wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat-containing protein 44 (Rab11-binding protein) (Rab11BP) (Rabphilin-11) (Q5JSH3)
Organism: Homo sapiens (Human)
Function: Downstream effector for RAB11. May be involved in vesicle recycling (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9R037}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9R037}. Endosome membrane {ECO:0000269|PubMed:32344433}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9R037}. Note=Colocalized with RAB11A, RAB8A, RAB10 and MICAL1 on endosomal tubules (PubMed:32344433). Colocalized with RAB11A along microtubules oriented toward lamellipodia. {ECO:0000250|UniProtKB:Q9R037, ECO:0000269|PubMed:32344433}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein B/C
- Vesicle-associated membrane protein-associated protein A
- Ras-related protein Rab-11A
Sequence:
MASESDTEEFYDAPEDVHLGGGYPVGSPGKVGLSTFKETENTAYKVGNESPVQELKQDVSKKIIESIIEESQKVLQLEDDSLDSKGKELSDQATASPIVARTDLSNIPGLLAIDQVLPEESQKAESQNTFEETELELKKCFPSDETCEKPVDETTKLTQTSSTEQLNVLETETEVLNKEAVEVKGGGDVLEPVSSDSLSTKDFAAVEEVAPAKPPRHLTPEPDIVASTKKPVPARPPPPTNFPPPRPPPPSRPAPPPRKRKSELEFETLKTPDIDVPKENITSDSLLTASMASESTVKDSQPSLDLASATSGDKIVTAQENGKAPDGQTVAGEVMGPQRPRSNSGRELTDEEILASVMIKNLDTGEEIPLSLAEEKLPTGINPLTLHIMRRTKEYVSNDAAQSDDEEKLQSQPTDTDGGRLKQKTTQLKKFLGKSVKRAKHLAEEYGERAINKVKSVRDEVFHTDQDDPSSSDDEGMPYTRPVKFKAAHGFKGPYDFDQIKVVQDLSGEHMGAVWTMKFSHCGRLLASAGQDNVVRIWALKNAFDYFNNMRMKYNTEGRVSPSPSQESLSSSKSDTDTGVCSGTDEDPDDKNAPFRQRPFCKYKGHTADLLDLSWSKNYFLLSSSMDKTVRLWHISRRECLCCFQHIDFVTAIAFHPRDDRYFLSGSLDGKLRLWNIPDKKVALWNEVDGQTKLITAANFCQNGKYAVIGTYDGRCIFYDTEHLKYHTQIHVRSTRGRNKVGRKITGIEPLPGENKILVTSNDSRIRLYDLRDLSLSMKYKGYVNSSSQIKASFSHDFTYLVSGSEDKYVYIWSTYHDLSKFTSVRRDRNDFWEGIKAHNAVVTSAIFAPNPSLMLSLDVQSEKSEGNEKSEDAEVLDATPSGIMKTDNTEVLLSADFTGAIKVFVNKRKNVS
Protein: MUC5B (Q91ZX5)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
PGPDSAEASTCQVHVNATVLRYKGCETEVNITFCEGSCSGISKYSMEAQAMERQCTCCQESKVHDVAVTMQCPDGTVIQHTYTHIDECNCAPACSSLPGTSMIAS
Protein: Glutaminase 2 (EC 3.5.1.2) (P0A6W0)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Glutamine synthetase
- 5-oxoprolinase subunit B
- Glutamate synthase large chain
- Glutamate decarboxylase beta
- Uncharacterized protein YneG
- Glutaminase 1
- Bifunctional protein PutA
- Glutamate decarboxylase alpha
- Glutamate racemase
- NADP-specific glutamate dehydrogenase
Sequence:
MAVAMDNAILENILRQVRPLIGQGKVADYIPALATVDGSRLGIAICTVDGQLFQAGDAQERFSIQSISKVLSLVVAMRHYSEEEIWQRVGKDPSGSPFNSLVQLEMEQGIPRNPFINAGALVVCDMLQGRLSAPRQRMLEVVRGLSGVSDISYDTVVARSEFEHSARNAAIAWLMKSFGNFHHDVTTVLQNYFHYCALKMSCVELARTFVFLANQGKAIHIDEPVVTPMQARQINALMATSGMYQNAGEFAWRVGLPAKSGVGGGIVAIVPHEMAIAVWSPELDDAGNSLAGIAVLEQLTKQLGRSVY
Protein: CSD domain-containing protein (Q57U61)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLFHTTPCSVNGVPLVSFNAVAPFNASMGGPPVATPPGQRTLTTFYSDPTASWQAAVPLGKIASPPPPSRGSAASTPPSLTGSSPSVQHSSPNSQLGFRGHSGIIITSGGGGNVHQFHPHPQQHPTMSGNSSINSTSNMSPLPPGAMPACAWNLSMSPPPPSSQPIYVVLPHGPAPTAGGPMPPGAALTAARAPSSLPTTLPSRRGNGMMYQLGEWYEGVVKRYNPMRGFGFLTATHHLQVIPPDVDNRAGSVSDADGQNSQQTASPPQATLLRTPVTVGDVFVHQSYIRMQGFRALSTGDRVAFRVGKLPGKDANQAVSVQLLSTAKPATGATPTEEEEEDVQGSSSTTATTVLSGFSLTQHSSKDHEGDAQNSAPGVTEHDVTDESVTHSDITVERLLAHITRHAIPSSVASTAEPLDGTDATNDDNIGGNDNMKCSRDGWVENAPTQRRHLPFCPRLEEVAAALEATDFLGEAELTSPPAQWGLLSPSTDARGLFGGFDGK
Protein: Probable U3 small nucleolar RNA-associated protein 11 (U3 snoRNA-associated protein 11) (Q9M223)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Putative U3 small nucleolar ribonucleoprotein
- U3 small nucleolar ribonucleoprotein protein IMP3
- AT3g56990/F24I3_70
- At4g28200
- Nucleolar-like protein
- Ribosomal RNA-processing 7 protein
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- U3 small nucleolar RNA-associated protein 18 homolog
- KRR1 small subunit processome component
- Protein SLOW WALKER 1
Sequence:
MSSLRNAIPRPAHKERSQPEARKRFGILEKHKDYIIRANAYHKKQETLKILRQKAAFKNPDEFNFKMINSKTVDGRHRPKDEVNKYSAEELMIMKTQDIGYVFQKWQSEKNKIDKLTASLQCTGDQSSRRHVYYAEDREEARELEVQGRSKSDISTVEIPKDIKKKMDRSYRDLEGRKSRAKDLEKLYTDMSMQKELQKKGRKRKLRDDELLNPNGKAVYKWRADRKR
Protein: Meiotic sister chromatid recombination protein 1 (Q03104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- 12 kDa heat shock protein
- Catalase T
- Reticulon-like protein 2
- Aldehyde dehydrogenase [NAD
- Glutamate decarboxylase
- Carboxypeptidase Y inhibitor
- Restriction of telomere capping protein 3
- Trehalose synthase complex regulatory subunit TSL1
- Protein FMP16, mitochondrial
- 6-phosphogluconolactonase 4
Sequence:
MKQFKLVNAVSASFVLIGLVLANSDSVFDKWTQEDLADYLRDNKKSLEKYATDSIEDLKTEASQVWDKHAQPKPWWQVWSSDSSSVSNSNPGWFGYTGSSDHPVSDWLFDTWSTDSLRNFLKKNGVDVDDAKASKDSLVKTAKENFNKISKSLKSSGYYPSSSYFDSWSTKDLQNWLNDNGIDYDKAVQSKDELVQKVKENIYRTSEKAEQQRLGLLESLDLAHQQILDTSGQIKDTVFDKWSSDQLTNWLESHKVNIDKNMAKKHDYLVRMAKENSANLKDDIYWYLDYMKRESSPFLTKTPEYVGSVWDSSKNFLTNLYSKFRGKTDNVINDTFLVGLDSWPKDKLKMFLDARGIKYSMLSTEHQLRELVKKSRNEKLKILPKDYQKYFDNSNWSLDDIKGWFADKKDDFQDSQTYSTIMQDFDKVSKNTNDAKDQIAKTWSNTFQSWSQEDLLQYLKSFGVPVKQTSTKDDLINLAKQNTQWLFGTVKEPAYKRYLHNVKNWSKSILGFN
Protein: Proliferating cell nuclear antigen (PCNA) (Q54K47)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Probable replication factor C subunit 4
- Probable replication factor C subunit 3
- Flap endonuclease 1
- DNA polymerase delta catalytic subunit
- Probable replication factor C subunit 2
- DNA-directed DNA polymerase
- DNA mismatch repair protein Msh6
- Probable replication factor C subunit 5
- DNA helicase
- DNA polymerase epsilon catalytic subunit A
Sequence:
MFEARLLQASLLKKILESIKDLVESANFDCSPEGISLQAMDGTHVTLINLVLRNEGFETYNCDRSLSLGLSLVSLSKILKCAGNDDTLTIRARDNESDTVTFVFESPKNDRVSDFEIKLIDIKNEQYSIRKSDYSAVIKMPSAELQRICRDLSIIGEIVTISANKEGVKFSVSGDSGSGNITIKPTSDSDVPAEQATVIESKEPVVLNFALKFLSNFTKATPLSPMVTLSMSEGIPVVVEYKIDDLGFLGFFLAPKIE
Protein: P2X purinoceptor (B4DEG2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU000681}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000681}.
Interaction partners:
Sequence:
MPTYRPPSHRWVFLIKKGYQDVDTSLQSAVITKVKGVAFTNTSDLGQRIWDVADYVIPAQNEGIPDGACSKDSDCHAGEAVTAGNGVKTGRCLRRENLARGTCEIFAWCPLETSSRPEEPFLKEAEDFTIFIKNHIRFPKFNFSKSNVMDVKDRSFLKSCHFGPKNHYCPIFRLGSVIRWAGSDFQDIALEGGVIGINIEWNCDLDKAASECHPHYSFSRLDNKLSKSVSSGYNFRFARYYRDAAGVEFRTLMKAYGIRFDVMVNGKGAFFCDLVLIYLIKKREFYRDKKYEEVRGLEDSSQEAEDEASGLGLSEQLTSGPGLLGMPEQQELQEPPEAKRGSSSQKGNGSVCPQLLEPHRST
Protein: Beta-glucosidase 15 (AtBGLU15) (EC 3.2.1.21) (O64879)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-glucosidase involved in the rapid degradation of flavonol 3-O-beta-glucoside-7-O-alpha-rhamnosides during abiotic stress recovery. No activity with quercetin 3-O-alpha-rhamnoside, quercetin 3-O-beta-galactoside and rutin.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:25468534}.
Interaction partners:
- Endoglucanase 19
- At5g60630
- Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone:MOK16
- F2J10.10 protein
- 16S rRNA
- Probable leucine-rich repeat receptor-like protein kinase At5g49770
- Probable cysteine protease RD21C
- Late embryogenesis abundant
- ACT domain-containing protein ACR7
- CHP-rich zinc finger protein
Sequence:
MRGNYLSLLVVLIVLASNDVLANNNSSTPKLRRSDFPEDFIFGSATSAYQVEGGAHEDGRGPSIWDTFSEKYPEKIKDGSNGSVADNSYHLYKEDVALLHQIGFNAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATMFHWDTPQALEDAYGGFRGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTDGNGATEPYIVGHNLILSHGAAVQVYREKYKASQQGQVGIALNAGWNLPYTESPKDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKGRLPIFTAQQSKMLKGSYDFIGINYYSSTYAKDVPCSTKDVTMFSDPCASVTGERDGVPIGPKAASDWLLIYPKGIRDLVLYAKYKFKDPVMYITENGRDEFSTNKIFLKDGDRIDYYARHLEMVQDAISVGANVKGFFAWSLLDNFEWAMGYTVRFGLVYVDFKDGCKRYPKKSAEWFRKLLNEKKND
Protein: Glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase) (GlyRS) (Glycyl-tRNA synthetase 1) (P41250)
Organism: Homo sapiens (Human)
Function: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17035524}. Cell projection, axon {ECO:0000269|PubMed:17035524}. Secreted {ECO:0000250|UniProtKB:Q9CZD3}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9CZD3}. Note=In transfected COS7 cells, not detected in mitochondria, nor in Golgi apparatus (PubMed:17035524). Secreted by motor neuron, possibly through the exosome pathway (By similarity). {ECO:0000250|UniProtKB:Q9CZD3, ECO:0000269|PubMed:17035524}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:17529987, ECO:0000269|PubMed:26327585}. Cytoplasm {ECO:0000269|PubMed:26327585}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17529987, ECO:0000269|PubMed:26327585}. Cell projection, axon {ECO:0000269|PubMed:25168514}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, mitochondrial
- Gephyrin
- Asparagine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
Sequence:
MPSPRPVLLRGARAALLLLLPPRLLARPSLLLRRSLSAASCPPISLPAAASRSSMDGAGAEEVLAPLRLAVRQQGDLVRKLKEDKAPQVDVDKAVAELKARKRVLEAKELALQPKDDIVDRAKMEDTLKRRFFYDQAFAIYGGVSGLYDFGPVGCALKNNIIQTWRQHFIQEEQILEIDCTMLTPEPVLKTSGHVDKFADFMVKDVKNGECFRADHLLKAHLQKLMSDKKCSVEKKSEMESVLAQLDNYGQQELADLFVNYNVKSPITGNDLSPPVSFNLMFKTFIGPGGNMPGYLRPETAQGIFLNFKRLLEFNQGKLPFAAAQIGNSFRNEISPRSGLIRVREFTMAEIEHFVDPSEKDHPKFQNVADLHLYLYSAKAQVSGQSARKMRLGDAVEQGVINNTVLGYFIGRIYLYLTKVGISPDKLRFRQHMENEMAHYACDCWDAESKTSYGWIEIVGCADRSCYDLSCHARATKVPLVAEKPLKEPKTVNVVQFEPSKGAIGKAYKKDAKLVMEYLAICDECYITEMEMLLNEKGEFTIETEGKTFQLTKDMINVKRFQKTLYVEEVVPNVIEPSFGLGRIMYTVFEHTFHVREGDEQRTFFSFPAVVAPFKCSVLPLSQNQEFMPFVKELSEALTRHGVSHKVDDSSGSIGRRYARTDEIGVAFGVTIDFDTVNKTPHTATLRDRDSMRQIRAEISELPSIVQDLANGNITWADVEARYPLFEGQETGKKETIEE
Protein: E3 ubiquitin-protein ligase HACE1 (EC 2.3.2.26) (HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1) (HECT-type E3 ubiquitin transferase HACE1) (Q8IYU2)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golgi disassembly, ubiquitination serving as a signal for Golgi reassembly later, after cell division. Specifically interacts with GTP-bound RAC1, mediating ubiquitination and subsequent degradation of active RAC1, thereby playing a role in host defense against pathogens. May also act as a transcription regulator via its interaction with RARB.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:21988917}. Cytoplasm {ECO:0000269|PubMed:21988917}. Endoplasmic reticulum {ECO:0000269|PubMed:21988917}. Note=A significant portion localizes to the endoplasmic reticulum. Targeted to Golgi membrane via its interaction with Rab proteins. {ECO:0000269|PubMed:21988917}.
Interaction partners:
- Endosome/lysosome-associated apoptosis and autophagy regulator 1
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYDAQMKSLLRIVRMFCHVFRIGPSSPSNGIDMGYNGNKTPRSQVFKPLELLWHSLDEWLVLIATELMKNKRDSTEITSILLKQKGQDQDAASIPPFEPPGPGSYENLSTGTRESKPDALAGRQEASADCQDVISMTANRLSAVIQAFYMCCSCQMPPGMTSPRFIEFVCKHDEVLKCFVNRNPKIIFDHFHFLLECPELMSRFMHIIKAQPFKDRCEWFYEHLHSGQPDSDMVHRPVNENDILLVHRDSIFRSSCEVVSKANCAKLKQGIAVRFHGEEGMGQGVVREWFDILSNEIVNPDYALFTQSADGTTFQPNSNSYVNPDHLNYFRFAGQILGLALNHRQLVNIYFTRSFYKHILGIPVNYQDVASIDPEYAKNLQWILDNDISDLGLELTFSVETDVFGAMEEVPLKPGGGSILVTQNNKAEYVQLVTELRMTRAIQPQINAFLQGFHMFIPPSLIQLFDEYELELLLSGMPEIDVSDWIKNTEYTSGYEREDPVIQWFWEVVEDITQEERVLLLQFVTGSSRVPHGGFANIMGGSGLQNFTIAAVPYTPNLLPTSSTCINMLKLPEYPSKEILKDRLLVALHCGSYGYTMA
Protein: Uncharacterized mitochondrial carrier P23A10.06 (Q9P7X9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inactive zinc metalloprotease C354.09c
- Iron-sulfur assembly protein 2
Sequence:
MQIGAATEGVEADLSVNAEPDVKPIAKMLSACVGSVITTLTVTPLDVVKTRLQSESISQYSSTQPISSAKILGKGRPAPKPLGGPVSGLYQIARHEGVRSLWRGLVPSLTMLLPANTVQFLGYEQLLPLYSDWGFPAAAAIAGASARTISATIVSPIELFRTRVQAVGGHYPPGHAREIANEVFDGLKLMIHQKGILNLWSGVSVTLWRDVPFSAFYWWSYERIRLFLLGHPSLQAFSSSQSTKDLYINFVSGGISGTLATLLTQPFDVSKTAKQVHGHTLTRGQFMLTLWKRGGPKALWKGTLPRCVKVAPSCAIMISSYHLTKKYFSESVDAY
Protein: Ephrin type-A receptor 8 (EC 2.7.10.1) (EPH- and ELK-related kinase) (Tyrosine-protein kinase receptor EEK) (O09127)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system also plays a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9053851}; Single-pass type I membrane protein {ECO:0000255}. Cell projection {ECO:0000269|PubMed:17875921}. Early endosome membrane {ECO:0000269|PubMed:20496116}. Note=Undergoes clathrin-mediated endocytosis upon EFNA5-binding and is targeted to early endosomes (PubMed:20496116). {ECO:0000269|PubMed:20496116}.
Interaction partners:
- Ephrin-A5
- Ephrin-A1
- Ephrin-A2
- Ephrin-A3
- Ephexin-1
- Ephrin-A4
- Tyrosine-protein kinase ABL1
- Ephrin-B3
- Ras GTPase-activating protein 1
- Ephrin-B1
Sequence:
MAPARARLSPALWVVTAAAAATCVSAGRGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFRPIHTYQVCNVMSPNQNNWLRTNWVPRDGARRVYAEIKFTLRDCNSIPGVLGTCKETFNLHYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRGVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACMACELGFYKSAPGDQLCARCPPHSHSATPAAQTCRCDLSYYRAALDPPSAACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSHCEACGSGTRFVPQQTSLAQASLLVANLLAHMNYSFWIEAVNGVSNLSPEPRSAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLNHPPGKFPETQFSAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGESGEVCYGRLQVPGQRDVPVAIKALKAGYTERQRQDFLSEAAIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDAFLRTHDGQFTIVQLVGMLRGVGAGMRYLSDLGYIHRDLAARNVLVDGRLVCKVSDFGLSRALEDDPEAAYTTAGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNQDVISSVEEGYRLPAPMGCPRALHQLMLDCWHKDRAQRPRFAHVVSVLDALVHSPESLRATATVSRCPPPAFARSCFDLRAGGSGNGDLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLSSTQGPRRHL
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (Q586W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368061}.
Interaction partners:
- DNA replication complex GINS protein SLD5
- Uncharacterized protein
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- GINS subunit domain-containing protein
- DNA helicase
- Cell division cycle 45
- GINS subunit domain-containing protein
- DNA polymerase II subunit 2
- Uncharacterized protein
Sequence:
MLSNRTLTEEQTLIRRHFIDFFESERYEEKYHQLVQEMMAASGSRLLLDMGDLLDFTPTATGFDTTAGLGLNQSASLGACIIREPGKYVPLLELALHDVVLRQQPEYLKVDYRSRAVHVGFEGPVGTVRSPRELYAQHLNTMVALEGIITRQSSNRPRVLETVHYCPETNKFSRKEFRDQLTPMIDSRHLPTVNVMPKTDMEGNVLRTELGLSTFMDSQCAILQEAPERAPTGQLPRTVELRFDDDLVDIVKPGDRVTLVGVYMAYTTSDNKSFQSIVLVNHVIPVQAFTMYRRVPSIEEKLFAFAAKCTQTDGPAGVLNSLSMAVAPTIYGMTNERKAVLLLMVGGVERVAHQSHVRGDINVLLVGEPSTAKSQLLRFVLGVAPLALSTTGKGSSGVGLTAAVSIDAYTGERSLSAGAMVLADRGILCIDEFDKMSAQDRVAMHEAMEQQTVTIAKAGIHASLNARCSVLAAANPIYGFYSVHHRLAFNVGLPESLLSRFDLTFIVLDKHSSEHNRRIGRHILRNHMTAEPVEIDQNITKTVVDSVDSVWAQSGRQGGGAGGGLDFRMTTTSSGETIVGVDFLRAYVQLAKLGRPTLTEASQQLVSQHYVQLRAEQQEGSKDGFFVTARTLEAIVRLATANAKLRLSSTVDEDDVKSAMELLRASVHAATAASQQRAEDNKATAMEKRQGAKRSAEGLTNGAGVDIISGAGNTRRQRQEVEETAAGAVASPAEEMALTTAESSKEITLSRVSNMLRLIQRQDRQPAVRLSDVHARLGGSLSMEELRQAVSELQGDSFVYEAIGEDEWVQFI
Protein: Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (Bladder and breast carcinoma-overexpressed gene 1 protein) (Leukocyte receptor cluster member 4) (Lysophosphatidylinositol acyltransferase) (LPIAT) (Lyso-PI acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 7) (O-acyltransferase domain-containing protein 7) (h-mboa-7) (Q96N66)
Organism: Homo sapiens (Human)
Function: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1-acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Prefers arachidonoyl-CoA as the acyl donor, thus contributing to the regulation of free levels arachidonic acid in cell. In liver, participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23510452, ECO:0000269|PubMed:30959108}; Multi-pass membrane protein {ECO:0000305|PubMed:30959108}. Note=Localized in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. {ECO:0000269|PubMed:23510452}.
Interaction partners:
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Transmembrane 6 superfamily member 2
- Voltage-gated chloride channel TMC4
- 1-acylglycerol-3-phosphate O-acyltransferase PNPLA3
- 17-beta-hydroxysteroid dehydrogenase 13
Sequence:
MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGLTLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSYLLFFRALSLLGLPTPTPFTNAVQLLLTLKLVSLASEVQDLHLAQRKEMASGFSKGPTLGLLPDVPSLMETLSYSYCYVGIMTGPFFRYRTYLDWLEQPFPGAVPSLRPLLRRAWPAPLFGLLFLLSSHLFPLEAVREDAFYARPLPARLFYMIPVFFAFRMRFYVAWIAAECGCIAAGFGAYPVAAKARAGGGPTLQCPPPSSPEKAASLEYDYETIRNIDCYSTDFCVRVRDGMRYWNMTVQWWLAQYIYKSAPARSYVLRSAWTMLLSAYWHGLHPGYYLSFLTIPLCLAAEGRLESALRGRLSPGGQKAWDWVHWFLKMRAYDYMCMGFVLLSLADTLRYWASIYFCIHFLALAALGLGLALGGGSPSRRKAASQPTSLAPEKLREE
Protein: Thioredoxin H7 (AtTrxh7) (Q9XIF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of a number of cytosolic enzymes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Calcium ion-binding protein
- ADP-ribosylation factor C1
- Berberine bridge enzyme-like 7
- Berberine bridge enzyme-like 6
- Peroxidase 38
Sequence:
MGSNVSSVHDVHSSMEITSNGFVVEIESRRQWKSLFDSMKGSNKLLVIDFTAVWCGPCKAMEPRVREIASKYSEAVFARVDVDRLMDVAGTYRAITLPAFVFVKRGEEIDRVVGAKPDELVKKIEQHRV
Protein: GEX Interacting protein (G4SI07)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein F15G9.1
- Cysteine-rich protein 1
Sequence:
MSEYGSAANLSNFRERTGSPSYASLGKHRDDYNRFETARHAMNSRANRSQTSQEKEEIRFGGFGDRAGSGVELTGFNWSGGEVINSPQQLPKAIKPRTMFYSPIGDGTVAADGYELKRRPMDLSPKVTVTQLQHIERGAKGHDGVNIIEKNWSTGGSVPASEAGFGSEYGPGSGRNSRAGGGAFSPEPLPKPANTNGRPAPAPPANDFGNYQPKSDPFPATTRPASGLGGDGGNPFGGSQSNLGPKDGRNSVASSVFSDPSYRLDTKTGYLITNPRELIHQFATMTPVATIDDSVNNTPATHITQKQSYYKRTEETTEEQFAPHAPYKANHPVASPNKFVRQLRDDNLTHSQREANTHTEPVYQRDPNYNQRFQEIRTKSTSYSRGGDDIDQLTQQLVSGMHSGKSRYN
Protein: Iron-binding protein IscA (Iron-sulfur cluster assembly protein) (B7J5X1)
Organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270))
Interaction partners:
- Iron-sulfur cluster assembly scaffold protein IscU
- Co-chaperone protein HscB homolog
- 2Fe-2S ferredoxin
- Nitrogen fixation protein NifU
- Cysteine desulfurase IscS
- Chaperone protein HscA homolog
- Fe-S assembly protein IscX
- Iron-sulfur cluster assembly transcription factor IscR
Sequence:
MALTLSESAARQVRKSIAKRGKGLGIRIGVKTSGCSGLSYVMEFVDVPNPEDLVFPHDDVNLFVDPKSLIYLDGTELDFTREGLNEGFRFNNPNVKDACGCGESFTT
Protein: Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase FPG1) (Formamidopyrimidine-DNA glycosylase 1) (AtFPG-1) (Formamidopyrimidine-DNA glycosylase 2) (AtFPG-2) (Protein MutM homolog 1) (AtMMH-1) (Protein MutM homolog 2) (AtMMH-2) (O80358)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Can process efficiently 4,6-diamino-5-formamidopyrimidine (FapyA), 2,6-diamino-4- hydroxy-5-formamidopyrimidine (FapyG) and the further oxidation products of 8-oxoguanine (8-oxoG), such as guanidinohydantoin and spiroiminodihydantoin. Has marginal activity towards 8-oxoG. Has AP (apurinic/apyrimidinic) lyase activity. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Endonuclease III homolog 1, chloroplastic
- Dephospho-CoA kinase
- Uracil-DNA glycosylase, mitochondrial
- Adenine DNA glycosylase
- Probable inactive uracil-DNA glycosylase
- DNA-
- Uncharacterized protein At2g38710
- Helicase and polymerase-containing protein TEBICHI
- N-glycosylase/DNA lyase OGG1
- DNA repair protein UVH3
Sequence:
MPELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKTIISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKGVAVTKYKRSAVKDSEEWPSKYSKFFVELDDGLELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKKITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTSIKEVIEKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPELQKLYGKDAEKAAKVRPAKRGVKPKEDDGDGEEDEQETEKEDESAKSKKGQKPRGGRGKKPASKTKTEESDDDGDDSEAEEEVVKPKGRGTKPAIKRKSEEKATSQAGKKPKGRKS