wanglab/gogpt-training-data huggingface dataset:
Protein: Jade family PHD finger 2 (A0A087X085)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEKRRKYSISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDYYILADPWRQEWEKGVQVPAGAEAIPEPVVRILPPLEGPPAQASPSSTMLGEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDELTLERVLEELETLCHQNMARAIETQEGLGIEYDEDVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQPKCLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEHSDGGPRNEPTSEPTEPSQAGEDLEKVTLRKQRLQQLEEDFYELVEPAEVAERLDLAEALVDFIYQYWKLKRKANANQPLLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQIFHLQMKLIEQDLCRERSGRRAKGKKSDSKRKGCEGSKGSTEKKEKVKAGPDSVLGQLGLSTSFPIDGTFFNSWLAQSVQITAENMAMSEWPLNNGHREDPAPGLLSEELLQDEETLLSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFDTETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS
Protein: BHLH transcription factor (Os02g0433600 protein) (cDNA clone:001-017-H10, full insert sequence) (cDNA clone:J023031O20, full insert sequence) (Q67U21)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Os02g0524600 protein
- Os02g0682500 protein
- Os07g0522900 protein
- protein-serine/threonine phosphatase
Sequence:
MDPRSSQAQEDGFFHPRDGACPADSSGKTECKTQGSIATRKVQKADREKMRRDRLNEQFQELGSTLDPDRPRNDKATILSDAIQMLKDLTSQVNKLKAEYTSLSEEARELTQEKNELRDEKVSLKFEVDNLNTQYQQRMRVLYPWTGMEPSVVIGPPLPYPFSVPVPVPVPIPSGAVPMHPQLQAYPYFRNQTSGTVSNPCTPYMAYTQPIHPPTDQLSNQFSAPVQHSSSNRSHSMAQDSRSKSSALQQVSCRGKHDDFDDVATDLELKTPGSSAPLQSEIANKDSSSDLKKKQQFIQETKGSSLTEGSSSSSRCSSSGPPDVSNSIEGGSVADDQRSTVQT
Protein: Kinetochore protein nnf1 (NMS complex subunit nnf1) (Q09858)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:36705602}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:36705602}. Note=Associates with the outer kinetochore. {ECO:0000269|PubMed:36705602}.
Interaction partners:
- Centromere protein mis12
- Kinetochore protein nuf2
- Kinetochore protein spc25
- Kinetochore protein spc24
- Kinetochore protein ndc80
- Outer kinetochore KNL1 complex subunit spc7
- Kinetochore protein mis14
- Kinetochore protein mis13
- DASH complex subunit spc34
- DASH complex subunit dad4
Sequence:
MTSRKEQLDAFLSRTLSETIAHIPLEKFAQCFPSMKKGKVIAVIHQQLIEFFEKSCKQEYANLIKERDLNKKLDMLDECIHDAEFRKLHGESEVDISNKQPQEILKAHLYSHKRELLDKLNQDLLDIDKENEGLSTQIAAEEKATEDCISRMQSLIQKLEKTVYGMNEKNLAKEAHDTLNDLLPYIQNPSSTWTNALNEQGNIER
Protein: Protamine-like protein (PL-I) (Q08GK9)
Organism: Mullus surmuletus (Striped red mullet)
Function: Replaces histones in the chromatin of sperm during the haploid phase of spermatogenesis. Compacts sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:16965539}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:16965539}.
Interaction partners:
Sequence:
PSTTSSKSPKRRAKSPRRKRTGPTVSDLILMAMSASSDRGGLSLAALKKDLKGRGYDVVRNKGRVLMAIKRLVANKSVVKAKGFYKLNKNPPTPRRRVAKRKKPKAKRAKRGRKRKAAPKKKSAKKKRKRRRRKSKSPKKARKARRAKSPRRARSPRRSKSPRKAKRRTTKTRRRAKK
Protein: Acetaldehyde dehydrogenase (EC 1.2.1.10) (Acetaldehyde dehydrogenase [acetylating]) (Q52060)
Organism: Pseudomonas sp. (strain CF600)
Function: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Can also act on propanal and butanal to form propanoyl-CoA and butanoyl-CoA, respectively. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. NADP(+) can replace NAD(+) but the rate of reaction is much slower.
Interaction partners:
Sequence:
MNQKLKVAIIGSGNIGTDLMIKVLRNAKYLEMGAMVGIDAASDGLARAQRMGVTTTYAGVEGLIKLPEFADIDFVFDATSASAHVQNEALLRQAKPGIRLIDLTPAAIGPYCVPVVNLEEHLGKLNVNMVTCGGQATIPMVAAVSRVAKVHYAEIVASISSKSAGPGTRANIDEFTETTSKAIEVIGGAAKGKAIIIMNPAEPPLIMRDTVYVLSAAADQAAVAASVAEMVQAVQAYVPGYRLKQQVQFDVIPESAPLNIPGLGRFSGLKTSVFLEVEGAAHYLPAYAGNLDIMTSAALATAERMAQSMLNA
Protein: Amyloid-beta A4 precursor protein-binding family A member 3 (Adapter protein X11gamma) (Neuron-specific X11L2 protein) (Neuronal Munc18-1-interacting protein 3) (Mint-3) (O96018)
Organism: Homo sapiens (Human)
Function: May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19726677}.
Interaction partners:
- Amyloid-beta precursor protein
- Syntaxin-binding protein 1
- Hypoxia-inducible factor 1-alpha inhibitor
- Xaa-Pro aminopeptidase 2
- N-terminal EF-hand calcium-binding protein 3
Sequence:
MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL
Protein: Small ribosomal subunit protein bS20 (30S ribosomal protein S20) (P9WH41)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds directly to 16S ribosomal RNA.
Interaction partners:
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein bS18A
- Large ribosomal subunit protein bL34
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS4
Sequence:
MANIKSQQKRNRTNERARLRNKAVKSSLRTAVRAFREAAHAGDKAKAAELLASTNRKLDKAASKGVIHKNQAANKKSALAQALNKL
Protein: ESX-1 secretion-associated protein EspB (Antigen MTB48) (P9WJD9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for host-cell death and may support an EsxA-independent virulence function. Secreted processed form of EspB binds to phosphatidic acid and phosphatidylserine. Inhibits IFN-gamma-induced autophagy in murine macrophages.
Subcellular location: Secreted {ECO:0000269|PubMed:17676952, ECO:0000269|PubMed:23869560}. Note=Secreted via the ESX-1 / type VII secretion system (T7SS) (PubMed:17676952). Secretion requires both EspK and EccCb1, but not EspA, EspC and EspD (PubMed:17676952, PubMed:23869560). {ECO:0000269|PubMed:17676952, ECO:0000269|PubMed:23869560}.
Interaction partners:
- ESX-1 secretion-associated protein EspL
- ESX-1 secretion-associated protein EspK
- ESX-1 secretion-associated protein EspE
- Mycosin-1
- ESX-1 secretion system protein EccE1
- ESAT-6-like protein EsxB
- 6 kDa early secretory antigenic target
- ESX-1 secretion-associated protein EspC
- ESX-1 secretion-associated protein EspA
- ESX-1 secretion-associated protein EspI
Sequence:
MTQSQTVTVDQQEILNRANEVEAPMADPPTDVPITPCELTAAKNAAQQLVLSADNMREYLAAGAKERQRLATSLRNAAKAYGEVDEEAATALDNDGEGTVQAESAGAVGGDSSAELTDTPRVATAGEPNFMDLKEAARKLETGDQGASLAHFADGWNTFNLTLQGDVKRFRGFDNWEGDAATACEASLDQQRQWILHMAKLSAAMAKQAQYVAQLHVWARREHPTYEDIVGLERLYAENPSARDQILPVYAEYQQRSEKVLTEYNNKAALEPVNPPKPPPAIKIDPPPPPQEQGLIPGFLMPPSDGSGVTPGTGMPAAPMVPPTGSPGGGLPADTAAQLTSAGREAAALSGDVAVKAASLGGGGGGGVPSAPLGSAIGGAESVRPAGAGDIAGLGQGRAGGGAALGGGGMGMPMGAAHQGQGGAKSKGSQQEDEALYTEDRAWTEAVIGNRRRQDSKESK
Protein: Probable M18 family aminopeptidase 2 (EC 3.4.11.-) (P9WHT1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Type 1 encapsulin shell protein
- Dye-decolorizing peroxidase
Sequence:
MAATAHGLCEFIDASPSPFHVCATVAGRLLGAGYRELREADRWPDKPGRYFTVRAGSLVAWNAEQSGHTQVPFRIVGAHTDSPNLRVKQHPDRLVAGWHVVALQPYGGVWLHSWLDRDLGISGRLSVRDGTGVSHRLVLIDDPILRVPQLAIHLAEDRKSLTLDPQRHINAVWGVGERVESFVGYVAQRAGVAAADVLAADLMTHDLTPSALIGASVNGTASLLSAPRLDNQASCYAGMEALLAVDVDSASSGFVPVLAIFDHEEVGSASGHGAQSDLLSSVLERIVLAAGGTREDFLRRLTTSMLASADMAHATHPNYPDRHEPSHPIEVNAGPVLKVHPNLRYATDGRTAAAFALACQRAGVPMQRYEHRADLPCGSTIGPLAAARTGIPTVDVGAAQLAMHSARELMGAHDVAAYSAALQAFLSAELSEA
Protein: Craniofacial development protein 1 (Bucentaur) (Q8SXI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RuvB-like helicase 1
- DNA methyltransferase 1-associated protein 1
- Histone H2A.v
- RuvB-like helicase 2
- Uncharacterized protein, isoform B
- Vacuolar protein sorting-associated protein 72 homolog
- LP09246p
- YEATS domain-containing protein 4
- Lethal
- Uncharacterized protein, isoform B
Sequence:
MNSQKEYVSDCETDDDYYVDLLTSGKGSDKSESDVSDKSENYPGLKSKHTAKALRKTRHCDGDNREYRSKECDDLHSEEESEKSRSDALWADFLGDIDTKSVINQKTDYTEGNAASATNTNTHETCNKYDKNDTAIIKTAQQYDSKRTTLSVSTLGKIKRSSAEKSIGTMINKFEKKKKLTVLERSQLDWKIFKQDEGIDELLCSHNKGKDGYLDRQDFLERTDLRQFEMEKKLRLSRRPY
Protein: CD59 glycoprotein (1F5 antigen) (20 kDa homologous restriction factor) (HRF-20) (HRF20) (MAC-inhibitory protein) (MAC-IP) (MEM43 antigen) (Membrane attack complex inhibition factor) (MACIF) (Membrane inhibitor of reactive lysis) (MIRL) (Protectin) (CD antigen CD59) (P13987)
Organism: Homo sapiens (Human)
Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Secreted. Note=Soluble form found in a number of tissues.
Interaction partners:
- Complement decay-accelerating factor
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Membrane cofactor protein
- Complement component C9
- T-cell surface antigen CD2
- Caveolin-1
- Complement C3
- Complement factor H
- Complement receptor type 1
- Vitronectin
Sequence:
MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP
Protein: SPT3, SAGA and STAGA complex component (B0QZW5)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNNAAASPMSTTTSSSGRNAGKTISFAAELQSMMFSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVISAEDLLFLMRKDKKKLRRLLKYMFIRDYKSKIIKGIDEDDLLEEKLSGSSGTNKRQKIAQDLINSIDQTGELLAMFEDNELDDVKQERMERAERQTRTMDSAQYAEFCESRQLSFSKKASKFRDWLDCSSMEIKPNVIAMEILAYLAYETVAQLVDLALLVRQDMVSKAGDPFSHAISATFIQYHNSAEGSSCLKSSPDSPENTPPPTPTAPSSGSQHSEHCGLWCRGSQRCHPALPHQRGHSTLRPQDWPSLPIHKCLPKEWDGFPGLLRGPWPCLPPRRGSGSPRSFLPVLPENKIGFYVLL
Protein: Homeobox protein DBX1-B (Developing brain homeobox protein 1-B) (Homeobox protein hlx2) (Q9PTU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MMLPSVIAPPAMYPSFLRPSSALSLPPALQSAFTTHSSFLVEDLLRISRPAAFMHRSIPSPSASPPATGVTTLNTTSSAVHVAMSTALAKRSSSPQTSISSDPNYLKFGVNAILASTTRNASPPPPVQGMNAKTFPFPCFDGSFHPFIRASYFPASSSAVPIPGTFAWPLTARGKPRRGMLRRAVFSDVQRKALEKMFQKQKYISKPDRKKLATKLGLKDSQVKIWFQNRRMKWRNSKERELLSSGGCREQTLPTKMNPNPDLSDVGKRFEHEAVLRESPRAPFCQSRGDHEFNADLHFKSPSISSKHSDFSESEDEEITVS
Protein: Flotillin (E7EMK3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004543}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004543}. Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
Sequence:
MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVPCPCLLDCKWGNSKGFWKLCQVCQISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAELPASVHALTGVDLSKIPLIKKATGVQV
Protein: Transcriptional activator VP30 (Ebola VP30) (eVP30) (Minor nucleoprotein VP30) (Q05323)
Organism: Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Function: Multifunctional protein that acts as a viral transcriptional activator. Promotes read-through of an RNA hairpin in the NP open reading frame to enhance viral transcription. Mechanistically, nonphosphorylated VP30 hexamers form a ternary complex with the viral leader RNA. Clamps the RNA template and the complex VP35-polymerase L together, thereby increasing the polymerase affinity for the RNA template to increase transcription initiation despite the presence of RNA secondary structures. Assists also stop-start transcription at gene junctions to promote transcription of downstream genes. Interaction with NP plays a critical role in transcription initiation by recognizing the RNA stem loop. Interaction with host RBBP6 interferes with NP-VP30 interaction and inhibits viral RNA synthesis. Also acts as a suppressor of RNA silencing by interacting with host DICER1 and TARBP2/TRBP (By similarity).
Subcellular location: Virion. Host cytoplasm {ECO:0000269|PubMed:27755595, ECO:0000269|PubMed:28915404}. Note=Present in viral inclusion bodies due to its interaction with NP. {ECO:0000269|PubMed:28915404}.
Interaction partners:
Sequence:
MEASYERGRPRAARQHSRDGHDHHVRARSSSRENYRGEYRQSRSASQVRVPTVFHKKRVEPLTVPPAPKDICPTLKKGFLCDSSFCKKDHQLESLTDRELLLLIARKTCGSVEQQLNITAPKDSRLANPTADDFQQEEGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTP
Protein: Probable transcription factor At4g00610 (Storekeeper-like protein At4g00610) (O65270)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- SPX domain-containing membrane protein At1g63010
- Bifunctional purple acid phosphatase 26
- Probable inorganic phosphate transporter 1-6
- Fe
- GLABROUS1 enhancer-binding protein-like 2
- Probable inorganic phosphate transporter 1-7
- Inorganic phosphate transporter 2-1, chloroplastic
- Probable inorganic phosphate transporter 1-2
- Probable inorganic phosphate transporter 1-8
Sequence:
MVSVQNLKTDQLLNFLFKNPTKFLSRFSPMAKNKTLVTPSTVKKSSDVASTSKKLSGVASPAKKPSGVTSPVKKPLEAVASTSSEEEEEDEPSSDSESGSESESDTEAEPMTLAAAAPSSSNEKRQSEGKPEEERAKTETETGKKPLLFQRLWTDEDEIVFLQGMIKFAKDTGKNVSEDMNGFFEKLKDSISFEVKTDQFVNKIRSMKRKYIENKKTTTEHDKKCYELAEIIWVSDGDATALVKPKKKKLKVDEESDWFERSFVDGAFKELGPGVDEETWKKNWSLVPVKKRKRIEEKVKSMQADELKTTWQKIDVVHEMRSLMAKYV
Protein: DNA repair protein XRCC3 (X-ray repair cross-complementing protein 3) (O43542)
Organism: Homo sapiens (Human)
Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C.
Subcellular location: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair.
Interaction partners:
- Breast cancer type 2 susceptibility protein
- DNA repair protein XRCC2
- DNA repair protein RAD51 homolog 3
- DNA repair protein RAD51 homolog 1
- DNA repair protein RAD51 homolog 2
- Fanconi anemia group G protein
- HCG2039718, isoform CRA_g
- DNA repair protein RAD52 homolog
- DNA repair protein RAD51 homolog 4
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
Sequence:
MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSAPHLPPSSCSYTISAEGVRGTPGTQSH
Protein: Adaptor protein complex AP-3 small chain sigma3 (Orange) (RE10615p) (Q9W1E8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004180}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- Carmine, isoform A
- AP-3 complex subunit delta
- AP-3 complex subunit beta
- AP-1 complex subunit gamma
- AP-2 complex subunit alpha
- Adaptor protein complex 1, mu subunit
- Transcription factor cwo
- Large ribosomal subunit protein eL8
- Adaptor protein complex 2, mu subunit, isoform A
- AP complex subunit beta
Sequence:
MIKAILVFNNHGKPRLSKFYQYFDESLQQQIIKETFQLVSKRDDNVCNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHADAVHHILSELVMGGMVLQTNMNDIMARIEEQNKIVKQEAGISAAPARAVSAVKSMNIPQQIKDIKLPDLPQAIKDFKF
Protein: Protein arginine N-methyltransferase 1 (EC 2.1.1.319) (Major type I protein arginine N-methyltransferase) (Type I PRMT) (hnRNP arginine N-methyltransferase) (P38074)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in a variety of RNA-binding proteins such as heterogeneous nuclear ribonucleoproteins (hnRNPs) and small nuclear ribonucleoproteins (snRNPs). Methylates NAB2, NPL3, HRP1 and YRA1, shuttling hnRNPs involved in mRNA processing and export, facilitating their export out of the nucleus. Methylation of NPL3 weakens its interaction with THO2, a component of the TREX (transcription/export) complex important for transcriptional elongation and recruitment of mRNA export factors. Methylates the hnRNP HRB1, but does not influence its subcellular location. Methylates the nucleolar proteins GAR1, NOP1 and NSR1. Methylates the snRNP SNP1 and modulates the cotranscriptional recruitment of splicing factors. Dimethylates free histone H4 (HHF1/HHF2) at 'Arg-4' (H4R3me2a) and plays a role in preservation and establishment of silent chromatin domains. Mono- and dimethylates ribosomal protein S2 (RPS2) at 'Arg-11'. Methylates the catalytic subunit of the SWI/SNF chromatin-remodeling complex SNF2.
Subcellular location: Nucleus {ECO:0000269|PubMed:8668183}.
Interaction partners:
- Histone H4
- Protein arginine N-methyltransferase 2
- Small ribosomal subunit protein uS5
- Nuclear localization sequence-binding protein
- Serine/arginine
- rRNA 2'-O-methyltransferase fibrillarin
- Nuclear polyadenylated RNA-binding protein 4
- Single-stranded nucleic acid-binding protein
- H/ACA ribonucleoprotein complex subunit GAR1
- ATP-dependent RNA helicase DBP2
Sequence:
MSKTAVKDSATEKTKLSESEQHYFNSYDHYGIHEEMLQDTVRTLSYRNAIIQNKDLFKDKIVLDVGCGTGILSMFAAKHGAKHVIGVDMSSIIEMAKELVELNGFSDKITLLRGKLEDVHLPFPKVDIIISEWMGYFLLYESMMDTVLYARDHYLVEGGLIFPDKCSIHLAGLEDSQYKDEKLNYWQDVYGFDYSPFVPLVLHEPIVDTVERNNVNTTSDKLIEFDLNTVKISDLAFKSNFKLTAKRQDMINGIVTWFDIVFPAPKGKRPVEFSTGPHAPYTHWKQTIFYFPDDLDAETGDTIEGELVCSPNEKNNRDLNIKISYKFESNGIDGNSRSRKNEGSYLMH
Protein: ABC1 family protein C21C3.03, mitochondrial (Q9P7M0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MISFSHWNSHIRSGLSLSMIPSANSRFAFIIQRNYIPVVNSQNTRWKRLCGTQSVWSPYKKKHVLVNRLKHISLFPKPIFARKFTTRQKSEDQKQWRILRITFLVLPFTVGGLWILYRVKNRKNNIFSFDELELEERSNRPRSIFGKIKQFFNILLRSFNLFIIFSPIIITLPFIALISFLHLRSLSSLTVSIWLRFLVTQLERAGATFIKLGQWAASRTDLFPPAFCKTLSKLHSHVTPHSLAYTQSVICKTYKVESIEEIFVNFNPIPIGVGAIAQVYTATIKKAATQQDNSYFTSMLQSIGFRQKNISDAPVTQDVAIKVLHPNVEKYISLDLQILGFFAKLINLVPSMKWLSLPDEVKVFGAMLNQQLNLHYEALHLNQFRLNFRGNRYVEFPAPYDDYTTNQILLEDYMPGIPLSAFLKHKSGPFNKLLANTGNNALFQMLIVDNFTHADLHPGNVLVKFYKGIPKTIFNQDNEINDSIYKILSTCSTEEWDSAMEELNILGYRPTLVFLDAGLVTKLSTQDQKNFLDLFQAVLTFHGYEAGLLMVERSRQTERVINKDIFALKMEHLLNEIQKSTLSLKSLQIGTILQEVMTMAREHHVRIEANFANTVLSILLVEGAGRQLYPEMDLLSNATPYLRSASSKSNVSLTNPMVQLWIALEARQFLLLSTSKETVEKWVKSDMIAPNI
Protein: SSD domain-containing protein (Q20404)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
Sequence:
MGHKNETSRVTRIWNSLSYKIGSTVARYPVITIIFCLVLSAVMSIKLALTPKVSAIDGYASDDSMSRHEFKTFQQFLDSDGPGITTAILIRSSITNGSLLEEQRLKEVVKVSDFISTNFKLNVSGVEKNFNQFCRGFCQANEPVRQYYNGLQILGKNQTDGISKRIDLSYPTSNFFGRKFSLIPNFFGISMSPEGQHLNSSNLIVLYFRAERYPDWSTKTVKQWELRVRDHFAKEYSSDLIIVDVMSQTVVESEIVRAGLSLQPFLIVGFVIMSIFCTVTTMFSAVYLYSQKATFNKVALSIIACINPFMACGTAMGILFFCGVTFSPIMCITPFLVLAISVDDSFLMLHAWNRLESWRTAPLDKPMREHMMGEVLVETGPAISISAFTNMLAFTIGAITSPPEIRIFCFGNAAAIFMDMFYQATFYTACMTLLGDTKNSEGVSEKTKRIQERMGNVVGRFLKWYVNAISNIFVSFGIVLVWAVFIGFAVLGLTRLHVELRPSKFFLKDSPMLYMDRLRTNEVVPYYTPVHVIVNNPGDLTNDSNVERLVELKEKLEHMPNAIGAPSTKFFLDDFVQYRSSFAEEIEMDIAEDDSESEKSDIEQFLEWPEFSFWRGFLRFDNQTHPHNVTKFMFTTGFHGQDLKDWNKRGQLLKRWRGAVEEFKDDFNTTVFTEDAFFLDMIDSIPTVTWQTTLATFIFVSLVCFLFISDILTVMIVSVATLVTSVGVFGYLSLLGVTLDPVIMSIAIMCIGFSVDIPAHVAFHFYAAKAKKHASSHSQPSPHQVTSPDIVHSTSTTSSSDSSISTPNSFETNLNFALSSVGFPVIQAGVSTDFCALPLGFMELYMAKMFALSLTLCVSLSLIHGLIVIPALLSVQHHIVHAVKRCFGRN
Protein: Uncharacterized MFS-type transporter C1683.03c (Q9P6J7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MMNYVKSLGTYNTRNMEKESSKDLVQNEDTPLPVQKISMSLFHEIVFVFIACTAQLMTQAGLGQSIAPNNIIGKSLGTTNPGQLSWFPASYSLTVGTFILIAGRLGDIYGHKKMFVLGYIWFCIWSLISGFSYYAKSVIMFDVCRALTGIAPAFLLPNALALLGRVYPPGKKKNLIFALFGATAPNGFLLGSVFSGIFAQLSWWPWTYWTTAIVCIVFAIIGYFAIPHIEADEVEEKQKFDYLGAFFGVSGLVLINFSWNQGPVVGWQVPYVYILLIIGFLSLVVFVLVEKRVVQPILAPSMMNSEMGCVLICVAAGWACFGIWMYYLWQFLENLRFATPLLVTAQLTPVGISGCAAALTTGYLLKRLKPTKIMVVSMIAFTVGTILIATAPIHQTYWAQTFVSIIVTPWGMDMSFPAATLMLSDFVPKQHQGIAASLVSTVVNYSISIGLGIAGTVETHLNHKGVDLIRGYRSAWYMGTGFGGLGVCVAILTVFASYLKVGQQKSPKFPLIMKNTKAV
Protein: Conserved protein (O05296)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MAWQQPSPRIRELIREGARIALNPSPEWIEELDRATIAANPAIANDPVLAKVVQTANRANLVYWAAANLRDPGARVPANLGTEPLRMARDLVRRGLDTVAFNIYRTGEHIGWRFWMGIAFELTSDPQELRELLDVSARSVNDFIEATLTGIAAQVQSEHDELTRSTHAERLEVVGLILDGAPISPERAEAKLGYPLSRAHTAAIIWSDELDGDHSYLDRAADLFCHAVGSTRPLTVVAGAASRWAWVTDADGLDIDTVQAAVDNAPGARIAIGTTANGVEGFRRSHLEALITQRTLSRLRSTQRVAFFADVKMVALISQNPDAASEFITSTLGDLESASPDLQTALLTFINEQCNASRAAKRLHTHRNTFLRRLESAQRLLPRPLDHTSVHVAVALEALQWRGNKAHALSSPGRRSNSVPA