wanglab/gogpt-training-data huggingface dataset:
Protein: GPI mannosyltransferase 4 (EC 2.4.1.-) (GPI mannosyltransferase IV) (GPI-MT-IV) (Q09837)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Putative uncharacterized protein C13G1.16
- Putative uncharacterized protein C30B4.09
- GPI ethanolamine phosphate transferase 3
- GPI-anchor transamidase
- GPI transamidase component gaa1
- Uncharacterized protein PB16A4.07
- Uncharacterized protein C25B8.20
- Probable Dol-P-Man:Man
- Alpha-1,2-mannosyltransferase alg9
- GPI mannosyltransferase 3
Sequence:
MFKNRKYAIIYTFLLILRFWFSQGSSYIHPDEHLQSFQIFANKLFGWKVELPWEFTTKKPIRSVVPLNVMLLPIFLLCRCICKSNCSPYPILLFTRLYMCLISLLIDLSIWNIVPLNARWSALLLYSSSFMATTFQTHTFTNSIETIFFFLTILFLSKLNSVPLNKKISYLYTFLLAIVSVLGFFTRITFLAFVIAPYIYFSVRCFKKNVNNPKDIFLHLCIFVSVSFATVLACILEDYKFYGVFVITFWNNLKYNSQIENLSQHGLHSRLTHFFTNMPLLCGPLIFVPKLWDVRKPATWLWLLPVFILSLFPHQEPRFLLPAASIFIVNSGCLVRSYWIKFLFVMYAVVLAVFFGIMHQNGVIPAVLEVKNIIEQRNVTTMENCNLYFNPEMPTTIYFWKIYSAPTWMLARPKFSQINTSHLYNYSTKQMISKFWETYYEEVKVVNLPEENTTEFQASTLLVCPVAMLQTSSYLQNLTMLHYIPYHVDLDDTDELPLAELIMNHGIGIFTAKEICENNTITNELPTVLRSVG
Protein: Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (P01024)
Organism: Homo sapiens (Human)
Function: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.
Subcellular location: Secreted.
Interaction partners:
- Properdin
- Complement receptor type 1
- Membrane cofactor protein
- Complement factor I
- Complement factor H-related protein 1
- Integrin alpha-M
- Complement receptor type 2
- V-set and immunoglobulin domain-containing protein 4
- Complement factor H
- Complement decay-accelerating factor
Sequence:
MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN
Protein: Serine-rich coiled-coil domain-containing protein 1 (Coiled-coil serine-rich protein 1) (Q9C0I3)
Organism: Homo sapiens (Human)
Interaction partners:
- Nuclear distribution protein nudE-like 1
Sequence:
MGDSGSRRSTLVSRLPIFRRSINRRHDSLPSSPSSSNTVGVHSSSPSSTNSSSGSTGKRRSIFRTPSISFHHKKGSEPKQEPTNQNLSISNGAQPGHSNMQKLSLEEHIKTRGRHSVGFSSSRNKKITRSLTEDFEREKEHSTNKNVFINCLSSGKSEGDDSGFTEDQTRRSVKQSTRKLLPKSFSSHYKFSKPVLQSQSISLVQQSEFSLEVTQYQEREPVLVRASPSCSVDVTERAGSSLQSPLLSADLTTAQTPSEFLALTEDSVSEMDAFSKSGSMASHCDNFGHNDSTSQMSLNSAAVTKTTTELTGTVPCAIMSPGKYRLEGQCSTESNSLPETSAANQKEVLLQIAELPATSVSHSESNLPADSEREENIGLQNGETMLGTNSPRKLGFYEQHKAIAEHVKGIHPISDSKIIPTSGDHHIFNKTSHGYEANPAKVLASSLSPFREGRFIERRLRSSSEGTAGSSRMILKPKDGNIEEVNSLRKQRAGSSSSKMNSLDVLNNLGSCELDEDDLMLDLEFLEEQSLHPSVCREDSYHSVVSCAAVVLTPMEPMIEMKKREEPEFPEPSKQNLSLKLTKDVDQEARCSHISRMPNSPSADWPLQGVEENGGIDSLPFRLMLQDCTAVKTLLLKMKRVLQESADMSPASSTTSLPVSPLTEEPVPFKDIMKDECSMLKLQLKEKDELISQLQEELGKVRHLQKAFASRVDKSTQTELLCYDGLNLKRLETVQGGREATYRNRIVSQNLSTRDRKAIHTPTEDRFRYSAADQTSPYKNKTCQLPSLCLSNFLKDKELAEVIKHSRGTYETLTSDVTQNLRATVGQSSLKPTAKTEGLSTFLEKPKDQVATARQHSTFTGRFGQPPRGPISLHMYSRKNVFLHHNLHSTELQTLGQQDG
Protein: Aminomethyltransferase folate-binding domain-containing protein (Q57TW5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
LQGLFTNDLRQLQPGGSLWGCFLHHTGRVMCDAYLYQSTRTPEGQVTIMIDVHCGVADTLLEHLKEYRMRKKLEIRSAAEELVVVAAATIGNSISSCGDNAGSSPSSSSATYGGDQELSGPQGVDSFDTLAETFTDPRSFALPATLRKMIVPRKGAPPTLDSEKLYKKFLYAAGVGEGPEVFRPSKTLPFEANTDLLRGVSFHKGCYMGQELTHRTHVMLVTRKRTVPLFLQGELFDGKGGEKTPHVEGTLVIGNQKVGEVLTACGNVGLGLLRLNHVDITTRSFPGLSLSDGTTVDARIPEWWDEKELRKVLTKS
Protein: Ammonium transporter AmtB-like domain-containing protein (Q17463)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable Na
Sequence:
MWSVLHRRQFAIIAGLMQTVFIVLFAKYVKYIDPLDDSRRVYSGTDYPLFQDVHLMIFVGFGFLMAFLKRYGFSAVSVNLLLSAFVIQFAMLLRGFMTVAFQETGLFSIGIPEMISAESSCAAVLITMGVLLGRLTPVQFLLLAFFETGINVLVEHYVFNYLHVNDSGRSLSVHTFGAYFGLAAACVGHKKNVMEMDEHGGIHHSDLFSMIGTLLLWVFFPSFNAAIQEPEDARHRAIMNTYLAMASGTVTTFMISSCVDTLGRFNMIHIQSSTLAGGVAIGSSANAVLHPYHAVIVGVIAALLSVIGHAWISPRLERTFHLFDTCGVHNLHGMPGILAGLLSIGFAYFYEPESYGKTLYHIYPYWIGGELHGDRENVSQAQYQALGLLTILVTAVIGGLLTGCILKIKVWNQVDDPDFPHGEMNYYAQSDVNFLSKYKHAQEQERLREREQMQEIY
Protein: High mobility group protein B2 (High mobility group protein 2) (Q3U566)
Organism: Mus musculus (Mouse)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDLAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSENRPKIKIEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEEEEDEEEEEEDEE
Protein: Ig-like domain-containing protein (Q95PJ6)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSTSFIRRLAFVGLLLGVHAYHSRPKSEEHSPKHAASSSDLFEDDDQSTTLESIARLSAPAHVPIEQPQTSDTEILEHLLTRGYDHRVRPPGEDGTIHGGPVVVSVNMLLRSISKIDNVNMEYSVQLTFRESWVDKRLSFGVKGDAQPDFLILTAGQEIWMPDSFFQNEKQAYKHMIDKPNVLIRVHKDGTILYSVRISLVLSCPMHLQYYPMDVQQCFIDLASYAYTTKDIEYVWKEETPVQLKAGLSSSLPSFQLTNTSTTYCTSKTNTGSYSCLRTIIQLRRQFSYYLLQLYIPSCMLVIVSWVSFWIDRTAVPARVTLGVTTLLTMTTQSSGINAKLPPVAYIKAIDVWIGACMTFIFCALLEFAWVTYIANKQDANKRARTEREKAELPFLQNSHNDVWVPREVAEQEREVMTVRMNRRQTNSVWKWIKTKTEWNDKSKRADLISRVMFPVLFLTFNISYWTHYGQYGVAIST
Protein: Anti-silencing protein 2 (P32448)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Derepression of silent mating type loci when overexpressed.
Interaction partners:
Sequence:
MPKNRGVLDAITRSVIDGSDQESSSSFNSDKEYAAVTKGLSSSRVQKKSSLRQMKSKVKELQSLVNHYRENEAALVSSAKLLSGEIIGYEIKMASLHGKMKSILDENNALKETHKSSAEKRIELVRLPSSKEERNYDEYTLLVNLKKEICAKLQDYKNVQNTVNTKLDEIHTFHEKYYEGLELSLDSKVFDAESSKELAKVRRELNNVRKNSEIKVNNLKMQLLQATKSLEHLKKQAKAKDDYLKCIPELVDKANLTMLSYKKSIANQRETIEALQAELSQQSETKGQIETETQNQVQIPTNVTLVDPFEENNPEDLFAIQEQELQDLRLHKKMADERSRTTHLHLERKNNTIKLLQSYVQSLIQRLPPAQRKHHLGIFQKLGSEKSCPLAPAVASTYAPLLLLSQHSNHQEIDNTPQRLLLAAPDGQSYSEKSTTLNLDYSSRKSYLSRLQPPHIANLKSLTLKTLPRVPTDSPQLPSKDKSQETAKKDDRPKLVANEPVTLDTSTPPVAQSLADSKHCSGLHK
Protein: Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (6-O-methylguanine-DNA methyltransferase) (MGMT) (O-6-methylguanine-DNA-alkyltransferase) (P9WJW5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
Interaction partners:
- Probable bifunctional transcriptional activator/DNA repair enzyme AlkA
- Putative 8-oxo-dGTP diphosphatase 2
- Putative mutator protein MutT4
- Type ISP restriction-modification enzyme LLaBIII C-terminal specificity domain-containing protein
- Probable DNA-3-methyladenine glycosylase I TagA
- Uncharacterized protein Rv1318c
- Endonuclease NucS
Sequence:
MIHYRTIDSPIGPLTLAGHGSVLTNLRMLEQTYEPSRTHWTPDPGAFSGAVDQLNAYFAGELTEFDVELDLRGTDFQQRVWKALLTIPYGETRSYGEIADQIGAPGAARAVGLANGHNPIAIIVPCHRVIGASGKLTGYGGGINRKRALLELEKSRAPADLTLFD
Protein: Probable sterol O-acyltransferase 2 (EC 2.3.1.-) (Sterol-ester synthase 2) (Q9UU82)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P25628}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Probable sterol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Probable diacylglycerol pyrophosphate phosphatase 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Lysophospholipid acyltransferase
- Phosphatidylglycerol/phosphatidylinositol transfer protein
- Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
Sequence:
MIAATPAKSKPSDVNLEQTFKGVSETSKIDLRRSRAAYRPLELSPTPSIFARNYQRNAVDFTGFFVLFWVAVSIMIFMSFLENFELTGRPVVGTIFKYFQSNLLDLAKADLAMSSMFLLAFPFQKIFALGYLRWYGLGVYLYSILILLFLSHCVLRCCLSNWSWTHRAMFILHSMVILMKLHSYNVVNGWYSYCYHSLNKLQSKKTDLDDDERSSVEFYEHCLNHHGNTYPENLTIPNALDFLFMPSLCYQLYYPRTAHVRIHYLIECALGTFGCIFLLVIISDHFMVPVLAKAIRTIIEAPEDASATYFAIRLGHTVAFLMFPFMLSFLLVFWVIFEGVCNFSAEITRFADRNFYDDWWNCWTWDQFARTWNKPVHYFLLRHVYVPLNSFMSKSLSTFFTFFVSSVLHELVMGCITLKIRGYGLFFQMTQIPYIIIQRQKFVRRHRLLGNIAFWFSIIIGIALIAALYILF
Protein: Plant invertase/pectin methylesterase inhibitor superfamily protein (Putative DC1.2 homolog) (Ripening-related protein-like; contains similarity to pectinesterase) (Q9LVA3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable folate-biopterin transporter 7
- Pectinesterase inhibitor 12
- Probable pectinesterase 66
- AT4g15750/dl3915c
- Ras guanine nucleotide exchange factor Q-like protein
- Transducin/WD40 repeat-like superfamily protein
- Pectinesterase inhibitor 2
- Pectinesterase inhibitor 1
- Probable pectinesterase/pectinesterase inhibitor 17
- Pectin lyase-like superfamily protein
Sequence:
MGESFRLFNHHHFLTTFLIIIAMLKLVHTTTTTTTTTTTNTEFVKSSCTFTTYPRLCFSSLSTHASLIQTSPKLMAHAALNITLASAKVTSAMMVRLSNSRLKPKEVSAMRDCVEELGDTLEELRKSIGEMCQLSGSNYEVYISDIQTWVSAALTDVNTCTDGFEGEDMDGKVKVLVRGRILVIAHLTSNALALINHFASIHG
Protein: ATP synthase subunit alpha (Q08BA1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase F1 subunit epsilon
- ATP synthase F1 subunit delta.
- ATP synthase peripheral stalk-membrane subunit b.
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase subunit gamma.
- ATP synthase F
- ATP synthase subunit g
- ATP synthase subunit beta
- ATP synthase subunit d
- ATP synthase-coupling factor 6, mitochondrial
Sequence:
MLSVRVAAALARTLPRRAGFVSKNVAAACVGAKNLHTARPWLQKTGTAEVSSILEEKILGADTGAELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNEGTEEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRSDGKISEASDAKLKEIVLNFLSSFE
Protein: Palmitoyltransferase ZDHHC21 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 21) (DHHC21) (GABA-A receptor-associated membrane protein 3) (Zinc finger DHHC domain-containing protein 21) (Q9D270)
Organism: Mus musculus (Mouse)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane. This affects rapid intracellular signaling by sex hormones via ERK and AKT kinases and the generation of cAMP, but does not affect that mediated by their nuclear receptor (By similarity). Palmitoylates FYN, regulates its localization in hair follicles and plays a key role in epidermal homeostasis and hair follicle differentiation. Through the palmitoylation of PLCB1 and the regulation of PLCB1 downstream signaling may indirectly regulate the function of the endothelial barrier and the adhesion of leukocytes to the endothelium. Has also a palmitoyltransferase activity toward ADRA1D, positively regulating its activity and expression and may thereby play a role in vascular contraction. May also palmitoylate eNOS and LCK.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IVQ6}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:19956733}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8IVQ6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Complex I assembly factor ACAD9, mitochondrial
- Nitric oxide synthase 3
- Palmitoyltransferase ZDHHC13
- Estrogen receptor
Sequence:
MGLRIHFVVDPHGWCCMGLIVFVWLYNIVIIPKIVLFPHYEEGHIPGILIIIFYGISIFCLVALVRASLTDPGRLPENPKIPHAERELWELCNKCNLMRPKRSHHCSRCGHCVRRMDHHCPWINNCVGEDNHWLFLQLCFYTELLTCYALMFSFCHYYYFLPLKKRNLDLFVVRHELAIMRLAAFMGITMLVGITGLFYTQLIGIITDTTSIEKMSNCCEEISRPRKPWQQTFSEVFGTRWKILWFIPFRQRQPLRVPYHFANHV
Protein: DNA repair protein brc-2 (G5EG86)
Organism: Caenorhabditis elegans
Function: Required for the homologous recombination repair of DNA double strand breaks, thereby playing a role in chromosome integrity. Acts by targeting rad-51 to sites of DNA damage and stabilizing rad-51-DNA filaments by blocking ATP hydrolysis catalyzed by rad-51. Promotes rad-51 mediated displacement-loop (D-loop) formation during strand invasion between the invading single-stranded DNA (ssDNA) and the homologous duplex DNA. Also functions independently of rad-51 in DNA double-strand break (DSB) repair by promoting DNA single-strand annealing (SSA) when the homologous recombination (HR) and non-homologous end joining (NHEJ) pathways are compromised. Binds selectively to single-stranded (ssDNA) via its C-terminus. Involved in telomere maintenance and replicative senescence.
Subcellular location: Nucleus {ECO:0000269|PubMed:15798199}. Chromosome {ECO:0000269|PubMed:15798199}. Note=Diffusely localized in the nucleus. Recruited to sites of DNA damage upon induction of DNA double strand breaks by ionizing radiation (IR) or in meiosis. {ECO:0000269|PubMed:15798199}.
Interaction partners:
- DNA repair protein RAD51 homolog
- Breast cancer type 1 susceptibility protein homolog
- FANCD2
- FANCI helical domain-containing protein
- BRCA1-associated RING domain protein 1
- DNA endonuclease activator Ctp1 C-terminal domain-containing protein
- DNA repair and recombination protein RAD54-like
- FANCM homolog
- Regulator of telomere elongation helicase 1 homolog
- RAD51-like protein 1
Sequence:
MGDSSKKVKDSFDTISEPDSFDEPKGVPISMEPVFSTAAGIRIDVKQESIDKSKKMLNSDLKSKSSSKGGFSSPLVRKNNGSSAFVSPFRREGTSSTTTKRPASGGFEDFEAPPAKKSTSSSSKKSKKHSKKEKKKEFKEIHADVLRVSRIYEKDKFRIILQESSSTPLILATCSYNRGSDIKFGDRIHVDAEVCKKSSSGDVTEIYIDRVLKNKENGAKSGIRRHSIAKKPFCIKPRFIHELSDTKIKKTVVQVNLLDLNLDFYAGCSKCKHSLPEAANQCEFCKDSQGKSELSMYSRVRVMDFSGQMFINVTTKNMKKLLDLLGYEGFDNWFRFKDPQERQNYVFRPVMVEIEKSNDEWECTDVAEVDWKDFGSYLKHKEDKKKRRSKKKHP
Protein: Serine and arginine rich splicing factor 3 (A0A8I6A2L6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRVTIMSLLTTL
Protein: C->U-editing enzyme APOBEC-2 (EC 3.5.4.36) (mRNA(cytosine(6666)) deaminase 2) (Q9Y235)
Organism: Homo sapiens (Human)
Function: Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Interaction partners:
- Putative C->U-editing enzyme APOBEC-4
- Apolipoprotein B-100
- Cytidine deaminase
- C->U-editing enzyme APOBEC-1
- APOBEC1 complementation factor
Sequence:
MAQKEEAAVATEAASQNGEDLENLDDPEKLKELIELPPFEIVTGERLPANFFKFQFRNVEYSSGRNKTFLCYVVEAQGKGGQVQASRGYLEDEHAAAHAEEAFFNTILPAFDPALRYNVTWYVSSSPCAACADRIIKTLSKTKNLRLLILVGRLFMWEEPEIQAALKKLKEAGCKLRIMKPQDFEYVWQNFVEQEEGESKAFQPWEDIQENFLYYEEKLADILK
Protein: Secreted phosphoprotein 24 (Spp-24) (Secreted phosphoprotein 2) (Q13103)
Organism: Homo sapiens (Human)
Function: Could coordinate an aspect of bone turnover.
Subcellular location: Secreted.
Interaction partners:
- Alpha-2-HS-glycoprotein
- Homeobox protein cut-like 1
- Matrix Gla protein
- Hsp90 co-chaperone Cdc37-like 1
Sequence:
MISRMEKMTMMMKILIMFALGMNYWSCSGFPVYDYDPSSLRDALSASVVKVNSQSLSPYLFRAFRSSLKRVEVLDENNLVMNLEFSIRETTCRKDSGEDPATCAFQRDYYVSTAVCRSTVKVSAQQVQGVHARCSWSSSTSESYSSEEMIFGDMLGSHKWRNNYLFGLISDESISEQFYDRSLGIMRRVLPPGNRRYPNHRHRARINTDFE
Protein: Lonely heart, isoform A (EC 3.4.24.-) (Q9VKV3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Pericardin
Sequence:
MAKLLLIFSILTILATIHDSSFVQADLTTKERIKKHQDWLREHRKPKTKKKISINSYYELANLWHTRKDLSSPKQKPNNKEEYLENETTSKISNKSDEKVLKSSTIISLNATNPSTSTFKSVLETTTLPSVTTKDLFESGNVATTRQTPKVEEVFSSPNPPQEATSSTSKKAKKKVYPYPRWDKWSDWSSCSRSCGGGVKYQVRKCINRNLLTNNQLTSNACVGYFKRYQLCNDVPCDEQSPDFRASQCSAYNDKEFHGHRYRWEPYVKDDAECELNCMPFGMKSFATLNESVIDGTPCGHPAEYFRSQFWERAVCVDGACKAVQASGEIDGLYAHSGSVSCGGLLCRPVTGIFTRNPLPEHAYIHVTTLPVGASNISITELKNSINLLVLRTSNELAIFNGENTVSESGSYEAVGAVFDYHRIDGAEDSNGVTEWITSIGPIRDSLQLMVFTKSANNTGVKYEYMLPIVSESEENEMSLESSDGLLRSGMEDTSSSSSSRAGRKRIFNWKVIGFSSCTKSCGGGTQTPIIRCIRKNPLRYYSQRRCTHSVKPVLNENLLHCNTQPCPAYWRFDDWGECRCSSSGGLRRREVSCVQELASGLVIHVDKAACMEDQPPMQKQCECPKNRRRNLSRYRLSGPSESSSNSSQVKRSKIDGSDATAIWLVSDWNQYCSVTCGSGVEYRTVFCDRSKAGEQRCDPSTTPESRRPCEKPACELGDWFTGPWSSCNGDCFDLTRTREVLCIRSQLITEHSECTPELKPQSVEKCSHEEVEYCAARWHYSDWSECTKPCGGGTQRRSVRCLEYDIKMNALRESTHCRYTNREPIYRNCNVQACAEVPKTEVTPVCADKFSNCQWASQAKLCSYDYYRDNCCFSCTGGI
Protein: Uncharacterized protein YjbE (P0AF45)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized lipoprotein YjbF
- Uncharacterized lipoprotein YjbH
- Uncharacterized protein YjbG
- UDP-glucose 6-dehydrogenase
Sequence:
MKKVLYGIFAISALAATSAWAAPVQVGEAAGSAATSVSAGSSSATSVSTVSSAVGVALAATGGGDGSNTGTTTTTTTSTQ
Protein: Uncharacterized protein (Q4GZ99)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
- Trans-sialidase
- Uncharacterized protein
Sequence:
MFVRSFCFLRKYGSKSKTPDLKTSFTKTTNFRKAEKISITTTDGEIVKGRGKIRRRTHSALKEAIGAMEHPAIWLWYPWRMNPEPPTPHMPQRRALKNVHGAVFNDLTPVQKKRQEQMLYGVNIPETRQMKFEEQHPLLAGALRKLEGQPKGFPFWYRKYPTRRHAYEYRFSIPVEMLDGYNDDVKKALSKGMMSIQEKQFAQEAMYMERYAEHDFDTTSPAVLAVKRALKCRVLRNHLLTNPHNNIIKTVLANTERKLNHALRRLRKVDFKKYWEIIRDHDVQDILQPPNLVTYRQGSYWKYDWNAGLAISTNLADVMDPRGLNGCVETGRSRSEVARDLGLSYTRPLHENEKKQLSHQAVYYERLAKFKMEQPEAARAMERERFVRKFSGMFVKMDIRSGAPDFPSTYRRLLGTKVVRWASKRHGPN
Protein: Septin-6 (Q14141)
Organism: Homo sapiens (Human)
Function: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis. May play a role in HCV RNA replication. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15774761}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15774761}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15774761}. Cleavage furrow {ECO:0000269|PubMed:15774761}. Midbody {ECO:0000269|PubMed:15774761}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:25588830}. Note=In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle. Found in the sperm annulus (PubMed:25588830). {ECO:0000269|PubMed:25588830}.
Interaction partners:
- Septin-2
- Septin-7
- Uncharacterized protein C17orf47
- Septin-9
- Septin-11
- Septin-5
- Septin-12
- Neuronal-specific septin-3
- Septin-1
- Septin-8
Sequence:
MAATDIARQVGEGCRTVPLAGHVGFDSLPDQLVNKSVSQGFCFNILCVGETGLGKSTLMDTLFNTKFEGEPATHTQPGVQLQSNTYDLQESNVRLKLTIVSTVGFGDQINKEDSYKPIVEFIDAQFEAYLQEELKIRRVLHTYHDSRIHVCLYFIAPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADAISKSELTKFKIKITSELVSNGVQIYQFPTDDESVAEINGTMNAHLPFAVIGSTEELKIGNKMMRARQYPWGTVQVENEAHCDFVKLREMLIRVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPDSKPFSLQETYEAKRNEFLGELQKKEEEMRQMFVQRVKEKEAELKEAEKELHEKFDRLKKLHQDEKKKLEDKKKSLDDEVNAFKQRKTAAELLQSQGSQAGGSQTLKRDKEKKNNPWLCTE
Protein: Inner membrane protein YpjD (P64432)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- UPF0053 inner membrane protein YfjD
- Thiol:disulfide interchange protein DsbC
Sequence:
MPVFALLALVAYSVSLALIVPGLLQKNGGWRRMAIISAVIALVCHAIALEARILPDGDSGQNLSLLNVGSLVSLMICTVMTIVASRNRGWLLLPIVYAFALINLALATFMPNEYITHLEATPGMLVHIGLSLFSYATLIIAALYALQLAWIDYQLKNKKLAFNQEMPPLMSIERKMFHITQIGVVLLTLTLCTGLFYMHNLFSMENIDKAVLSIVAWFVYIVLLWGHYHEGWRGRRVVWFNVAGAVILTLAYFGSRIVQQLIS