wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (O14228)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Bifunctional purine biosynthetic protein ADE1
- Phosphoribosylglycinamide formyltransferase
- Amidophosphoribosyltransferase
- Adenylosuccinate lyase
- Phosphoribosylaminoimidazole carboxylase
- Bifunctional purine biosynthesis protein ade10
- Uncharacterized urease accessory protein ureD-like
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate synthetase
- Probable dihydroorotase
Sequence:
MLVYYGGSALSVQSKKKILELTVSGVSDLNAVYFYLIYTKSNSSLNCESLRPILSDLQESEFKPDGTTMVYVFPRPGTISPWSSKATNIANVCGYKDVIRIERGIAYSVVFKDDISEEMLKSALNHLYDRMTEALRFKLPEEDEVFDKHEPAPLVRIELNCGQGGDKQAATERLNHANKKFGLALAPDEIDYLVECYTSEPSLKSREPTDVELFMFGQVNSEHCRHKIFNADWTIDGEKKDYSLFKMIRNTHLKNPQYTISAYSDNAAVFEGNSGTLFAPVNGIWSMKDEPVEFLGKVETHNHPTAVSPFPGAATGSGGEIRDEGAVGQGSLSKAGLAGYSVSDLNIPGYKQPWELDVGKPYHIATSLDIMLEAPIGSSAFNNEFGRPCINGYFRTFCMEVPRGDGTLEIRGYHKPIMAAGGIGRIRKQHAFKKSIAPGSPIIVLGGPALLVGLGGGAASSMNAGEGSEELDFASVQRGNPEMQRRAQMVIDACTTMDENIIQSIHDVGAGGVSNALPELVHDAGLGARFELRDIPCIEPSMSPMQIWCCESQERYVLSVKSEDLDTFKSICERERCPYGVVGYSTVEQRLILTDRLYNTTPIDLPMEVLFGKPPKMSRVAETQTIPLSKFDSSLKSYLAPSSDPILDAVERVLRMPAVASKSFLITIGDRSVTGLIARDQMVGPWQVPVADVGVTVTSYGKGINTGEALAMGEKPISALVSAAASARMAVAECIMNLVAASIPALDRIRLSANWMAAPSHPGEGAKLYEAVQAIGLELCPSLGISIPVGKDSMSMSMKWNEDGREKSVTAPLSLIITGFSPVDDLYSIWTPQLRKVEDIGSTSLIFIDLANGKQRLGGSILAQSYKQLGDEVPDLDNLDTFKNFINVITQLHKTNYIQAYHDKSDGGLFVTLSEMAFAGHVGIECELDSLSSDNIAALFNEELGAVIQVCDRDIAKVLELFAANGLSTCVHRIGKVLSGQAQTISFSRSGKIIFKSTRSKLHGIWHETSYKMQEIRDNPECARQEMENIADNNDPGLGYHLTFDPNVSVTADLALTSRPKVAILREQGVNGYLEMAYAFYASGFTAVDVHMTDILSGRVHLDDFVGIAACGGFSYGDVLGSGNGWATSILLHEDARNEFYRFFNERKDTFGLGICNGCQLFSRLKSLIPGAKSWPMFTFNESAQYEGRAVMLKIDETSGSKSIFTESMAGSSLPVVVAHGEGRAVFDSESDYEQFKKEGLDLIYYVNNYNERTSRYPFNPNGSRDAIAGVRSPCGRFLAMMPHPERVVLKVANSYYPHSKASEWGVHGPWIRLFQSARKWVG
Protein: Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial (CybS) (CII-4) (Malate dehydrogenase [quinone] cytochrome b small subunit) (QPs3) (Succinate dehydrogenase complex subunit D) (Succinate-ubiquinone reductase membrane anchor subunit) (Q95123)
Organism: Bos taurus (Bovine)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O14521}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MALWRLSVLCGAREGRALFLRTPVVRPALVSAFLQDRPAQGWCGTQHIHLSPSHHSGSKAASLHWTGERVVSVLLLGLIPAAYLNPCSAMDYSLAATLTLHSHWGIGQVVTDYVHGDAVQKAAKTGLLVLSAFTFAGLCYFNYHDVGICKAVAMLWKL
Protein: Anaphase-promoting complex subunit 1 (20S cyclosome/APC complex protein apc1) (Cell untimely torn protein 4) (Q9URV2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Mutations to this protein prevent the exit from mitosis.
Interaction partners:
- Anaphase-promoting complex subunit 11
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit hcn1
Sequence:
MLELKTNVIQDPELKDSLDLQENDRVEIIGDAVHYIVNDHLNRVFNYTVDQQKIHAALITTFASGKKAIVVILDDIGYVYYVGDNNNDSYIINVPFSTESAWSSPSGLYLQRHRSSDENLNTDLPHIFCLNDPLDELTLIKFDGKKILSLFDSIVYVVGEIVVTHNKKEKKLSFWRSRFIDPESDQSIKSSRNRRRESSFSREKNPDLTRSDSIHYTANTRLSEKFEEQGLAYSTIFSHIESFPITGSTSFDSILGNGVLVITTLVKELEKGYMMLFRLVRDRSPYFLDSLQLHAINLSAIKSKHLQKIVVLSSKGKVSLESPMSPSLPIEGTFRSFRVHGATLYLEDTDGVQRYISLDNRASNSLVKWCLSVIRYVLPLREYEIFYTGHLYALFAFKLSHDEAFISSILACFTFFSRDKVHVEPIEDCNEAYSLSSKFHFKKEILIASQLSSHLDYSTFKNYLMPLAITLHFISEELRLDSVVKPRKDQLVALLLQITTWLKWPRYCEYYNFDIAETFLSIPLSIQVDVEEPVGPTSILQWIIECLRSQSTVPFYGLESYGLPHSCSTMFPQTLSLMQLLDCLLNPNMTLQNLVEEMVRLGISRKRCERYPFGILCIIFTVLEIAAEEYSPNWESEELRLVNRLDVDSFLHPKTPKWVFNKQDQEVKEIKALTSTVTDSTLVDTQSFHPYKVVTDMIFREDRRLAEVNKLLNYSSQITIMTEHFDVDLSSVPMQQKVAQCICVRTLSVPIGAGMLTYGSKNPLPTEKVTPRLFNFTLHLHPGTLIIQPNKEFVTQELTEWPEFNVGVALGLSISKFSKEINTSWIMFNRPETLTAYHAGFLFGLGLNGHLKALATWHSFIYLTSKHDTTSIGLLLGLASSYLGSMDAKVTKLLSVHISALLPVGSNELNISPLTQTAGILGIGLLFHDSCHRRMSEVTMEEILASNESELKNEGYKLAAGFSLGLINLGRGSNLPGMSDLKLVSRLQVGISSQATFQSLEAGSPGAIMALTMIYMKTNDLEVAKKIDIPKSRYLLDFYRPDLILLRVAGKNLIMWDEVKADYEWVKYQIPDIMLSQFDLQEKKVLSSDDLLLYNVLAGICFSLGLRFAGTGNPKAKEILINFLDSFIRLCHLPAKTHDERVTAVTVIRCTQIVALSSSCVMAGYCDLDVLRRLRVLHGRMEPVNYGAQMATHMALGILSLGGGRYSLSRSNLAIAALLISFYPQFPRTTQDNRAHLQAARNLWALAVEERCIIPRNQDTKQPCIVPLNVVQKSGAVQKLEAPILLPPYDSISSVSTLGDKYWNLKIDLDNNSDYRELLRESQTLTLMPYDRTSSKEEPLNLFPKLKDTSSPLWNLVKTSRLFQSSNSPLNVASLQESNNKTSLGVKLLLSMDFDNLTRDRLLSLQILLQFFESCWTGVLLNKFHSRQYLFLSRDLVEDLSLRVWEYVYSHNHNEESV
Protein: Paired box protein Pax-5 (B-cell-specific transcription factor) (BSAP) (Q02548)
Organism: Homo sapiens (Human)
Function: Transcription factor that plays an essential role in commitment of lymphoid progenitors to the B-lymphocyte lineage. Fulfills a dual role by repressing B-lineage inappropriate genes and simultaneously activating B-lineage-specific genes. In turn, regulates cell adhesion and migration, induces V(H)-to-D(H)J(H) recombination, facilitates pre-B-cell receptor signaling and promotes development to the mature B-cell stage. Repression of the cohesin-release factor WAPL causes global changes of the chromosomal architecture in pro-B cells to facilitate the generation of a diverse antibody repertoire.
Subcellular location: Nucleus {ECO:0000269|PubMed:31941781}.
Interaction partners:
- Protein C-ets-1
- Transcription factor COE1
- DNA-binding protein Ikaros
- Interferon regulatory factor 4
- B-cell antigen receptor complex-associated protein alpha chain
- Transducin-like enhancer protein 4
- B-cell lymphoma 6 protein
- Runt-related transcription factor 1
- B-lymphocyte antigen CD19
- PR domain zinc finger protein 1
Sequence:
MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQTTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTLPGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPYYYSAAARGAAPPAAATAYDRH
Protein: SUMOylated effector protein AmpA (P100) (Q2GIB5)
Organism: Anaplasma phagocytophilum (strain HZ)
Function: Secreted effector that hijacks host cell SUMOylation during A.phagocytophilum infection and is important for the pathogen's intracellular survival.
Subcellular location: Secreted {ECO:0000269|PubMed:20212090, ECO:0000269|PubMed:25308709}. Host membrane {ECO:0000269|PubMed:20212090}; Multi-pass membrane protein {ECO:0000305|PubMed:20212090}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:25308709}. Note=Localizes to the A.phagocytophilum-occupied vacuolar membrane (AVM) (PubMed:20212090). Potentially traverses the AVM 3 or fewer times by means of the 3 bilobed hydrophobic alpha-helical domains that are predicted to be in each direct repeat (PubMed:20212090). Colocalizes with SUMO2/3 on the AVM and in the host cytosol throughout the infection cycle (PubMed:25308709). Only late during the infection cycle AmpA colocalizes with SUMO1, which terminally caps poly-SUMO2/3 chains (PubMed:25308709). Is probably not secreted via the type IV secretion system (T4SS) (PubMed:20212090). {ECO:0000269|PubMed:20212090, ECO:0000269|PubMed:25308709}.
Interaction partners:
Sequence:
MYGIDIELSDYRIGSETISSGDDGYYEGCACDKDASTNAYSYDKCRVVRGTWRPSELVLYVGDEHVACRDVASGMHHGNLPGKVYFIEAEAGRAATAEGGVYTTVVEALSLVQEEEGTGMYLINAPEKAVVRFFKIEKSAAEEPQTVDPSVVESATGSGVDTQEEQEIDQEAPAIEEVETEEQEVILEEGTLIDLEQPVAQVPVVAEAELPGVEAAEAIVPSLEENKLQEVVVAPEAQQLESAPEVSAPAQPESTVLGVAEGDLKSEVSVEANADVAQKEVISGQQEQEIAEALEGTEAPVEVKEETEVLLKEDTLIDLEQPVAQVPVVAEAELPGVEAAEAIVPSLEENKLQEVVVAPEAQQLESAPEVSAPAQPESTVLGVTEGDLKSEVSVEADAGMQQEAGISDQETQATEEVEKVEVSVETKTEEPEVILEEGTLIDLEQPVAQVPVVAEAELPGVEAAEAIVPSLEENKLQEVVVAPEAQQLESAPEVSAPVQPESTVLGVTEGDLKSEVSVEADAGMQQEAGISDQETQATEEVEKVEVSVEADAGMQQELVDVPTALPLKDPDDEDVLSY
Protein: Serine/threonine-protein kinase SRK2G (EC 2.7.11.1) (Arabidopsis protein SK1) (OST1-kinase-like 8) (SNF1-related kinase 2.1) (SnRK2.1) (P43292)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000269|PubMed:18433157}.
Interaction partners:
- Protein phosphatase 2C 7
- Protein phosphatase 2C 77
- Protein phosphatase 2C 37
- Probable protein phosphatase 2C 75
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 78
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
Sequence:
MDKYDVVKDLGAGNFGVARLLRHKDTKELVAMKYIERGRKIDENVAREIINHRSLKHPNIIRFKEVILTPTHLAIVMEYASGGELFDRICTAGRFSEAEARYFFQQLICGVDYCHSLQICHRDLKLENTLLDGSPAPLLKICDFGYSKSSILHSRPKSTVGTPAYIAPEVLSRREYDGKHADVWSCGVTLYVMLVGAYPFEDPNDPKNFRKTIQRIMAVQYKIPDYVHISQECKHLLSRIFVTNSAKRITLKEIKNHPWYLKNLPKELLESAQAAYYKRDTSFSLQSVEDIMKIVGEARNPAPSTSAVKSSGSGADEEEEEDVEAEVEEEEDDEDEYEKHVKEAQSCQESDKA
Protein: Vitelline membrane protein 15a-2 [Cleaved into: Trypsin-modulating oostatic factor (TMOF) (OOSH)] (P19425)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Has an oostatic activity. Inhibits trypsin biosynthesis in the midgut epithelial cells which indirectly reduces the vitellogenin concentration in the hemolymph resulting in inhibition of oocyte development.
Subcellular location: Secreted {ECO:0000269|PubMed:14506222, ECO:0000269|PubMed:2394318}. Note=Secreted from the ovary, starting 18 hours after a blood meal, circulates in the hemolymph.
Interaction partners:
Sequence:
MNKIIAALVLFTAVIGALADYPAPPPPPPKPYHAPPPPPYHAPPHHAPAPLHPVVHTYPVKAPAAKCGANLLVGCAPSVAHVPCVPVHPHPPPPAHY
Protein: Odontogenic ameloblast-associated protein (Apin) (A1E960)
Organism: Mus musculus (Mouse)
Function: Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q3HS83}. Cytoplasm {ECO:0000250|UniProtKB:A1E959}. Nucleus {ECO:0000250|UniProtKB:A1E959}.
Interaction partners:
- Amelotin
- Enamelin
- Secretory calcium-binding phosphoprotein proline-glutamine-rich 1
- Kallikrein-4
- Ameloblastin
- Amelogenin, X isoform
Sequence:
MKIIILLGLIGASSSAPLISQRLLSASNSHELLLNLNNGQLLPLQFQGAFNSWIPPFPGFLQQQQAQVSGRPQFTLSTLESFAGLFPNQIPLSRQVGLAQGGQAGQPDLSQQQTPPQTQQSASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQTVTSSPQHTGQQLFEEQIPFYNQFGFAPPQAEPGVPGGQQHLAFDSFVGTAPETPGMPVEGSLLYPQKEPISFKHDNAGVFMPTTSPKPSTDNFFTSGIDPTIAPEQKVKTDSLREP
Protein: E3 ubiquitin-protein ligase MARCHF1 (EC 2.3.2.27) (Membrane-associated RING finger protein 1) (Membrane-associated RING-CH protein I) (MARCH-I) (RING finger protein 171) (RING-type E3 ubiquitin transferase MARCHF1) (Q8TCQ1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q6NZQ8}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:14722266}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:19117940}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:19117940}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- T-lymphocyte activation antigen CD86
- HLA class II histocompatibility antigen, DR alpha chain
- HLA class II histocompatibility antigen, DP alpha 1 chain
- Ubiquitin-conjugating enzyme E2 H
- Ubiquitin-conjugating enzyme E2 R1
- Ubiquitin-conjugating enzyme E2 D1
- Transferrin receptor protein 1
Sequence:
MLGWCEAIARNPHRIPNNTRTPEISGDLADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTAKKLEKNFSCNVNTDIKDAVVVPVPQTGANSLPSAEGGPPEVVSV
Protein: Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Gp58) (Intracellular mannose-specific lectin MR60) (Lectin mannose-binding 1) (P49257)
Organism: Homo sapiens (Human)
Function: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Multiple coagulation factor deficiency protein 2
- Protein transport protein Sec31A
- Surfeit locus protein 4
- Coagulation factor VIII
- Protein transport protein Sec16A
- Coatomer subunit beta
- Protein transport protein Sec24C
- Golgin subfamily A member 2
- Endoplasmic reticulum resident protein 44
- Protein transport protein Sec23A
Sequence:
MAGSRQRGLRARVRPLFCALLLSLGRFVRGDGVGGDPAVALPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGADGLAIWYAENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQNDGASQALASCQRDFRNKPYPVRAKITYYQNTLTVMINNGFTPDKNDYEFCAKVENMIIPAQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPAEEIFESVGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISKRGAGMPGQHGQITQQELDTVVKTQHEILRQVNEMKNSMSETVRLVSGMQHPGSAGGVYETTQHFIDIKEHLHIVKRDIDNLVQRNMPSNEKPKCPELPPFPSCLSTVHFIIFVVVQTVLFIGYIMYRSQQEAAAKKFF
Protein: Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) (Protein p15) (P11187)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04110}.
Interaction partners:
Sequence:
MQISQAGINLIKSFEGLQLKAYKAVPTEKHYTIGYGHYGSDVSPRQVITAKQAEDMLRDDVQAFVDGVNKALKVSVTQNQFDALVSFAYNVGLGAFRSSSLLEYLNEGRTALAAAEFPKWNKSGGKVYQGLINRRAQEQALFNSGTPKNVSRGTSSTKTTPKYKVKSGDNLTKIAKKHNTTVATLLKLNPSIKDPNMIRVGQTINVTGSGGKTHKVKSGDTLSKIAVDNKTTVSRLMSLNPEITNPNHIKVGQTIRLS
Protein: Exocyst complex component 5 (Exocyst complex component Sec10) (Q18406)
Organism: Caenorhabditis elegans
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 3
- Exocyst complex component 7
- Exocyst complex component 6
- Exocyst component Exo84 C-terminal domain-containing protein
- Exocyst complex component 4
- Exocyst complex component 2
- Exocyst complex component 1
- Rab8
- ADP-ribosylation factor 6
- Ras-related protein Rab-10
Sequence:
MRFEEEIGSLQMLCDQFQNKINTLEKQMNEEKKDYVQKLHRLHEKNGEAIDKMKQLDHTMQAVSTKVVHLGDQLESVDQPRSRAHDAHQLMQHFDEFLSDQPLNSMIFTDPDKLLESADLVHKLYSISQELNKDKFANVQARIGQRYKVVEDLLIEEFVRSQRDEKKMAEVAKILSEFKGYSGCVDRYVDFLCQSIHPRGDGGEILADCLQLCRTQQPRISAIFPSPHTVMQKLVLNIFTGRMKETITARLRECKDTDDQEHYLRDLAYLYSSTLKMCKELEKLHISPDSAFLSTLTDSIFQRYIATYCSEELKYLNDQCSNLLQRFYESKKHVKKQIGGGLHELKRDVAARLMNVETYGGETFVAEDVAISILQETKNAFGRANQLCDKEELPRHVENIVDVLLKYLYGEHLDYAVETGLAGISLAESKTEPPAYFFSVVAKCTSVILLMIKQFEDPIFPIIKETIVEPSVAKKWQQSLRSLESKMSLGLERQLNSIVGYVKFLFSEQKKTDFRPDSQQIDIRVSPQCQLASRFLANQVAAMELGCDGENLEALQSDLATRLFKFMLTHIQQFTYNSTGAVLLLCDVGELRTLVSKWRVQNALTQWESLQALTNLLAVLPDQVNETAHSSLLENVDRQLIHDFVRLRTDFRSIKNFQI
Protein: TSSK6-activating co-chaperone protein (SSTK-interacting protein) (SIP) (SSTK-IP) (Q96A04)
Organism: Homo sapiens (Human)
Function: Co-chaperone that facilitates HSP-mediated activation of TSSK6.
Interaction partners:
Sequence:
MERHTSHPNRKVPAKEEANAVPLCRAKPSPSYINLQASSPPATFLNIQTTKLPSVDHKPKECLGLLECMYANLQLQTQLAQQQMAVLEHLQASVTQLAPGRGSNNSSLPALSPNPLLNHLPQFSK
Protein: Nucleoside transporter 1 (PfNT1) (Equilibrative nucleoside transporter 1) (Equilibrative nucleoside transporter type 1) (PfENT1) (Q8IDM6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000269|PubMed:11682491, ECO:0000269|PubMed:16751273}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Hypoxanthine phosphoribosyltransferase
- Nucleoside transporter 3, putative
Sequence:
MSTGKESSKAYADIESRGDYKDDGKKGSTLSSKQHFMLSLTFILIGLSSLNVWNTALGLNINFKYNTFQITGLVCSSIVALFVEIPKIMLPFLLGGLSILCAGFQISHSFFTDTQFDTYCLVAFIVIGVVAGLAQTIAFNIGSTMEDNMGGYMSAGIGISGVFIFVINLLLDQFVSPEKHYGVNKAKLLYLYIICELCLILAIVFCVCNLDLTNKNNKKDEENKENNATLSYMELFKDSYKAILTMFLVNWLTLQLFPGVGHKKWQESHNISDYNVTIIVGMFQVFDFLSRYPPNLTHIKIFKNFTFSLNKLLVANSLRLLFIPWFILNACVDHPFFKNIVQQCVCMAMLAFTNGWFNTVPFLVFVKELKKAKKKKEIEIISTFLVIAMFVGLFCGIWTTYIYNLFNIVLPKPDLPPIDVTQ
Protein: AT11552p (Testis1) (Q24182)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MANNFNTRKVMQVAEEGAPPVHIPIMVGNEIIVLTQQDIRRVEDTRVISYSRVGPNGQFLPLDTSSPGAVYFPPPNTTHFCTLDDLIRNASDKRETSNPLKTVASVSTQLVWSKKKSGSEHRLPLCYDAGTSTSGLMTNTGCQHCPKCETQHSSCQTQMFAKTQTTVEREMPRNASCQTKDTATPTRTSIVKAPQNVGCQTQSCLSENTYMKNEPANSRCQAQRNTNSTGCGTYSDLFETTSAESYTSAECDYTSSVESTCQHCKSQPTCTDQTLIVPMQPQVQSPVPPQEQPCTSRHIRFDLCTQVNNFEPHVEPHFYRTIPLGQNPYPRAQVSKPSVPKHTGWTNLNPDHEILQQELSQNASP
Protein: Maturin (Maturin neural progenitor differentiation regulator protein) (Q7ZX36)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in early neuronal development; required for cell cycle exit and differentiation of primary neurons (By similarity). Cooperates synergistically with pak3 to promote primary neural differentiation within the neural plate. May play a role in promoting megakaryocyte differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N3F0}.
Interaction partners:
Sequence:
MDFQQLADVADKWCSNTPFDLIATEETERRMDFYADPGVSFYVLCPESGCGDHFHVWSESEDCLPFLQLAQDYISSCGKKTLHEILEKVFKSFRPLLGLPDVDDDTFEEYNADVEEEEPEADHQQMGVSQQ
Protein: Glucose transporter 2A (Q06222)
Organism: Trypanosoma brucei brucei
Function: Facilitative glucose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MTERRDNVSHAPDAIEGPNDGAHAEDTSPGFFSFENLGVAQVQVVGGTLNGFSIGFVAVYILLYEVATNCSLFKTTEACKAVGSYGCEWKDTEVCSWKKECDSDSDGVNPCESLIGYSSLYSGIFASAMIVGSMVGSIIAGKCITMFGLKKSFIIVGVMSVVASALNHISVATNEFWVLCAGRVLMGIGLGVVCVICPMYVNENAHPKLSKVDGVLFQVFITFGIMLAAMLGLILDKTVNYDNDPDMAGRFHGFCAVSSVLSVAMFLVGMFLRESTATFSQDDDGKADGGMDPNEYGWGQMLWPLFMGAVTAGTLQLTGINAVMNYAPKITENLGMDPSLGNFLVMAWNFVTSLVAIPLASRFTMRQMFITCSFVASCMCLFLCGIPVFPGVAEEKVKNGVATTGIALFIAAFEFGVGSCFFVLAQDLFPPSFRPKGSSFVVMMQFIFNILINLLYPITTEAISGGATGDQDKGQAVVFILFGLIGLICFVLQFFYLYPYDANQDHENDHGTEPVERILSPVDVPTPRN
Protein: Cytochrome b-c1 complex subunit 8-1, mitochondrial (Complex III subunit 8-1) (Complex III subunit VIII) (Ubiquinol-cytochrome c oxidoreductase subunit 8-1) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) (Q9SG91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08525}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 10, mitochondrial
- TonB-dependent heme receptor A
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
Sequence:
MGKQPVKLKAVVYALSPFQQKIMTGLWKDLPEKIHHKVSENWISATLLVTPVVGTYWYAQYFKEQEKLEHRF