wanglab/gogpt-training-data huggingface dataset:
Protein: DNA replication licensing factor Mcm5 (EC 3.6.4.12) (Minichromosome maintenance 5 protein) (DmMCM5) (Q9VGW6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P33992}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P33992}.
Interaction partners:
- DNA replication complex GINS protein PSF3
- Probable DNA replication complex GINS protein PSF2
- CDC45L
- Double parked, isoform A
- DNA replication licensing factor Mcm3
- Origin recognition complex subunit 2
- DNA replication licensing factor Mcm2
- Origin recognition complex subunit 5
- DNA replication licensing factor MCM4
- Cell division control protein
Sequence:
MEGFDDAGVFFSDNFGGDNQQDAQINLQAVKKKYKEFIRTFNEENFFYKYRDTLKRNYLNGRYFLEIEMEDLVGFDETLADKLNKQPTEHLEIFEEAAREVADEITAPRPEHEEHMHDIQILLSSNANPTNIRQLKSDCVSKLVKIAGIIVAASGISAKATRMSIQCLSCSTVIPNLKVNPGLEGYALPRKCNTEQAGRPKCPLDPFFIMPDKCKCVDFQTLKLQELPDFVPQGEIPRHLQLFCDRSLCERVVPGNRVLIQGIYSIRKVGKPSRRDGREKAVVGVRAPYMRVVGITVDSEGAGAISRYSNITSDEEEHFRRMAASGDIYERLSQSLAPSIFGSRDIKKAITCMLFGGSRKRLPDGLCRRGDINVLLLGDPGTAKSQLLKFVEKVAPIAVYTSGKGSSAAGLTASVMKDPQTRNFVMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSIFGRWDDTKGEENIDFMPTILSRFDMIFIVKDIHDESRDITLAKHIINVHLSSNKSAPSEPAEGEISLSTFKKYIHYCRTHCGPRLSEAAGEKLKSRYVLMRSGAGQQEKASDKRLSIPITVRQLEAVIRISESLAKIRLQPFATDEHVNEALRLFQVSTLDAAMTGSLAGAEGFTTEEDQETLNRIEKQLKRRFAIGSQVSEQNILQDFLRQKYEERTVMKVIHTMIRRGELQHRMQRKMLYRIC
Protein: Exostosin-like 1 (EC 2.4.1.224) (Exostosin-L) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostosis-like protein) (Q92935)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate (HS). Transfers N-acetyl-alpha-D-glucosamine to the nascent HS chain (GlcNAcT-II activity). Appears to lack GlcNAcT I and GlcAT-II activities.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Exostosin-like 3
- X-box-binding protein 1
- Heat shock protein 75 kDa, mitochondrial
Sequence:
MQSWRRRKSLWLALSASWLLLVLLGGFSLLRLALPPRPRPGASQGWPRWLDAELLQSFSQPGELPEDAVSPPQAPHGGSCNWESCFDTSKCRGDGLKVFVYPAVGTISETHRRILASIEGSRFYTFSPAGACLLLLLSLDAQTGECSSMPLQWNRGRNHLVLRLHPAPCPRTFQLGQAMVAEASPTVDSFRPGFDVALPFLPEAHPLRGGAPGQLRQHSPQPGVALLALEEERGGWRTADTGSSACPWDGRCEQDPGPGQTQRQETLPNATFCLISGHRPEAASRFLQALQAGCIPVLLSPRWELPFSEVIDWTKAAIVADERLPLQVLAALQEMSPARVLALRQQTQFLWDAYFSSVEKVIHTTLEVIQDRIFGTSAHPSLLWNSPPGALLALSTFSTSPQDFPFYYLQQGSRPEGRFSALIWVGPPGQPPLKLIQAVAGSQHCAQILVLWSNERPLPSRWPETAVPLTVIDGHRKVSDRFYPYSTIRTDAILSLDARSSLSTSEVDFAFLVWQSFPERMVGFLTSSHFWDEAHGGWGYTAERTNEFSMVLTTAAFYHRYYHTLFTHSLPKALRTLADEAPTCVDVLMNFIVAAVTKLPPIKVPYGKQRQEAAPLAPGGPGPRPKPPAPAPDCINQIAAAFGHMPLLSSRLRLDPVLFKDPVSVQRKKYRSLEKP
Protein: Protein S100-A6 (Calcyclin) (Prolactin receptor-associated protein) (S100 calcium-binding protein A6) (P05964)
Organism: Rattus norvegicus (Rat)
Function: May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity).
Subcellular location: Nucleus envelope {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Calcyclin-binding protein
- Protein S100-A10
- Annexin A2
- Annexin A1
- Annexin
- Advanced glycosylation end product-specific receptor
- Protein S100-A4
- E3 ubiquitin-protein ligase SIAH1
Sequence:
MACPLDQAIGLLVAIFHKYSGKEGDKHTLSKKELKELIQKELTIGAKLQDAEIARLMDDLDRNKDQEVNFQEYVAFLGALALIYNEALK
Protein: Hepatocyte nuclear factor 1-beta (HNF-1-beta) (HNF-1B) (Transcription factor 2) (TCF-2) (Variant hepatic nuclear factor 1) (vHNF1) (P23899)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Binds to the FPC element in the cAMP regulatory unit of the PLAU gene (By similarity). Transcriptional activity is increased by coactivator PCBD1 (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Hepatocyte nuclear factor 6
- Hepatocyte nuclear factor 4-alpha
- Hepatocyte nuclear factor 3-beta
- COUP transcription factor 2
Sequence:
MVSKLTSLQQELLSALLSSGVTKEVLIQALEELLPSPNFGVKLETLPLSPGSGADLDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQTVQSSGNMTDKSSQDQLLFLFPEFSQQNQGPGQSEDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHNLNPLLTHGSPHHQPSSSPPNKLSGVRYSQPGNNEVTSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHSLLSPDSKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQSLNTSQAQGVPVINSVASSLAALQPVQFSQQLHSPHQQPLMQQSPGSHMAQQPFMAAVTQLQNSHMYAHKQEPPQYSHTSRFPSAMVVTDTSSINTLTSMSSSKQCPLQAW
Protein: 2',3'-cyclic nucleotide 3' phosphodiesterase (C9K0L8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSGAKDKPELQFPFLQDEDTVATLLECKTLFILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEK
Protein: Fasciclin-like arabinogalactan protein 1 (Fasciclin-like arabinogalactan protein 9) (B1NHU5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Catalase isozyme 2
- Tubulin beta chain
- Tubulin beta-7 chain
- 2-nitropropane dioxygenase
Sequence:
MASSSPLSPILLSLFLVFICGVSAQTAPAPAPSGPLNFTGILDKNGQYTYFLQLLAQTQVGSQVQTQLKTTTEGFTVFAPTDNAFNNLKPGTVNNLDPQQKVQLVLYHVIPKYYSLNDLQFVSNPVRTQAGQDFGLNVTGLNNQVNVSSGVVETQINNALYQKKPLAIYQADKVLLPEEFFEAKSPAAAPSPATKKSSTGSKSNSRASATADEPASADNSGSAGRNMGLGFVVGLALACMGFLS
Protein: DNA-binding protein inhibitor ID-2-A (Inhibitor of DNA binding 2-A) (XId2) (Inhibitor of differentiation 2-A) (Q9PWJ5)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Inhibits the activity of both neurogenic (neurod1/neuroD) and myogenic (myod1/myoD) bHLH factors. May play a role in the regulation of the circadian clock.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P41136}. Nucleus {ECO:0000250|UniProtKB:P41136}.
Interaction partners:
Sequence:
MKAFSPVRSVRKSSLTEHSLGIARSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQLTLDSHPSIVSLHHLPRVGGNTSRTPLTPLNTDISILSLQAAEFSSEFTDESKSLCP
Protein: EMI domain-containing protein 1 (Emilin and multimerin domain-containing protein 1) (Emu1) (Q91VF5)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12221002}.
Interaction partners:
Sequence:
MGGPRAWTLLCLGLLLPGGGAAWSVPGARFSGRRNWCSYVVTRTVSCHVQNGTYLQRVLQNCPWPMGCPGNSYRTVVRPLYKVTYKTVTAREWRCCPGHSGVTCEEGSPGLLEPTWTDSGMRRMAVRPTALSGCLNCSKVSELTERLKALEAKVAVLSVTEQTVPSVPATPEDSALLWGSPAARGSPGDGSLQDRLDSWGLPGPTGPKGGTDSQSPVRIRGPPGPQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPYGQVSLHGDPLLSNTFTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPMGAPGSPGHMGIPGPSGPKGTSGHPGEKGERGLPGEPGPQGLMGVPGEPGPKGDPGEKSHWGEGLHQLREALKILAERVLILETMIGLYEPDLGSGAGPDGTGTPSLLRGKRGGHPTNYPIITPRRRSERS
Protein: Transcription factor E2F7 (E2F-7) (Q96AV8)
Organism: Homo sapiens (Human)
Function: Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15133492}.
Interaction partners:
- Transcription factor E2F8
- Transcription factor E2F1
- Cell division control protein 6 homolog
- Cellular tumor antigen p53
- Transcription factor Dp family member 3
- Hypoxia-inducible factor 1-alpha
- Abnormal spindle-like microcephaly-associated protein
Sequence:
MEVNCLTLKDLISPRQPRLDFAVEDGENAQKENIFVDRSRMAPKTPIKNEPIDLSKQKKFTPERNPITPVKFVDRQQAEPWTPTANLKMLISAASPDIRDREKKKGLFRPIENKDDAFTDSLQLDVVGDSAVDEFEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRNLQRLGEEQKYEEQMAYLQQKELDLIDYKFGERKKDGDPDSQEQQLLDFSEPDCPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDAPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSSDEELVDVSASVLPELKRETYGQIQVCAKQKLARHGSFNTVQASERIQRKVNSEPSSPYREEQGSGGYSLEIGSLAAVYRQKIEDNSQGKAFASKRVVPPSSSLDPVAPFPVLSVDPEYCVNPLAHPVFSVAQTDLQAFSMQNGLNGQVDVSLASAASAVESLKPALLAGQPLVYVPSASLFMLYGSLQEGPASGSGSERDDRSSEAPATVELSSAPSAQKRLCEERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRASIPLKDIHVNGQLPAAEEISGKATANSLVSSEWGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPAGLNGFNVLLSGSQTPPTVGPSSGQLPSFSVPCMVLPSPPLGPFPVLYSPAMPGPVSSTLGALPNTGPVNFSLPGLGSIAQLLVGPTAVVNPKSSTLPSADPQLQSQPSLNLSPVMSRSHSVVQQPESPVYVGHPVSVVKLHQSPVPVTPKSIQRTHRETFFKTPGSLGDPVLKRRERNQSRNTSSAQRRLEIPSGGAD
Protein: Proto-oncogene DBL (Proto-oncogene MCF-2) [Cleaved into: MCF2-transforming protein; DBL-transforming protein] (P10911)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15157669}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane.; SUBCELLULAR LOCATION: [Isoform 3]: Membrane. Note=Colocalizes with CDC42 to plasma membrane.
Interaction partners:
- Transforming protein RhoA
- Pleckstrin
- Pleckstrin-2
- Cell division control protein 42 homolog
- Guanine nucleotide exchange factor MSS4
- Rho guanine nucleotide exchange factor 1
- Rho-related GTP-binding protein RhoG
- Ezrin
- Guanine nucleotide-binding protein subunit alpha-13
- A-kinase anchor protein 13
Sequence:
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELAETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHRQISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQKALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAGFRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSSGPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQNDEKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYFYPTYDENEEENRPLMRPVSEMALLY
Protein: Poly(3-hydroxyalkanoate) polymerase subunit PhaC (PHA polymerase) (EC 2.3.1.-) (PHB synthase subunit PhaC) (Poly(hydroxyalkanoic acid) synthase subunit PhaC) (PHA synthase subunit PhaC) (Polyhydroxyalkanoic acid synthase) (Poly-beta-hydroxybutyrate polymerase) (PHB polymerase) (Poly(3-hydroxybutyrate) polymerase) (P45370)
Organism: Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum)
Function: Polymerizes D(-)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end. This subunit has catalytic activity that is enhanced 100-fold by PhaE, the non-catalytic subunit.
Subcellular location: Cytoplasm {ECO:0000305}. Note=Associates with the exterior of poly(3-hydroxybutyric acid) granules (PHB) when grown under 'storage' conditions. {ECO:0000269|PubMed:7957260}.
Interaction partners:
- Poly
- Acetoacetyl-CoA reductase
- Acetyl-CoA acetyltransferase
- Uncharacterized protein Alvin_0064
Sequence:
MFPIDIRPDKLTQEMLDYSRKLGQGMENLLNAEAIDTGVSPKQAVYSEDKLVLYRYDRPEGAPEAQPVPLLIVYALVNRPYMTDIQEDRSTIKGLLATGQDVYLIDWGYPDQADRALTLDDYINGYIDRCVDYLREAHGVDKVNLLGICQGGAFSLMYSALHPDKVRNLVTMVTPVDFKTPDNLLSAWVQNVDIDLAVDTMGNIPGELLNWTFLSLKPFSLTGQKYVNMVDLLDDPDKVKNFLRMEKWIFDSPDQAGETFRQFIKDFYQNNGFLNGGVVLGGQEVDLKDITCPVLNIFALQDHLVPPDASRALKGLTSSPDYTELAFPGGHIGIYVSGKAQKEVTPAIGKWLNER
Protein: Thioredoxin-interacting protein (Vitamin D3 up-regulated protein 1) (Q8BG60)
Organism: Mus musculus (Mouse)
Function: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1) (By similarity). Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10843682}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 3
- Thioredoxin
- Thioredoxin, mitochondrial
- DNA damage-inducible transcript 4 protein
- E3 ubiquitin-protein ligase Itchy
- Caspase-1
- Tyrosine-protein phosphatase non-receptor type 11
- Guanine nucleotide exchange factor VAV2
- Mitogen-activated protein kinase kinase kinase 5
- Interleukin-1 beta
Sequence:
MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVAKVLWMQGSQQCKQTLDYLRYEDTLLLEEQPTAGENEMVIMRPGNKYEYKFGFELPQGPLGTSFKGKYGCVDYWVKAFLDRPSQPTQEAKKNFEVMDLVDVNTPDLMAPVSAKKEKKVSCMFIPDGRVSVSARIDRKGFCEGDDISIHADFENTCSRIVVPKAAIVARHTYLANGQTKVFTQKLSSVRGNHIISGTCASWRGKSLRVQKIRPSILGCNILKVEYSLLIYVSVPGSKKVILDLPLVIGSRSGLSSRTSSMASRTSSEMSWIDLNIPDTPEAPPCYMDIIPEDHRLESPTTPLLDDVDDSQDSPIFMYAPEFQFMPPPTYTEVDPCVLNNNNNNNNVQ
Protein: CKLF-like MARVEL transmembrane domain-containing protein 3 (Chemokine-like factor superfamily member 3) (Q99LJ5)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- CKLF-like MARVEL transmembrane domain containing 1
- Chemokine-like factor
- CKLF-like MARVEL transmembrane domain-containing protein 4
- CKLF-like MARVEL transmembrane domain-containing protein 7
- CKLF-like MARVEL transmembrane domain-containing protein 8
Sequence:
MWPPDAEPEPDPESAHGPRSGRTVPGLRALLPARAFLCSLKGRLLLAESGLSFITFICYVVSSASAFLTVPLLEFLLAVYFLFADAMQLNDKWQGLCWPMMDFLRCVTAALIYFVISITAVAKYSDGAYKAAGVFGFFATIVFAIDFYLIFNEVAKFLKQGDSGNETTAHRTEEENSNSDSDSD
Protein: Large ribosomal subunit protein uL11m (54S ribosomal protein L19, mitochondrial) (Q9UTK2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P53875}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL13m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS17m
Sequence:
MASTRTTIIKLIVPAGKATPTPPIGPALGARGLKSIDFCKEFNARTAGWMPNTPVPCKITVTPQRTFTFTIHTPPTSWLISKTLDLEKGSSSPLHDIKGQLSLKHIYEIAKLKSTDPSLQGIELLSLCKSVIGTAKSMGVKVVP
Protein: RAD52 motif-containing protein 1 (B4DZ74)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MHLLVPPPQHSLFTAFSQFGLLYSVRVFPNAAVAHPGFYAVIKFYSARAAHRAQKACDRKQLFQKSPVKVRLGTRHKAVQHQALALNSSKCQELANYYFGFNGCSKRIIKLQELSDLEERENEDSMVPLPKQSLKFFCALEVVLPSCDCRSPGIGLVEEPMDKVEEGPLSFLMKRKTAQKLAIQKALSDAFQKLLIVVLGKTVLIILEVLQFQ
Protein: Prohibitin (C9JZ20)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048}.
Interaction partners:
Sequence:
MAAKVFESIGKFGLALAVAGGVVNSALYNDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ
Protein: DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8) (Q9UJA3)
Organism: Homo sapiens (Human)
Function: Component of the MCM8-MCM9 complex, a complex involved in the repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-links (ICLs) by homologous recombination (HR). Required for DNA resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the MRN complex to the repair site and by promoting the complex nuclease activity. Probably by regulating the localization of the MNR complex, indirectly regulates the recruitment of downstream effector RAD51 to DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is dispensable for DNA replication and S phase progression. However, may play a non-essential for DNA replication: may be involved in the activation of the prereplicative complex (pre-RC) during G(1) phase by recruiting CDC6 to the origin recognition complex (ORC). Probably by regulating HR, plays a key role during gametogenesis (By similarity). Stabilizes MCM9 protein.
Subcellular location: Nucleus {ECO:0000269|PubMed:12527764, ECO:0000269|PubMed:18072282, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:26300262}. Chromosome {ECO:0000269|PubMed:15684404, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26215093}. Note=Localizes to nuclear foci (PubMed:26215093). Localizes to double-stranded DNA breaks (PubMed:23401855). Binds chromatin throughout the cell cycle (PubMed:15684404). {ECO:0000269|PubMed:15684404, ECO:0000269|PubMed:23401855, ECO:0000269|PubMed:26215093}.
Interaction partners:
- DNA helicase MCM9
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM5
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM2
- Protein MCM10 homolog
- DNA replication factor Cdt1
Sequence:
MNGEYRGRGFGRGRFQSWKRGRGGGNFSGKWREREHRPDLSKTTGKRTSEQTPQFLLSTKTPQSMQSTLDRFIPYKGWKLYFSEVYSDSSPLIEKIQAFEKFFTRHIDLYDKDEIERKGSILVDFKELTEGGEVTNLIPDIATELRDAPEKTLACMGLAIHQVLTKDLERHAAELQAQEGLSNDGETMVNVPHIHARVYNYEPLTQLKNVRANYYGKYIALRGTVVRVSNIKPLCTKMAFLCAACGEIQSFPLPDGKYSLPTKCPVPVCRGRSFTALRSSPLTVTMDWQSIKIQELMSDDQREAGRIPRTIECELVHDLVDSCVPGDTVTITGIVKVSNAEEGSRNKNDKCMFLLYIEANSISNSKGQKTKSSEDGCKHGMLMEFSLKDLYAIQEIQAEENLFKLIVNSLCPVIFGHELVKAGLALALFGGSQKYADDKNRIPIRGDPHILVVGDPGLGKSQMLQAACNVAPRGVYVCGNTTTTSGLTVTLSKDSSSGDFALEAGALVLGDQGICGIDEFDKMGNQHQALLEAMEQQSISLAKAGVVCSLPARTSIIAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEHHDHLLSEHVIAIRAGKQRTISSATVARMNSQDSNTSVLEVVSEKPLSERLKVVPGETIDPIPHQLLRKYIGYARQYVYPRLSTEAARVLQDFYLELRKQSQRLNSSPITTRQLESLIRLTEARARLELREEATKEDAEDIVEIMKYSMLGTYSDEFGNLDFERSQHGSGMSNRSTAKRFISALNNVAERTYNNIFQFHQLRQIAKELNIQVADFENFIGSLNDQGYLLKKGPKVYQLQTM
Protein: Protocadherin gamma B2 (Protocadherin gamma subfamily B, 2) (Q91XX7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MRRGSGSGPAWWLQVLSPFLLLLFHGALADQIRYSIPEELAKNSIVGNLARDLGLSVQNLPTRKLRVSAEKDYFTVNPESGDLLVGDRIDREQVCGKQPQCVLEFDIVAEKPLNIFHVAVILQDVNDNAPLFKQSEVDLNIGESTRPGKAFPLDPALDLDAGSNSLQKYYLTDNEYFEVTEKETPDGRKYPELILKRFLDREEHNFHQLVLTAVDGGDPPRSGTTQIRIQVTDINDNPPMFSQDVFSVTLREDVPPGFSVLQVTATDQDEGVNAEITYAFHNVDEQVERIFNLDKRTGEITTKDNLDFETAKSYTLNVEAKDPGDLASHCSIQVKILDENDCVPEVIVTSVFTPLPEDSPLGTVIALIKTRDRDSGENGDVYCHVLGNEGFVLKSSSKNYYKLVTDRTLDREAIPEYNVTIVAADRGKPPLSSNVIITLHISDVNDNAPVFHQASYLVHVAENNPPGTSIAQVSASDPDLGSNGLISYSIIASDLEPRALSSFVSVNQDSGVVFAQRAFDHEQLRSFQLTLQARDHGSPTLSANVSMRVLVGDRNDNAPRVLYPTLEPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASDPGLFSLGLRTGEVRTARALGDRDSARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDDPLPSDPQSELQFYLVVALALISVLFLLSVILAIALRLRHSSRSAAWGCFQPGLSSNLATGVLPNYNEGTLPYSYNVCIASQSAKTEFNFLNVTPEVAPQDLLCGDDSWVPGTLGDTDVPFVSDSISKQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK