wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatase PSR1 (EC 3.1.3.-) (Plasma membrane sodium response protein 1) (Q07800)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has phosphatase activity in vitro. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR2. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10777497, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Growth regulation protein
- Protein MSN5
- Probable phosphatase PSR2
- Meiotic mRNA stability protein kinase SSN3
- Protein BMH2
- Transcription initiation factor IIF subunit alpha
Sequence:
MGFISSILCCSSETTQSNSNSAYRQQQSSSLNKNRSVKHSNTKSRTRGVHQTNSPPSKTNSAATFSSTERSTGKSGISTNDNEKKKPSSPTAAVTATTTNNMTKVEKRISKDDLYEEKYEVDEDEEIDDEDNRRSRGIVQEKGDAVKDTSRQKKQQQQQQQQSQPQPQPQSQSQSQSQSQSQQRGPTVQVSSDHLIQDMNLSRVSSSSQASETSNDADDEDDEDEEYIDLTLLQQGQYHAPGYNTLLPPQDESTKGKKCLILDLDETLVHSSFKYLRSADFVLSVEIDDQVHNVYVIKRPGVEEFLERVGKLFEVVVFTASVSRYGDPLLDILDTDKVIHHRLFREACYNYEGNYIKNLSQIGRPLSDIIILDNSPASYIFHPQHAIPISSWFSDTHDNELLDIIPLLEDLSVKTSLDVGKILDVTI
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q57XG5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKQNSAAKLAFFELMVVVSNVQGNVGSADNSYVYKKLCTFVGLARNPTAPEAQLPVTPQELTDLETINATLSDPTWLDLFFKDGNDKDDIAEIPTQLKSNPGWSDNWGRWLQAAKLAKADTDKSTMKRFNLQTAAPANAKYIKTFVERALVIVNAKAAALADDITNTKQVTKEDIKKELVAAITGAADGVLTLPIKDNLFATAAAANMQTTCEAKDNTNGAATIGAVFACLCIKGNGQTGDQICDHSGAAIQWEAATGGPQMTDVKALIDGCPAMQDTTVTPELLVNTLRDIYSTISINSGNGYLRTFKTGNCQGHNANGFCVKISGLTSDDDTKFKQLPWVSKIINLSNDIGKVNKHNRAVHLLQAEARQQIAALKVLGRQPALTEFPPAPPTLDRRTQQAEEGKCKPQNTTPTECPTEHCEYDEKATDGNSCKPKPVKENTAETTGNQAGEAAATNRCTAHKDKLACENDKTGDKQNCAWRKGNGGEPEPEKEMCHDSSFLPDKKIAFSVVSAAFVGLVAFENYKDFCLIL
Protein: Potassium voltage-gated channel, subfamily G, member 4, isoform CRA_b (Voltage-gated potassium channel subunit Kv6.3) (Q547S7)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MPMPSRDGGLHPRHHHYGSHSPWSQLLSSPMETPSIKGLYYRRVRKVGALDASPVDLKKEILINVGGRRYLLPWSTLDRFPLSRLSKLRLCRSYEEIVQLCDDYDEDSQEFFFDRSPSAFGVIVSFLAAGKLVLLQEMCALSFQEELAYWGIEEAHLERCCLRKLLRKLEELEELAKLHREDVLRQQRETRRPASHSSRWGLCMNRLREMVENPQSGLPGKVFACLSILFVATTAVSLCVSTMPDLRAEEDQGECSRKCYYIFIVETICVAWFSLEFCLRFVQAQDKCQFFQGPLNIIDILAISPYYVSLAVSEEPPEDGERPSGSSYLEKVGLVLRVLRALRILYVMRLARHSLGLQTLGLTVRRCTREFGLLLLFLAVAITLFSPLVYVAEKESGRVLEFTSIPASYWWAIISMTTVGYGDMVPRSVPGQMVALSSILSGILIMAFPATSIFHTFSHSYLELKKEQEQLQARLRHLQNTGPASECELLDPHVASEHELMNDVNDLILEGPALPIMHM
Protein: Delta(14)-sterol reductase LBR (EC 1.3.1.70) (Lamin B receptor) (Q6DI34)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}. Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004473}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004473}.
Interaction partners:
Sequence:
MPPARFQIGDTVMGRWPGSNLYYEVKVMSFDNKTRLYTVIYKDGTELELKESDITSVVIFQTAGRSRSRSRSPGRSPGRSSARSPGRPRRSRSRSPARTPRRASSRSTEVRKEKLKEVLEVRLTPVAMKHENNSSNSKSEKKGENNTAKAAPVVTEEKTETESENQTGGRYNLRRRKDQGDGKAVELKKAVESEPLLQTKAPAAVKTADLEFGGRVGVLFLMFLLPVAVLVLLILCGQKDASLQSFPLELPALQSVWDCQVFGIVLLWLLFQAVLSLLPVGKLVEGMPLKNGKTLKYRINGFYALLLTAVAAGVAVYQEVDLSYIHAHFLQFYTSALLIATLLSIYLFIRSRWASKDELAPGGNSGYIIYDFFMGRELNPRIKSFDIKFFCEMRPGLMGWVLINFAMLLAEMKQQNLENPSPAMLLVNIFQLLWVIDGLWHEEKLLTMMDIMYDGFGFMLTFGDLAFVPFTFTCQAYYLVNHPNELSVFWIITLIAMNGVGYYIFRKANSQKFAFRKNPSDPAVSHLKTIPTATGKSLIVSGLWGFVRHPNYLGDIIMALAWSLPCGFNNLVPYFYLIYLVTLLVHRNARDERQCRKKYGSAWEEYCKAVPYRIFPRVY
Protein: CASK protein (A5D7B9)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVEHVCTAPQWVPVSWVY
Protein: SUMO-activating enzyme subunit 2 (EC 2.3.2.-) (Anthracycline-associated resistance ARX) (Ubiquitin-like 1-activating enzyme E1B) (Ubiquitin-like modifier-activating enzyme 2) (Q9UBT2)
Organism: Homo sapiens (Human)
Function: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and the nucleus, sumoylation is required either for nuclear translocation or nuclear retention.
Interaction partners:
- SUMO-activating enzyme subunit 1
- Small ubiquitin-related modifier 1
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 2
- Ran GTPase-activating protein 1
- BTB/POZ domain-containing protein KCTD2
- UV excision repair protein RAD23 homolog A
- Ubiquitin-like protein NEDD8
- Small ubiquitin-related modifier 4
- Sentrin-specific protease 1
Sequence:
MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLDEKENLSAKRSRIEQKEELDDVIALD
Protein: Cell division protein FtsZ (Q6GHP9)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
Interaction partners:
Sequence:
MLEFEQGFNHLATLKVIGVGGGGNNAVNRMIDHGMNNVEFIAINTDGQALNLSKAESKIQIGEKLTRGLGAGANPEIGKKAAEESREQIEDAIQGADMVFVTSGMGGGTGTGAAPVVAKIAKEMGALTVGVVTRPFSFEGRKRQTQAAAGVEAMKAAVDTLIVIPNDRLLDIVDKSTPMMEAFKEADNVLRQGVQGISDLIAVSGEVNLDFADVKTIMSNQGSALMGIGVSSGENRAVEAAKKAISSPLLETSIVGAQGVLMNITGGESLSLFEAQEAADIVQDAADEDVNMIFGTVINPELQDEIVVTVIATGFDDKPTSHGRKSGSTGFGTSVNTSSNATSKDESFTSNSSNAQATDSVSERTHTTKEDDIPSFIRNREERRSRRTRR
Protein: Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (CD40L receptor) (A0A8I6A4J5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLPLPQLCALWGCLLTAVHLGQCVTCSDKQYLQGGECCDLCQPGNRLVSHCTALEKTQCQPCDSGEFSAHWNREIRCHQHRHCELNQGLQVKKEGTAVSDTVCTCKEGQHCASKECETCAQHTPCGPGFGVVQMATETTDTVCQPCPVGFFSNGSSLFEKCHPWTSCEDQKLMVLREGTSQTDTLCEKVVKKPKDNEVLPPEARGQDPVEIEDYPGHNTAAPVQETLHGCQPVAQEDGKESRISVQERQVTGSMALKPLV
Protein: Espin-like protein (Q3UYR4)
Organism: Mus musculus (Mouse)
Function: Binds to but does not cross-link actin. Required for the formation and maintenance of inner ear hair cell stereocilia and staircase formation. Essential for normal hearing.
Subcellular location: Cell projection, stereocilium {ECO:0000269|PubMed:26926603}.
Interaction partners:
- Myosin-IIIb
- Myosin-IIIa
- Epidermal growth factor receptor kinase substrate 8-like protein 2
- Whirlin
- Twinfilin-2
- Unconventional myosin-XV
- Epidermal growth factor receptor kinase substrate 8
- Espin
- Gelsolin
- Fascin-2
Sequence:
MEAQQALVASKDGDMATLERLFEAGALRPDITDDLGAGLVHHATRAGHLDCVKFLVQRAKLPGNQQAHNGATPVHDAAATGNLAELCWLVRDAGCGLQDQDASGVSPLHLAARFGHPALVEWLLREGHAATLETLEGALPLHHAAVSGDLTCLKLLTAAHSSGVNQRTCSGASPLYLACQEGHLHLAQFLVKDCGADVRLRALDGMSSLHAAAAHGHYSLVVWLVTFTDIGLTARDNEGATALHFAARGGHTPILDRLLLMGAPIMRDSWGGTPLHDAAENGHMECCQTLLSHHVDPFLRDEDGYTAIDLAEYHGHQDCAQFLREMSRPVRVLMTPPPPPFPPPPLLAAKLSLEEERRGDSGLKSPSSATLSPVWPAQPVPREPMACTAPLRVTTPDALQGPEVEARDSRAGLATLQLDGLPAGDLDMLVPTQDERGRPIPEWKRQVMVRKLQARLGADHPPEDQDQSQRQDSGPTAAEQATWRYSQTHQAILGPFGELLTEDDLVYLEKQINDLQLRRRCQEYESELGRLAAQLQALLPEPLVSITVNSHFLPRAPGLEDEEAPVLATELEASEEPGKAEPRGQPLPFWCSHIGRLVRSMSLLLKGMNGLAQGEEKPPSPVPQDLGKETIAGPSRSEAQREIQECGVSVRTLRGNFEFAPDLPCALNSGPCELGVRPGQCLRGCWSAPPQPRGDAMGGEPGPGDTEEASDSGISCEEAPSEAGAGPGLDLASLRKERIVMLFLGHWKKSAYTPALRTAACRTLEAQRARSRGPEAAGSPRPSSPQPSDGPRLGHLWQQRGIITHLLGTWKAIMAHVPARQLRRLSRRERGPLSPEQFLPHVDGAPVPYNSLSLDLFMLGYFQLLECDLPAEERKMRHLLCFEVFEHLGAHGWEAVRAFHKAVTDEVAAGRRAWTDGFEDIKARFFGSSQGPPWDVEPGRKLGLTPLGSLPHASLPGSGPEPAVPPRLGSDSQGSSFNSGDICGYIDRSFAFWKEKEAEMFNFGE
Protein: Myosin-3 (Myosin heavy chain 3) (P13541)
Organism: Mus musculus (Mouse)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, fast skeletal muscle
- Myosin light chain 4
- Troponin I, slow skeletal muscle
- Troponin T, fast skeletal muscle
- Myogenin
- Myosin light chain 3
- Troponin C, skeletal muscle
- Myosin regulatory light chain 11
- Troponin T, slow skeletal muscle
Sequence:
MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYVKGKIKSSQDGKVTVETEDSRTLVVKPEDVYAMNPPKFDKIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFSLVHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDERLAKLITRTQAVCRGFLMRVEFQKMMQRRESIFCIQYNIRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEEMQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDACRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE
Protein: Protein phosphatase 1 regulatory subunit 3C (Protein phosphatase 1 regulatory subunit 5) (PP1 subunit R5) (Protein targeting to glycogen) (PTG) (Q5U2R5)
Organism: Rattus norvegicus (Rat)
Function: Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Glycogen [starch] synthase, muscle
- Glycogen [starch] synthase, liver
- Protein phosphatase 1 regulatory subunit 3A
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 3B
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1, regulatory subunit 3D
- Glycogenin-1
Sequence:
MSCTRMIHVLDPRPLTSSVMPVDMAMRICLAHSPPLKSFLGPYNGLQRRHFVNKPKPLKPCLSVKQEAKSQKEWKSPHSQAKKRVVFADSKGLSLTAIHVFSDLPEEPAWDLQFDLLDLNDISSSLKLHEEKNLVFDFPQPSSDYLSFRDRFQKNFVCLENCSLQDRTVTGTVKVKNVSFEKKVQVRITFDTWKTYTDVDCVYLKNVYGSSDSDTFSFAIDLPRVIPTEEKIEFCISYHANGRVFWDNNEAQNYRIVHVQWKPDGVQTQVAPKDCAFQQVPLKTELEPTVFGSPRLASGLFPEWQSWGRVENLASYR
Protein: Barrier-to-autointegration factor (Breakpoint cluster region protein 1) [Cleaved into: Barrier-to-autointegration factor, N-terminally processed] (O75531)
Organism: Homo sapiens (Human)
Function: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA. Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging. Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner. Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface. Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity. Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses. Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1. Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy. In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394}. Nucleus envelope {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase (PubMed:16495336, PubMed:24600006). The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus (PubMed:16495336, PubMed:24600006). May be included in HIV-1 virions via its interaction with viral GAG polyprotein (PubMed:14645565). {ECO:0000269|PubMed:14645565, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
Interaction partners:
- Emerin
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Inner nuclear membrane protein Man1
- Prelamin-A/C
- Lamina-associated polypeptide 2, isoform alpha
- Actin-like protein 6A
- Histone H3.1
- Histone H3.3
- Histone H3-7
- Histone H3.1t
Sequence:
MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
Protein: Zinc transporter ZIP13 (Solute carrier family 39 member 13) (Zrt- and Irt-like protein 13) (ZIP-13) (Q2M1K6)
Organism: Rattus norvegicus (Rat)
Function: Acts as a zinc-influx transporter.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8BZH0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96H72}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q96H72}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96H72}.
Interaction partners:
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A2
- Zinc transporter 7
- Probable proton-coupled zinc antiporter SLC30A4
- Zinc transporter ZIP11
- Proton-coupled zinc antiporter SLC30A1
- Probable proton-coupled zinc antiporter SLC30A3
- Zinc transporter
Sequence:
MPGCPCPGCGMAGQRLLFLTVLALELLERAGGSQPALRSLGAAAACRLDSKESESWGALLSGERLDTWICSLLGSLMVGLSGVFPLLVIPLEMGTMLQSEAGAWRLKQLLSFALGGLLGNVFLHLLPEAWAYTCNISPGVEGQSLQRQQQLGLWVIAGFLTFLALEKMFLNCKEEDPSQAPSKDPTAAALNGGHCLAQPAAEPGLRAVVRNLKVSGYLNLLANTIDNFTHGLAVAASFLVSKKIGLLTTMAILLHEIPHEVGDFAILLRAGFDRWTAAKLQFSTALGGLLGACFAICTQSPKGVEETVVWTLPFTSGGFLYVALVNVLPDLLEEDDPWHLNPPLPTGTPCSRCCCSAPVSW
Protein: Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS) (O95363)
Organism: Homo sapiens (Human)
Function: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6AYQ3}. Mitochondrion {ECO:0000250|UniProtKB:Q6AYQ3}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- Phenylalanine--tRNA ligase alpha subunit
- Leucine-rich repeat-containing protein 47
- Tyrosine--tRNA ligase, cytoplasmic
- Arginine-hydroxylase NDUFAF5, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, mitochondrial
- Asparaginyl-tRNA synthetase
- Valine--tRNA ligase
Sequence:
MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVEGRF
Protein: YTH domain-containing protein 1 (Splicing factor YT521) (YT521-B) (Q9VZQ1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs. Acts by acting as a reader of m6A methylation. Required for sex determination and dosage compensation via Sxl alternative splicing: m6A methylation acts as a key regulator of Sxl pre-mRNA and promotes female-specific alternative splicing of Sxl, which determines female physiognomy. M6A methylation is also required for neuronal functions.
Subcellular location: Nucleus {ECO:0000269|PubMed:27919077, ECO:0000269|PubMed:27919081, ECO:0000269|PubMed:28675155}.
Interaction partners:
- N
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage and polyadenylation specificity factor subunit 6
- Probable cleavage and polyadenylation specificity factor subunit 2
- N
- Cleavage stimulation factor subunit 1
- Pre-mRNA-splicing regulator female-lethal
- Protein suppressor of forked
- Cleavage and polyadenylation specificity factor subunit 1
- Nuclear RNA export factor 1
Sequence:
MPRAARKQTLPMREMADLDAVHLGLDENEADIAEELQDFEFNTRSEASESNGGDSSDSEPSISSVSTATSSLAGSSKRKTKKPAKQSPQPAVETKSSKSSAKNKAKREPTPEELNGGKKKKRTDSGTKKTTSSEASDKVKSKSPDTEDRQPSAKKSRTKIPSNANDSAGHKSDLSEAEDEKPSLPTLESDSESSDSDSGTQHKRNGGNGGGNGRGKPSSKSSTPEKDSVGGGTHSHSQKGYDYMTKLNYLFRDTRFFLIKSNNSDNVQLSKNKSVWATLPQNDANLNQAFKEARNVLLIFSVNESGKFAGFARMAAPSRRDIPQVAWVLPPSISPKALGGVIELDWICRKELSFNATLHLHNTWNEGKPVKIGRDGQEIEPKIGGELCRLFPEDEQIELTPILKKSKETARVMREKGIHVIYKPPRSLSSRGHGGGGRGGGRGSNHDHLGPMRHKRSYHGAPHHRPYRHHHGMGLPPGGGFKRSGSPYRQMGGAAGAPPGGPGDMAMPSWERYMSSAAAAEAYVADYMRNMHGQLPPLPFVPPFAQLPIPGAGAGAAGALPPGAAAAMYEQLPPPVRYYDGPGAPPLPDYPPPQRPPPPGFDKAPSYEEFAAWKNAGLPTVPPPGFPVYGGAANGGSNGAGGLAAAQAAAAGGGMGAGGGSGGGMGGPGGYRNRDGNNGSAGGRRREYGNRSGGGGSSRDSRPFRERGGGGGQRSYRDNRR
Protein: Complement C2 (EC 3.4.21.43) (C3/C5 convertase) (Q6MG73)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Complement C3
- Complement C1r subcomponent
- Complement C1q subcomponent subunit B
- Mannose-binding protein A
- Complement C4
- Mannose-binding protein C
- Complement C4A
- Complement C1s subcomponent
- Complement C1q subcomponent subunit C
- Complement C1q subcomponent subunit A
Sequence:
MAPLLALLALLQLGPGLAALSCPQNVNIVGGNFTLSRGWAPGSVLIYSCPLGRYPSPAWRECQSNGQWQTPRASSLPTLRSSRLAKAVCKPVRCPAPTSFENGIYIPRLGSYPVGGNLSFECEHGFTLRGSPVRYCRPNGVWDGETAVCDNGASHCPNPGISVGTMRTGSSFDLGDKVSYRCSSTNLVLTGSVERECLSNGVWSGSEPICRQPYSYDFPEDVASALGTSFTHLLGATNPIQKRTENLGRKIQIQRSGHLNLYLLLDASQSVSEKDFNIFKESAFLMVDRIFSFEIKVSVAIITFASRPKIIMSVLNERSQNVMEVMDSLDSVCYKDHENATGTNTYEALNSVYLMMNNQMDRLGMETSAWQEIRHAIILLTDGKSNMGGSPKPAVDNIREILGISRNRNDYLDIYAIGVGKLDVDWKELNELGSKKDGERHAFILQDAKAVQQVFEHILDVSKLTDTICGVGNMSVNASDQERTPWQVTFKPKSKETCQGSLISDQWVLTAAHCFHDAQMEDRHLWRVIVGDPTSHHGKEFHVEEVLVAPGFNVHAKQSQGISEFYADDIALLKLSQRVKMSSHARPICLPCTVGANMALRRSPGSTCKDHETELLSQQKVPAHFVALNGNRMNINLRTGPERTSCIEAVSQNKGSFPGLTNVSEVVTDQFLCSGMEGDDSPCKGESGGAVFLERRYRFFQVGLVSWGLFDPCHGSSNKNLRRKPPHGVVPRDFHISLFRLQPWLRQHLDGVLDFLPL
Protein: Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine transferase) (Q99447)
Organism: Homo sapiens (Human)
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 kinase alpha
- Choline/ethanolamine kinase
- Ethanolaminephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Ethanolamine kinase 2
- Ethanolamine kinase 1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Ethanolamine-phosphate phospho-lyase
- Phosphoethanolamine/phosphocholine phosphatase
- Cholinephosphotransferase 1
Sequence:
MIRNGRGAAGGAEQPGPGGRRAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKTEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLEAARQQAAQPLGERDGDF