wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear egress protein 2 (P03185)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network (By similarity). Inhibits host IKBKE and IRF3, thereby impairing type I IFN signaling.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:10708440, ECO:0000269|PubMed:15731265}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:33391252}. Note=Also localizes at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
Interaction partners:
Sequence:
MASPEERLLDELNNVIVSFLCDSGSLEVERCSGAHVFSRGSSQPLCTVKLRHGQIYHLEFVYKFLAFKLKNCNYPSSPVFVISNNGLATTLRCFLHEPSGLRSGQSGPCLGLSTDVDLPKNSIIMLGQDDFIKFKSPLVFPAELDLLKSMVVCRAYITEHRTTMQFLVFQAANAQKASRVMDMISDMSQQLSRSGQVEDTGARVTGGGGPRPGVTHSGCLGDSHVRGRGGWDLDNFSEAETEDEASYAPWRDKDSWSESEAAPWKKELVRHPIRRHRTRETRRMRGSHSRVEHVPPETRETVVGGAWRYSWRATPYLARVLAVTAVALLLMFLRWT
Protein: Uncharacterized protein YKL187C (P34231)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}.
Interaction partners:
Sequence:
MRIEKHRTPLSKGIIWTILSVCLLFMFTTLILVIVATAGSTANYKPLTNIYIGEADIKHINVSKVIPQIGPILTILGSALTAPNSSLDDIFGAMKNIADTPALTPLLTLLSNADNTTVTIESLTELAPLAISGNPASSTRQLTEINGLLKYSDNATETLDGLSRLVSASLSSASSNSSSDSTTLVLDLLKDSDNPQNSTDALLTLNNLTMSEKAQLLPVFRLFAFSTNQTATMTALATLMNTTISSSLAQTLLTQLQNTISNGGSLNNTFSTLQPLVPQASAPAFDAVELLLNQTTSTNQTLSTLSDLLEQNLTQSSSAKKAFAALTQLMENSDNSTMVVTSVQSLAAVTNTTQSTQQLIGLDDVISSSSNTNETLSILSELQSGLSGNSSSVQYIPYLFSLLGASTDPKTTFSSLVTLTSWAQENPQTFLPILDILADAKSVQPISAEELNAMTPNILEYLKIPIYYRLSIFTLCHANLENKILDCNSPHAVQNLDFRSIIYDALVTSDFQPYLNALNISANDLYLEGKLLHREHQYVPAVRSVLALNLLAIIFSFFTMIFIILLYFNRYMFKQPLWLIALALHVCVGVATVLAAIIISVMIAIIKSGTADDKYGVVFKAGPAYTGLIWTAFALSFIATGLIIYTWWRNRRSGRYMSGSVTNRKGEIYTYGDGSAISADRFGDHNLGDDDDADFEKQVNRNEITAIDNSSSANNTDVTGSTSNRTELSHPDVTPKDSNGPVNNNAHLVA
Protein: Plant cysteine oxidase 5 (AtPCO5) (EC 1.13.11.20) (Q9LXT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of N-terminal cysteine residues (N-Cys), thus preparing the protein for N-end rule pathway-mediated proteasomal degradation, upstream of the N-end rule enzymes ATE1, ATE2 and PRT6 (Probable). Controls the preparation of the group VII ethylene response factor (ERF-VII) proteins for degradation via the 26S proteasome N-end rule pathway (Probable). Acts as an oxygen sensor that controls the stability of ERF-VII proteins, which are stabilized in flooding-induced hypoxia, and regulate transcriptional adaptation to these adverse conditions (Probable).
Subcellular location: Nucleus {ECO:0000305|PubMed:24599061}. Cytoplasm {ECO:0000305|PubMed:24599061}.
Interaction partners:
- E3 ubiquitin-protein ligase PRT6
- Arginyl-tRNA--protein transferase 1
- Arginyl-tRNA--protein transferase 2
- Ethylene-responsive transcription factor RAP2-12
- Aminopeptidase
Sequence:
MPYFIQRLFNTCKSSLSPNGPVSEEALDKVRNVLEKIKPSDVGLEQEAQLVRNWPGPGNERNGNHHSLPAIKYLQLHECDSFSIGIFCMPPGSIIPLHNHPGMTVLSKLVYGSMHVKSYDWAEPDQSELDDPLQARPAKLVKDIDMTSPSPATTLYPTTGGNIHCFKAITHCAIFDILSPPYSSTHGRHCNYFRKSPMLDLPGEIEVMNGEVISNVTWLEEYQPPDNFVIWRVPYRGPVIRK
Protein: Neprilysin-like 21 (Q9Y136)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- GH23891p
Sequence:
MGIKAKHNAKQLLCICIAGHVLSAMVAAAPTSEEDLKQDTPYMKELLRQAKTAEIESFMDQKADPCNDFYAFSCGNYKRINSALSMQVVTTGVFETLTKGLNRKILKMLNTPHDSHDTPEDIKVKHFYESCLQIKELNSTYSEKLKRLIAEFGTMPLLEGSSWQEDDFDWLNTTARMAYRYGITPIFGIEVNKDLASNTRNRIYLGQQDFPLEARSMYVDDATAVYRQKYRNNIQRILQRYLGVKMDLAKKTAKELIDFEVDLAQGLVDESEGLDVGELTQLLTVDEIQRRYSPTLDIDRLLFVSMGERISDQIYEYNNRYQQNLVEVIKRTPKRTVANYIFFRLIWEFVETPSDSPEKQMKACVDLTKKYFAKNLDNMFYRRYNNEKSSREIDNMWRQLKSTFNETLRSSPALNWIERPTRNLAMAKLQAMTLEVNNYADDNFTEEFAELNLQSDDYVENVRYTSLLGAKQMREMLHKPAKPFEAGSQLSYTPANILIENTIKVPVALLQPFYIWSDVYPNAIMFGTLASLIGHELIHGFDDSGRKFDEKGNSKDWWDEKSSSNFLKRRDCFTKQYGRYVYDGIQLKESTAQSENIADNGGMRLAYTAYRKWYENQLTLPNGAQDMTKETLPNLRYTAKQLFFISFAQSWCNDAHPSVKALQVSTDQHMPGRFRVIGSLSNFEEFSKEFNCPAGSAMNPSEKCILY
Protein: Integrin alpha 6 subchain (Q924W2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
DNDADPMSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETDHDESLVPVPANSYLGFSLDSGKGIVSKDDITFVSGAPRANHSGAVVLLKRDMKSAHLLLEYIFDGEGLASSFGYDVAVVDLNADGWQDIVIGAPQYFDRDGEVXGAVYVYINQQGRWSNVKPVRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSPTGIITKPTQVLEGTTPFFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINILKTITVTPSRIDLRQKSMCGSPSGICLKVKACFEYTAKPSGYNPPISILGILEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLNRQKQRACMEETLWLQENIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSNEAKTVQTDVHFLKEGCGDDNVCNSNLKLEYKFGTREGNQDKFSYLPIQKGIPELVLKDQKDIALKITVTNGPSDPRNPRKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSSVTFYLILSTTEVTFDTTDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEEEVGSLIEYEFRVINLGKPLKNLGTATLNIQWPKEISNGKWLLYLMKVESKGLEQVVCEPHNEINFLKLKESHNSRKKRELPEKQIDDSRKFSLFSERKYQTLNCSVNVRCVNIRCPLRGLDSKASLVLRSRLWNSTFLEEYSKLNYLDILVRASIDVTAAAQNIKLPHAGTQVRVTVFPSKTVAQYSGIAWWIILLAVLAGILMLALLVFLLWKCGFFKRNKKDHYDATYHKAEIHTQPSDKERLTSDA
Protein: GBLP_NEUCR Guanine nucleotide-binding protein beta subunit-like protein (Cross-pathway control WD-repeat protein cpc-2)Gbeta like protein (G5EB28)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 60S ribosomal protein L21, putative
- 40S ribosomal protein S29
- 60S ribosomal protein L6
- 60S ribosomal protein L7
- 40S ribosomal protein S6
- Ribosomal protein L26
- Uncharacterized protein
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- 60S ribosomal protein L12
- 60S ribosomal protein L23
Sequence:
MAEQLVLRGTLEGHNGWVTSLATSLENPNMLLSGSRDKTLIIWNLTRDEQAYGYPKRSLEGHSHIVSDCVISSDGAYALSASWDKSLRLWELSSGQTTRTFVGHTNDVLSVSFSADNRQIVSGSRDRTIKLWNTLGDCKYTITDKGHTEWVSCVRFSPNPQNPVIVSAGWDKLVKVWELASCRLQTDHIGHTGYINTVTISPDGSLCASGGKDGVTMLWDLNESKHLYSLHAGDEIHALVFSPNRYWLCAATSSSITIFDLEKKSKVDELKPEYIEKGKKSREPECVSLAWSADGQTLFAGYTDNKIRAWGVMSRA
Protein: At5g65760 (Lysosomal Pro-X carboxypeptidase) (Serine carboxypeptidase S28 family protein) (Q1JPM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine carboxypeptidase-like 26
- Prolyl endopeptidase
- Serine carboxypeptidase-like 34
- Serine carboxypeptidase-like 42
- Proteasome subunit alpha type-5-B
- Serine carboxypeptidase-like 46
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- ATP-dependent Clp protease proteolytic subunit 2, mitochondrial
- Serine carboxypeptidase-like 25
Sequence:
MASHFCLLLIFTFFTLVFPSNGSSLSSSKLLPRFPRYTFQNREARIQQFRGDRNEYRYETKFFSQQLDHFSFADLPKFSQRYLINSDHWLGASALGPIFLYCGNEGDIEWFATNSGFIWDIAPKFGALLVFPEHRYYGESMPYGSREEAYKNATTLSYLTTEQALADFAVFVTDLKRNLSAEACPVVLFGGSYGGMLAAWMRLKYPHIAIGALASSAPILQFEDVVPPETFYDIASNDFKRESSSCFNTIKDSWDAIIAEGQKENGLLQLTKTFHFCRVLNSTDDLSDWLDSAYSYLAMVDYPYPADFMMPLPGHPIREVCRKIDGAGSNASILDRIYAGISVYYNYTGNVDCFKLDDDPHGLDGWNWQACTEMVMPMSSNQENSMFPGYGFNYSSYKEECWNTFRVNPRPKWVTTEFGGHDIATTLKSFGSNIIFSNGLLDPWSGGSVLKNLSDTIVALVTKEGAHHLDLRPSTPEDPKWLVDQREAEIRLIQGWIETYRVEKEAKVSLLKRSW
Protein: Flavin reductase (NADPH) (FR) (EC 1.5.1.30) (Biliverdin reductase B) (BVR-B) (EC 1.3.1.-) (Biliverdin-IX beta-reductase) (Green heme-binding protein) (GHBP) (NADPH-dependent diaphorase) (NADPH-flavin reductase) (FLR) (S-nitroso-CoA-assisted nitrosyltransferase) (SNO-CoA-assisted nitrosyltransferase) (EC 2.6.99.-) (P30043)
Organism: Homo sapiens (Human)
Function: Broad specificity oxidoreductase that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:38056462, ECO:0000269|PubMed:7929092}.
Interaction partners:
- Biliverdin reductase A
- Heme oxygenase 1
- Heme oxygenase 2
- Tartrate-resistant acid phosphatase type 5
- Riboflavin kinase
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MAVKKIAIFGATGQTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPRPAHVVVGDVLQAADVDKTVAGQDAVIVLLGTRNDLSPTTVMSEGARNIVAAMKAHGVDKVVACTSAFLLWDPTKVPPRLQAVTDDHIRMHKVLRESGLKYVAVMPPHIGDQPLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTDEYDGHSTYPSHQYQ
Protein: NPC1-like intracellular cholesterol transporter 1 (Npc1l1) (Niemann-Pick C1-like protein 1) (Q6T3U3)
Organism: Rattus norvegicus (Rat)
Function: Plays a major role in cholesterol homeostasis. Critical for the uptake of cholesterol across the plasma membrane of the intestinal enterocyte. Involved in plant sterol absorption, it transports sitosterol, although at lower rates than cholesterol. Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption and is approved for the treatment of hypercholesterolemia. May have a function in the transport of multiple lipids and their homeostasis, thereby influencing lipid metabolism regulation (By similarity). May be involved in caveolin trafficking from the plasma membrane (By similarity). Acts as a negative regulator of NPC2 and down-regulates its expression and secretion by inhibiting its maturation and accelerating its degradation (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:17135346}; Multi-pass membrane protein. Cell membrane {ECO:0000269|PubMed:29880681}; Multi-pass membrane protein. Note=Subfractionation of brush border membranes from proximal enterocytes suggests considerable association with the apical membrane fraction. Exists as a predominantly cell surface membrane expressed protein. {ECO:0000269|PubMed:14976318}.
Interaction partners:
- ATP-binding cassette sub-family G member 5
- Sterol regulatory element-binding protein 2
- ATP-binding cassette sub-family G member 8
- NPC intracellular cholesterol transporter 2
- Scavenger receptor class B member 1
- Sterol regulatory element-binding protein 1
- P-type phospholipid transporter
- Cytochrome P450 7A1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Apolipoprotein B-100
Sequence:
MAAAWLGWLLWALLLSAAQGELYTPKHEAGVCTFYEECGKNPELSGGLTSLSNVSCLSNTPARHVTGEHLALLQRICPRLYNGPNTTFACCSTKQLLSLESSMSITKALLTRCPACSDNFVSLHCHNTCSPDQSLFINVTRVVERGAGEPPAVVAYEAFYQRSFAEKAYESCSQVRIPAAASLAVGSMCGVYGSALCNAQRWLNFQGDTGNGLAPLDITFHLLEPGQALPDGIQPLNGKIAPCNESQGDDSAVCSCQDCAASCPVIPPPEALRPSFYMGRMPGWLALIIIFTAVFVLLSAVLVRLRVVSNRNKNKAEGPQEAPKLPHKHKLSPHTILGRFFQNWGTRVASWPLTVLALSFIVVIALAAGLTFIELTTDPVELWSAPKSQARKEKSFHDEHFGPFFRTNQIFVTARNRSSYKYDSLLLGSKNFSGILSLDFLLELLELQERLRHLQVWSPEAERNISLQDICYAPLNPYNTSLSDCCVNSLLQYFQNNRTLLMLTANQTLNGQTSLVDWKDHFLYCANAPLTFKDGTSLALSCMADYGAPVFPFLAVGGYQGTDYSEAEALIITFSLNNYPADDPRMAQAKLWEEAFLKEMESFQRNTSDKFQVAFSAERSLEDEINRTTIQDLPVFAVSYIIVFLYISLALGSYSRCSRVAVESKATLGLGGVIVVLGAVLAAMGFYSYLGVPSSLVIIQVVPFLVLAVGADNIFIFVLEYQRLPRMPGEQREAHIGRTLGSVAPSMLLCSLSEAICFFLGALTPMPAVRTFALTSGLAIILDFLLQMTAFVALLSLDSKRQEASRPDVLCCFSTRKLPPPKEKEGLLLRFFRKIYAPFLLHRFIRPVVMLLFLTLFGANLYLMCNINVGLDQELALPKDSYLIDYFLFLNRYLEVGPPVYFVTTSGFNFSSEAGMNATCSSAGCKSFSLTQKIQYASEFPDQSYVAIAASSWVDDFIDWLTPSSSCCRLYIRGPHKDEFCPSTDTSFNCLKNCMNRTLGPVRPTAEQFHKYLPWFLNDPPNIRCPKGGLAAYRTSVNLSSDGQVIASQFMAYHKPLRNSQDFTEALRASRLLAANITADLRKVPGTDPNFEVFPYTISNVFYQQYLTVLPEGIFTLALCFVPTFVVCYLLLGLDMCSGILNLLSIIMILVDTIGLMAVWGISYNAVSLINLVTAVGMSVEFVSHITRSFAVSTKPTRLERAKDATVFMGSAVFAGVAMTNFPGILILGFAQAQLIQIFFFRLNLLITLLGLLHGLVFLPVVLSYLGPDVNQALVQEEKLASEAAVAPEPSCPQYPSPADADANVNYGFAPELAHGANAARSSLPKSDQKF
Protein: Nucleobase/nucleoside transporter 8.1 (Q386F0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- C3H1-type domain-containing protein
Sequence:
MALGFSSAGEVYMYATCILLGVSLLMPLNALVSAPRFMVDYYKYVSGKEDAEPNLPFFWKNIFTFYNVVSLASQVIAGPTVLTRAARRLSLSVRFALSITLMMSEVFVVLMMPVIKVPQTVAIVLLCLVTIFAGIGKSYHEATCYVLVASMPSKFMSAVMFGVSLCGVITSTLQCIIKASMEDTYESVLTQSYIYFSLGLLIMAGTLAMALCLRYNSYAQEHVAEYRMLKLQEQGVDAESQNDEKEPVAEGKGEGEGKSEGAMTTAEQLTATAVMPVARIIRMMLVTVFCGFFLTLFIFPSLIIPIDRDHNWFATIAILLYNCGDAIGRFSTSFKCVWPPRRALLYATFARFIFVLPFMLCIYQYIPGHVGPYIFSFLLGLTNCVGAMSMVYGPITPGLETAGQKLMAGQLMGISLLSGIAAASVLAMIVVVFLP
Protein: Centromere protein U (MLF1-interacting protein) (D6R9S4)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKDKAGQKCKPIDVFDFPDNSDVSSIGRLGENEKDEETYETFDPPLHSTAIYADEEEFSKHCGLSLSSTPPGKEAKRSSDTSGNEASEIESVKISAKKPGRKLRPISDDSESIEESDTRRKVKSAEKISTQRHEVIRTTASSELSEKPAESVTSKKTGPLSAQPSVEKENLAIESQS
Protein: E3 ubiquitin-protein ligase SMURF2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF2) (SMAD ubiquitination regulatory factor 2) (SMAD-specific E3 ubiquitin-protein ligase 2) (A2A5Z6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane {ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft {ECO:0000250|UniProtKB:Q9HAU4}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts. {ECO:0000250|UniProtKB:Q9HAU4}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 6
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 3
- E3 ubiquitin-protein ligase SMURF1
- Ubiquitin carboxyl-terminal hydrolase 15
- TGF-beta receptor type-2
- Protein patched homolog 1
- Mothers against decapentaplegic homolog 4
Sequence:
MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVPLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVNTRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (Q584S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- AMP deaminase, putative
- Adenosine monophosphate deaminase, putative
- AMP deaminase
- Nucleoside hydrolase, putative
- Inosine-adenosine-guanosine-nucleoside hydrolase
- Adenylate kinase, putative
- Adenylate kinase, putative
Sequence:
MSSAPLRVYVQCNPLLDVSAHVSDEFLVKYGLERGTAILLSERQKGIFDDIEKMPNVRYVPGGSGLNVARVAQWMQQAYKGKFVTYVGCIADDRYGKVLKEAAEHEGIVMAVEHTTKAGSGACAVCITGKERTLVADLGAANHLSSEHMRSPAVVRAMDESRIFYFSGFTLTVDVNHVLQACRKAREVDGLFMINLSAPFIMQFFSAQLGEVLPYTDIIVANRHEAKEFANMMKWDTDCVEEIARRAVSEVPYTGTKGRVVVFTRDIEPTVIATKDGVETVPVPQLDQDKVIDMNGAGDAFVGGFLSAYAVGKDLRRCCETGHYTAQEVIQQDGCSFPEKPSFSP
Protein: Zgc:171804 protein (A9JSU5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYTHSQMYTNDPGAVVPVAELPSCTALGQSPETEHIRSTQNNTYVRTKIKVTTGELPTEAPPVVPSVTTSPPVSIATHCSPPVTKPLMVQSSGATYVCQVCQKVFQFQRMLNRHLKCHSEQKRHLCDFCGKGFNDTFDLKRHVRTHTGVRPYKCELCDKAFTQRCSLESHMKKIHGVTQQYAYKERRSKLYVCEECGHTASTQDALLRHLHTEHPNSAFLRAKGARRHSPSLNGTKDDTSQPGSPLSLNSDDNAES
Protein: 26S proteasome complex subunit rpn15 (mRNA export factor dss1) (O14140)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Acts as a ubiquitin receptor of the 26S proteasome, by interacting with ubiquitin chains linked by 'Lys-63' and 'Lys-48'. Involved in nuclear export of specific sets of mRNAs. Links the mRNA adapter mlo3 to rae1 for targeting mRNA-protein complex to the proteins of the nucleoporin complex (NPC). Involved in recombinational repair of DNA. Plays a critical role in linking repair and checkpoint factors to damaged DNA sites by specifically recruiting rad24 and cdc25 to the DSBs.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit rpn8
- 26S proteasome regulatory subunit rpn12
- Probable 26S proteasome regulatory subunit rpn6
- Probable 26S proteasome regulatory subunit rpn9
- 26S proteasome regulatory subunit rpn11
- Probable 26S proteasome regulatory subunit rpn3
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit 8 homolog
Sequence:
MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN
Protein: Probable pyruvate kinase, cytosolic isozyme (PK) (EC 2.7.1.40) (O65595)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key regulatory enzyme of the glycolytic pathway that catalyzes the final step of glycolysis, converting ADP and phosphoenolpyruvate (PEP) to ATP and pyruvate by essentially irreversible transphosphorylation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q2RAK2}.
Interaction partners:
- L-lactate dehydrogenase
- Cytosolic enolase 3
- Bifunctional enolase 2/transcriptional activator
- Enolase 1, chloroplastic
- D-lactate dehydrogenase [cytochrome], mitochondrial
- NADP-dependent glyceraldehyde-3-phosphate dehydrogenase])
- Inosine triphosphate pyrophosphatase
- Malate dehydrogenase 3, cytoplasmic
- Malate dehydrogenase 1, cytoplasmic
- Malate dehydrogenase 2, peroxisomal
Sequence:
MAMEQRPKTKIVCTLGPASRSVPMVEKLLMAGMSVARFNFSHGSYEYHQETLDNLRQAMLNTGMLCAVMLDTKGPEIRTGFLKDGKPIQLKQGQEITISTDYDLKGDEKTICMSYKKLAQDVNPGMVILCADGTISLKVLSCDKEKGTVRCRCENTSMLGERKNVNLPGVVVDLPTLTEKDKQDILEWGVPNQIDMIALSFVRKGSDLVQVRKLLGKHAKTILLMSKVENQEGVANFDDILINSDAFMIARGDLGMEIPIEKIFLAQKVMIYKCNFMGKPVVTATQMLESMIKSPRPTRAEATDVANAVLDGTDCVMLSGETAAGAYPELAVRTMAKICVEAESTLDYGDIFKRIMLHAAVPMSPMESLASSAVRTATSSRATLMMVLTRGGSTARLVAKYRPGIPILSVVVPEITSDSFDWACSNEAPARHSLIYRGLVPVLYAGSARASIDESTEETLEFASEYGKKKQLCKTGDSVVALFRTGNAIVIKILTVK
Protein: Calmodulin-binding receptor-like cytoplasmic kinase 2 (EC 2.7.11.1) (Q8VZJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Calcium-binding protein CML39
- O-fucosyltransferase 20
- Calmodulin-binding protein 60 C
Sequence:
MPSRRRHSYTVGSPATTSSNYSNTTFTDRSFPTTPARTSTDTTTSIARRISGIFINCFTPPDSVSSNYIDNSKSSSDNNIRSRRSSTGSSSVQRSYGNANETEHTRFTFDEIYDATKNFSPSFRIGQGGFGTVYKVKLRDGKTFAVKRAKKSMHDDRQGADAEFMSEIQTLAQVTHLSLVKYYGFVVHNDEKILVVEYVANGTLRDHLDCKEGKTLDMATRLDIATDVAHAITYLHMYTQPPIIHRDIKSSNILLTENYRAKVADFGFARLAPDTDSGATHVSTQVKGTAGYLDPEYLTTYQLTEKSDVYSFGVLLVELLTGRRPIELSRGQKERITIRWAIKKFTSGDTISVLDPKLEQNSANNLALEKVLEMAFQCLAPHRRSRPSMKKCSEILWGIRKDYRELLNTSL
Protein: Protein CASC3 (Q960S3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasm, Stress granule {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MRKWQPASGGDRWSHDRFEATEQAPKSRAELLQTYGYDIRNEDAPPRARRRRRYTRGPSKYSRNWEDEQAYLKASNKERKPPRPQDFPALNERKPRGPRTSSSREEKENRRSVAAEGLVPEKQQPLASSSNPHRSQERERERERERERDREPKNRNFGRMNGGPGRQNGMEFKKNNRGQQLRERERGPDQLDNRNQKPSTPRSNQQQQPQQQPHHQQQPQQQRQPSQPQQSPQTPLSTSNLSQRLQQVQQRNDPSHVGSVQMHSLASQNQAPQQQQQQPLHQEQRNAPKRYSSLRRSQQEASQHLAEQQQQQMQQQLHLQQQQQQQQSQIMIQDPHVLMQIAYQQQELQAQLQTMQLGPPTAAGAVPTPPKPHAPPAAAYPQAQAAPYYVTGTEPVPVPVPQAPYVNPASAAYLPTTPAAVAYAQAGPPVVTQPTPPPAQAPPATQPAQPYQNYNTVGGTTYFVPPAQTTSRPSALPQRRPTNAIPILPPSEKHKVKGGAKEEGISDNIDHIIDNMFVQRPSAFQATGEGATPGGGTKEEAAATPPAAEQNLQPVPATGQE