wanglab/gogpt-training-data huggingface dataset:
Protein: Large T antigen (LT) (LT-AG) (EC 5.6.2.4) (DNA 3'-5' helicase large T antigen) (P03072)
Organism: JC polyomavirus (JCPyV) (JCV)
Function: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03070}.
Interaction partners:
Sequence:
MDKVLNREESMELMDLLGLDRSAWGNIPVMRKAYLKKCKELHPDKGGDEDKMKRMNFLYKKMEQGVKVAHQPDFGTWNSSEVPTYGTDEWESWWNTFNEKWDEDLFCHEEMFASDDENTGSQHSTPPKKKKKVEDPKDFPVDLHAFLSQAVFSNRTVASFAVYTTKEKAQILYKKLMEKYSVTFISRHGFGGHNILFFLTPHRHRVSAINNYCQKLCTFSFLICKGVNKEYLFYSALCRQPYAVVEESIQGGLKEHDFNPEEPEETKQVSWKLVTQYALETKCEDVFLLMGMYLDFQENPQQCKKCEKKDQPNHFNHHEKHYYNAQIFADSKNQKSICQQAVDTVAAKQRVDSIHMTREEMLVERFNFLLDKMDLIFGAHGNAVLEQYMAGVAWIHCLLPQMDTVIYDFLKCIVLNIPKKRYWLFKGPIDSGKTTLAAALLDLCGGKSLNVNMPLERLNFELGVGIDQFMVVFEDVKGTGAESRDLPSGHGISNLDCLRDYLDGSVKVNLERKHQNKRTQVFPPGIVTMNEYSVPRTLQARFVRQIDFRPKAYLRKSLSCSEYLLEKRILQSGMTLLLLLIWFRPVADFAAAIHERIVQWKERLDLEISMYTFSTMKANVGMGRPILDFPREEDSEAEDSGHGSSTESQSQCFSQVSEASGADTQENCTFHICKGFQCFKKPKTPPPK
Protein: Protein croquemort (Q9VJA7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
- Nimrod C3
Sequence:
MRCGCCSVRQQKIWVFSMGGLILAIGIFLASAWPAVSRQWIRSLLPLAPNSFIYNRWVTTPTPVYSTVFLFNWTNPGDLNTEGVKPHFEQLGPYTFSDFKVKEDLEWNQPQVTYFGKRTWHFLPEKSNGSLDDVVIAPHFPTLTAALYSRRLRRILRKVMNFTLNREGGATHMTHTAGQWLFDGYYDHLLDFVEQLHSPLLPVYDNTFGWFYERNNSKTAEGNFTLHTGRGDLSQLGDLLLWNGENTTGFYPGECGKVNGSTGELWSPYRTWDQPTTIFLPDAARYLNLFPKENLTIDGIDVWRYESTNLTIDNGQLSPDTECFCLKNRECPRNGVLDYGPPAFNGPFYMSHPHFFLTDQMYRENTTGLQPEESEHGMYVIMEPTLGIPLSLRGQLMISTKVVRDEAIDLFKNVAYDHYAPLFTMRLHAELDEGLTKLLKLALNAAIIGMYTGIGLVLLGMSIVVTGIFITKKHKWHSEQRPDKHLQCTQN
Protein: Coordinator of PRMT5 and differentiation stimulator (Cooperator of PRMT5) (Q9CQ13)
Organism: Mus musculus (Mouse)
Function: Histone-binding protein required for histone H4 methyltransferase activity of PRMT5. Specifically required for histone H4 'Arg-3' methylation mediated by PRMT5, but not histone H3 'Arg-8' methylation, suggesting that it modulates the substrate specificity of PRMT5. Specifically interacts with the N-terminus of histone H4 but not with histone H3, suggesting that it acts by promoting the association between histone H4 and PRMT5. Involved in CCNE1 promoter repression (By similarity). Plays a role in muscle cell differentiation by modulating the recruitment of PRMT5 to the promoter of genes involved in the coordination between cell cycle exit and muscle differentiation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Methylosome protein WDR77
- Serine/threonine-protein kinase RIO1
Sequence:
MDPQAATGRGPGERSSQEAPSAEAGFATADLSGRETETELAVDRLASGAQSIPADIPAHAEGPSSEEEGFAVEKEADGELYAWELSEGPSCPPMEQAADLFNEDWDLELKADQGNPYDADDIQGSISQEIKPWVCCAPQGDMIYDPSWHHPPPLIPHYSKMVFETGQFDDAED
Protein: Serum amyloid A protein (Q2HXZ9)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MKLSTGIIFCFLILGVSSQRWASFLKEAGQGAKDMWRAYSDMREANYKNSDKYFHARGNYDAAQRGPGGAWAAKVISDARENVQRVTDLFKHGDSGHGVEDSRADQAANAWGRSGKDPNHFRPRGLPDKY
Protein: RING finger protein unkempt homolog (Zinc finger CCCH domain-containing protein 5) (Q9C0B0)
Organism: Homo sapiens (Human)
Function: Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25737280}.
Interaction partners:
- HLA class I histocompatibility antigen, C alpha chain
Sequence:
MSKGPGPGGSAASSAPPAATAQVLQAQPEKPQHYTYLKEFRTEQCPLFVQHKCTQHRPYTCFHWHFVNQRRRRSIRRRDGTFNYSPDVYCTKYDEATGLCPEGDECPFLHRTTGDTERRYHLRYYKTGICIHETDSKGNCTKNGLHCAFAHGPHDLRSPVYDIRELQAMEALQNGQTTVEGSIEGQSAGAASHAMIEKILSEEPRWQETAYVLGNYKTEPCKKPPRLCRQGYACPYYHNSKDRRRSPRKHKYRSSPCPNVKHGDEWGDPGKCENGDACQYCHTRTEQQFHPEIYKSTKCNDMQQSGSCPRGPFCAFAHVEQPPLSDDLQPSSAVSSPTQPGPVLYMPSAAGDSVPVSPSSPHAPDLSALLCRNSSLGSPSNLCGSPPGSIRKPPNLEGIVFPGESGLAPGSYKKAPGFEREDQVGAEYLKNFKCQAKLKPHSLEPRSQEQPLLQPKQDMLGILPAGSPLTSSISSSITSSLAATPPSPVGTSSVPGMNANALPFYPTSDTVESVIESALDDLDLNEFGVAALEKTFDNSTVPHPGSITIGGSLLQSSAPVNIPGSLGSSASFHSASPSPPVSLSSHFLQQPQGHLSQSENTFLGTSASHGSLGLNGMNSSIWEHFASGSFSPGTSPAFLSGPGAAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAGPEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKAVFHMQSVKCLKCQEQKRAVLPCQHAALCELCAEGSECPICQPGRAHTLQS
Protein: Zinc finger protein ZAT11 (Q9SLD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in stress responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2-type zinc finger family protein
Sequence:
MKRERSDFEESLKNIDIAKCLMILAQTSMVKQIGLNQHTESHTSNQFECKTCNKRFSSFQALGGHRASHKKPKLTVEQKDVKHLSNDYKGNHFHKCSICSQSFGTGQALGGHMRRHRSSMTVEPSFISPMIPSMPVLKRCGSSKRILSLDLNLTPLENDLEYIFGKTFVPKIDMKFVL
Protein: E3 ubiquitin-protein ligase TRIM37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM37) (Tripartite motif-containing protein 37) (Q6PCX9)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase required to prevent centriole reduplication (By similarity). Probably acts by ubiquitinating positive regulators of centriole reduplication (By similarity). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes. Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome (By similarity).
Subcellular location: Chromosome {ECO:0000250|UniProtKB:O94972}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O94972}. Peroxisome membrane {ECO:0000250|UniProtKB:O94972}; Peripheral membrane protein {ECO:0000250|UniProtKB:O94972}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000250|UniProtKB:O94972}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- Zinc finger protein AEBP2
- E3 ubiquitin-protein ligase RING1
- Histone-lysine N-methyltransferase EZH2
- Polycomb protein Suz12
- Polycomb complex protein BMI-1
- Histone-binding protein RBBP4
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Protein Jumonji
- Polycomb group RING finger protein 1
Sequence:
MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNRQNDTVILRFQVRSPTFFQKCRDQHWYITQLEAAQTGYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDSPETRTKKAGSCSDMLLEGGPTCASVRETKEDEDEEEKIQNEDYHHELSDGDLDLDLVGEDEVNHLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNSMELEEGELMEDAAAAGPPGSSHSYVGASSRMSRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSMENLWGLQPRPSASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKTTLSDIKGSSVASTDMQTNLFCADQAALTTCGPENSGRLQDLGMELLAKSSVAGCYIRNPTNKKNSPKSARAIAGSLSLRRAVDSGENSRSKGDCQVLAEGSSGSSQSGSRHSSPRALTHGIIGDLLPKSEDRQCKALDSDAVVVAVFNGLPTVEKRRKMVTLGTNAKGGRLEGMQMADLESHSEAGEVQPTLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSMGAFNDPFLAQPPDEDSHSSFPDGEQIDPENLHFNPDEGGGR
Protein: Homeobox and leucine zipper encoding (U3KPW8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
QMEKVKTWFMAQRLRCGISWSSEEIEETRARVVYRRDQLHFKSLLSFTHHAGRPPEEVPPPPVPAPEQVGIGIGTASWNHSTTVPQPQARDKPPPIALIASSCKEESASSVTPSSSSTSSSFQVLANGATAASKPLQPLGCVPQSVSPSEQALPPHLEPAWPQGLRHNSVPGRVGPTEYLSPDMQRQRKTKRKTKEQLAILKSFFLQCQWARREDYQKLEQITGLPRPEIIQWFGDTRYALKHGQLKWFRDNAVPGAPSFQDPAIPTPPPSTRSLNERAETPPLPIPPPPPDIQPLERYWAAHQQLRETDIPQLSQASRLSTQQ
Protein: Phosphatase and actin regulator 4 (Protein Humpty dumpty) (Humdy) (Q501J7)
Organism: Mus musculus (Mouse)
Function: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway.
Subcellular location: Cytoplasm. Cell projection, lamellipodium.
Interaction partners:
Sequence:
MEDPSEEAEQPSGDPGMGMDSVEAGDTTPPTKRKSKFSALGKIFKPWKWRKKKSSDKFKETSEVLERKISMRKPREELVKRGVLLEDPEQDGEDSGKLSHAALKNGHTTPIGSARSSSPVLVEEEPERSLRNLTPEEESKKRLGSTGSQPNSEAEPGPEHAPKQPLLPPKRPLSSSCEAKEVPAGSTARSVSSTSGSTTVTSAATTAATDMTKTVKSFVGPTPAPAPAPRTLPAAPASANTAATTTAPAKQPPIPPPKPAQRNSNPIIAELSQAMNSGTVLSKPSPPLPPKRGIPSTSIPSLEPAASFTTKTANDQREKTVSLCLEPPLIIPPSSPSPPLPTHIPPEPPRSPLVPAKTFQIVPEVEFSSSSDLFQDISQQEDQKTEVPKKIQDQSFGESHIPSRLPPLPLHIRIQQALTSPLPVTPPLEGTHRAHSLLFENSDSFSEDTGTLGRTRSLPITIEMLKVPDDEEEEQTCPFVEDVTSTSATPSLPLCLREEEKESDSDSEGPIKYRDEEEDDDDDESHQSALANRVKRKDTLAMKLSSRPSEPETNLNSWPRKSKEEWNEIRHQIGNTLIRRLSQRPTAEELEQRNILQPKNEADRQAEKREIKRRLTRKLSQRPTVAELLARKILRFNEYVEVTDAHDYDRRADKPWTKLTPADKAAIRKELNEFKSSEMEVHVDSKHFTRYHRP
Protein: Kinesin motor domain-containing protein (Q23124)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Kinesin-like protein
Sequence:
MDGVRIKNDFYNNHTNDLKHQIAQLERKTATIPKLENQLHKAKNQNKVLRRESALFPSASCADVSRVEDQKVKTLRNELADLKLKLRQLEDDNKEKDMENDRLIQENRTLKREKLKLINCFKTQMAEKDAIIRELNDEVVDLRGQIRVAIRVRDFERDGSSNFSIISQNEVQLQQTTGQSNTYSFEHVFFPPTAQSGVFGEIKELIMCALHGKNVCLIAYGPTGSGKTFTMRGEDSADSEGVIPRAIRFMLEQSKRDLAMIGWNYKFQASFIEVYNEEVYDLLDGKQKLEVKINGSKTNVVGLKKIEIGNISDVDVILNLADSQRSVASTASNEHSSRSHAIFQIFVDGQNASGEMVQCCLNLVDLAGSERAKETQARGKQFTELTNINQSLSTLKKCIRAQMTKMSHVPYRDSKLTMVLREYLGAGSSKTMFIAHANPRDVAETKRTLEFTSELRSTNLGKAVVQTGQKL
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B (EC 3.1.1.-, EC 3.1.1.3)) (Q9VJH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MHWRLVIGLLLLASFNRETIGKRFLNLKPIPIQHEDESSTEGSTNPTPTSTTTPSNRDITIGPCKWAIGRSCPDPDVKYYIYTRHNPMDRQCLHIDESLEKSNLTDSYFNPRYPTKIIIHGYNSDMFLHPLQQMREEYLAKADYNIIYVDWSILSPGPCYISAVHNTKHAGTCTAQLVERLVETGNTDIHVIGFSLGAQVPNYIARNLSSFMLPRITGLDPAMPLFITSGKADKLDPSDASYVDVIHTNALVQGKMERCGHADFYMNGGIMQPGCNGQKINSFACSHQRAPAYFLESIRSPKGFWGWACSGYISYLLGMCPPTNFLLEAGENIRPTTRGMFMIDTNDSSPFALGKWTDLPTLGAKQPQWRVPTQKLKAPPNQGVDPLLHHIDQFGKLAANFNNLQMWPTEQDPYEHWTSFSPEQKENDSDGDSVEEQDPVEFIEPDDRQMISTEARPTQSWWDYRRNLTYGFMEDNIFSVPTVD
Protein: Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 4) (LACS 4) (O35547)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially activates arachidonate and eicosapentaenoate as substrates. Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs. Modulates prostaglandin E2 secretion (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60488}; Single-pass type III membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:O60488}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Beta-alanine-activating enzyme
- Lysophospholipid acyltransferase 5
- Lysosomal thioesterase PPT2
- Palmitoyl-protein thioesterase 1
- Phospholipid hydroperoxide glutathione peroxidase
- Palmitoyl thioesterase CPT1C
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MKLKLNVLTIVLLPVHLLITIYSALIFIPWYFLTNAKKKNAMAKRIKAKPTSDKPGSPYRSVTHFDSLAVIDIPGADTLDKLFDHAVAKFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEVTDYTTGRVGAPLICCEIKLKDWQEGGYTVHDKPNPRGEIVIGGQNISMGYFKNEEKTAEDYSVDENGQRWFCTGDIGEFHPDGCLQIIDRKKDLVKLQAGEYVSLGKVEAALKNCPLIDNICAFAKSDQSYVISFVVPNQKKLTLLAQQKGVEGSWVDICNNPAMEAEILKEIREAANAMKLERFEIPIKVRLSPEPWTPETGLVTDAFKLKRKELKNHYLKDIERMYGGK
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 (Centaurin-beta-2) (Cnt-b2) (Q6ZQK5)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).
Subcellular location: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:Q15057}.
Interaction partners:
- Ras-related protein Rab-35
- ADP-ribosylation factor 6
- MICAL-like protein 1
Sequence:
MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEAANILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDRLVVDAAKEKREMEQKHSTIQQKDFSSDDSKLEYNVDAANGIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDSPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIATAYREKGDESEKLDKKSSPSTGSLDSGNESKEKLLKGESALQRVQCIPGNTSCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEAKLEKMGVKKPQPGQRQEKEAYIRAKYVERKFVDKYSALLSPSEQEKRIISKSCEDQRLSHARASVHTPVKSNDSGIQQCSEDGRESLPSTVSANSLYEPEGERQESSVFLDSKHLNPGLQLYRASYEKNLPKMAEALAHGADVNWANSDENQATPLIQAVLGGSLVTCEFLLQNGANVNQRDVQGRGPLHHATVLGHTGQVCLFLKRGANQHATDEEGKDPLSIAVEAANADIVTLLRLARMNEEMRESEGLYGQPGDETYQDIFRDFSQMASNNPEKLNRFQQDSQKF
Protein: Myosin light chain kinase A (MLCK-A) (EC 2.7.11.18) (P25323)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phosphorylates a specific serine in the N-terminus of a myosin light chain (By similarity). Phosphorylates regulatory myosin light chain (mlcR) during chemotaxis. mlcR phosphorylation increases the motility and actin-activated ATPase activity of myosin, contributing to chemotaxis.
Interaction partners:
- Probable serine/threonine-protein kinase DDB_G0290859
Sequence:
MTEVEKIYEFKEELGRGAFSIVYLGENKQTKQRYAIKVINKSELGKDYEKNLKMEVDILKKVNHPNIIALKELFDTPEKLYLVMELVTGGELFDKIVEKGSYSEADAANLVKKIVSAVGYLHGLNIVHRDLKPENLLLKSKENHLEVAIADFGLSKIIGQTLVMQTACGTPSYVAPEVLNATGYDKEVDMWSIGVITYILLCGFPPFYGDTVPEIFEQIMEANYEFPEEYWGGISKEAKDFIGKLLVVDVSKRLNATNALNHPWLKSNNSNNTIDTVKMKEYIVERQKTQTKLVN
Protein: Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine transferase) (O88637)
Organism: Rattus norvegicus (Rat)
Function: Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway. Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis.
Interaction partners:
- Choline/ethanolamine kinase
- Choline kinase alpha
- ethanolamine kinase
- Ethanolamine kinase 2
- Selenoprotein I
- Choline/ethanolaminephosphotransferase 1
- Ethanolamine-phosphate phospho-lyase
- Phosphoethanolamine/phosphocholine phosphatase
- Cholinephosphotransferase 1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MIRNGHGAGGAAGLKGPGGQRTVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKPPHPTPAGDTLSSEVSSQCPGGQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKTEIVPDRDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLEALRQQEAQPRGETD
Protein: Histone H2A (Q582M3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU003767}.
Interaction partners:
- Histone H2A
- SNF2 DNA repair protein, putative
- RuvB-like helicase
- Histone H4
- Histone H3 variant
- Histone H3, putative
- Histone H4
- HIT-type domain-containing protein
- RuvB-like helicase
- Uncharacterized protein
Sequence:
MSLTGDDAVPQAPLVGGVAMSPEQASALTGGKLGGKAVGPAHGKGKGKGKGKRGGKTGGKAGRRDKMTRAARADLNFPVGRIHSRLKDGLNRKQRCGASAAIYCAALLEYLTSEVIELAGAAAKAQKTERIKPRHLLLAIRGDEELNQIVNATIARGGVVPFVHKSLEKKIIKKSKRGS
Protein: Growth arrest-specific protein 2 (GAS-2) (P11862)
Organism: Mus musculus (Mouse)
Function: May play a role in apoptosis by acting as a cell death substrate for caspases. Is cleaved during apoptosis and the cleaved form induces dramatic rearrangements of the actin cytoskeleton and potent changes in the shape of the affected cells. May play a role in chondrocyte proliferation and differentiation, and in limb myogenesis. May be involved in the regulation of the apoptosis in the interdigital tissues of the developing hindlimb. May be involved in the membrane ruffling process.
Subcellular location: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:8120096}. Membrane {ECO:0000269|PubMed:8120096}; Peripheral membrane protein {ECO:0000269|PubMed:8120096}. Note=Component of the microfilament system (PubMed:1607387). Colocalizes with actin fibers at the cell border and along the stress fibers in growth-arrested fibroblasts (PubMed:8120096). Mainly membrane-associated (PubMed:8120096). When hyperphosphorylated, accumulates at membrane ruffles (PubMed:8120096). Colocalizes with detyrosinated alpha-tubulin along the length of microtubule bundles in inner and outer pillar cells (PubMed:33964205). {ECO:0000269|PubMed:1607387, ECO:0000269|PubMed:33964205, ECO:0000269|PubMed:8120096}.
Interaction partners:
- Growth arrest-specific protein 1
- Caspase-3
- Caspase-7
Sequence:
MMCTALSPKVRSGPGLSDMHQYSQWLASRHEANLLPMKEDLALWLTNLLGKEITAETFMEKLDNGALLCQLAATVQEKFKESMDANKPAKTLPLKKIPCKASAPSGSFFARDNTANFLSWCRDLGVDETCLFESEGLVLHKQPREVCLCLLELGRIAARYGVEPPGLIKLEKEIEQEETLSAPSPSPSPSSKSSGKKSTGNLLDDAVKRISEDPPCKCPTKFCVERLSQGRYRVGEKILFIRMLHNKHVMVRVGGGWETFAGYLLKHDPCRMLQISRVDGKTSPVQSKSPTLKDMNPDNYLVVSATYKAKKEIK
Protein: U6 snRNA-associated Sm-like protein LSm5p (D6XIG3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVKSERRSFLSFLGCRVSVDLDDGSTLVGRLVSFSPTSNLILTDAERRKPLKRRRGSIRNECYNCVLFVRGSSVLSVKHSSGVTTDATVIDSITGRQTVVSKTIQAASQSLDTPLR
Protein: Probable pyridoxal 5'-phosphate synthase subunit pdx1 (PLP synthase subunit pdx1) (EC 4.3.3.6) (Q54J47)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by pdx2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit pdx2
- Pyridoxine-5'-phosphate oxidase
- Pyridoxal kinase
- Ribokinase
- GMP synthase
- Probable transaldolase
- Transketolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Ribose-phosphate pyrophosphokinase A
- Ribose-phosphate pyrophosphokinase C
Sequence:
MENLTENQATNNNSPFRIKSSLAQMLKGGVIMDVVTPEQARIAEEAGACAVMALEKIPADIRHFGGVARMSDPGMIKEIMNAVTIPVMAKVRIGHFVEAQILQEIGVDYIDESEVLTIADNENHIDKSEFKVPFVCGCRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHARAVNKEIKKIQNMDPHELYTYAKEIQAPLELVKEVKRLGRLPVVNFAAGGVATPADAAMMMQLGMDGVFVGSGIFKSGDPAKRAKAIVQAVTHFNNPQIVAKVSENLGEAMVGINVDTLKDKENQNWSTKEK