wanglab/gogpt-training-data huggingface dataset:
Protein: Polycomb group protein Psc (Protein posterior sex combs) (P35820)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (BX-C) complexes, and hence for the maintenance of segmental determination.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase RING1
- Polyhomeotic-proximal chromatin protein
- Polycomb group protein Pc
- Histone-lysine N-methyltransferase E
- Polycomb protein Su
- JmjC domain-containing histone demethylation protein 1
- Polyhomeotic distal, isoform A
- Polycomb protein Scm
- Polycomb protein esc
- Polycomb protein esc
Sequence:
MMTPESKAIQPAAATTKQTAEATATTTMAHTQQKSQLSTLAKTTTTTATNKAAKSVVSNANSSGNNSSKKLALSQSQKTTTTTTPPTTTTTTTAAAAAEATTNADKMQKQQQLKQQLFAACSIKVKSENTLATTANAALAAATTTTTTATPALATGKAAKTILENGIKKESTPPAVESVEASSSSSSSSSSSSSSSSSWPTTRRATSEDASSNGGASADEEKSEEDPTAAVAASSTATTTSDLATTSRPRPVLLTAVNPHIICHLCQGYLINATTIVECLHSFCHSCLINHLRKERFCPRCEMVINNAKPNIKSDTTLQAIVYKLVPGLYERELMRKRAFYKDRPEEAALATPEQRGDDTEHLIFSPSDDMSLSLEYAELGELKTDSEPELVDTLRPRYLQCPAMCRVSHLKKFVYDKFEIDAQRFSIDIMYKVKTIVLLDYYTLMDIAYIYTWKRDAPMRFYYRVYESPQPLVKPAPRRVLPLKLEKQERENQEQQLAVEVASSKVEPVSLPEDQKAEASIKVEEQESTREIVKEVIKDVAATPPTETLKLVINRNMLDKREKSHSPQMSSKSSSKSSPCTPVSSPSEPNIKLKIDLSKQNSVTIIDMSDPERREIVKPLKPEKESRSKKKDKDGSPKSSSSSSSSSSGERKRKSPSPLTVPPLTIRTERIMSPSGVSTLSPRVTSGAFSEDPKSEFLKSFALKPIKVKVESPERTLNNRAITPPSPSVQQSASPKSKGNNLDDSILMKPPSCMPPKSIASSKRKSKEPVKAVSKKQKLSPPLPTVDFKIRLPVTNGNSSGTASPKIEKPLMPPPAKPPMLAPRKLQPSAQFAPPPSPIHHHAGVQMSAPGNRTPIAKRYQPILPKASRPNPFANIPNDVNRLLKDAGTEIKSIGGGSVENNSNAAQKPHLYGPKGESKMGPPALPATTPSQGNKNVGKQAGNLPMSAPPNKGNSSNNYLNLALFNSSKCKGKEAPPGCRTPMYTPNSPIYSPSSPQYVPSYNIPTMPTYKYTPKPTPNSGSGNGGSGSYLQNMLGGGNGGSLGGLFPSPPTKSDQNTNPAQGGGGSSSATQSGGNNGIVNNNIYMPNEDAPEKQQVKVKSLLNSCNINIPSSLSITISRDNGDSSSPNNGQHPKHKSPVNNYIEIVKLPDQPQDQVQAAKEAQKRQSPPAAVPGHLAAKLPPPPPSKAIPSPQHLVSRMTPPQLPKVATPPPPSSPRVITPPKTSPPANAAKVTPLKPVLTPTQVDKKTPSPEKRTAAQMGSHSPTASENKSPKGGPAGVANSTGGAQNGDPAAKKFRPILPRQNGMPELAPKLPTLAPFVGFNPLQNPAAGKKVPPSKKSPNAGAAAHQSGQQKLVNGGQSQPAQQKTSPPAQKNQQQVKKVSKNPTPPPPSLPAVGKMMPHPVMHSQNAPLSIASSASAAAVASGQLDLSNFLKENLRRVHAAQAAQAAQVAAAANQSNMMYNLAQMGHMTPAMYNYQQAYFREQLSRMQRVGNEVFNDYLQKLKTAAATGGGGPVEGELKPMLPTVTLPSPGATPPAASPKTSPLPAGKLTAAATAPQTKGNSSSGAANARQQTAATGNNGATVPAASLPPATKSK
Protein: Transcriptional activator of sulfur metabolism MET4 (Methionine-requiring protein 4) (P32389)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Positive trans-acting factor capable of stimulating the transcription of the MET genes from the methionine biosynthetic pathway. MET4, MET28 and CBF1 are required for full induction of MET25 and MET16 gene transcription. MET4 controls as well the derepression of MET6. Required for the transcription of genes necessary for sulfur amino acid biosynthesis. Involved in the transcription activation of MET28 and MET30. Required for MET3 gene expression via assembly of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes. Involved in response to cadmium and arsenic. Cadmium-activated MET4 also induces glutathione biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Centromere-binding protein 1
- Transcriptional activator of sulfur metabolism MET28
- Transcriptional regulator MET31
- Transcriptional regulator MET32
- F-box protein MET30 subunit MET30)
- General control transcription factor GCN4
- Glutamate--cysteine ligase
- Homocysteine/cysteine synthase
- Phosphoadenosine phosphosulfate reductase
- Sulfate adenylyltransferase
Sequence:
MKQEQSHEGDSYSTEFINLFGKDTATHPSSNNGANNNGMGSTNSLDQFVATASSSSSLVTSSENRRPLIGDVTNRGNTNLYDHAVTPEILLEQLAYVDNFIPSLDNEFSNVDWNVNTTHNNANNNGADTFSSINANPFDLDEQLAIELSAFADDSFIFPDEDKPSNNNNNSNNGNDDHSNHDVLHEDPSTNNRQRNPHFLTQRRNTFLTSQYDQSKSRFSSKNKRNGNNGETNNFGDNMQNNHPFEPNFMGSPSQFPADATNMTSIDHGGFTNVDITSTENNTTGDNGVDALSNLLHRTTHTPNRSSPLSNVTSAQNSSSQQRKHSESKVDSNSDNNSSNKAPNITVPDYSIIPTSVLVTLLPRVNVPNGAYNSLISAGFDNDQIDAIAAIMAYHHQKKIRENNSNNNKNINTNDSQEAPILKNINELLSVLIPPSPAETRGPTTLSTSPSFNEHGVVAEASFLSSILELGIKHPKSNNIHNQRQPSRNDHKISRESDGNNGNDNVHHNNAVIKSSTTRGDEIAKIRSEPTLNASSSDHKENSLKRSHSGDLKNKKVPVDRKYSDNEDDEYDDADLHGFEKKQLIKKELGDDDEDLLIQSKKSHQKKKLKEKELESSIHELTEIAASLQKRIHTLETENKLLKNLVLSSGETEGIKKAESLKKQIFEKVQKE
Protein: Transcriptional antiactivator ExsD (Q9I321)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Negative regulator of the type III secretion system regulon. Acts by disrupting transcriptional activator ExsA self-association and DNA-binding activity in absence of inducing signals. Upon host cell contact, this interaction is disrupted by the anti-antiactivator protein ExsC leading to ExsA activation.
Interaction partners:
- HTH-type transcriptional regulator ExsA
- Transcriptional anti-antiactivator ExsC
- Type 3 secretion system secretin
- Type III export apparatus protein
- Exoenzyme T
- Type III secretion regulatory protein ExsE
- Type 3 secretion system chaperone PscG
- Type 3 secretion system pilotin
- Type III inner-rod protein PscI
- Type III secretion protein PcrV
Sequence:
MEQEDDKQYSREAVFAGRRVSVVGSDARSRGRVPGYASSSLYRESGIISARQLALLQRMLPRLRLEQLFRCEWLQQRLARGLALGREEVRQILLCAAQDDDGWCSELGDRVNLAVPQSMIDWVLLPVYGWWESLLDQAIPGWRLSLVELETQSRQLRVKSEFWSRVAELEPEQAREELARVAKCQARTQEQVAELAGKLETASALAKSAWPNWQRGMATLLASGGLAGFEPIPEVLECLWQPLCRLDDDVGAADAVQAWLHERNLCQAQDHFYWQS
Protein: B-cell receptor-associated protein 31 (BCR-associated protein 31) (Bap31) (p28) (Q61335)
Organism: Mus musculus (Mouse)
Function: Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins. Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by stimulating the translocation of NDUFS4 and NDUFB11 from the cytosol to the mitochondria via interaction with TOMM40 (By similarity). In response to ER stress, delocalizes from the ER-mitochondria contact sites and binds BCL2 (By similarity). May be involved in CASP8-mediated apoptosis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein {ECO:0000255}. Note=May shuttle between the ER and the intermediate compartment/cis-Golgi complex. Associates with the mitochondria-associated endoplasmic reticulum membrane via interaction with TOMM40. {ECO:0000250|UniProtKB:P51572}.
Interaction partners:
- Mitochondrial fission 1 protein
- Phosphofurin acidic cluster sorting protein 2
- Caspase-8
- Vesicle-associated membrane protein-associated protein B
- Calnexin
- Dynamin-1-like protein
- Ubiquitin-conjugating enzyme E2 N
- Cell death-inducing p53-target protein 1
- Mitochondrial import receptor subunit TOM40 homolog
- Mitofusin-2
Sequence:
MSLQWTTVATFLYAEVFAVLLLCIPFISPKRWQKVFKSRLVELVVTYGNTFFVVLIVILVLLVIDAVREILKYDDVTEKVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAEDGDKLDIGNTEMKLEENKSLKNDLRKLKDELASTKKKLEKAENEALAMQKQSEGLTKEYDRLLEEHAKLQASVRGPSVKKEE
Protein: Postreplication repair E3 ubiquitin-protein ligase rad18 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase rad18) (Q02398)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- Myosin-binding domain-containing protein
- non-specific serine/threonine protein kinase
- DNA repair protein RAD51 homolog
- DNA 3'-5' helicase
- ATP-dependent RNA helicase dbp4
- ATP-dependent RNA helicase dbp3
- DNA repair protein rad5
- E2 ubiquitin-conjugating enzyme
- Sister chromatid cohesion acetyltransferase Eco1, putative
Sequence:
MEPTFDIPDSTDWLDTPLTLLAPFETSLRCQVCKDFFDNPVITSCSHTFCSLCIRRCLSTEGKCPTCRSSDQELKLRRNWVVQELVEGFKNARPSILQLARMAQTGTDDSGDLAAEEPASKKRKIEPNAIVGTDGLPEEGIRTRSQSRGASRQPQATPVQVIDDGNDEDYMPDGLVPCPVCGRRMKEEAVFRHLDSCTGTAEELKPAAFGSLAPGPRKSFLAATGKPPERLPVINYSLLKDTVLRKKLKDLGIPNWGPRALLQRRHTEWLNLWNANCDSRTPKPKRELLRELDVWERTQGGNSVTPTDPTNAVMNKDFNTEEWSANYDTDFKALIANARKKNDAVIRSTIPNASQANSDTPRSAQLVDQPIEASLTPQDVDEKSTMNPQDAIDNRTEVPPVPDPPQALSGIDRAVNSPMKNVTEGDAQAIPISSSASTHKTPH
Protein: Homoaconitase, mitochondrial (EC 4.2.1.36) (Homoaconitate hydratase) (Q92412)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- homoisocitrate dehydrogenase
- Putative aconitate hydratase, mitochondrial
- Saccharopine dehydrogenase [NAD
- Ulp1 protease family protein
- Saccharopine dehydrogenase [NADP
- Cytochrome c
- 5-aminolevulinate synthase, mitochondrial
Sequence:
MQSRLVSQSGLGRRWAVLRCALSKTYQRRTLTSTRRQFQDVFQSQLEDPTSAALFSALNSSKAVPQTLTEKIVQKYSVGLPQGKFVKSGDYVTIQPHRCMTHDNSWPCALKFMSIGASRLHNPDQIVMTLDHDVQNKSDKNLKKYRQIEEFATQHGVEFYPAGRGIGHQIMIEEGFAWPGTLAVASDSHSNMYGGVGCLGTPIVRTDAASVWATGKTWWQIPPVAKVTFKGVLPPGVTGKDVIVALCGLFNKDDVLNHAIEFTGSEETMRSLSVDTRLTIANMTTEWGALSGLFPIDSVLKGWLRGKATTAAMGLADGPFKTRAAERFTHPLLEQLFENPLTADKGAKYAKELFLDLSSLSPYVSGPNSVKVATPLKELEAQNIKVDKAYLVSCTNSRASDIAAAAKVFKEAAEKNGGKIPKIADGVKFYIAAASIPEQLAAEGNGDWQTLLEAGATQLPAGCGPCIGMGQGLLEPGEVGISASNRNFKGRMGSTEAKAYLGSPEVVAASALSGKLSGPGWYQTPEGWTEVIRGEGDGIREEDRMLTNEEALEKIIGQLDDLVADGEKRFASETPAVEESEQGLTEIYPGFPERVSGELVFCDADNVNTDGIYPGKYTYQDDVPPETMARVCMENYDPEFSTTAKEGDILVSGFNFGCGSSREQAATAILAKKIPLVVSGSFGNIFSRNSINNALMGLEVPRLVNRLRETFGSGDKVLTRRTGWTLTWDVRKSQIEVQEGPGGPKWTHKVGELPPNVQEIIAKGGLEKWVKNAIGA
Protein: Interferon alpha-16 (IFN-alpha-16) (Interferon alpha-WA) (P05015)
Organism: Homo sapiens (Human)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha-17
- Interferon alpha-10
- Interferon alpha/beta receptor 1
- Interferon alpha-7
- Interferon alpha-14
- Interferon alpha-5
- Interleukin-2
- Interferon alpha-21
- Interferon alpha/beta receptor 2
- Interferon gamma receptor 1
Sequence:
MALSFSLLMAVLVLSYKSICSLGCDLPQTHSLGNRRALILLAQMGRISHFSCLKDRYDFGFPQEVFDGNQFQKAQAISAFHEMIQQTFNLFSTKDSSAAWDETLLDKFYIELFQQLNDLEACVTQEVGVEEIALMNEDSILAVRKYFQRITLYLMGKKYSPCAWEVVRAEIMRSFSFSTNLQKGLRRKD
Protein: Probable polyketide synthase 17 (dipks17) (EC 2.3.1.-) (Q869X2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable polyketide synthase.
Interaction partners:
Sequence:
MTFNNIKDENNDDIAIIGMGFRFPGGGNNPYQFWNQLSNKMDGISKIPTEKWSRSFYEQKYINNEYGGVLKDEEWKNFDPLFFGISPKEAPIIDPQQRLLMTTLWEAFEDANIKPSTFRGSDTAVFIGMMNTDYQRCQFRDISYVNPYITPGTAGSFISNRLSFSFDLRGPSMTLDTACSSSLNAVYLGCQAIANGDSKMAIVGGVNGIFDPCFSMTFSGLNMLGHKGQCRSFDAGADGYIRSEGGGVCILKKYSDAIKDGDRIYCVIKGGSSNVDGYNAKTNIIQPSMKAQGENIEIALKKSGVNPSDIYYIEAHGTGTPVGDPIEIEAISRIFKDNHTPDAPLYIGSVKSNIGHLESAAGIASLIKVALSLKNRSLVPNIHFEKPNPLIKFEDWNIRVVTDEIQFPINKLINMGINCFGLSGSNCHMILSEAPINYDELLKTTNNNSTSSSSNDDKKEYLIPFSANCNISLDKYIEKLISNQSIYKDTILFKDFVKHQTISKSNLIKRKVITASDWDDFLNKRNETTSTSSLTSTISAPASSTPVIYVFTGQGPQWRDMGKALYETESVFKDAIDHCDKLLANYFGYSILQKLLSLESEDSPEIHHPILAQPSIFLIQVGLVALYKSFGISPSIVVGHSFGEIPSALFSDVISLETAVKIVYYRGLAQNLTMGTGRLLSIGIGADAYLEKCALLYPEIEIACYNDPNSIVITGSEQDLLGAKSTLSAEGVFCAFLGTPCSFHSSKQEMIKEKIFKDLSDLPESNVPCVPFFSTITGSQLSHKGFYNVQYIYDNLRMPVEFTKAISNIFNFIEENESYKNAIFLEIGPHPTLGFYIPKCKPSNSTITSKPIIVSPLHKKKEELTQFKLAISTLYCNGVEIDFASGQQLLPTSSSSGGGDISSFKESTNKLPRYQWDFEEYWDEPNQSKMVKRGPSNNLLGHDQFAGNTLMELFIDIDKSAHQYLKGHKIKGKYLFPGSGYIDNILRQFNGQDITIFNLEFSNPFFLKDGVQHHLQTSITPTTKGEFKVEFFIKDNRNSTKWTKTSNGRIGLFKHNPKNNKLDIEKLKSQCSFTTLTKSEVYNKLLLLSLPYGPTFQRVESCSIGDGCSFFKLSMSPCSEFDKDFLNPSIIDCAFHGLLVLSEGPQEIVFDRLQDMKFYSSNVPSTRPQFIYAFAKFDKIEGNSTHGSLNIILEDGTLLISIKNVKCTSLIRLKKQSIKYPSQNVYSHHWQSKDSPLTLIENQLIEEKSSESKINFEKLLNDKLFNYYLIRLLNQSIKSEFIEFDYKTSTVDTLDIGSKNAKLLEKIQSILNPIDSLDQSIDITSLKQAIIVKSSFKNEIKLVEKSIKRIVSLLKGGESEHFSPSNPSSPNDTPRNNSNNCSSKNNAASSDDADDDTNNEETINQLNNEPFNFSNSQFISNQNQLISKTIVNSFDRLINSIEIGEKKLIKIIDLSSIYQNYQLSKLLLLQLNQLLINLSNNNNIEIEYTIPSNTKNIDSITEETKSISNVLNIKYRSFDLQDDLESNGYLNSNYDLIITSLLLVSTNSIDSNEVLSKLYKLLLPKGQLILMEPPKGVLSFNLLFANDFKQSLEIKSEQEIKSLIIYCGFTKIETNLNTKDDEEQQQPPPPSILIVQAEKRDIESMSLTFSSDPKSLNSSYSNCIFIVSKEQKENPTSYIQEYFDITEFFCQNATIIEADDSELLTKTIESGVGKNDIIFFLVSLEELTIENYKQVTMQYTLVNQILLRNNLSTRFALLTYDSQNGGKNYLGSSLIGTFRYFLEFRSLNIFSIDVDKDSIDNLTLFLRLVDLSTIGDRETIVRNNKIFVQKIFKEPKLLSPSNNYEKNTNNLFLYSNSNLDFSFQSKEKLLHGCVEIKVMSTGINYKDSLFYRGLLPQEVFSKGDIYSPPFGLECAGYITRVAPSGVTRFKVGDQVVGFASHSLSSHVTTHQNKIVLKPENISFNEAAAVCVVYATSYYSIFHIGAFIADKESILVHSATGGVGLASLNLLKWKRNQLKKHGNSEISNDASIYATVGSKEKIDYLQEKYGDLITAIYNSRDTEYCDEIKQQSAQGGVDLILNTLSGDYLSSNFRSLSQVGRIMDLSVTQLVENDSLDFSNFKYHVGYNTIDLDRATKYNSKIIRDILTEVFDAISDGSLENIPVKVFPAIQVKTAIEYINERVHIGKIVVDFENFEQDILKPALQEKENPIQLNKVKKLEHTCDTLNNTILITGQTGIAVHILKWIISGSVLNSNKSQQQVTDFIILSRSSLKWELENLINQTKHKYGDRFRFHYKSVNIADLNSTRTAIDQVYSSCKNVSPIKSVLHFATVYEYILPENITQTVIDNTHNPKAVGAINLHNLSIEKDWKLENFILFSSIGAIIGGSKQCAYSSANLVLDSLSNYRKSIGLASTSINWGGLDAGGVAATDKSVASFLEGQGILLVSLSKILGCLDSVFQPSNSHLSNFMLSSFNIDNLLSSAPQMKRKMDHHLTNYKTSSASSDDSLGDSGSTQAKVISTISELLSIHPSKLNLDTRLKDYGIDSLLTVQLKNWIDKEFTKNLFTHLQLSSSSINSIIQRISSKSTSTSTPNPTNTSKQTATKKT
Protein: Sr-CI (Q6V6S0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EFFWTLAVIVIYCIGHIHGRCERSIDLDNGSINYRQRNVVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFTTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTSTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPMTTTSTTFTTSTTSTRPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTLKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNS
Protein: Structural maintenance of chromosomes protein (Q8AWB8)
Organism: Gallus gallus (Chicken)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
- Stromal antigen 2.
- Uncharacterized protein.
- RAD21 cohesin complex component
- WAPL domain-containing protein.
- Extra spindle pole bodies like 1, separase.
- SCD domain-containing protein.
- Sister chromatid cohesion protein PDS5 homolog A
- Structural maintenance of chromosomes protein
- Establishment of sister chromatid cohesion N-acetyltransferase 2.
- Sister chromatid cohesion protein PDS5 homolog B
Sequence:
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEEIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYSKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVLNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTLARSDDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSTESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAEHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG
Protein: Pentatricopeptide repeat-containing protein At3g13880 (Q9LRV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g02370
- Pentatricopeptide repeat-containing protein At2g28050
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Pentatricopeptide repeat-containing protein At1g06270
- Pentatricopeptide repeat-containing protein At3g48250
- Nuclear pore complex protein NUP155
Sequence:
MLLQFRAKTFFNNIAQDSLVTLITKRVGLGYRFLSSLCQPKNTALDSEGYKILFQTAAKSGSVVLGKLAHGHMIKSSLNPCLYLLNNLLNMYCKCRELGFARQLFDRMPERNIISFNSLISGYTQMGFYEQAMELFLEAREANLKLDKFTYAGALGFCGERCDLDLGELLHGLVVVNGLSQQVFLINVLIDMYSKCGKLDQAMSLFDRCDERDQVSWNSLISGYVRVGAAEEPLNLLAKMHRDGLNLTTYALGSVLKACCINLNEGFIEKGMAIHCYTAKLGMEFDIVVRTALLDMYAKNGSLKEAIKLFSLMPSKNVVTYNAMISGFLQMDEITDEASSEAFKLFMDMQRRGLEPSPSTFSVVLKACSAAKTLEYGRQIHALICKNNFQSDEFIGSALIELYALMGSTEDGMQCFASTSKQDIASWTSMIDCHVQNEQLESAFDLFRQLFSSHIRPEEYTVSLMMSACADFAALSSGEQIQGYAIKSGIDAFTSVKTSSISMYAKSGNMPLANQVFIEVQNPDVATYSAMISSLAQHGSANEALNIFESMKTHGIKPNQQAFLGVLIACCHGGLVTQGLKYFQCMKNDYRINPNEKHFTCLVDLLGRTGRLSDAENLILSSGFQDHPVTWRALLSSCRVYKDSVIGKRVAERLMELEPEASGSYVLLHNIYNDSGVNSSAEEVRELMRDRGVKKEPALSWIVIGNQTHSFAVADLSHPSSQMIYTMLETMDNVDFVDYTLVHFCSVT
Protein: Matrix metalloproteinase-23 (MMP-23) (EC 3.4.24.-) (Femalysin) (MIFR-1) (Matrix metalloproteinase-21) (MMP-21) (Matrix metalloproteinase-22) (MMP-22) [Cleaved into: Matrix metalloproteinase-23, soluble form] (O75900)
Organism: Homo sapiens (Human)
Function: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:11328856}; Single-pass type II membrane protein {ECO:0000269|PubMed:11328856}. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000305}.
Interaction partners:
- Cyclin-dependent kinase 13
- Cyclin-dependent kinase 11A
- Cyclin-dependent kinase 11B
- Hemopexin
Sequence:
MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG
Protein: RB binding protein 7, chromatin remodeling factor (Q5JP01)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKVCDSFLVSVCQEMKSRDSSVKLYQTRGSTIEKNVLYVVLHGDAHRVHWSPHNETILASSGTDRRLNVWDL
Protein: Uncharacterized protein (Q384B3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGAHSLNFPFSVCVCVCAHFHFTGLLTLSLLFPFFLTSPSLTSVALAVDTSRSACLPSSTGGGETGRCEKSATKREGQKETAFLQGGAEEMRRLILAQTLRVAGRHCPPVAMFLQRFYRGHGISTALPLHYSKRHRKREGRMYGKPLRPVSDGENGASGDGGVLTRWEAVVSSRHQCESPVQTLAKSEKPKKAENTVAGKKTGSSRFSHRRDHSAYPSGVQPAPLATSGLPTQSSERQQQKQIGQQQVPLDALHRLFKVHAVMRTNYEALGKCTKVLKSFSTACAEALLQLGVLQKEQPSAMERKGFIYVQLCKSGATEASKNGTSSPCFVLPPESPLYRTTIKFPTITVEHVLTTTVSSGCGAKDSGGDIMSVDMEGAAPFPMGHCESRPSTSAGNGVTAEYDCEGDVLSHGAAWNSIIEGFGQLALNLKQNASVSDFAQLAETLAYFKWVKDEEQVGWGTEDCVVKKFREAMANAKDTSASGSDPNTSDVSAALAAIAESFLRKIPRVDCIGSAVAHRGGERTAPSVHAIDVMLNLALRMCLSQWHAMSHFERMNIVLFCTYPWFAEDLSIAAGLCLTQSYLQSLLRADADVTYQHTFHYVRRVSRLCWPCIHDTDSAPVKKLLFPRDPQGTAVSSHALEAVSVEEKDNQLNQKEGLQGEEQATTTSESKLMWLPSFKDASCVSYGSSMKQRAAYELLLLWMTCVNPSGLHRSSPHGRYVSATGIAIIDVDLFVTQRFRTGKSKDEWLLLHPVEGDVVASVTIRTMVQHCETPYTLTRLFFCNFHSVLPHIWGGIGARRREILWTAWCRAVAQPLVNTLSGSDEGQREDDGGMQTLQITVDNADRTLDYLKPLISALTSDELFLRLIMRCADKSLEEMAREIGSGNNTLPLNKWCAQLAGFVYSVALALHCRAKREGCNRDGGPSRPNTATDSANKKVVSGKQTDNLPKGTQEDISDLQLQFKAAVSALLRKLSAGDTQVAEQLLHHFYEPHFSGDQEREVVEDIQRHLQQVCDSQSRDALHAWIECSARASCEATVPLKEELLCKWQRTVLEADAGLPVVLPTIVECCRGLVGLVKKRGRNISGRRQGQQRGTESTTVGEESSCKEVFSKEELPVVITVLSRAMLSRTSTVSTVGLTKISSEISTLLSSCGYETADGNTSGGGRNGRELCDTNTATITSATAGERTVELELILSGEIDQKAGELPWITILEAVQLQLVPYTVVKNLLTSFKGGCDNGKERLRWQELQRDFQRKRHHRLVGNTLVFRWYGCAVPNDEGWEDGSGLMRPMAEDRDNVHSASHQGRTSTELGAFTRRLLKTLARAEVTRLNDRKEITTQTFVVGPSDDSATRHPTPGQEEDASLHRLDLLFRVHTLAAHILMTASTKKPHMIHELYDTLLHLVEKVMPTTPNALGNASDLLLLWLVGSAVAVGLRFRPNFLIKWPSAPEVSSGNLKSCPSAEEKTVHILRDIEPYLQSELLRPTVRLRFVINVLVALRSLELLGARIDVEGLHMDQLLIRASADRRLLSRHVNLFLIGCSALQSTQSSILHTALHLREAKYNLSFAEIERAFVAIALSADTFARQHEALMEQNYQQQQNRTLSVAVAANNTTPALRVSPVQLRHAWSALGRRVLENAGESPTDLFVRGLQCAAAVGCIDSALYQQLLSYVVEFRWKDLHILDWVMILRTVRQSFENRRNLEAYLKEPLQAFMLTMTVSGDNSTEQSVQKVNLKNHEGEQLLEGLCLFAEALPGLFIGDRELWGLLWQALGSQWSACFNAASNIEEQQRITAWLQEINASYAWAARAAGFRGLDEPTAL
Protein: G-protein coupled receptor 161 (G-protein coupled receptor RE2) (Q8N6U8)
Organism: Homo sapiens (Human)
Function: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded (By similarity). {ECO:0000250}.
Interaction partners:
- Beta-arrestin-2
- Forkhead box protein E3
- cAMP-dependent protein kinase catalytic subunit alpha
- Beta-arrestin-1
- Tubby-related protein 3
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase type I-beta regulatory subunit
- Intraflagellar transport protein 140 homolog
Sequence:
MSLNSSLSCRKELSNLTEEEGGEGGVIITQFIAIIVITIFVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHREPGYTAFWQIWCALFPFLVMLVCYGFIFRVARVKARKVHCGTVVIVEEDAQRTGRKNSSTSTSSSGSRRNAFQGVVYSANQCKALITILVVLGAFMVTWGPYMVVIASEALWGKSSVSPSLETWATWLSFASAVCHPLIYGLWNKTVRKELLGMCFGDRYYREPFVQRQRTSRLFSISNRITDLGLSPHLTALMAGGQPLGHSSSTGDTGFSCSQDSGTDMMLLEDYTSDDNPPSHCTCPPKRRSSVTFEDEVEQIKEAAKNSILHVKAEVHKSLDSYAASLAKAIEAEAKINLFGEEALPGVLVTARTVPGGGFGGRRGSRTLVSQRLQLQSIEEGDVLAAEQR