVAVPEGLPLAVTLTLAYSMRKMMADKALVRRLSACETMGSATTICSDKTGTLTLNEMTVVECYAGLQKMDSPDSSSKLPSAFTSILVEGIAHNTTGSVFRSESGEIQVSGSPTERAILNWAIKLGMDFDALKSESSAVQFFPFNSEKKRGGVAVKSPDSSVHIHWKGAAEIVLGSCTHYMDESESFVDMSEDKMGGLKDAIDDMAARSLRCVAIAFRTFEADKIPTDEEQLSRWELPEDDLILLAIVGIKDPCRPGVKNSVLLCQQAGVKVRMVTGDNIQTAKAIALECGILASDSDASEPNLIEGKVFRSYSEEERDRICEEISVMGRSSPNDKLLLVQSLKRRGHVVAVTGDGTNDAPALHEADIGLAMGIQGTEVAKEKSDIIILDDNFESVVKVVRWGRSVYANIQKFIQFQLTVNVAALVINVVAAISAGEVPLTAVQLLWVNLIMDTLGALALATEPPTDHLMDRAPVGRREPLITNIMWRNLFIQAMYQVTVLLILNFRGISILHLKSKPNAERVKNTVIFNAFVICQVFNEFNARKPDEINIFRGVLRNHLFVGIISITIVLQVVIVEFLGTFASTTKLDWEMWLVCIGIGSISWPLAVIGKLIPVPETPVSQYFRINRWRRNSSG
Protein: DNA polymerase catalytic subunit (EC 2.7.7.7) (EC 3.1.26.4) (P04293)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication.
Subcellular location: Host nucleus {ECO:0000305}. Note=The protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250}.
Interaction partners:
Sequence:
MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTGPTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSGGFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASFRGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDATTRFILDNPGFVTFGWYRLKPGRNNTLAQPAAPMAFGTSSDVEFNCTADNLAIEGGMSDLPAYKLMCFDIECKAGGEDELAFPVAGHPEDLVIQISCLLYDLSTTALEHVLLFSLGSCDLPESHLNELAARGLPTPVVLEFDSEFEMLLAFMTLVKQYGPEFVTGYNIINFDWPFLLAKLTDIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKIKLSSYKLNAVAEAVLKDKKKDLSYRDIPAYYAAGPAQRGVIGEYCIQDSLLVGQLFFKFLPHLELSAVARLAGINITRTIYDGQQIRVFTCLLRLADQKGFILPDTQGRFRGAGGEAPKRPAAAREDEERPEEEGEDEDEREEGGGEREPEGARETAGRHVGYQGARVLDPTSGFHVNPVVVFDFASLYPSIIQAHNLCFSTLSLRADAVAHLEAGKDYLEIEVGGRRLFFVKAHVRESLLSILLRDWLAMRKQIRSRIPQSSPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTIGREMLLATREYVHARWAAFEQLLADFPEAADMRAPGPYSMRIIYGDTDSIFVLCRGLTAAGLTAVGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVIYGGKMLIKGVDLVRKNNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRRITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQTREVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSPADPPGGASKPRKLLVSELAEDPAYAIAHGVALNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPEVWHPPDDVAARLRTAGFGAVGAGATAEETRRMLHRAFDTLA
Protein: Calcineurin subunit B (Calcineurin regulatory subunit) (Protein phosphatase 2B regulatory subunit) (Q9UU93)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Peptidyl-prolyl cis-trans isomerase
- Calcium-channel protein cch1
- Transcriptional regulator prz1
- Myosin 1 light chain cam2
- Uncharacterized protein C13G6.15c
- Cell division control protein 31
- Vacuolar calcium ion transporter
Sequence:
MGQSQSQIFEDLISNSSFSNEEIERIRKRFIKIDANQSGSIDRNEFLSIPSVASNPLASRLFSVVDEDGGGDVDFQEFINSLSVFSVHGNKEEKLKFAFKIYDIDRDGYISNGELYLVLKMMVGTNLREDQLQQIVDKTIMEVDKDRDGKISFEEFKDIVSGSNVTSSMTLDSF
Protein: LIM homeobox 1, isoform B (M9PJE4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGSASEDDDDDDPPHLRATALGLGVLGPNGPDSAGGPLGTSDISVQSMSTDSKNTHDDSDQGSLDGDPDGRGDSQAENKSPDDANGSKRRGPRTTIKAKQLEVLKTAFNQTPKPTRHIREQLAKETGLPMRVIQVWFQNKRSKERRMKQITSMGRPPFFGGARKMRGFPMNLSPGGLDDGPGFPYFAADAKFEFGYGGPFHPHDGPYFPGHPGGPMPFNAPGGPMDHSGPIPMVNEFGLTPEATFLGQAGGPPMQLQSAVGPPPPPPPPSAEHLMAAAAAAAQQQAAQQQQQQQQQQQQQQQQNAQQAANQTQQQQQQNGPRTNSPEFMSSANFSEPQNMQNEGLVW
Protein: Uncharacterized protein (Q9CRQ9)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
Interaction partners:
Sequence:
SGNYRQCPWGTASVQILIPPRACSDISHACGTGSLVAAIWAALHLRILLLSAVTFLFLADFLKNRRPKNYPPWPMRLPFVGCLFHLDPKQPHLSLQQFVKKYGNVLSLDFANIPSVVITGMPLIKEIFTQMEHNFMNRPVTLLRKHLFNKNGLIFSSDQTWKEQRRFALMTLRNFGLGKRSLEERIQEEAHYLVEAIRDEGGQPFDPHFNISNAVSNIICSITFGERFDYHDSQFQEMLRLLDEAMCLESSMMCQLYNIFPRILQYLPGSHQTLFRNWRKLQLFVSDIVNNHRRDWDPDEPRDFIDAFLTEMTKYPDKTTTSFNEENLICSTLDLFFAGTETTSTTLRWALLCMALYPEVQEKMQAEIDRVIGQARQPNLADRDSMPYTNAVIHEVQRMGNIIPFNVPREVAVDTQLAGFNLPKGIMVLSNLTALHRDPSEWTTPDTFNPEHFLENGQFKKRESFLPFSMGKRACLGEQLARSELFIFITTLFQKFTFKPPVNEKLSLQFRMAATVSPVSHRLCAIPRL
Protein: DNA-binding protein Ikaros (Ikaros family zinc finger protein 1) (Lymphoid transcription factor LyF-1) (Q13422)
Organism: Homo sapiens (Human)
Function: Transcription regulator of hematopoietic cell differentiation. Binds gamma-satellite DNA. Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (fikzfterminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells. Confers early temporal competence to retinal progenitor cells (RPCs) (By similarity). Function is isoform-specific and is modulated by dominant-negative inactive isoforms.
Subcellular location: Nucleus {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:21548011, ECO:0000269|PubMed:22106042, ECO:0000269|PubMed:23071339}. Note=In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events. {ECO:0000269|PubMed:17135265, ECO:0000269|PubMed:22106042}.; SUBCELLULAR LOCATION: [Isoform Ik2]: Nucleus. Note=In resting lymphocytes, distributed diffusely throughout the nucleus. Localizes to pericentromeric heterochromatin in proliferating cells. This localization requires DNA binding which is regulated by phosphorylation / dephosphorylation events (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Ik6]: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protein cereblon
- Histone deacetylase 1
- Paired amphipathic helix protein Sin3a
- Chromodomain-helicase-DNA-binding protein 4
- Paired box protein Pax-5
- DNA damage-binding protein 1
- Runt-related transcription factor 1
- Erythroid transcription factor
- Transcription factor COE1
- Histone deacetylase 2
Sequence:
MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS
Protein: Caveolin-2 (Q9WVC3)
Organism: Mus musculus (Mouse)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).
Subcellular location: Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-1
- Caveolin-3
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Proto-oncogene tyrosine-protein kinase Src
- Epidermal growth factor receptor
- Tyrosine-protein kinase Fyn
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin 5
Sequence:
MGLETEKADVQLFMADDAYSHHSGVDYADPEKYVDSSHDRDPHQLNSHLKLGFEDLIAEPETTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRSFSSVSMQLSHD