wanglab/gogpt-training-data huggingface dataset:
Protein: Drebrin-like protein (Actin-binding protein 1) (SH3 domain-containing protein 7) (Q62418)
Organism: Mus musculus (Mouse)
Function: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:9891087}. Cell projection, lamellipodium {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:12913069}. Cell projection, ruffle {ECO:0000269|PubMed:12913069}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:23223303}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000269|PubMed:11309416}. Perikaryon {ECO:0000269|PubMed:11309416}. Cell projection, neuron projection {ECO:0000269|PubMed:11309416}. Cell membrane {ECO:0000250|UniProtKB:Q9JHL4}; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000305|PubMed:11309416}; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane {ECO:0000269|PubMed:16452483}; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome {ECO:0000269|PubMed:22303001}. Early endosome {ECO:0000250|UniProtKB:Q9UJU6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density {ECO:0000250|UniProtKB:Q9JHL4}. Note=Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q9JHL4, ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17476322, ECO:0000269|PubMed:22303001}.
Interaction partners:
- Adenylyl cyclase-associated protein 1
- F-actin-capping protein subunit beta
- Adenylyl cyclase-associated protein 2
- Protein cordon-bleu
Sequence:
MAVNLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEELVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMANFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESTSFQDVGPQAPVGSVYQKTNAISEIKRVGKDNFWAKAEKEEENRRLEEKRRAEEERQRLEEERRERELQEAARREQRYQEQHRSAGAPSPSSRTGEPEQEAVSRTRQEWESAGQQAPHPREIFKQKERAMSTTSVTSSQPGKLRSPFLQKQLTQPETSYGREPTAPVSRPAAGVCEEPAPSTLSSAQTEEEPTYEVPPEQDTLYEEPPLVQQQGAGSEHIDNYMQSQGFSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
Protein: Protein PHOX1 (Protein MADB1) (Putative myosin adapter B1) (F4IRM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylate clamp type tetratricopeptide repeat protein that may act as a potential Hsp90/Hsp70 co-chaperone. Contributes to polar growth of root hairs.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28096376}; Peripheral membrane protein {ECO:0000269|PubMed:28096376}.
Interaction partners:
- TOM1-like protein 6
- Myosin-17
- Flowering time control protein FY
- TOM1-like protein 2
- Serine/threonine-protein kinase AFC1
- ATP-dependent zinc metalloprotease
- Translation initiation factor eIF2 assembly protein
- Protein SUPPRESSOR OF FRI 4
- Aspartyl protease family protein 2
- Probable WRKY transcription factor 19
Sequence:
MGKPTGKKKNNNYTEMPPTESSTTGGGKTGKSFDRSATKSFDDDMTIFINRALELKEEGNKLFQKRDYEGAMFRYDKAVKLLPRDHGDVAYLRTSMASCYMQMGLGEYPNAINECNLALEASPRFSKALLKRARCYEALNKLDFAFRDSRVVLNMEPENVSANEIFERVKKVLVGKGIDVDEMEKNLVNVQPVGAARLRKIVKERLRKKKKKSMTMTNGGNDGERKSVEAVVEDAKVDNGEEVDSGRKGKAIEEKKLEDKVAVMDKEVIASEIKEDATVTRTVKLVHGDDIRWAQLPLDSSVVLVRDVIKDRFPALKGFLIKYRDSEGDLVTITTTDELRLAASTREKLGSFRLYIAEVSPNQEPTYDVIDNDESTDKFAKGSSSVADNGSVGDFVESEKASTSLEHWIFQFAQLFKNHVGFDSDSYLELHNLGMKLYTEAMEDIVTGEDAQELFDIAADKFQEMAALAMFNWGNVHMSKARRQIYFPEDGSRETILEKVEAGFEWAKNEYNKAAEKYEGAVKIKSDFYEALLALGQQQFEQAKLCWYHALSGEVDIESDASQDVLKLYNKAEESMEKGMQIWEEMEERRLNGISNFDKHKELLQKLGLDGIFSEASDEESAEQTANMSSQINLLWGSLLYERSIVEYKLGLPTWDECLEVAVEKFELAGASATDIAVMVKNHCSSDNALEGMGFKIDEIVQAWNEMYDAKRWQIGVPSFRLEPLFRRRSPKLHDILENVFSGPQ
Protein: Beta(1-4) galactosyltransferase (B0EWZ9)
Organism: Moraxella catarrhalis (Branhamella catarrhalis)
Interaction partners:
Sequence:
MIQNFVISVKTATKRREHIMCEFGKQGIAFEFFDAVTPTDISKYAQKLSIPIINNQRLTDGEKACFLSHVALWQQMIDENLDYMAIFEDDVYLGNDSQQFLQELTIWLQQNAVDVIKLETWVEKIHIKKAVTVLNHRQLCPLKTFHTGTAGYVISQQGAKIILDYLSTLDAFEFFPIDHVIFDAIISKMSVLQVNPAMVIQAHLVSEDDTFKSLLETQRKQNVNQHRRRTLADYGKKYYRSIGKRTFFQRIAFQ
Protein: Brachyury 2 (Brachyury2) (Q8K4Y2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEFSRKLLERDGRFADMDAEHRARSLLDYMVPRERTQADVPPRERTQADVPPRELEEEDSPTPEQQPQAGPALRFLKCQSPESPQRRPHLKTGRHQVTLCGTSKLSEHERGTLAPARRTTDPRPTAPLTLAHVIQTHPVVEAKTASRYWVNNVDEE
Protein: Probable dihydrodipicolinate synthetase (Q9I490)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- 2,5-dioxovalerate dehydrogenase
- 2,5-dioxovalerate dehydrogenase
- FAD dependent oxidoreductase domain-containing protein
- Probable oxidoreductase
- Bifunctional trans-3-hydroxy-L-proline dehydratase/2-epimerase
- NAD
- Delta
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxyproline 2-epimerase
- PKHD-type hydroxylase PiuC
Sequence:
MSKHVNWSGVFPAVTTQFNADFSVNLEETHTVISNLVRDGVSGLVVCGSVGENTSLTIEEKMAVTEVAKDASGGRVPVICGIAEFTSAGAAKVAKAVERVGVDGIMVMPALVYSSKPHETAEHFRSVASGTDLPVMVYNNPPIYRNDVTPDILVSLADCENIVCFKDSSGDTRRFIDVRNQVGERFILFAGLDDVVLESVAVGAQGWISGMSNVFPKEGETIFRLARAGRFAEAMPIYEWLMPILHLDARPDLVQCIKLCEQLAGRGSALTRPPRLALRGADREHVERIMAKALASRPALPDVGL
Protein: Polyhomeotic-like protein 2 (hPH2) (Early development regulatory protein 2) (Q8IXK0)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.
Subcellular location: Nucleus {ECO:0000269|PubMed:21282530}. Note=Co-localizes with SAMD7 in nuclear polycomb bodies. {ECO:0000250|UniProtKB:Q9QWH1}.
Interaction partners:
- Chromobox protein homolog 8
- Polycomb complex protein BMI-1
- Chromobox protein homolog 2
- Polycomb group RING finger protein 2
- E3 ubiquitin-protein ligase RING1
- E3 ubiquitin-protein ligase RING2
- Polyhomeotic-like protein 1
- Chromobox protein homolog 7
- E3 SUMO-protein ligase CBX4
- Chromobox protein homolog 6
Sequence:
MENELPVPHTSSSACATSSTSGASSSSGCNNSSSGGSGRPTGPQISVYSGIPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPELGTGSPARPPTPAQVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFQHTSAVILQLQPASPPQQCVPDDWKEVAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQAIVKPQILTHVIEGFVIQEGAEPFPVGRSSLLVGNLKKKYAQGFLPEKLPQQDHTTTTDSEMEEPYLQESKEEGAPLKLKCELCGRVDFAYKFKRSKRFCSMACAKRYNVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQPTGTVPLSVTAALQLTHSQEDSSRCSDNSSYEEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPSEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKDS
Protein: Zinc finger and SCAN domain-containing protein 21 (Renal carcinoma antigen NY-REN-21) (Zinc finger protein 38 homolog) (Zfp-38) (Q9Y5A6)
Organism: Homo sapiens (Human)
Function: Strong transcriptional activator (By similarity). Plays an important role in spermatogenesis; essential for the progression of meiotic prophase I in spermatocytes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein 397
- Zinc finger and SCAN domain-containing protein 20
- NADPH oxidase 4
- Zinc finger and SCAN domain-containing protein 23
- Zinc finger protein 174
- Zinc finger protein 232
- Zinc finger protein 446
Sequence:
MMTKVLGMAPVLGPRPPQEQVGPLMVKVEEKEEKGKYLPSLEMFRQRFRQFGYHDTPGPREALSQLRVLCCEWLRPEIHTKEQILELLVLEQFLTILPQELQAWVQEHCPESAEEAVTLLEDLERELDEPGHQVSTPPNEQKPVWEKISSSGTAKESPSSMQPQPLETSHKYESWGPLYIQESGEEQEFAQDPRKVRDCRLSTQHEESADEQKGSEAEGLKGDIISVIIANKPEASLERQCVNLENEKGTKPPLQEAGSKKGRESVPTKPTPGERRYICAECGKAFSNSSNLTKHRRTHTGEKPYVCTKCGKAFSHSSNLTLHYRTHLVDRPYDCKCGKAFGQSSDLLKHQRMHTEEAPYQCKDCGKAFSGKGSLIRHYRIHTGEKPYQCNECGKSFSQHAGLSSHQRLHTGEKPYKCKECGKAFNHSSNFNKHHRIHTGEKPYWCHHCGKTFCSKSNLSKHQRVHTGEGEAP
Protein: Gamma-glutamyl hydrolase (EC 3.4.19.9) (Conjugase) (GH) (Gamma-Glu-X carboxypeptidase) (Q62867)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Exhibits either endo- or exopeptidase activity depending upon the tissue of origin. When secreted, it acts primarily as an endopeptidase (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:Q92820}. Lysosome {ECO:0000250|UniProtKB:Q92820}. Melanosome {ECO:0000250|UniProtKB:Q92820}. Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. {ECO:0000250|UniProtKB:Q92820}.
Interaction partners:
- Folylpolyglutamate synthase
- Dihydrofolate reductase
- Lipid droplet-regulating VLDL assembly factor AUP1
- Reduced folate transporter
Sequence:
MASLGRLLCAWVLLLCGLASPGLSGSYERGSKRPIIGIIMQECYGNMTKLGRFYIAASYVKFIESAGARVVPIRLDLNDAQYETLFRSINGVLLPGGGANLTHSGYSRVAKIFFTKALESFDNGDYFPVWGTCLGLEELSVLVSNDNLLTLTNTSSVKLPLNFTRDSKQSRMFRNLPEELLNSLASENLTANFHKWSLSVKNFTENEKLKKFFNILTVNTDGKTEFISSMEGYKYPIYAVQWHPEKAPFEWKKLRGISHAPNAVKTSFYLAKFFISEALKNDHHFENELEETESLIYQFCPVYTGNISSFQQAYMFN
Protein: Signal recognition particle subunit SRP68 (SRP68) (Signal recognition particle 68 kDa protein) (Q9UHB9)
Organism: Homo sapiens (Human)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER. Binds the signal recognition particle RNA (7SL RNA), SRP72 binds to this complex subsequently. The SRP complex possibly participates in the elongation arrest function (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10618370}. Nucleus, nucleolus {ECO:0000269|PubMed:10618370}. Endoplasmic reticulum {ECO:0000269|PubMed:28369529}.
Interaction partners:
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SRP72
- Signal recognition particle 19 kDa protein
- Signal recognition particle 14 kDa protein
- Signal recognition particle 9 kDa protein
- Signal recognition particle receptor subunit beta
- Signal recognition particle receptor subunit alpha
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL20
Sequence:
MAAEKQVPGGGGGGGSGGGGGSGGGGSGGGRGAGGEENKENERPSAGSKANKEFGDSLSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTLNFKMGNRHKFTGKKVTEELLTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSRLRKAVKHAEELERLCESNRVDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIYEKLASAFTEEQAVLYNQRVEEISPNIRYCAYNIGDQSAINELMQMRLRSGGTEGLLAEKLEALITQTRAKQAATMSEVEWRGRTVPVKIDKVRIFLLGLADNEAAIVQAESEETKERLFESMLSECRDAIQVVREELKPDQKQRDYILEGEPGKVSNLQYLHSYLTYIKLSTAIKRNENMAKGLQRALLQQQPEDDSKRSPRPQDLIRLYDIILQNLVELLQLPGLEEDKAFQKEIGLKTLVFKAYRCFFIAQSYVLVKKWSEALVLYDRVLKYANEVNSDAGAFKNSLKDLPDVQELITQVRSEKCSLQAAAILDANDAHQTETSSSQVKDNKPLVERFETFCLDPSLVTKQANLVHFPPGFQPIPCKPLFFDLALNHVAFPPLEDKLEQKTKSGLTGYIKGIFGFRS
Protein: Tudor and KH domain-containing protein homolog (Partner of PIWIs protein) (BmPAPI) (H9JD76)
Organism: Bombyx mori (Silk moth)
Function: Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins (Siwi or Ago3) and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs: acts by recruiting the exonuclease PNLDC1/trimmer to Siwi-bound pre-piRNAs.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:23970546}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to the outer surface of mitochondria. {ECO:0000269|PubMed:23970546}.
Interaction partners:
- Piwi-like protein Siwi
- Piwi-like protein Ago3
- Pre-piRNA 3'-exonuclease trimmer
- Small RNA 2'-O-methyltransferase
Sequence:
MSLNTKLALPIALGLSLVTVTAFVAYYVLKRDEEENDNKTVKITKINTIEIHVPKSIVPALIGRNGSNIKDLQKKSGAQIHFKKFTDQDYDVCVVRGRADTTQLAETLIHDFIKQQPTIMSESITVPSWSCGRIIGSGGENVNDISHRSGARVKVESPKSTDKVAEHLVTFRGTKEQIEVAKKLVENCVSLERCRREIEQSKRPPRHSSSPPSPCPSPGDRDADADAQGDVDHTRVKYKRPETTGPSIEVYVSAVSSPSRFWVQFVGPQVAQLDDLVAHMTEYYSKKENREAHTLRHVSVGQVVAAVFRHDGRWYRARVHDIRPNEFDSSQQVADVFYLDYGDSEYVATHELCELRADLLRLRFQAMECFLAGVRPASGEEAVSPSGQTWDKWHPQAVERFEELTQVARWKALVSRTCTYKKTATAEGEKDKEIPGIKLFDVTDEGELDVGAVLVAEGWAVAGPAPSPRPSPPRGHTTPFGDLSKSKVLSMTGGGGRSSSVPKDHKDDGSNVLTVEGDDSKDKDGITASKSLASGLEKSDRHPLSISNFDLSYPDPSRNKQLNGSDDFLHGERQNIDNEITIDTLVPPSPLSNAPILSKTLQDEFKANMNRIDSHHSNLENLGKSAFEK
Protein: Growth factor receptor-bound protein 10 (GRB10 adapter protein) (Maternally expressed gene 1 protein) (Q60760)
Organism: Mus musculus (Mouse)
Function: Adapter protein which modulates coupling of a number of cell surface receptor kinases with specific signaling pathways. Binds to, and suppress signals from, activated receptors tyrosine kinases, including the insulin (INSR) and insulin-like growth factor (IGF1R) receptors. The inhibitory effect can be achieved by 2 mechanisms: interference with the signaling pathway and increased receptor degradation. Delays and reduces AKT1 phosphorylation in response to insulin stimulation. Blocks association between INSR and IRS1 and IRS2 and prevents insulin-stimulated IRS1 and IRS2 tyrosine phosphorylation. Recruits NEDD4 to IGF1R, leading to IGF1R ubiquitination, increased internalization and degradation by both the proteasomal and lysosomal pathways. A similar role in the mediation of ubiquitination has also been suggested with INSR. Negatively regulates Wnt signaling by interacting with LRP6 intracellular portion and interfering with the binding of AXIN1 to LRP6. Positive regulator of the KDR/VEGFR-2 signaling pathway. May inhibit NEDD4-mediated degradation of KDR/VEGFR-2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18286479}. Note=When complexed with NEDD4 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R before the sorting of the receptor to the lysosomal compartment.
Interaction partners:
- Insulin-like growth factor 1 receptor
- E3 ubiquitin-protein ligase NEDD4
- Insulin receptor
- Insulin-like growth factor 1
- Serine/threonine-protein kinase mTOR
- GRB10-interacting GYF protein 2
- Insulin-2
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- GRB10-interacting GYF protein 1
- Insulin receptor substrate 1
Sequence:
MNNDINSSVESLNSACNMQSDTDTAPLLEDGQHASNQGAASSSRGQPQASPRQKMQRSQPVHILRRLQEEDQQLRTASLPAIPNPFPELTGAAPGSPPSVAPSSLPPPPSQPPAKHCGRCEKWIPGENTRGNGKRKIWRWQFPPGFQLSKLTRPGLWTKTTARFSKKQPKNQCPTDTVNPVARMPTSQMEKLRLRKDVKVFSEDGTSKVVEILTDMTARDLCQLLVYKSHCVDDNSWTLVEHHPQLGLERCLEDHEIVVQVESTMPSESKFLFRKNYAKYEFFKNPVNFFPDQMVNWCQQSNGGQAQLLQNFLNTSSCPEIQGFLQVKEVGRKSWKKLYVCLRRSGLYYSTKGTSKEPRHLQLLADLEESSIFYLIAGKKQYNAPNEHGMCIKPNKAKTEMKELRLLCAEDEQIRTCWMTAFRLLKYGMLLYQNYRIPQRKGLPPPFNAPMRSVSENSLVAMDFSGQIGRVIDNPAEAQSAALEEGHAWRKRSTRMNILSSQSPLHPSTLNAVIHRTQHWFHGRISREESHRIIKQQGLVDGLFLLRDSQSNPKAFVLTLCHHQKIKNFQILPCEDDGQTFFTLDDGNTKFSDLIQLVDFYQLNKGVLPCKLKHHCIRVAL
Protein: Fanconi anemia group J protein homolog (EC 5.6.2.3) (DNA 5'-3' helicase FANCJ) (Q3YK19)
Organism: Gallus gallus (Chicken)
Function: DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the 'Fanconi anemia' pathway of DNA repair, after FANCD2 ubiquitination. Probably not involved in the repair of DNA double-strand breaks by homologous recombination.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BX63}.
Interaction partners:
- Uncharacterized protein.
- DNA topoisomerase II binding protein 1
- Tower domain-containing protein.
- DNA mismatch repair protein MLH1
- Fanconi anemia group M protein
- Uncharacterized protein.
- Uncharacterized protein.
- DNA repair protein RAD51 homolog 3
- Partner and localizer of BRCA2
- Uncharacterized protein.
Sequence:
MSSDVSQYTIGGVKIMFPCKAYPSQLAMMNAIVKGLNNRQHCLLESPTGSGKSLALLCSALSWQQSLYEKSLLKSSCEKEDREPAASLPCRCVCHSRSESSEATAGASHGAACSNNYETGGSVKHGDQLSDTECKENNTLASKLSAKKRASACGNECDDFQVERKRIRPLETEQQVRKRHCFSKEVQLVDALEVYNQRKNGELIVHSEKSVKNTSPQTLFSSCTECSCSSGKETRKDSGNTKKKANGDQTFIPKIFFGTRTHKQIAQITRELKRTAYSGVPMTILSSRDYTCIHPVVSSSNSNRNELCVELLEGKHGKSCLYYHGVHKLSEHYALQSAHNTYQAWDIEDLVSLGKKLRACPYFAARELMVGADIVFCPYNYLLDPQIRESMEINLKGQVVILDEAHNIEDSAREAVSYSVTESQLNAAREELDFMVNNNIRQKDHEQLRAMCCSLTNWLRESSSQLVETGYETSCKVWSGKEMLNHFHDMGITNISFPILQKHLSAVLEKEEKISMFGKEELVEIPIVSSATQIVLKGLFMVLLYLFKDNSRFADDYRVALQQTYAWTNDNQPDVSDTSAFFTKTKHKRNLRHKTVVHMLNFWCLNPAVAFSDLNDVRTVVLTSGTLSPMDSFSSELGVKFSIQLEANHVIRNSQVWVGTIGTGPNGRKLCATFQHTETFEFQDEVGALLLSVCQKVGQGILCFLPSYKLLDKLKDRWIHTGLWRNLELVKTVIAEPQGGAKSDFDELLKIYYDAIKFKGEKDGALLIAVCRGKVSEGLDFCDENARAVITIGIPFPNVKDLQVELKRKYNDQHKTTRGLLPGSQWYEIQAYRALNQALGRCIRHRSDWGALILVDDRFRNNPNKYITGLSKWIRQQVQHHENFGSALESLHAFAERNQKGIDFSSQCSNEVFHVPLNSKEPSSASQQEATIHLSPDVPVKSEEQSFVPETHLTTTINSINPGPSNQPGGQKVDVESCSHNGIQRRKHMDSTPRRPANKTEKKSDRTNSDFMKEHCCFKPLTSTPLPVATNCVSTASSKQRKNVNSASELIGGVNQCQSSFTLEHKPSIPESHLETTNFSVKSTEAPVAEEHLDEQKLQIEPCSELPSVGGRPELSVLEISAEDEDESLYFTPELYDDAESEEQEMRPLDPDENQIECGKPTVADDLFVISTSKTLSEPKEMINDDGRNTSLHGTMLSDISKNSTVNIEKMTNGEEAEQVESQEVDTKKRKISLSRSRNKGVSPFLLDSTST
Protein: Probable cytochrome P450 4d21 (EC 1.14.-.-) (CYPIVD21) (Q9VLZ7)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- GH15759p
- Probable cytochrome P450 304a1
Sequence:
MWILLGIAVLIMTLVWDNSRKQWRVNTFEKSRILGPFTIPIVGNGLQALTLRPENFIQRFGDYFNKYGKTFRLWILGECLIYTKDLKYFESILSSSTLLKKAHLYRFLRDFLGDGLLLSTGNKWTSRRKVLAPAFHFKCLENFVEIMDRNSGIMVEKLKNYADGKTCVDLFKFVSLEALDVTTETAMGVQVNAQNEPNFPYTKALKSVVYIESKRLASVSMRYNWLFPLAAPLVYRRLQKDIAIMQDFTDKVIRERRAILERARADGTYKPLIMGDDDIGGKAKMTLLDILLQATIDNKPLSDVDIREEVDVFIFAGDDTTTSGVSHALHAISRHPKVQECIYEELVSVLGPDPDASVTQTKLLELKYLDCVIKETMRLHPPVPILGRYIPEDLKIGEITIPGNTSILLMPYYVYRDPEYFPDPLVFKPERWMDMKTTSNTPPLAYIPFSSGPKNCIGQKFANLQMKALISKVIRHYELLPLGADLKATYTFILSSSTGNNVGLKPRTRVK
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4JD62)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGASDALTYSLMAQQPPSGPPHAGGQQITPGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: Ubiquitin-like-conjugating enzyme ATG10 (Autophagy-related protein 10) (Q18991)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin-like protein atg-12
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related protein 5
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy-related protein 13 homolog
- Autophagy-related protein 9
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- non-specific serine/threonine protein kinase
- Autophagy-related protein 2
- Autophagy-related protein 18
Sequence:
MLTEQQFRDEIRGFVDKMNENNFHWQLKEIGKYARETHLKTLSDGRVITSETHILYNSTYQVPTIWFNFFENNGSPLPFRTVIRDVLNISETEESEASIRSRISHYEHPFMGVLYYNIHPCNTSNIMKELNTDRSYLMSWFSVYGQQIGLKLPDRVL
Protein: Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 6 (C1PGW0)
Organism: Zinnia elegans (Garden zinnia) (Zinnia violacea)
Function: Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19383897}; Single-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:19383897}.
Interaction partners:
Sequence:
MATIFIVFVSFGCVFVLGIAAFVLCCLIKKWKCSKAIEKNEMVHVDQHLQVHENILQGPNGMKTVAITVDDDLHVHDEEECVKNEKLGTASTSKA