wanglab/gogpt-training-data huggingface dataset:
Protein: Testis-specific gamma-tubulin ring protein 91 (Q4LDP4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Gamma-tubulin complex component
- Gamma-tubulin complex component 4 homolog
- Gamma-tubulin complex component
- Gamma-tubulin complex component 2 homolog
- Testis-specific gamma-tubulin ring protein 128
- Grip163
- Tubulin gamma-1 chain
- Tubulin gamma-2 chain
- Grip71
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
METQPFKIELDEEMADYFKQPPGEDGNTEAYDLHMGILELSVSLGNFTHDVEKSVNFIAASNTTSKCSFDLELLNDFRIKFEQMEQEMDAEERALHDTRGNLFMRLYNELVDKEPDETKRCDYLKLFYDLFDSNKAPQESSTIRMEVSDRIHGQVQEILEPINRSPDAKEISSDSKLNMYFESKIFPNEVNTHSLPMILDLNKEICYQDKKAELHQVHTEIAHVEGYSLLESFAEIITCPTKGIRIDYGIAMLTEPKGISAELKASKTDLKMETISSNVHENNISIASHDDLANTSLIDVHFEGYSLIESYAEIITCPKDIRIDYGIAVLSELEDISAEPKDSKNDSKMETILSNVYGNNTSIASDDGFANISFNDKAILAVDDYIDCVSSMEPVDSSFKYNFTLVSSVVTNEQGLKSDNEEVIDTNMLKGINDGTEEMNDEFPEKVEVSKGLEDKNISSVVFDEADALNDPENATYSAFTDDLSKINDYCENSKKPEKPEARTSIKSDLNQYDSIRSANSSQPLPSTTTASRSMKSSYKGVSKIPIRVNSRKFSEIKCNKITIDAENEVGEKEMMVTEKEIPTFSEGEEMDADGISTLQDIDPKSPIVSPKREDQTLSQLRQAVSDVKVNILKEVDKSLELTFKKSSDILLNNSSRGIVKSELKNFGRNSKFTDELRVQHSETLSQNIYRPNDSATHNKSCKSLPNKSPRKKLDTSLPKFNEKNQTAGLNTKMVKCDDKPDDISSPRRDNDCSFAKNALNLKTTPEKSEQFFAYKGSGKIIELQISESTQLFLELEQYVQNEVENSNCLKVENSKNEDIADQIKDPKDQSSLTHNLSIDICRECCDQENREMISPTCSHINHICKDNKSGQMVCADEVDKSEDLSPLSLRIDEYTECCDLRINPEELNEFVDEKMMSPTLSQISQTSNLVKLQVLKTMDEFLSDVSAINNTIVDEEVEIDTPMLVESLREVSNEDLIINISEGFSDISPMSTPGHPPDDQDELSPILGQISKTVSDVKINILNEVDKSLSEITVKSVSAILQKRKSKEYFSNQHKSQDFDYLTDDLSGESVVKVSPLKNVDRFISEWTQKNPSDSILGKPYPKNLRYTSETSELSESSERESLSRNSNQILYLCKSCNAMLNYSEEVNKYFAGDFCINKKKFKVSDRNDLSNLERKFRQKWHHQRYVIAAPRAIIKSFKSNPAYGWSPDDPNAPDFYEQLDQFFEVTGQKKYRAGCDILFASIQLRLSQVLKRIVRHAPKNTSFPDLITIVGVAQLEQLLTRKERAAYESMRWQSRDKGDQDLSAESLFTDALHGMMGYGSPHLKLSSLTGRLQLRSPHHQESISESYLLLALGHFGYFYRELKEHLARLAEQGDTALALRKCLQKYLLNLHQFYDVQKRNPSSLLSLYRRTRDFQRNFEWLLEVFNNVQKAKSIVVYLYKESSRRTGYQRNLLLKWLRLVIQPLIYNLHIWLLNGRLPSTDHDMFVIEQTKYSKVDEFWEKRYRITESFSGIFDPQLSEILISVGKTMEYSEKYLAINFESCVPRKEVRCMLLETFDKFLRHGDQEPLYNFVRNLHLEISSKVLKYLRKTKINPEYLFSGLHKYIMLTDLNFIMEFINALESVLGEPESSFNIQLFNEMKNKMLHKSVRDIYIDKSESEGSRCWSKLILRWKMPTHWRALLGEDSKAYEVIFKAMWRFHYVYYVLNERVHRQQIRFQNHIECTYFEGLNDTLKCFSKLTNACLRLMNVLMEYFLDYLLEPAFARLLWYCRNAITVDELLVANRKYLKTIILGSLQTKNLRKYLERLYDLILQLDNKHWKFLRLCQTSVEYVIRVRKEKPQSIFSTYYRERMLQFRWTCQNYSDVINEMKDQFDLAMISFLLCLHLADDDSLRSLAKRLDPEHYYMEKDNRLDLVQYFEFRRKLERKRSL
Protein: Enhancer of mRNA-decapping protein 3 (O94752)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stimulates decapping of both stable and unstable mRNA during mRNA decay. Stimulates decapping presumably by preventing the DCP1-DCP2 decapping complex from adopting an inactive conformation.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:16823372}. Note=Is concentrated in several cytoplasmic foci called P bodies (or cytoplasmic processing bodies) which represent sites of mRNA decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
Interaction partners:
- mRNA decapping complex subunit 2
- Putative ATP-dependent RNA helicase ste13
- mRNA-decapping enzyme subunit 1
- LSM1-LSM7 complex subunit lsm1
- Probable tubulin--tyrosine ligase C12B10.04
- 5'-3' exoribonuclease 1
- Enhancer of mRNA-decapping protein 4-like protein pdc1
- Protein sum2
- LSM complex subunit lsm4
- Deadenylation-dependent mRNA-decapping factor pdc2
Sequence:
MSVADFYGSNVEVLLNNDSKARGVITNFDSSNSILQLRLANDSTKSIVTKDIKDLRILPKNEIMPKNGTKSPSTNSTKLKSAETYSSKNKWSMDCDEEFDFAANLEKFDKKQVFAEFREKDKKDPAKLLVSHNKSPNRNYHHKQNVLGPSVKDEFVDLPSAGSQINGIDAVLSSSSNGHVTPGSKKGSRETLKKKPFVDENIPAELHTTTGDILKPITPEQLSQGIALAIAKTSTDIVVENAAQLLSQFVFSVLGGHKRLSSRNHNSQPLVCILVGSHDHASAAVAAGRRLCAIGIKVVLRLLTPFNVDNRQLLMFQAAGGYIPTENFDQFLNKLTSPIELVVDVLTGFHPSIDKNSHALIQWANDLNVLILSVDIPSGYTVQKKNTAILPKWTLALGAVTTTLAQAALVKQAAGVSVFVGNLGTGSQTWAELGILESQVTGQYLAQISCTSTN
Protein: Arrestin domain-containing protein C31A2.12 (Q09729)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Meiotically up-regulated gene 170 protein
- Uncharacterized protein C557.05
Sequence:
MNILSRKENVASYFDIRVAAEHDLIVIQGLADSAEPTPLSGSVVLCLNEAISVKAISLKLVGKCRISWSEPSPTVRGGQRHNKQEYVVYEKNWIFVPYTGANRTLRAGNYEYPFHVMLPGDIAESVEGLQSCYVVYRLKASIDRTGLASKMVKKKHIRLIRALPADAIEYTQTISVDNTWPNKIEYTISVPTKAYAIGSYIPIHFVLVPLLKRLTIGKISITLKEYITLHVAHGYNGLPASKDEVRTVRSLQTEELEEFSDHYELTKNLELPSSLVECLQDCDLDGIKIRHKLKFSVSLRNPDGHISELRAALPVVLMIPPQLFGDRAEVESLRENFESFNQPLPSYQNSMYDRLYDGLSYSNLDTPLPSGATTPRRRDSMEPTYASNEAHRRQLIAGLTELALQQQPQGRSPNEHSPSNHPEDFPPSFSLGSNPSSGAASAVITRNPSETSLADLSRVPSYKEATRSAVPLESPLQSTLPSYEDVARIEHLSRPPSPGIVTPPQRTSPSFFVSPTESTRQSLDSRRSFEHSTSSSSGISPSHSSASLAHLSQASNPNGSSSAPHRPTSARVGSHRNALDALRRARMLPSGFSRRN
Protein: STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) (Serologically defined breast cancer antigen NY-BR-96) (Q7RTN6)
Organism: Homo sapiens (Human)
Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248}. Cytoplasm {ECO:0000269|PubMed:12805220, ECO:0000269|PubMed:14517248}.
Interaction partners:
- Calcium-binding protein 39
- Serine/threonine-protein kinase STK11
- Calcium-binding protein 39-like
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- STE20-related kinase adapter protein beta
- Protein transport protein Sec61 subunit gamma
- Translocation protein SEC63 homolog
- Golgin subfamily A member 2
- Translocation protein SEC62
Sequence:
MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKTNDASSESIASFSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEELEVDDWEF
Protein: FtsZ (Q52R31)
Organism: Escherichia coli
Interaction partners:
Sequence:
DSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELITRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLEDIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNAT
Protein: Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP) (Q9WTR0)
Organism: Mus musculus (Mouse)
Function: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Note=Localized at the cell surface of melanoma cells. {ECO:0000250}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
- Collagenase 3
- Metalloproteinase inhibitor 3
- Lens fiber membrane intrinsic protein
Sequence:
MILLAFSSGRRLDFVHRSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFNIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRRAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSVPPADPRRHDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGNGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITIWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRDKEGLSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV
Protein: EF-hand domain-containing protein (Q386Q3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVATGTCNASTVVGVPPCAAASLFSDVMFMKEFGVSGLMTCCLQENACKPTDIGAVRRITLNIPMYVDKVLREKLIEVTNGAHQMISRMEYLPCACDDRRRSPFGFDGTRVLKSAVTTFTVTRVTTNPNKCFVDVSTNFTVDVALPPEGTASTKDEVLFNDIKHFWQQYVERTVLAASEYLLSIALPRIKRSVEAMYDSAYHDLEEAVCRLSVNRGKVLERPEILRIMEKALDAWSHTRRELKHQEMLNHRLEDDFQGARLVAAAAASAAAAAAAAASESQQKEQEYVGVSAVGKAADLPQPRVSVTSAGRRPTTNIDGGKTISGESAAAETKAVDEGSDIIEHNPFFSPTGGRTLSVHQVDEEEKVLNKEALELAAREARLQDISALIESFVTDKGLVDEVTAHALFTKLDVMRRGYVTEQEVVKVLRQLDPLGVYEDRNGAMKMLAAYREALSVGVYNKQGSEKVDSPHSKGLQSGDDMEQVSLMCQPSTFCSVKGGSGFLPVSDELKSVEGNRATLSAVLRRYCNLKEAMQDDAVRARASEMLHKYAFKVRGRLHYDEFCLMMLHVLKDY
Protein: Immunoglobulin J chain (P01592)
Organism: Mus musculus (Mouse)
Function: Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component.
Subcellular location: Secreted {ECO:0000269|PubMed:1517233}.
Interaction partners:
- Polymeric immunoglobulin receptor
- Ig heavy chain V-III region J606
- Marginal zone B- and B1-cell-specific protein
- Immunoglobulin lambda-like polypeptide 1
- B-cell antigen receptor complex-associated protein alpha chain
- B-cell antigen receptor complex-associated protein beta chain
- Ig lambda-2 chain C region
- Immunoglobulin heavy variable V6-4
- POU domain class 2-associating factor 1
- Interleukin-2
Sequence:
MKTHLLLWGVLAIFVKAVLVTGDDEATILADNKCMCTRVTSRIIPSTEDPNEDIVERNIRIVVPLNNRENISDPTSPLRRNFVYHLSDVCKKCDPVEVELEDQVVTATQSNICNEDDGVPETCYMYDRNKCYTTMVPLRYHGETKMVQAALTPDSCYPD
Protein: Protein sidekick-1 (Q8AV58)
Organism: Gallus gallus (Chicken)
Function: Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:12230981}.
Interaction partners:
- Kyphoscoliosis peptidase
Sequence:
MVGRKVDREIIARRNSRRDGMMMKLNFCFFFCRRWWAFLLLQLHMLQALAQDDVAPYFKTEPGLPQIHLEGNRLVLTCLAEGSWPLEFKWLHNDSEITTYSSEYKYIIPALQRSDAGFYQCIVRNRMGALLQRRSEVQVAYMGNFMDANQKKTVTEGEAAVLNFMHIFSYPRPQVTWFRDGHKIIPSSRIAITLENQLVILATSVADAGGYYAQAVNEKNGENKTSPLIHLSIASATDPSDPTAPIIVIPPQNKSVVVGTSEVTLECVASARPVERLSIMWKRNGIKITSGISSFGRRLTITNPTSADVGMYFCEAKLRDSTEEPARAKAFISLMVPPYFTAEPEGVILAEVEKDVDILCQAMGVPIPSLVWYKDSVPLSKLQNPRYKVLLSGGLRIHALRPQDAGIFQCFASNKAGEIQTYTYLDVTNIKPAFIQPPEDTTVTEGMTAMLTCEVSGAPKPAISWKKGNQILASGSVQIPRFVLLESGGLQITPVFLQDAGNYTCHAVNSEGALNAFVMLTVWNRTFIVHPPENSTVIKGTTATLRCEATHDPRISIRYVWKKDSVVINPSSSSRITVEKDGTLLISQTWSGDIGDYTCEVISFGGNDSRMARLEVIELPHSPQNLLATLNSSYSRSVVLSWVRPFDGNSPVLYYMVELSENNSPWKVHLSNLDPKMTSVTVSGLTPARTYQFRVCAVNQVGKGQYSSETSRLMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPESEHNGVLHGYILRYRLAGLPGEYQYKNITSAEINYCLVTDLIIWTQYEIQVASYNGAGLGAFSRPVTEYTLQGVPTAPPQNVQVEAVNSTTIQFLWSPPPQQFINGINQGYKLLAWPVDAPGSVTVVTIAPDFHGVHSGCITNLKKYTTYYTSVLCFTTPGDGPRSAPQLLRTLEDKPGAVGHLSFTEILDTSLKVSWQEPVEKNGIITGYQLSWEVYGRNESRLTRTLTNTTLEYKITGLSSLTTYTIEVAAVTAKGSGWVTSSTISSGVPPELPGAPSNLVISNISPRSATLQFRPGYDGKTSICKWIVEGQVGVLGEEEEWVSLHEVDNEPDAQMLEVPNLTPYTHYRFRMRQVNVVGASPLSQPSRVIQTLQAPPDVAPGSVSVRTASESSLRMRWVPLPDTQYNGNPESVGYRIKFWRVDLQPSALLKVISDRLERECTIQDLEEWTEYELQIQAFNAIGAGPWNEVVGVRTRESVPSAPPENVSAEAVSSTQILLTWSAVPESEQNGLILGYKILYKAKDLDSEPRSQTVRGNHTQSCLLSGLRKYVLYEIRVLAFTRIGDGVPSSPVLTERTKDDAPGPPIRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRLASSSPNKFTTVEVGSTVRQFTATDLTPESAYIFRTSAKTRQGWGEPLEATVITTEKRERPAPPQQLTTPQSDVSSRSLQLHWVPGSDGSSPIRYFTVQVRELPNGDWQTYSSSISHEATSCIIESLNPFTSYKLRVKATNDIGDSDYSAETEAVTTLQDVPDEPPSSVLVTPHTTSSVLVQWQPPKAESLNGLLLGYRIYYRELDYDAGSATESKAVKNPSALRAELTPQSSFKTVNSSSALTTYELTQLKKYKRYEVLMTAYNVIGESPTSTPVEVFVGEAAPAMAPQNIQVNSLSASQLELTWDPPPADSQNGNIQGYKIYYWEGDVQNDTEKVKVFSSLRQLSASKNLTSHTRYLVCISAFNAAGDGPRSRPSAGRTHQAAPSAPSFLVFSEITSTTLNVSWGEPTAANGVLQGYRVVYEPLAPVQGVSKVVTVDIKGNWQRWLKVRDLTKGMTYLFRVQARTIAYGPELQANVTAGPAEGSPGSPHEILVTKSASGLTVQWTEGDSGEKPTTGYIIEARPSDEGLWDMFVKDIPRSATSYTVSLDKLKQGVTYEFRVVAVNEFGYGEPSVPSVAVSAQTEAPFYEEWWFLLVMALSSLILILLVVFALVLHGQSKKYKNCSTGKTISNVEESVTLDNGGFTALELNSRHLNIKSTFSKKNGTRSPPRPSPGGLHYSDEDICNKYNGAVLTEGLGLNEKPLEMSESEATDSDYEDELPKHSFVNHYMSDPTYYNSWKRQQKGVKHPTSYRYEECSASETEPYFQTVITTQSSGGVYTPTGQPAPGSRTPVTGFSSFV
Protein: Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III) (Q91VB2)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12637513}. Golgi apparatus membrane {ECO:0000269|PubMed:12637513}; Peripheral membrane protein {ECO:0000269|PubMed:12637513}. Cell membrane {ECO:0000269|PubMed:12637513}; Peripheral membrane protein {ECO:0000269|PubMed:12637513}.
Interaction partners:
- Nitric oxide synthase 3
- Calmodulin-1
- Calmodulin-4
- Calmodulin 5
- Calmodulin-like protein 3
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Calmodulin-like protein 4
- Calcium/calmodulin-dependent protein kinase type II subunit beta
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MGRKEEEDCSSWKKQTTNIRKTFIFMEVLGSGAFSEVFLVKQRVTGKLFALKCIKKSPAFRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDASLVIQQVLSAVKYLHENGIVHRDLKPENLLYLTPEENSKIMITDFGLSKMEQNGVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESKLFEKIKEGYYEFESPFWDDISESAKDFICHLLEKDPNERYTCEKALRHPWIDGNTALHRDIYPSVSLQIQKNFAKSKWRQAFNAAAVVHHMRKLHMNLHSPSVRQEVENRPPVSPAPEVSRPDSHDSSITEAPILDPSTPLPALTRLPCSHSSRPSAPSGGRSLNCLVNGSLRISSSLVPMQQGPLATGPCGCCSSCLNIGNKGKSSYCSEPTLFRKANKKQNFKSEVMVPVKAGGSTHCRGGQTGVCLVM
Protein: Protein pleiotropic regulator PRL2 (Q39190)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pleiotropic regulator.
Interaction partners:
- Pre-mRNA-splicing factor SPF27 homolog
- Cell division cycle 5-like protein
- Pre-mRNA-processing factor 19 homolog 2
- Cwf15 / Cwc15 cell cycle control family protein
- Pre-mRNA-processing factor 19 homolog 1
- ARM repeat superfamily protein
- Pre-mRNA-splicing factor SYF2
- Transducin/WD40 repeat-like superfamily protein
- Tetratricopeptide repeat
- AT3G18790 protein
Sequence:
MTMIALNREVETQSLKKLSLKSVRRAREIFSPVHGQFPQPDPESKRIRLCHKIQVAFGGVEPASKPTRIADHNSEKTAPLKALALPGPKGSKELRKSATEKALVVGPTLPPRDLNNTGNPGKSTAILPAPGSFSERNLSTAALMERMPSRWPRPEWHAPWKNYRVLQGHLGWVRSVAFDPSNEWFCTGSADRTIKIWDVATGVLKLTLTGHIGQVRGLAVSNRHTYMFSAGDDKQVKCWDLEQNKVIRSYHGHLHGVYCLALHPTLDVVLTGGRDSVCRVWDIRTKMQIFVLPHDSDVFSVLARPTDPQVITGSHDSTIKFWDLRYGKSMATITNHKKTVRAMALHPKENDFVSASADNIKKFSLPKGEFCHNMLSLQRDIINAVAVNEDGVMVTGGDKGGLWFWDWKSGHNFQRAETIVQPGSLESEAGIYAACYDQTGSRLVTCEGDKTIKMWKEDEDATPETHPLNFKPPKEIRRF
Protein: Wings apart-like protein 1 (AtWAPL1) (F4I7C7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulator of sister chromatid cohesion in meiosis which negatively regulates cohesin association with chromatin, acting as an antagonist of CTF7. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (By similarity). Essential for the prophase removal of cohesin during meiosis thus determining the timely release of meiotic cohesion. Important for proper spindle attachment and assembly during meiosis. Helps to prevent abnormal centromere association during prophase I in meiocytes. Required for early embryonic patterning. Also involved in chromosome segregation during mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7Z5K2}. Chromosome {ECO:0000250|UniProtKB:Q7Z5K2}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion 1 protein 4
- Sister chromatid cohesion protein SCC4
- Sister chromatid cohesion protein SCC2
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Binding protein.
- Structural maintenance of chromosomes protein 4
- Sister chromatid cohesion 1 protein 1
- Sister chromatid cohesion 1 protein 3
- Tudor/PWWP/MBT superfamily protein.
Sequence:
MIIVKLTANRICCSLLQLRRSYEHFYIFVFLPEIPLFRFSHLKLFPKNLQIQRLVSAMMERTYGRRKPGIPRTLSDSLNDSVSQTEYLSSSSSPDIEPIDYSLLPFSSQESSSLWHSSSRSNFREDYPQNGGVVRRAKRVRNGAEAAAFTSTLLEAQEFGELMEHEDEVNFALDGLRKGHQLRIRRASLSSLLSICASQHQRRSLRAQGISQSIIDAILVLSLDDIPSNLAAATLFFALTADGQDEHFMESPKCIKFLIKLLKPVIVTSTEGKPRNIGFKLLSLLKDVDAARDPVKMDDPSSSDILSRVQELLVNCKEMRLNDSYITETTRPELSTKWVALLAMERACVSKISFDDTSGSVKKTGGNFKEKLRELGGLDAVLEVVMDCHAVMERWVEYDALSVQEKKDNLHKQSLMLLLKCLKIMENATFLSTDNQNHLLGFKKCLGSHDSRMSFTELTISVIKMLSGLHLRGGFSSPNTNNVNSHYSNGGNHDSVLEANRKVTNEVVTISSDTYSTVGSISTRNGSVSQRSQSIIHLDFSPTSMSGSQSSVSGNEPTTSKTRVGSTISGSFAGRLASLGSDIARTTLRTTQAGEPICKKFGEFAPPEESEDPFAFDLEDYKPSKWAVVSVNQKKSRAQKKKGCYKQSKDESLYQLFSSQEESSNHRLNSQEESSNRDCSTSLQPSHCTNDIDEECLCLLFDCLLTAVKVLMNLTNDNVVGCRQVGGCRGLESMAELIARHFPSFTRSQLFSEMEKTGSSHQKKDKYLTDQELDFLVAILGLLVNLVERDGVNRSRLASASVPITKPEELQESEQEMIPLLCSIFLTNQGSAETKEETTTFTLDDEEAVLEGEKEAEKMIVEAYSALLLAFLSTESRSIRNSIKDYLPKRNLAILVPVLERFVAFHMTLNMIPPETHKAVMGVIESCKSP
Protein: Steroid 5-alpha reductase C-terminal domain-containing protein (Q54W87)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MLGIYLSVFLIQFVGFLHSAFLIKSKRYYDVFGCGTFVLVGLLSLVKNYYYEIEHIGESGYVYGLRRALIVSIFIIVWSSRLVIFLNDRIKRNKKDKRFDKVRNNPKKFFIYWFMQSLWINFTITPLLLVTHQHFSISLSLIDYILILLWSTFFTIEAVADGQKTLFLGKPENKGKFINQGLWKRLCRHPNYFSEIMMHWIIYFICFRGLDSYWYKFISLISPLFISFLMLKISTPMMEKISDEKFSGNPQYQEYKKSTYKIIPFIN
Protein: Ubiquitin-like domain-containing protein (O44820)
Organism: Caenorhabditis elegans
Interaction partners:
- E1 ubiquitin-activating enzyme
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin-ribosomal protein eL40 fusion protein
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-conjugating enzyme E2 variant 1
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 3
- UV excision repair protein RAD23
Sequence:
MLLSIKTSTGKNITVEAPKSVKTEVRDKQGVVFTVSYDKGTGNQIIEMEDTVQDVKIQEAQQAPLRESEEVTEDPISVESSEVIGNLNVKVAETQQELHHEGIRIYVENAGRTCTLDTSASDTMASVKAKIWEKLRILPNTQKLLLENWDLDLFSDHSTLFDNSFENGSTLRLEVSIEKEIDVFVKTYTGKTITISI
Protein: Kynurenine 3-monooxygenase (PfKMO) (EC 1.14.13.9) (Kynurenine 3-hydroxylase) (Q84HF5)
Organism: Pseudomonas fluorescens
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Probably required for the synthesis of quinolinic acid and the siderophore quinolobactin.
Interaction partners:
Sequence:
MTATDNARQVTIIGAGLAGTLVARLLARNGWQVNLFERRPDPRIETGARGRSINLALAERGAHALRLAGLEREVLAEAVMMRGRMVHVPGTPPNLQPYGRDDSEVIWSINRDRLNRILLDGAEAAGASIHFNLGLDSVDFARQRLTLSNVSGERLEKRFHLLIGADGCNSAVRQAMASVVDLGEHLETQPHGYKELQITPEASAQFNLEPNALHIWPHGDYMCIALPNLDRSFTVTLFLHHQSPAAQPASPCFAQLVDGHAARRFFQRQFPDLSPMLDSLEQDFEHHPTGKLATLRLTTWHVGGQAVLLGDAAHPMVPFHGQGMNCALEDAVALAEHLQSAADNASALAAFTAQRQPDALAIQAMALENYVEMSSKVASPTYLLERELGQIMAQRQPTRFIPRYSMVTFSRLPYAQAMARGQIQEQLLKFAVANHSDLTSINLDAVEHEVTRCLPPLSHLC
Protein: Cytokine-like nuclear factor N-PAC (NPAC) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60 homolog) (Nucleosome-destabilizing factor) (Putative oxidoreductase GLYR1 homolog) (Q8T079)
Organism: Drosophila melanogaster (Fruit fly)
Function: Nucleosome-destabilizing factor that is recruited to genes during transcriptional activation and colocalizes with a subset of trimethylated 'Lys-36' histone H3 (H3K36me3)-enriched regions. Binds DNA (in vitro). Facilitates Pol II transcription through nucleosomes. Facilitates male-specific lethal (MSL) histone acetyltransferase complex targeting to active genes on the X chromosome. Stimulates the acetylation of 'Lys-56' of nucleosomal histone H3 (H3K56ac) by nej. May have oxidoreductase activity (By similarity).
Subcellular location: Chromosome {ECO:0000269|PubMed:23295261, ECO:0000269|PubMed:29759984}. Note=Localization to open chromatin depends on H3K36 trimethylation by Set2. {ECO:0000269|PubMed:23295261}.
Interaction partners:
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
- Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- aldehyde dehydrogenase
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- (S)-3-amino-2-methylpropionate transaminase (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT)
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Uncharacterized protein, isoform B
- aldehyde dehydrogenase
- JIL-1 anchoring and stabilizing protein, isoform A
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MSKNKKLSLSGGDTTEKFIYKPKDLIWAKMKGFTPWPGMIVDPPLDLLSQQRRANTKCVFFFGSRNFAWIEENNIKPFEGPWKEELAKVSKPAAFRHAMTDIEKYIDDPAEVDEQVNKSCGAPNHATEADFDKIRDGLDSEEIVGEEATADGNNGVVAHVVGSPDEGDGLDVEINADSSASPVTSPAVTTKAAGKRTPKAKSVAATSVKSTKGSAKSAQKRRTSAQQSPSGPSNAKRGKRDVSGEALQDADEASSTPTGRRRVETDALLASIAAKRAPNAIALLDRPVVTRPEAQVIDMSSRSNTLADRDIVPSEQTFGFLGLGMMGSTIVKDLIYTGHKVVVWNRTIDKCQPFAEAGAEVKDTPMDVVEAADVIFCCVSDPKGAKDLVFGNCGVLQLKDLNNKAYVEMSTIDPDTSLDIGEGIKQCNGRYLEAQIHGSRQEAAEGMLIILAGGDRSVFEECHSCFKTIAKNTFFLGNIGNACKVNLILQTILGVSLVGLAEALALADRFSISLNDIIDIFDLTSMKSPMLLAKGKEMAKGDFNPQQPLSHMQRDLRLVLNMAENLDQSMPVTSITNEVFKHTKRLGYSEHDSSAVFVRSRF
Protein: DNA repair protein RAD51 homolog (Q5TYR1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364139}.
Interaction partners:
- DNA repair protein RAD52 homolog
- BRCA2 DNA repair-associated.
- Exonuclease 1
- BLM RecQ-like helicase.
- RAD51 paralog C.
- Structure-specific endonuclease subunit MUS81
- Replication protein A 70 kDa DNA-binding subunit
- FA complementation group M.
- DNA repair protein
- Serine/threonine-protein kinase CHK1
Sequence:
MAMRNASRVEVEAEVEEEENFGPQPVSRLEQSGISSSDIKKLEDGGFHTVEAVAYAPKKELLNIKGISEAKADKILTEAAKMVPMGFTTATEFHQRRAEIIQISTGSKELDKLLQGGIETGSITEMFGEFRTGKTQLCHTLAVTCQLPIDQGGGEGKAMYIDTEGTFRPERLLAVAERYGLVGSDVLDNVAYARAFNTDHQTQLLYQASAMMTESRYALLIVDSATALYRTDYSGRGELSARQGHLGRFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFSADPKKPIGGNILAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD