wanglab/gogpt-training-data huggingface dataset:
Protein: Phenylalanine ammonia-lyase (EC 4.3.1.24) (Q6UD65)
Organism: Populus trichocarpa x Populus deltoides
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU003955}.
Interaction partners:
Sequence:
MEFCQDSRNGNGSLGFNTNDPLNWGMAAESLKGSHLDEVKRMIEEYRKPVVKLGGETLTIGQVTAIASRDVGVMVELSEEARAGVKASSDWVMDSMSKGTDSYGVTTGFGATSHRRTKQGGELQKELIRFLNAGIFGNDTESSHTLPRSATRAAMLVRFNTLLQGYSGIRFEMLEAITKLLNHNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPNGEPLSPAEAFTQAGIDGGFFELQPKEGLALVNGTAVGSGLASMVLFETNVLAILSEVLSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILDGSAYVKEAQKLHEIDPLQKPKQDRYALRTSPQWLGPLIEVIRTSTKMIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLAIASIGKLMFAQFSELVNDFYNNGLPSNLTGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVDILKLMSTTFLVGLCQAVDLRHIEENLKSTVKNTVSQVAKRVLTMGFNGELHPSRFCEKDLLKVVDREHVFSYIDDPCSATYPLMQKLRQVLVEHALVNGERETNSTTSIFQKIGSFEEELKTLLPKEVESARLEVENGNPAIPNRIKECRSYPLYKFVREELGTSLLTGEKVKSPGEEFDKVFTAICAGKLIDPLLECLKEWDGAPLPIC
Protein: 14-3-3 protein theta (14-3-3 protein tau) (P68255)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- 14-3-3 protein zeta/delta
- M-phase inducer phosphatase 2
- Bcl2-associated agonist of cell death
- 14-3-3 protein beta/alpha
- RAF proto-oncogene serine/threonine-protein kinase
- Serine/threonine-protein kinase A-Raf
- M-phase inducer phosphatase
- 14-3-3 protein epsilon
- WW domain containing transcription regulator 1
- Transcriptional coactivator YAP1
Sequence:
MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN
Protein: Paired box protein Pax-8 (R9W7C9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPHNSIRSGHGGLNQLGGAFVNGRPLPEVVRQRIVDLAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIRPGVIGGSKPKVATPKVVEKIGDYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTKVQQPFNLPMDSCVATKSLSPGHTLIPSSAVTPPESPQSDSLGSTYSINGLLGIAQPGSDKRKMDDSDQDSCRLSIDSQSSSSGPRKHLRTDAFSQHHLEPLECPFERQHYPEAYASPSHTKGEQGLYPLPLLNSTLDDGKATLTPSNTPLGRNLSTHQTYPVVADPHSPFAIKQETPEVSSSSSTPSSLSSSAFLDLQQVGSGVPPFNAFPHAASVYGQFTGQALLSGREMVGPTLPGYPPHIPTSGQGSYASSAIAGMVAGSEYSGNAYGHTPYSSYSEAWRFPNSSLLSSPYYYSSTSRPSAPPTTATAFDHL
Protein: Insulin-induced gene 1 protein (INSIG-1) (O15503)
Organism: Homo sapiens (Human)
Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139. Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12202038, ECO:0000269|PubMed:32322062}; Multi-pass membrane protein {ECO:0000269|PubMed:12202038}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- E3 ubiquitin-protein ligase AMFR
- Sterol regulatory element-binding protein 2
- Sterol regulatory element-binding protein 1
- Membrane-associated progesterone receptor component 1
- Insulin-induced gene 2 protein
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase RNF139
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
Sequence:
MPRLHDHFWSCSCAHSARRRGPPRASAAGLAAKVGEMINVSVSGPSLLAAHGAPDADPAPRGRSAAMSGPEPGSPYPNTWHHRLLQRSLVLFSVGVVLALVLNLLQIQRNVTLFPEEVIATIFSSAWWVPPCCGTAAAVVGLLYPCIDSHLGEPHKFKREWASVMRCIAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGLGLGITIAFLATLITQFLVYNGVYQYTSPDFLYIRSWLPCIFFSGGVTVGNIGRQLAMGVPEKPHSD
Protein: Basic helix-loop-helix (BHLH) DNA-binding superfamily protein (F4KAJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDIVDQELSNYWEPSSFLQNEDFEYDRSWPLEEAISGSYDSSSPDGAASSPASKNIVSERNRRQKLNQRLFALRSVVPNITKMDKASIIKDAISYIEGLQYEEKKLEAEIRELESTPKSSLSFSKDFDRDLLVPVTSKKMKQLDSGSSTSLIEVLELKVTFMGERTMVVSVTCNKRTDTMVKLCEVFESLNLKILTSNLTSFSGMIFHTVFIELRPNIYWVVWFLVFMSIFGPTIIVIWSIWFIKKKIILSLWRMKKNKRCCG
Protein: Succinate-CoA ligase subunit beta (EC 6.2.1.-) (B2RZ24)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TAQALGSSGLFNKHGFQMQQQQQQQRSLSLHEYLSMELLQEAGVSVPKGFVAKSSDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFTSGLKGGVKIVFSPEEAKAVSSQMIGQKLITKQTGAKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSQGGVNIEDVAAENPEAIVKEPVDIIEGVKKEQAVTLAKKMGFPSNIVDSAAENMIKLYNLFLKYDATMVEINPMVEDADGKVLCMDAKINFDSNSAYRQKKIFALQDWSQEDERDKDAADADINYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKRVQAILVNIFGGIMRCDIIAQGIVMAVKDLEIRIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAAKMVVKLSEIVTLAKEAHVDVKFQLPI
Protein: Lipoxygenase (EC 1.13.11.-) (A1XCI1)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MMQQLRHSQPSPCLCGLRAARPMLALGAAASRSRPAGKLQPSVCLGLGHVAPAAARGQPRPRAVADSALGASPTSVHVGGKLLLQNFAADSQQRLKLSIQLVSATVADPDGRGVKAEASVLDAVVGSGDSELDVDLIWDEALGAPGAVVVKNHSDFPVYLRLLSVPAGVGGADDEAAAVHFACNGWVYPVDKHPYRLFFTNDACVKEETPSALLKYREDELGALRGDGETTERPFQPWDRVYDYALYNDLGNPDLRQDLARPVLGGSQEYPYPRRTKTGRPAAKTDPRSESRAPLDEEIYVPCDERVGFASIPAPTLPPLGGHFRSLADVYRLFGLDDLGRLPEAKAVINSGAPFPVVPQVISVNPTHWRKDEEFARQMIAGANPVCIKRVTKFPLASELDRGVFGDQDSKITKDHVEKNMGGMTVQQAVEEGRLYVVDHHDWVMPYLKRINELPASEEKAEVSQRKVYAARTLLFLDGEDSSMLRPLAIELSSPHPEKEQLGAVSTVYTPPDSGDDGITAGRFSTWELAKVYASANDAAENNFVTHWLNTHASMEPIVIAANRQLSVLHPIHRLLKPHFRKTLHINAVARQIIVGSGDQRKDGSVFRGIDEVTYFPSKYNMEMSSKAYKAWNFTDLALPNDLIKRGLAKGDPKKPETVELAIKDYPYAVDGLDMWAAIKKWVADYCAIYYADDGAVARDSELQGWWSEVRNVGHGDLADAPWWPAMDCVADLVETCATVVWLSSAYHASISFGQYDYLGFVPNGPSITTRPVPGPDAGAEVTESDFLASVTPVTEALGFMSIASGPMGLKGTEVYLGQRPDTEQWTRERRAAEALAEFRARLEEVAGNIDRRNADPALKNRTGQVEVPYTLLKPTAQPGLVLRGIPNSITV
Protein: DNA endonuclease RBBP8 (EC 3.1.-.-) (CtBP-interacting protein) (CtIP) (Retinoblastoma-binding protein 8) (RBBP-8) (Retinoblastoma-interacting protein and myosin-like) (RIM) (Sporulation in the absence of SPO11 protein 2 homolog) (SAE2) (B1WC58)
Organism: Rattus norvegicus (Rat)
Function: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (By similarity). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chromatin following DNA damage. {ECO:0000250|UniProtKB:Q99708}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
- C-terminal-binding protein 1
- BRCA1-associated RING domain protein 1
- C-terminal-binding protein 2
- Double-strand break repair protein MRE11
- Nibrin
- DNA repair protein RAD50
- Exonuclease 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MSISGSSCGSPNSTDISSDFKELWTKLKEYHDKEVQGLQIKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLRLITELMNEKSALQEENKKLSEQLQQKMESGQQDQVAELECEENIIPDSPITSFSFSGINRLRRKENLHVRYVEQTHTKLEHSACTSELRKFSKGSTPAPVNSEEHEILVADTCDQSHSPLSKICGTSSYPADKLSSNLDAVVAETLGLDGQEESEPQGPVSPLGNELYHCLKEDHKKQPFMESAIRNEDNVRFSDSASKAPPRELTTRGSSPVFGPTSTVKTHLGLKTSFSPSLLDSGKKNLLSTAPFSSISVSRSEKVRSKSEDNALFTQQSAGSEVKVISQSFPSKQILTSKNVSDSVDEQGGADHMKDAVSDKHLVPLKSLGGKASKRKRTEEEGEHAVHCPQTCFDKENALPFPMENQFPVNGDHVMDKPLDLSDRFAANQRQEKNHGDETCKHKLKQVTIYEALKPVPKGSSSGRKALSGACTLAQDSAETYCLQQRTLQCSSKFSPDHNTQLQIKEENPVFKTPPRSQESLETENLFGDVKGIGSLVPIKVKGRSAHGGCELASVLQLNPCRVAKTKSLPSNHDMSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETMLLKMKKQEQREKSPNGDIKMNDSLEDMFDRTTHEEYESCLADNFSQVPDEEELSDTTKKPNIHGDKQDGIKQKAFVEPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPTNTPENFWEVGFPSTQTCLERGYIKEDLDPCPRPKRRQPYNAVFSPKGKEQRT
Protein: Mechanosensory protein 2 (Q27433)
Organism: Caenorhabditis elegans
Function: Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity). Positively regulates the activity of the putative mechanosensory transduction channel. May link the mechanosensory channel and the microtubule cytoskeleton of the touch receptor neurons. Required for the function of a set of six touch receptor neurons.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Degenerin mec-4
- Degenerin mec-10
- Mechanosensory abnormality protein 6
- Kunitz/Bovine pancreatic trypsin inhibitor domain protein
- MEC-5
- Tubulin alpha-3 chain
- AMP-binding domain-containing protein
- Papilin
- Band 7 domain-containing protein
- Tubulin beta-1 chain
Sequence:
MSATMSSARNSVVSLSSNGSVKVETRLVSNERSSSIQQEGAMLPSSSSKDDDLLSTSSDEVENMATRTLQQLEESTSIISANSDDDSVKKEKQAEKDVEKGNGKEEKANIQNEFGVCGWILTILSYLLIFFTLPISACMCIKVVQEYERAVIFRLGRLMPGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASRALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPIDLLSAFLQRTPPKVEEPPSLPKKIRSCCLYKYPDWVQGMVGSEGGGGHGHSHGGGGGGLGSSQGAFHPSQAGSGPSTTTTSGRPLLRSMREAQFHSAAPPISAPNQSQTSVSQLDPALLIR
Protein: Spore protein YabQ (P37559)
Organism: Bacillus subtilis (strain 168)
Function: Required for sporulation. Plays an important role in cortex and coat formation.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:11283287, ECO:0000269|PubMed:15231775}; Multi-pass membrane protein {ECO:0000269|PubMed:11283287, ECO:0000269|PubMed:15231775}.
Interaction partners:
- Spore protein YabP
- Cell division protein DivIC
- Stage III sporulation protein AC
- Sigma-K factor-processing regulatory protein BofA
- Anti-sigma-F factor Fin
- Stage IV sporulation protein FA
- Uncharacterized protein YqfD
- Uncharacterized protein YabS
- Stage II sporulation protein E
- Sporulation sigma-E factor-processing peptidase
Sequence:
MTLTTQFYTMLAMSGMGLWLGASLDTYRLFVIRAKTARWLLFIHDILFWIMQGLLFFYVLLHVNEGEFRIYIFLAVLLGVATYQSLCKRIYIKILKFVIYLVVSVYQFFKKLIQHVLFRPIVWTCGAIIWLAAFLFKKTYSLIGFLLLCLYKIVMVLCFPIRFIAKQCLKLLPVKMRLTFRRYFEKGAGFLKKKKKLLITIRTTITRFLKR
Protein: Cell division cycle protein 27 homolog (Q0P4V8)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Interaction partners:
Sequence:
MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKAHSCATPQCKYLLAKCCVDLSKLAEGEQILSGGVLNKQKSQEEIVTEFGDSACFTLSLLGHVYCKTDRLAKGAECYQKSLSLNPFLWSPFESLCEIGEKPDPEQTFKLTSLQNFSNCLPNTCTMTVNTHSVVQHRQPDTVLMETPQDTIELNRLNLESSNMKYPLNSDSSISYIDPGVISPDSLPLGTGTSILSKQAQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQTYSSCVLDVPSSGAPTKKSVARISQAGTKSVFSQSGNSRDVTPVLLVQTQGSGPQTSTTPQVLSPTIAAPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKMPNRKTKSKTSKGGVTQANMNDSLEISKLDSSIISEGKISSVAPQIQALTIQKAAAEGLMSLLRDMGKGYVALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELAEYLQAERVFSEVRRIESYRVEGMEIYSTTLWHLQKDVTLSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPGYAYAFTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSDKALDTLNKAISIDPKNPLCKFHRASILFANEKYKLALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEAVTQEEQISECYPYESVATDESQESSMTDADDTQLHAAESDEF
Protein: AT-rich interactive domain-containing protein 2 (ARID domain-containing protein 2) (BRG1-associated factor 200) (BAF200) (Zinc finger protein with activation potential) (Zipzap/p200) (Q68CP9)
Organism: Homo sapiens (Human)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regulating transcriptional activation of cardiac genes.
Subcellular location: Nucleus.
Interaction partners:
- Protein polybromo-1
- PHD finger protein 10
- Bromodomain-containing protein 7
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF complex subunit SMARCC2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- AT-rich interactive domain-containing protein 1A
- AT-rich interactive domain-containing protein 1B
Sequence:
MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSTVFGEEWKEKTDRDFVKFWKDIVDDNEVRDLISDRNKSHEGTSGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEEGNVKLLAANRTCLRFLLLSAHSHFISLRQLGLDTLGNIAAELLLDPVDFKTTHLMFHTVTKCLMSRDRFLKMRGMEILGNLCKAEDNGVLICEYVDQDSYREIICHLTLPDVLLVISTLEVLYMLTEMGDVACTKIAKVEKSIDMLVCLVSMDIQMFGPDALAAVKLIEHPSSSHQMLSEIRPQAIEQVQTQTHVASAPASRAVVAQHVAPPPGIVEIDSEKFACQWLNAHFEVNPDCSVSRAEMYSEYLSTCSKLARGGILTSTGFYKCLRTVFPNHTVKRVEDSSSNGQAHIHVVGVKRRAIPLPIQMYYQQQPVSTSVVRVDSVPDVSPAPSPAGIPHGSQTIGNHFQRTPVANQSSNLTATQMSFPVQGVHTVAQTVSRIPQNPSPHTHQQQNAPVTVIQSKAPIPCEVVKATVIQNSIPQTGVPVSIAVGGGPPQSSVVQNHSTGPQPVTVVNSQTLLHHPSVIPQQSPLHTVVPGQIPSGTPVTVIQQAVPQSHMFGRVQNIPACTSTVSQGQQLITTSPQPVQTSSQQTSAGSQSQDTVIIAPPQYVTTSASNIVSATSVQNFQVATGQMVTIAGVPSPQASRVGFQNIAPKPLPSQQVSSTVVQQPIQQPQQPTQQSVVIVSQPAQQGQTYAPAIHQIVLANPAALPAGQTVQLTGQPNITPSSSPSPVPATNNQVPTAMSSSSTPQSQGPPPTVSQMLSVKRQQQQQHSPAPPPQQVQVQVQQPQQVQMQVQPQQSNAGVGQPASGESSLIKQLLLPKRGPSTPGGKLILPAPQIPPPNNARAPSPQVVYQVASNQAAGFGVQGQTPAQQLLVGQQNVQLVPSAMPPSGGVQTVPISNLQILPGPLISNSPATIFQGTSGNQVTITVVPNTSFAPATVSQGNATQLIAPAGITMSGTQTGVGLPVQTLPATQASPAGQSSCTTATPPFKGDKIICQKEEEAKEATGLHVHERKIEVMENPSCRRGATNTSNGDTKENEMHVGSLLNGRKYSDSSLPPSNSGKIQSETNQCSLISNGPSLELGENGASGKQNSEQIDMQDIKSDLRKPLVNGICDFDKGDGSHLSKNIPNHKTSNHVGNGEISPMEPQGTLDITQQDTAKGDQLERISNGPVLTLGGSSVSSIQEASNAATQQFSGTDLLNGPLASSLNSDVPQQRPSVVVSPHSTTSVIQGHQIIAVPDSGSKVSHSPALSSDVRSTNGTAECKTVKRPAEDTDRETVAGIPNKVGVRIVTISDPNNAGCSATMVAVPAGADPSTVAKVAIESAVQQKQQHPPTYVQNVVPQNTPMPPSPAVQVQGQPNSSQPSPFSGSSQPGDPMRKPGQNFMCLWQSCKKWFQTPSQVFYHAATEHGGKDVYPGQCLWEGCEPFQRQRFSFITHLQDKHCSKDALLAGLKQDEPGQAGSQKSSTKQPTVGGTSSTPRAQKAIVNHPSAALMALRRGSRNLVFRDFTDEKEGPITKHIRLTAALILKNIGKYSECGRRLLKRHENNLSVLAISNMEASSTLAKCLYELNFTVQSKEQEKDSEMLQ
Protein: Apolipoprotein C-I (E9QFX0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLYLAAAVLMLVLAVHTEAQEEPTLEQHFTKFGTQMKEIAEDLADKTKTAFQNIEQSELGTKTRNWFNDQYEKLKQKMTETFN
Protein: Zinc finger protein 579 (Q8NAF0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable N-acetyltransferase 14
Sequence:
MDPQPPPPAQGSPPHRGRGRGRGRGRGRGRGRGRGGAGAPRAPLPCPTCGRLFRFPYYLSRHRLSHSGLRPHACPLCPKAFRRPAHLSRHLRGHGPQPPLRCAACPRTFPEPAQLRRHLAQEHAGGEVELAIERVAKETAEPSWGPQDEGSEPPTTAAAGATEEEAVAAWPETWPAGEPSTLAAPTSAAEPRESESEEAEAGAAELRAELALAAGRQEEKQVLLQADWTLLCLRCREAFATKGELKAHPCLRPEGEQEGEGGPPPRPKRHQCSICLKAFARPWSLSRHRLVHSTDRPFVCPDCGLAFRLASYLRQHRRVHGPLSLLAPLPAAGKKDDKASGARNSAKGPEGGEGAECGGASEGGEGQNGGDAAPARPPAGEPRFWCPECGKGFRRRAHLRQHGVTHSGARPFQCVRCQREFKRLADLARHAQVHAGGPAPHPCPRCPRRFSRAYSLLRHQRCHRAELERAAALQALQAQAPTSPPPPPPPLKAEQEEEGLPLPLANIKEEPPSPGTPPQSPPAPPVFLSASCFDSQDHSAFEMEEEEVDSKAHLRGLGGLAS
Protein: Sororin (Cell division cycle-associated protein 5) (Q9CPY3)
Organism: Mus musculus (Mouse)
Function: Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:21111234}. Chromosome {ECO:0000269|PubMed:21111234}. Cytoplasm {ECO:0000269|PubMed:21111234}. Note=Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown.
Interaction partners:
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5 homolog A
- Sister chromatid cohesion protein PDS5 homolog B
- Aurora kinase B
- Borealin
- Separin
- Nipped-B-like protein
- Shugoshin 1
- Cyclin-dependent kinase 1
Sequence:
MAERRTRSGGAAQRSGPRTSLTKPSKSSKRKSGSDLPNSFSEIWPRTTPAVPVRKAIVLKKIVAHAVEVPDVHTVRRSPRISFILEKENNPPLKVPTKEDLFKTCSVPGTPSSTPVLYTQNVEPDSGEAELDSRDLEMSQKVRRSYSRLQSLGCASTSTPGRRSFFGFEGPDDLPGVSPVVCSKLIETPKVPAKDLVPARTKDLVPDSTKDLVPARTLPGISPPVVKEKRKKKVPEILKSELDKWAVAMNAEFEAAEQFELLIE
Protein: Heat shock protein (HspR) (O25669)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Co-chaperone-curved DNA binding protein A
- Bifunctional DNA-directed RNA polymerase subunit beta-beta'
- RNA polymerase sigma factor RpoD
- Glutamine synthetase
- Chaperone protein DnaJ
- J domain-containing protein
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- Replication-associated recombination protein A
Sequence:
MCDYDEPLYLISVVAKILGVHPQTLRQYEKEGLIEPSRTDGKMRLYSQRDMDKIKTILRLTRDMGVNLAGVDIILRLKEKLDELDNLNKELQDALHKHSKNTKTPTKNLNTPTNFYELILFKK
Protein: Docking protein 4 (Downstream of tyrosine kinase 4) (Q99KE3)
Organism: Mus musculus (Mouse)
Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK4 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway (By similarity). Putative link with downstream effectors of RET in neuronal differentiation. May be involved in the regulation of the immune response induced by T-cells (By similarity).
Interaction partners:
- Proto-oncogene tyrosine-protein kinase receptor Ret
Sequence:
MATNFNDIVKQGYVKMKSRKLGIYRRCWLVFRKSSSKGPQRLEKYPDEKSVCLRGCPKVTEISNVKCVTRLPKETKRQAVAIIFTDDSARTFTCDSELEAEEWYKTLSVECLGSRLNDISLGEPDLLAPGVQCEQTDRFNVFLLPCPNLDVYGECKLQITHENIYLWDIHNPRVKLVSWPLCSLRRYGRDATRFTFEAGRMCDAGEGLYTFQTQEGEQIYQRVHSATLAIAEQHKRVLLEMEKNVRLLNKGTEHYSYPCTPTAMLPRSAYWHHITGSQNIAEASSYGESYGAAQASSETDLLNRFILLKPKPSQEDSSEAKTPAQ
Protein: Peroxisomal membrane 22 kDa (Mpv17/PMP22) family protein (Q9LV46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLKLWRWYQRCLTVHPVKTQVISSGFLWGFGDVTAQYITHSTAKRRLLRLTETNKDADADAEIKVKWKQDAEFKVNWKRVAITSMFGFGFVGPVGHFWYEGLDKFIKLKLRYVPKSTRFVAAKVAMDGLIFGPVDLLVFFTYMGFATGKNTAEVKEGLKRDFLPALALEGGAWPLLQIANFRYVPVQYQLLYVNIFCLVDSAFLSWVEQQKDAAWKQWFTSSFQPLKERGGQGGV
Protein: Forkhead box protein F1 (Forkhead-related activator 1) (FREAC-1) (Forkhead-related protein FKHL5) (Forkhead-related transcription factor 1) (Q12946)
Organism: Homo sapiens (Human)
Function: Probable transcription activator for a number of lung-specific genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sonic hedgehog protein
- Bone morphogenetic protein 4
- Transcription factor GATA-4
- Transcriptional activator GLI3
- Indian hedgehog protein
- Carbamoyl-phosphate synthase, mitochondrial
- Pulmonary surfactant-associated protein B
- Zinc finger protein GLI2
- Forkhead box protein F2
- Zinc finger protein GLI1
Sequence:
MSSAPEKQQPPHGGGGGGGGGGGAAMDPASSGPSKAKKTNAGIRRPEKPPYSYIALIVMAIQSSPTKRLTLSEIYQFLQSRFPFFRGSYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPMYSMMNGLGFNHLPDTYGFQGSAGGLSCPPNSLALEGGLGMMNGHLPGNVDGMALPSHSVPHLPSNGGHSYMGGCGGAAAGEYPHHDSSVPASPLLPTGAGGVMEPHAVYSGSAAAWPPSASAALNSGASYIKQQPLSPCNPAANPLSGSLSTHSLEQPYLHQNSHNAPAELQGIPRYHSQSPSMCDRKEFVFSFNAMASSSMHSAGGGSYYHQQVTYQDIKPCVM