wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase subunit 4, mitochondrial (O94373)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit a
- ATP synthase subunit d
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit 9, mitochondrial
- Putative ATP synthase subunit epsilon, mitochondrial
Sequence:
MSSKLFCLRSFPSVQRTAWQRLVLPSTRKFSLTPTTFDKTPSGRIPPDQKAANIISSVPSTSLLTKSGVLTVTAAALATAISKGIYVVNDESIVVASFLGLVGVFGTLGRKAYNEWSDKTIAKIGGIMQAARNDHTSAIRERIDQVASLQEVESVTQALFHTSKETARMEAEIFELEQRVALAKEAKSVLDSWVHHEANVRAEQQERLVEDVLARVNSKVSTQKFQQDALNESLGEIEKVLASA
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (Oligodendrocyte GTP-binding protein) (P33237)
Organism: Ovis aries (Sheep)
Function: Interferon-induced dynamin-like GTPase with antiviral activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx2
- Interferon-induced, double-stranded RNA-activated protein kinase
- Interferon regulatory factor 9
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- E3 ubiquitin-protein ligase TRIM21
- USP domain-containing protein
- Interferon-induced protein with tetratricopeptide repeats 1
- C-X-C motif chemokine
- Receptor transporter protein 4
Sequence:
MVLSDLDIKEPDSPESGLNGSDDMVREHETESKGNLYSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLRLKKLEKEGEWKGKVSFLDREIEISDASQVEKEISEAQIAIAGEGMGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPHDIEYQIKSLIRKYILRQETINLVVVPANVDIATTEALRMAQDVDPQGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQHRLSLDKALQRERIFFEDHTHFRDLLEEGRATIPCLAERLTNELIMHICKTLPLLENQIKETHQRITEELQKYGKDIPEEESEKMFSLIEKIDTFNKEIISTIEGEEHVGQYDSRLFTKVRAEFCKWSAVVEKNFEKGHEAIRKEIKQFENRYRGRELPGFVNYKTFEIIIKKQVIVLEEPAVDMLHTVTDIIRNTFTEVSGKHFSEFFNLHRTAKSKIEDIRLEQENEAEKSIRLHFQMEQLVYCQDQVYRRALQQVREKEAEEEKKKKSNHYYQSEDSEPSTAEIFQHLMAYHQEVSTRISSHIPLIIQFFVLRTYGEQLKKSMLQLLQDKDQYDWLLKERTDTRDKRKFLKERLERLSRARQRLAKFPG
Protein: NAD-dependent deacetylase sir2A (EC 2.3.1.286) (Silent information regulator sir2A) (Q54QE6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: NAD-dependent deacetylase, which plays an important role in the regulation of transcriptional repression.
Interaction partners:
- NAD-dependent deacetylase sir2D
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- NAD+ kinase family protein
- NAD+ kinase family protein
- NAD
- NAD-dependent deacetylase sir2E
Sequence:
MYAVNPIECIHLKDEYDTCINKSIFDKDLKITKCHACNDESENWICMTCGVVSCSRHVNGHAGEHFENTKHPISASFSDHSFWCYTCDTYVHNTPLFDICEILENIKSSNKKDKIVPKKDQKEEEEEDQVVPSASITTSSTTTSISKQTTVNNTTTTSSSSTTTTTTTTSTTINNNEEEEESESETDESSSEGEESLSLIQRMREMIFGVGRGPKIVAPSEQEESEEDESCVLKKPTIEEIAKYINSAKCKNIIVMTGAGISVAAGIPDFRSPKTGLYEKLDKYDLPYREAIFDIEYFKKNPKPFYVLSKELFPGSFNPTTVHYFIKLLSDKGLLLRNFTQNIDTLERIAGIPANKLVEAHGSFATSHCVSCKKEYSTEYVKERIFKDELPECTETSGCKGIVKPDIVFFGESLPSRFNDCAREDFTKCDLLLVIGTSLKVHPFASLINFAKGCPRVLINFEEVGTNPYGGFKFNQPSNKLDVKCIGDCQTLVLDLIKLLGWENEFNQIVKN
Protein: Respiration factor 2 (Zinc finger protein ZMS1) (P46974)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor that regulates expression of both nuclear and mitochondrial genes, and more specifically those required for glycerol-based growth and respiration.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MEPFAFGRGAPALCILTAAARINLDNFVPCCWALFRLSFFFPLDPAYIRNENKETRTSWISIEFFFFVKHCLSQHTFFSKTLAPKRNFRAKKLKDIGDTRIDRADKDFLLVPEPSMFVNGNQSNFAKPAGQGILPIPKKSRIIKTDKPRPFLCPTCTRGFVRQEHLKRHQHSHTREKPYLCIFCGRCFARRDLVLRHQQKLHAALVGTGDPRRMTPAPNSTSSFASKRRHSVAADDPTDLHIIKIAGNKETILPTPKNLAGKTSEELKEAVVALAKSNNVELPVSAPVMNDKREKTPPSKAGSLGFREFKFSTKGVPVHSASSDAVIDRANTPSSMHKTKRHASFSASSAMTYMSSSNSPHHSITNFELVEDAPHQVGFSTPQMTAKQLMESVSELDLPPLTLDEPPQAIKFNLNLFNNDPSGQQQQQQQQQQNSTSSTIVNSNNGSTVATPGVYLLSSGPSLTDLLTMNSAHAGAGGYMSSHHSPFDLGCFSHDKPTVSEFNLPSSFPNTIPSNSTTASNSYSNLANQTYRQMSNEQPLMSLSPKNPPTTVSDSSSTINFNPGTNNLLEPSMEPNDKDSNIDPAAIDDKWLSEFINNSDPKSTFKINFNHFNDIGFIYSPPSSRSSIPNKSPPNHSATSLNHEKASLSPRLNLSLNGSTDLPSTPQNQLKEPSYSDPISHSSHKRRRDSVMMDYDLSNFFSSRQLDISKVLNGTEQNNSHVNDDVLTLSFPGETDSNATQKQLPVLTPSDLLSPFSVPSVSQVLFTNELRSMMLADNNIDSGAFPTTSQLNDYVTYYKEEFHPFFSFIHLPSIIPNMDSYPLLLSISMVGALYGFHSTHAKVLANAASTQIRKSLKVSEKNPETTELWVIQTLVLLTFYCIFNKNTAVIKGMHGQLTTIIRLLKASRLNLPLESLCQPPIESDHIMEYENSPHMFSKIREQYNAPNQMNKNYQYFVLAQSRIRTCHAVLLISNLFSSLVGADCCFHSVDLKCGVPCYKEELYQCRNSDEWSDLLCQYKITLDSKFSLIELSNGNEAYENCLRFLSTGDSFFYGNARVSLSTCLSLLISIHEKILIERNNARISNNNTNSNNIELDDIEWKMTSRQRIDTMLKYWENLYLKNGGILTPTENSMSTINANPAMRLIIPVYLFAKMRRCLDLAHVIEKIWLKDWSNMNKALEEVCYDMGSLREATEYALNMVDAWTSFFTYIKQGKRRIFNTPVFATTCMFTAVLVISEYMKCVEDWARGYNANNPNSALLDFSDRVLWLKAERILRRLQMNLIPKECDVLKSYTDFLRWQDKDALDLSALNEEQAQRAMDPNTDINETIQLIVAASLSSKCLYLGVQILGDAPIWPIILSFAHGLQSRAIYSVTKKRNTRI
Protein: Ubiquitin-conjugating enzyme E2, putative (Q586L8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-activating enzyme E1, putative
- Leucine-rich repeat protein
- Small ubiquitin protein, putative
- Ubiquitin activating enzyme, putative
- Proliferating cell nuclear antigen
- Polyubiquitin, putative
- Ubiquitin-conjugating enzyme, putative
- SP-RING-type domain-containing protein
- SP-RING-type domain-containing protein
- SP-RING-type domain-containing protein
Sequence:
MSGLSLAQSRLREERKAWRKERPFGFWAKPREIKSVQHQQPNNVLTALAKSSAAPQTHQGSGSSQTAGDNSGGLDLLEWEAGIPGKPGTPFEGGEFRLFLHFSEDYPTKPPKCVFNPVLFHPNVYPSGTVCLSILNEEKDWRPSITIKQILLAIQELLDNPNINDPAQEEPFRVYTRDRQEYEERVRQEVAKHHRKRV
Protein: Gene model 561, (NCBI) (Small integral membrane protein 26) (Q3V460)
Organism: Mus musculus (Mouse)
Interaction partners:
- Oxidoreductase-like domain-containing protein 1
Sequence:
MRAEKASLWYRRMSLVYALGAWSLLGSAFFLSRKQKVSDCEEGQEDGSRNETPFSTSEDSDLETETVELGGGFYVKSFLKYSENSVPATQRFLTYLKSWTGGPGPQA
Protein: Structural maintenance of chromosomes protein 1 (High incidence of males protein 1) (O01789)
Organism: Caenorhabditis elegans
Function: Involved in chromosome cohesion during cell cycle and in DNA repair (By similarity). Required for chromosome segregation during mitosis. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Chromosome {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues (PubMed:12827206). Colocalizes with rec-8 along synapsed chromosomes during meiotic pachytene and diakinesis (PubMed:12827206). Diffuse nuclear accumulation in meiotic pachytene (PubMed:21856158). {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}.
Interaction partners:
- Cohesin subunit scc-3
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein 1
- Rad21_Rec8 domain-containing protein
- Cnd1 domain-containing protein
- Nipped-B-like protein scc-2
- Structural maintenance of chromosomes protein 6 homolog smc-6
- Condensin complex subunit capg-1
- Wings apart-like protein homolog 1
- N-acetyltransferase ESCO2
Sequence:
MRGGSSLDSFPGKGTLHTLEIENFKSYKGKHTIGPFTRFTAIIGPNGSGKSNLMDAISFVLGEKPSSLRVRKYADLIHGAPINKPVAKKCRVTMNYKYSDGKVKAFTRGVNNGTSEHLLDGQTVTSAAYSQEMESINIFIKARNFLVYQGAIENIAMKTPKERTQLFEELSRSHEFQAEYERLKVEMTKAEDDTQHNMNKRRGIAQEKREAKMEKDEAEKYQTMKNELAAKSTMLFLHQLFHCERTIDESKEEINAQKKTIASLEATRSKEEAKIAAVHQEHRKALREVQKMTRKLDQKETDLAEKQQNMLTLKVSVAHEHKKLEIAKKMLAAAESKAENNSTQLADLKKSKKELEKKKAAYEAEIQDMMQRGELNLSDEQVREYGQLKDQAQRESAMVQRELLMAEQVFEGDKSSLNHELRRQKEHQERVKAKEGDVRRIETQIATLAQRIKETEEETKILKADLKKIENDVVIDKSAAAEYNKELVAVVRQLSEASGDSAEGERNQRRTEALEGLKKNFPESVYGRLVDLCQPSHKRFNIATTKILQKHMNSIVCDTEETAAKAIVYLKDHRYPPETFLPNDALVVNPLNEKLREIKKPAGVKLVFDVINPQHQAARKALQFVCGNALVCESQEDAKQLAYGGGELKDRFKAVSMDGTLFQQSGVMSGGSADLRQKSKKWDEKVVKQLREKRNQLNEKIADLQKHRRRELEVESVRSKINGNEQRLAMMKRDLKNMREMQLERLQNELEGMTAEMNMLPPRISNCQEKLERSESTLKSLQTKSNEVADRIFADFCTRVGIASIRDYENREMRIKQEMEDKLRSFDDDIQKLAYEIDFVTEQDGNRKVEVEKEKVSQIDRQYKDMKKKEKTAAAALKEHTESMEQDKEVLEEKKALSHKLETEWNEVKKIAQVAMKDFTKAEKELLRLESLLTKKQYERHSLLHSVKLGQIALPLKSGSMADVEYEEDDGDDTASQSSQSATDGPSVSEEQIQREQHIKINYDSLPREYKDVDDDDGVRQMSNRLNVEIDELQKNVSKMNAPNLKANQRMAEVKEREAESTEELENARKKAKRIRQQFEKVKTDRYRRFQDFFDPVANTIDDIYKQLSRNTSAQAFLGADNMEEPYLDGIQYNCVAPGKRFRPMDNLSGGEKTIAALALLFAVHGRNPAPFFVLDEIDAALDNTNIGKVASYICESAREHMQIIVISLKEEFYNKADSLIGIFPYPAACTTSGVLTFDLTRFKQIGLNEMTENPPTPSIAT
Protein: Matrix protein VP40 (Marburg VP40) (mVP40) (Membrane-associated protein VP40) (P35260)
Organism: Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain Kenya/Musoke/1980))
Function: Plays an essential role virus particle assembly and budding. Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. The interaction with host E3 ubiquitin ligase SMURF2 facilitates virus budding. The interaction with the nucleocapsid and the plasma membrane may also facilitate virus budding. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur (By similarity). May play a role in genome replication (By similarity).
Subcellular location: Virion membrane {ECO:0000269|PubMed:14963134}; Peripheral membrane protein. Host late endosome membrane {ECO:0000269|PubMed:11799178}; Peripheral membrane protein {ECO:0000305|PubMed:14963134}. Host cell membrane {ECO:0000269|PubMed:11799178, ECO:0000269|PubMed:28580138}; Peripheral membrane protein; Cytoplasmic side {ECO:0000305|PubMed:14963134}. Host endomembrane system {ECO:0000269|PubMed:11799178}; Peripheral membrane protein. Note=In virion, localizes on the intravirional side of the membrane. In the host cell, it is found associated with virus-induced membrane proliferation foci and probably also in multivesicular bodies. These VP40-enriched membrane clusters are then redistributed to the plasma membrane where budding takes place. {ECO:0000269|PubMed:14963134}.
Interaction partners:
Sequence:
MASSSNYNTYMQYLNPPPYADHGANQLIPADQLSNQQGITPNYVGDLNLDDQFKGNVCHAFTLEAIIDISAYNERTVKGVPAWLPLGIMSNFEYPLAHTVAALLTGSYTITQFTHNGQKFVRVNRLGTGIPAHPLRMLREGNQAFIQNMVIPRNFSTNQFTYNLTNLVLSVQKLPDDAWRPSKDKLIGNTMHPAVSIHPNLPPIVLPTVKKQAYRQHKNPNNGPLLAISGILHQLRVEKVPEKTSLFRISLPADMFSVKEGMMKKRGENSPVVYFQAPENFPLNGFNNRQVVLAYANPTLSAV
Protein: AT-hook motif nuclear-localized protein 5 (Q8GXB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VYJ2}.
Interaction partners:
Sequence:
MDGREAMAFPGSHSQFYLQRGVFTNLTPSQVASGLHAPPPPPGMRPMSNPNIHHPQASNPGPPFSMAEHRHSDFGHSIHMGMASPAAVQPTLQLPPPPSEQPMVKKKRGRPRKYVPDGQVSLGLSPMPCVSKKSKDSSSMSDPNAPKRARGRPPGTGRKQRLANLGEWMNTSAGLAFAPHVISVGSGEDIVSKVLSFSQKRPRALCIMSGTGTVSSVTLREPASTTPSLTFEGRFEILSLGGSYLVNEEGGSKSRTGGLSVSLSGPEGHVIGGGIGMLIAASLVQVVACSFVYGASAKSNNNNNKTIKQEIKPKQEPTNSEMETTPGSAPEAAASTGQHTPQNFPAQGMSGWPVSGSGSGRSLDSSRNPLTDIDLTRG
Protein: CHK domain ov2 (GH14673p) (Q9VBS0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE19438p
- Protein ref
Sequence:
MTDQPTPQWVTKELFSSLLEQSNRNFKAIIKFVPTSAISKGENYLTIVLRIQIEMQLKDNSIEDVSYILKIPLVPEDEKNDFHEMFDAELDMYDHLIPELEDLYAKNTSISPKFKPVHLKFPGEPVKSDYILLEDLRKKGYRNADRTQGLEQFEVEAVLKKLAQWHAASAKRVVELGEYEKDIRESYFTTEHQKLLDEFNINFCMPFLECMQQYNLEPGQLVLISDYTSQLTDLNIEFGKNDPLELSVLNHGDFWCNNFMFKYKNASEVEDVCFVDFQLPKYGTPAQDLLCILMTSPKFSIKLDKFDYFIEYYHQQLVEHLTMLNYNRNAPTLSKFHAHLHRYSLWAFICAQRMLPIVLLPPDVDSHIGNVMGNSEEAIAFKRKMFLLPAYVDQIKVILPWLINRGYIR
Protein: Lymphotoxin-alpha (LT-alpha) (TNF-beta) (Tumor necrosis factor ligand superfamily member 1) (P09225)
Organism: Mus musculus (Mouse)
Function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (By similarity). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Subcellular location: Secreted {ECO:0000250}. Membrane {ECO:0000250}. Note=The homotrimer is secreted. The heterotrimer is membrane-associated. {ECO:0000250}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 1B
- Lymphotoxin-beta
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor receptor superfamily member 3
- Tumor necrosis factor receptor superfamily member 14
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 5
- CD40 ligand
- Tumor necrosis factor ligand superfamily member 11
- Interleukin-2
Sequence:
MTLLGRLHLLRVLGTPPVFLLGLLLALPLGAQGLSGVRFSAARTAHPLPQKHLTHGILKPAAHLVGYPSKQNSLLWRASTDRAFLRHGFSLSNNSLLIPTSGLYFVYSQVVFSGESCSPRAIPTPIYLAHEVQLFSSQYPFHVPLLSAQKSVYPGLQGPWVRSMYQGAVFLLSKGDQLSTHTDGISHLHFSPSSVFFGAFAL
Protein: Cold shock protein 2 (AtCSP2) (Cold shock domain-containing protein 2) (Glycine-rich protein 2) (AtGRP2) (Q41188)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone that binds to RNA, single- (ssDNA) and double-stranded (dsDNA) DNA, and unwinds nucleic acid duplex. Accelerates seed germination and seedling growth under cold stress, and contributes to enhancement of cold and freezing tolerance. Regulates flowering transition, and flower and seed development. Promotes seed germination under salt stress. May regulate respiratory oxygen uptake.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17963727}. Nucleus, nucleolus {ECO:0000269|PubMed:17123099, ECO:0000269|PubMed:17963727}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein 1
- Glycine-rich RNA-binding protein 2, mitochondrial
- Glycine-rich RNA-binding protein RZ1A
- Glycine-rich RNA-binding protein 7
Sequence:
MSGDNGGGERRKGSVKWFDTQKGFGFITPDDGGDDLFVHQSSIRSEGFRSLAAEEAVEFEVEIDNNNRPKAIDVSGPDGAPVQGNSGGGSSGGRGGFGGGRGGGRGSGGGYGGGGGGYGGRGGGGRGGSDCYKCGEPGHMARDCSEGGGGYGGGGGGYGGGGGYGGGGGGYGGGGRGGGGGGGSCYSCGESGHFARDCTSGGR
Protein: F-box only protein 6 (F-box protein that recognizes sugar chains 2) (F-box/G-domain protein 2) (Q9NRD1)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19716789}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- F-box only protein 2
- E3 ubiquitin-protein ligase RBX1
- F-box/WD repeat-containing protein 1A
- Serine/threonine-protein kinase Chk1
Sequence:
MDAPHSKAALDSINELPENILLELFTHVPARQLLLNCRLVCSLWRDLIDLMTLWKRKCLREGFITKDWDQPVADWKIFYFLRSLHRNLLRNPCAEEDMFAWQIDFNGGDRWKVESLPGAHGTDFPDPKVKKYFVTSYEMCLKSQLVDLVAEGYWEELLDTFRPDIVVKDWFAARADCGCTYQLKVQLASADYFVLASFEPPPVTIQQWNNATWTEVSYTFSDYPRGVRYILFQHGGRDTQYWAGWYGPRVTNSSIVVSPKMTRNQASSEAQPGQKHGQEEAAQSPYRAVVQIF
Protein: Ubiquinone biosynthesis protein coq9, mitochondrial (O13850)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq4, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein coq11
- Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- RING-box protein pip1
Sequence:
MLTLRSACQLTTKNLGLHKCISKTVISALGRRGYHSENYETSKISGKKALILENALEHVPQLGFTEDAIVQGGQALGYSNLSKALFPSGPMDLISYFFLKQRYALSSLKPHLTTIPETSGRVVQLIWSRLQGNRDIVQHLPQMIAICTYPSNLRKSLSSLAELSDEILYLAQDKSADFQWYTKRAAISAIYSASELFMSRDTSPNFEATYNFVQHRIQHAKALNDLRNDVLEWGSFQLNAVRSILRSRGI
Protein: Amino acid transporter, putative (Q57Y06)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MCIARENTSNTVPHNCFEPIGHTVVNNNVGNCETSQNVQSNEPQSGKQPPGEQSTQFAAFIPPGGTIASAFNIAATTLGAGIFGLPSSAGSSGLIMGMFYLFFISCMTIYSMRNLALAADRSKAPTYESVTFVLMGRRVAYAIAVLRALDGFTSCVAYVISVGDILSAILKGTNAPDFLKEKSGNRLLTAVVWACFMLPLAIPRHVDSLRYVSTFAVTFMVYFVIVIVVHSCMNGLSENIKNVSVGKSDTAAIILFNSGNEAIEGLGVFMFSYTCQDTAYEVYIDMKDRSVRKFVIAAIIAMSLCTALYIITAFFGYMDFGRAVSGSILLMYDPVKEPAVMVGMIGVLVKLVASYALLAMACRNALYSIAEKNVDSLPFWKHCVSVIVLSTAALLLGLFIPNVNTVLGFSGSITGGSLGFVFPALLIMYSGGFTWQKVGSLHYLATYVLLICGVVGIVFGTGASIWGTITG
Protein: Nuclear RNA export factor 7 (F7AR15)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XGQFTEDGELGSWFKVTVPCGRKYDKTQLMNSIHSLCSVPFTPVDFHCDKHRIQFFVPDFRIASALKDISYKIHNEYFQKIPIFVNPSVAPYSVQNRFTKEEMEQLKLAMRKRYDVSQHALCLKKLRFDPDLMKNNIHMILNHRSCMAATLQIIQENFPKLRTVWELEKMKGLKLEQLWLEGNPLCSTFPDRSSYIRAVLECFPELSYLDGRKLLLPTVMNTQERKLMKPCKDIFMGSEVIKNQVHRFLREYYLMYDSEERQGLLNIYHDQACFSLTIPFNPNDPDLNSMYVYFKDENDMKNFKEFHIQRQLLKYTKQDIVECLRGFPQTLHAFSSFQVNICFQMETMLCFSVCGLFKEEGTPKECVRAFMRIFIALLGSSNMYIVNDQLFVRNPSSEEINSAFVIPSPTSYSNFKLVLSQEQQRMVQAFSTQSGMKLEWSQKCLEDNKWDYARAAEVFTMLQTKCKIPKEFFKQ
Protein: STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) (Q7TNZ6)
Organism: Rattus norvegicus (Rat)
Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q7RTN6}.
Interaction partners:
- Serine/threonine-protein kinase STK11
- Calcium binding protein 39
- Calcium binding protein 39-like
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- STE20-related kinase adapter protein beta
- Translocation protein SEC63 homolog
- Translocation protein SEC62
- Protein kinase AMP-activated non-catalytic subunit gamma 3
- 5'-AMP-activated protein kinase subunit beta-2
Sequence:
MSFLANEASSESIASFSKPEIMSSFLPEGGCYELLSVIGKGFEDLMTVNSRYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFSHPNIVPYRATFIADNELWAVTSFMAYGSAKDLIGTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISTDGKVYLSGLRSNLSMISHGQRQRAVHDFPKYSIKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSIANPGLNDSLAAGSLRPANGDSPSHPYHRTFSPHFHNFVEQCLQRNPDARPNASTLLNHSFFKQIKRRASEALPELLRPVTPITSFEGSQSQDHSGILGLVTNLEDLEVDDWEF
Protein: Alpha-S1-casein [Cleaved into: Casoxin-D] (P47710)
Organism: Homo sapiens (Human)
Function: Important role in the capacity of milk to transport calcium phosphate.
Subcellular location: Secreted.
Interaction partners:
- Beta-casein
- Kappa-casein
- Alpha-lactalbumin
Sequence:
MRLLILTCLVAVALARPKLPLRYPERLQNPSESSEPIPLESREEYMNGMNRQRNILREKQTDEIKDTRNESTQNCVVAEPEKMESSISSSSEEMSLSKCAEQFCRLNEYNQLQLQAAHAQEQIRRMNENSHVQVPFQQLNQLAAYPYAVWYYPQIMQYVPFPPFSDISNPTAHENYEKNNVMLQW
Protein: Male-specific sperm protein Mst84Dc (Q01644)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cytosol aminopeptidase
- GEO13348p1
- GEO12122p1
- AT27166p
- Male-specific sperm protein Mst84Dd
- Homeobox protein goosecoid
- GH09231p
- Male-specific sperm protein Mst84Da
- 10 kDa heat shock protein, mitochondrial
- Uncharacterized protein, isoform A
Sequence:
MCCGPCGSCCGYYCCGPCCGPCGPRCGPCGSCCGPCGPCGPCCGPFGSCCGGCWC