wanglab/gogpt-training-data huggingface dataset:
Protein: Parathyroid hormone 2 receptor a (Parathyroid hormone type-2 receptor) (Q9PWB7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLTVSLLILCKPSSSPSPVKIIPVDDLPATAELRASVLRVSLPKTFIKSFLNHLLQAGEDGEITAEEQVQMLLDAKLQCLQKVSSDDPAVGVCVPEWDGLICWPQGFPGTLTKTPCPGYIYDFNHAAHAYRRCDSNGSSVLAESSNKTWVNYTECIKSPEPNKKRQVFFERLHIMYTVGYAVSFSSLLVAIFIIGYFRRLHCTRNYIHMHLFVSFMLRAASIFVKDHVVHTSAGLQESDAVLMNNFTNAVDVAPVDTSQYMGCKVTVLLFIYFLATNYYWILVEGLYLHSLIFMAFLSDSKYLWGFTLIGWGVPAVFVAAWAVVRATLADARCWELSAGNIKWIYQVPILTAIGLNFILFVNIVRVLATKIRETNAGRYDTRKQYRKLAKSTQVLVFVFGVHYIVFVGMPHTFEGLGWEERMYCELFFNSFQGFFVSIIYCYCNGEVQTEIKKTWTRWNLAFDWKGPVVCGSNRYGSVLTGLNNSTSSQSQLAAGGPGTRSTTLFSSRVYRSSGGPTVSTHATLPGYVLNSDADSLPPSIPEEPEDSAKQVDDILLKESLPTRPSSGLEDDEETL
Protein: A-kinase anchor protein 3 (AKAP-3) (A-kinase anchor protein 110 kDa) (AKAP 110) (Protein kinase A-anchoring protein 3) (PRKA3) (O88987)
Organism: Mus musculus (Mouse)
Function: May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11278869}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:31969357, ECO:0000269|PubMed:37709195}. Note=Dorsal margin of the acrosomal segment (PubMed:11278869). Ribs of the fibrous sheath in the principal piece of the sperm tail (PubMed:11278869, PubMed:31969357, PubMed:37709195). {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:31969357, ECO:0000269|PubMed:37709195}.
Interaction partners:
- Calcium-binding tyrosine phosphorylation-regulated protein
- Ropporin-1
- Outer dense fiber protein 1
- Sperm surface protein Sp17
- Ropporin-1-like protein
Sequence:
MADRVDWLQSQSGVCKVGVYSPGDNQHQDWKMDTSTDPVRVLSWLRKDLEKSTAGFQDSRFKPGESSFVEEVAYPVDQRKGFCVDYYNTTNKGSPGRLHFEMSHKENPSQGLISHVGNGGSIDEVSFYANRLTNLVIAMARKEINEKIHGAENKCVHQSLYMGDEPTPHKSLSTVASELVNETVTACSKNISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPGTKKSFFYKEVFESRNAGDAKEGGRSLPGDQKLFRTSPDNRPDDFSNSISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILLKKVLMKHAKEVVSDLIDSFMKNLHGVTGSLMTDTDFVSAVKRSFFSHGSQKATDIMDAMLGKLYNVMFAKKFPENIRRARDKSESYSLISTKSRAGDPKLSNLNFAMKSESKLKENLFSTCKLEKEKTCAETLGEHIIKEGLHMWHKSQQKSPGLERAAKLGNAPQEVSFECPDPCEANPPHQPQPPENFANFMCDSDSWAKDLIVSALLLIQYHLAQGGKMDAQSFLEAAASTNFPTNKPPPPSPVVQDECKLKSPPHKICDQEQTEKKDLMSVIFNFIRNLLSETIFKSSRNCESNVHEQNTQEEEIHPCERPKTPCERPITPPAPKFCEDEEATGGALSGLTKMVANQLDNCMNGQMVEHLMDSVMKLCLIIAKSCDSPLSELGEEKCGDASRPNSAFPDNLYECLPVKGTGTAEALLQNAYLTIHNELRGLSGQPPEGCEIPKVIVSNHNLADTVQNKQLQAVLQWVAASELNVPILYFAGDDEGIQEKLLQLSATAVEKGRSVGEVLQSVLRYEKERQLDEAVGNVTRLQLLDWLMANL
Protein: Proteasome subunit alpha type-4 (Macropain subunit C9) (Multicatalytic endopeptidase complex subunit C9) (Proteasome component C9) (Proteasome subunit L) (Proteasome subunit alpha-3) (alpha-3) (P25789)
Organism: Homo sapiens (Human)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9 (PubMed:34711951). Colocalizes with TRIM5 in the cytoplasmic bodies (By similarity). {ECO:0000250|UniProtKB:Q9R1P0, ECO:0000269|PubMed:34711951}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
- Proteasome maturation protein
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit 4
- Proteasome subunit beta type-8
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit beta type-9
- 26S proteasome non-ATPase regulatory subunit 1
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK
Protein: U3 small nucleolar ribonucleoprotein protein MPP10 (E7F5L8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|PIRNR:PIRNR017300}.
Interaction partners:
- PWP2 small subunit processome component.
- Nucleolar protein 58
- Si:dkey-251i10.3
- UTP6 small subunit processome component.
- WD repeat domain 3.
- Nucleolar protein 6
- WD repeat-containing protein 75
- IMP U3 small nucleolar ribonucleoprotein 4)
- Something about silencing protein 10
- WD repeat domain 43.
Sequence:
MATRDGGTLESCLQLLNSNTSHPELFLSVQDVLATDFRSLTKILYDLQKAHEPADCKGSPLEQLVVENFDEEQIWQELELQNSALLTHFEQAVEQAVTDDAITFLNDEDDDVEEDEEELEEVDDEEIADNLEQGSAEEEDDEDGEEETTQRLKPTSNGEDDFSGEDSDLDFDVDKFEKQTKQRQSAAGKLTKSKPNWTQSEVDDTFFKLSEMEAFLDDMDKREGKGNEGEEIDYFQDLPSDEDDELSFDKPVVKKKLKNKSSRNMKYKDFFAPVDGEPDPIPDEEKELESNDDYEGEEQDDDELEEEYEEDMNEEDFDMERDDDDIGDKVRDGSRRVTFDLPDDSEGEDVEDILGGKAKDVPKPESKSSFEKRQEKMVKQIEELENAALSEKPWQLSGEVTAQTRPENSMLEEDIAFDQASRMAPAITEETTLQLEDIIKQRIKDQVWDDVVRKEKPKEEVFEYKKRLTLDHEKSKLSLAEVYEQEYIKQTQEKKEEEENPAHVEIQKLMDSLFLKLDALSNFHFTPKPHVPEVKVVSNLPTITMEEVAPVNVSDATLLAPEEIKEKNKAGDILGDTEKTTTDKKRERRKKKKLKRLKIHEREKRQKLKEAARGGADDGKKKKSKAEVEQTIKKLTKGGKAKVLTNDGMDKALRSSQAFFSQLQDQVRSQVKGSKDQTGKKKKKQKEISVNKLKL
Protein: Actin-1 (EC 3.6.4.-) (Actin I) (PbACT I) (Q4Z1L3)
Organism: Plasmodium berghei (strain Anka)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into shorter and less stable actin filaments compared to ACT2/actin-2; this is thought to facilitate gliding motility and host cell invasion. Has ATPase activity. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi (By similarity). ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin (By similarity). Plays an essential role during the asexual blood stage (By similarity). At the segmented schizont stage, required for apicoplast migration and segregation into individual daughter merozoites (By similarity). Also, required for the separation of daughter merozoites in the final stages of cytokinesis (By similarity). Essential for merozoite invasion of, but not adhesion to or reorientation towards, host erythrocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21790945}. Nucleus {ECO:0000269|PubMed:21790945}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8I4X0}. Note=During host erythrocyte invasion, filamentous actin localizes close to the junction between merozoites and the host cell (By similarity). In schizonts, filamentous actin appears to connect apicoplasts (By similarity). Prior to gametocyte activation in the mosquito midgut, localizes to both the cytoplasm and the nucleus (PubMed:21790945). Following gametocyte activation, relocalizes completely to the cytoplasm, in an ACT2-dependent manner (PubMed:21790945). {ECO:0000250|UniProtKB:Q8I4X0, ECO:0000269|PubMed:21790945}.
Interaction partners:
Sequence:
MGDEEVQALVIDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQTKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERMTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLDLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKSYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVLSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITKEEYDESGPSIVHRKCF
Protein: Lymphocyte cytosolic protein 1 (Q5XI38)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKVFHGLKSTEVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMVNLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPRGDEEGIPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPGVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNRPPYPKLGGNMKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNILEDIGGGQKVNDDIIVNWVNTTLKEAQKSSSITSFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV
Protein: Protein kinase (Q9H4D1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGDGGTPWALALLRTFDAGEFTGWEKVGSGGFGQVYKVRHVHWKTWLAIKCSPSLHVDDRERMELLEEAKKMEMAKFRYILPVYGICREPVGLVMEYMETGSLEKLLASEPLPWDLRFRIIHETAVGMNFLHCMAPPLLHLDLKPANILLDAHYHVKISDFGLAKCNGLSHSHDLSMDGLFGTIAYLPPERIREKSRLFDTKHDVYSFAIVIWGVLTQKKPFADEKNILHIMVKVVKGHRPELPPVCRARPRACSHLIRLMQRCWQGDPRVRPTFQEITSETEDLCEKPDDEVKETAHDLDVKSPPEPRSEVVPARLKRASAPTFDNDYSLSELLSQLDSGVSQAVEGPEELSRSSSESKLPSSGSGKRLSGVSSVDSAFSSRGSLSLSFEREPSTSDLGTTDVQKKKLVDAIVSGDTSKLMKILQPQDVDLALDSGASLLHLAVEAGQEECAKWLLLNNANPNLSNRRGSTPLHMAVERRVRGVVELLLARKISVNAKDEDQWTALHFAAQNGDESSTRLLLEKNASVNEVDFEGRTPMHVACQHGQENIVRILLRRGVDVSLQGKDAWLPLHYAAWQGHLPIVKLLAKQPGVSVNAQTLDGRTPLHLAAQRGHYRVARILIDLCSDVNVCSLLAQTPLHVAAETGHTSTARLLLHRGAGKKAVTSDGYTALHLAARNGHLATVKLLVEEKADVLARGPLNQTALHLAAAHGHSEVVEELVSADVIDLFDEQGLSALHLAAQGRHAQTVETLLRHGAHINLQSLKFQGGHGPAATLLRRSKT
Protein: Oxaloacetate tautomerase FAHD1, mitochondrial (EC 5.3.2.2) (Acylpyruvase FAHD1) (EC 3.7.1.5) (Acylpyruvate hydrolase) (ApH) (Fumarylacetoacetate hydrolase domain-containing protein 1) (Oxaloacetate decarboxylase) (OAA decarboxylase) (ODx) (EC 4.1.1.112) (Q8R0F8)
Organism: Mus musculus (Mouse)
Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro (By similarity). Also has oxaloacetate decarboxylase activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q6P587}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6P587}.
Interaction partners:
- Fumarylacetoacetase
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Homogentisate 1,2-dioxygenase
Sequence:
MASTKPLSRFWEWGKNIVCVGRNYADHVKEMRSTVLSEPVLFLKPSTAYAPEGSPVLMPAYCRNLHHEVELGVLLGKRGEAIPEAAAMDYVAGYALCLDMTARDVQEECKKKGLPWTLAKSFTSSCPVSAFVPKEKIPDPHALRLWLKVNGELRQEGKTSSMIFSIPYIISYVSKIITLEEGDLILTGTPKGVGPIKENDEIEAGIDGVVSMRFKVKRSEY
Protein: Putative F-box protein At1g23770 (Q9ZUB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDTGFADSNNDSSPGEGSKRGNSGIEGPVPMDVELAAAKSKRLSEPFFLKNVLLEKSGDTSDLTALALSVHAVMLESGFVLLDHGSDKFSFSKKLLSVSLRYTLPELITRKDTNTVESVTVRFQNIGPRLVVYGTLGGSCKRVHMTSLDKSRFLPVIDLVVDTLKFEKQGSSSYYREVFMLWRMVKDELVIPLLIGLCDKAGLESPPCLMLLPTELKLKILELLPGVSIGYMACVCTEMRYLASDNDLWEHKCLEEGKGCLWKLYTGDVDWKRKFASFWRRKRLDLLARRNPPIKKSNPRFPTLFPDRRDRREPFDRFGPSDFYRFGLRDPRDRFGPRDPRDPHFYGFRY
Protein: PA2389 (Pyoverdine biosynthesis protein PvdR) (Q5DIV1)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MRRTRSTRRALLVAVCLSPLIALAAWQAYPFRSNNFDTVSVSRGSIESSVSALGTLQPRRYVDVGAQASGQIRKLHVEAGDDVTEGQLLVEIDPSTQQAKVDAGRYSIEMLKAQLAEQRAQYTLARQQYQRQQRLAAGGATRTEDVQSAQAQMLATQARIEMYQAQIRQAQASLRSDEAELGYTRIYAPMSGTVVAVDAREGQTLNAQQQTPLILRIAKLSPMTVWAQVSEADIGRVKPGMPAYFTTLSGEGRRWTGKVRQILPVPPKPLDQSNQGGGSPTSGSGGQSGSGRVVLYTVLVDVDNGDHQLMAEMTAQVFFVAATAENILTAPVAAIHDDGKGGQVAWVVGSNGKPQSRQIRTGISDRLRVQVLAGLEEGDRLLMAAPDGSDS
Protein: Double PHD fingers 2 (J3KMZ8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVVENVVKLLGEQYYKDAMEQCHNYNARLCAERSVRLPFLDSQTGVAQSNCYIWMEKRHRGPGLASGQLYSYPARRWRKKRRAHPPEDPRLSFPSIKPDTDQTLKKEGLISQDGSSLEALLRTDPLEKRGAPDPRVDDDSLGEFPVTNSRARKRILEPDDFLDDLDDEDYEEDTPKRRGKGKSKGKGVGSARKKLDASILEDRDKPYACDNSFKQKHTSKAPQRVCGKRYKNRPGLSYHYAHSHLAEEEGEDKEDSQPPTPVSQRSEEQKSKKGPDGLALPNNYCDFCLGDSKINKKTGQPEELVSCSDCGRSGHPSCLQFTPVMMAAVKTYRWQCIECKCCNICGTSENDDQLLFCDDCDRGYHMYCLTPSMSEPPEGSWSCHLCLDLLKEKASIYQNQNSS
Protein: Guanine nucleotide-binding protein subunit beta-1 (P17343)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. In the early embryo, controls the magnitude of the forces acting on centrosomes but is not required for generating asymmetric forces.
Interaction partners:
- G protein gamma domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit alpha
- Phosducin thioredoxin-like domain-containing protein
- Latrophilin-like protein 1
- Guanine nucleotide-binding protein alpha-16 subunit
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein alpha-12 subunit
- Guanine nucleotide-binding protein alpha-11 subunit
Sequence:
MSELDQLRQEAEQLKSQIREARKSANDTTLATVASNLEPIGRIQMRTRRTLRGHLAKIYAMHWASDSRNLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGSFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIVTSSGDMTCALWDIETGQQCTAFTGHTGDVMSLSLSPDFRTFISGACDASAKLWDIRDGMCKQTFPGHESDINAVAFFPSGNAFATGSDDATCRLFDIRADQELAMYSHDNIICGITSVAFSKSGRLLFAGYDDFNCNVWDSMRQERAGVLAGHDNRVSCLGVTEDGMAVCTGSWDSFLKIWN
Protein: AT31631p (Q86NU9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MFVRLWVRSFHKYDLLIAIGLITLIVYLCLPFRFASHYDYSEIIAENRFVYHLAHYHDAVQRGAEIRPGGEFRPEGCQARYSTAIIVPYRQREEQLHAFLTYMHNYLPQQLIHYRIFLVEQFDHKPFNRAMLFNIGAQVAAEYGFPCLILHDVDLLPLNSGQIYACSERPRHMSSALDHWRFRLPYRGLFGGVVAINTAQYQQINGMSNLYYGWGGEDDDLYERLQALNIDICRFAMEFSKYTMLKHKQEQPNANRVALLRSATLRQHSDGLNSLVYTEMERRMHSLFTHILVDT
Protein: Multidrug resistance protein Mmr (P9WGF1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Multidrug efflux pump. Confers resistance to tetraphenylphosphonium (TPP), erythromycin, ethidium bromide, acriflavine, safranin O, pyronin Y and methyl viologen.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11574548}; Multi-pass membrane protein {ECO:0000269|PubMed:11574548}.
Interaction partners:
- Probable transcriptional regulatory protein
- Drug efflux pump JefA
- Multidrug efflux pump Tap
Sequence:
MIYLYLLCAIFAEVVATSLLKSTEGFTRLWPTVGCLVGYGIAFALLALSISHGMQTDVAYALWSAIGTAAIVLVAVLFLGSPISVMKVVGVGLIVVGVVTLNLAGAH
Protein: NAD-specific glutamate dehydrogenase (EC 1.4.1.2) (O99877)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MMRRASYCAGHAFTSLTVVGSRRFFQGERCEAEIVKLTKERGMFSDASVEASVHQLMSRLSDSPYVRHYTDAEVSAHAHGFLCAKARSALGEPFEHFHESDDSAFYICRKDQASQLRAVRQLTKFVSRERETKQSVSVRCYTAGDSDIAVFTAKIRPFVNPNPEKGETDIGQLASSAFLEERSPEMQERYQDLINRFHESVVPVHTVREVDGEVCFSMIMAADRSYYIATLQTVIQEIPGAVVTRCFSETFSNDTHVYTYFVRGATSQQLSDRASLVPFLPTRPRSLITRLHEDMVFDTEQTVYTDAAVIRLLLTPQPTSEDYRHLRSLVSKEPNGLSRLNNLRTTLSLEMMSERYILTLISTYPEFMKEIYEDFQVGTTHERRCAIREKITTRFREDQRSEHDLGIFNAFLQFNEVVLKHNFFKQHKVALCFRLDPSFLRSLGYPRVPHGVFLLAGAQWRGFHVRFTDIARGAVRMIFSKDTMYRRNKRSVFQENYNLALTQLLKNKDIPEGGSKGTILVSSRYLNTFNQPLCERIFLQYADALLDVVIPGEEGIVDRLKTPEIIFLGPDEHTAGTFPSVGSLFSKKRGYSAWKSFTTGKDASLGGIPTTILIAMTTRSVRTMVRGVYEKLGLDEASQTKFLTGGPDGDLGSNEILLSKEKTLAVLDISASLFDPEGLNKEELKRLATARKQLRDFDKSKLSSKGFLVLTGDKNVTLPDGTHVSDGVSFRDEFHLTKYSAADVFVPCGGRPRSVTLANVGRFLNLSAADNDSLLAGGSIQLKTPKYKIIVEGANLFISQDARLAIERCGIVLIKDASANKGGVTSSSLEVYAGVALSDEEHAQHMCVKDPNNVPEFYKKYVLDIIERIESNARREFEAIWREQQVQEGMPKTLIADSLSEKNVRVRASILSSDMCENKELVRYVLSNYTPKTLLEVVPLETLMERVPLEYQKAICAMWLASEYVYTTGISGNEFDFFTFMTKHMEQAKHIS
Protein: RE18374p (Q8SY08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHSASLVHDDVIDQSDFRRGKPSVNALWNHKKVTMAGDYILSIASIMIARLRSDDVTIVLSQILTDLVQGEFMQLGSRETENERFAHYLTKTYRKTASLIANALKATAVIAQADDNVAEVAFQYGRNIGLAFQLVDDMLDFVSSTEQMGKPTAADLKLGLATAPVLFACEKYPELNPMVMRRFSEPGDVERAFELVHKSHGLEQTRFLAKKHCNEAIRLAQELTESPYQKGLQVVADLVINRMK
Protein: Transcription factor E2F1 (E2F-1) (O09139)
Organism: Rattus norvegicus (Rat)
Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. Directly activates transcription of PEG10. Positively regulates transcription of RRP1B.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q01094}.
Interaction partners:
- Retinoblastoma-associated protein
- Cyclin-A2
- Cyclin-A1
- Transcription factor
- Cyclin-dependent kinase 2
- Transcription factor
- Forkhead box O3
- Retinoblastoma-like protein 2
- Retinoblastoma-like protein 1
- E2F transcription factor 3
Sequence:
MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQVPTGPAAPPAGPRDPDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSRTMVGIGQRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDIQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSAETFQISLKSKQGPIDVFLCPEESAEGISPGRTSYQETSGEDRNADSGTAGPPPSPPSTSPTLDPSQSLLGLEQEAVLPRIGNLRAPMEEDRLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEAVDYHFGLEEGEGIRDLFDCDFGDLTPLDF
Protein: AT5g12010/F14F18_180 (Nuclease) (Q9LYH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein BYPASS1-LIKE
- Protein ROH1D
- At5g38000
- At4g27652
- Fantom protein
- Zinc finger protein CONSTANS-LIKE 8
Sequence:
MKAAVFRNEDGDEEEEEEEEEEVCNVFDGGEVESKRNNETKNLKGFFTSLLLMEEHEKQDQEARNAASRREMSDFQSNYRKRARTMSDYYSDLNDYYADAEESGDINLKKSRVSRAVASVAVAAASEIEAESSEITGSGSVRGTGSGQQRRLWVKDRSRAWWEECSRLDYPEEDFKKAFRMSKSTFELICDELNSAVAKEDTALRNAIPVRQRVAVCIWRLATGEPLRLVSKKFGLGISTCHKLVLEVCKAIKDVLMPKYLQWPDDESLRNIRERFESVSGIPNVVGSMYTTHIPIIAPKISVASYFNKRHTERNQKTSYSITIQAVVNPKGVFTDLCIGWPGSMPDDKVLEKSLLYQRANNGGLLKGMWVAGGPGHPLLDWVLVPYTQQNLTWTQHAFNEKMSEVQGVAKEAFGRLKGRWACLQKRTEVKLQDLPTVLGACCVLHNICEMREEKMEPELMVEVIDDEVLPENVLRSVNAMKARDTISHNLLHHGLAGTSFL
Protein: Mannan-binding lectin serine protease 2 (EC 3.4.21.104) (MBL-associated serine protease 2) (Mannose-binding protein-associated serine protease 2) (MASP-2) [Cleaved into: Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain] (O00187)
Organism: Homo sapiens (Human)
Function: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
Subcellular location: Secreted.
Interaction partners:
- Plasma protease C1 inhibitor
- Ficolin-2
- Mannose-binding protein C
- Complement C4-A
- Complement C4-B
- Ficolin-3
- Ficolin-1
- MBL associated serine protease 1
- Collectin-11
- Collectin-10
Sequence:
MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF
Protein: T19E23.2 (Q9SHF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQRRFDTSQNLGFFKKFINSNSPPSLFLDPLKISPPPMKRRRRNSKLKFEETSDQSPTSTAEFSFSLTKIAVSQICQSIGYKATDASALNTLTLTTTKFLQSLAELASSFSNTANRTEVNLFDIVNGLQDIALSTSDCFPGGSTVHDIESQCLIKSAVLRNLSDFVTYAPEIPFAKPLPRRERDGSFGGDLDHVAVTRSVDVTSVPAWLPPFPDSSLCSDRCSKDNRSDHLWENSDSVIRREILPESLKSKSGGRLPVMRDKVRFKMEQRDWSSGGDTRLERSRDNNNGESGRDLEVKKKIREGYTYCAGEWPF
Protein: FYVE-type domain-containing protein (Q9N3Y4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MIGATGSGGTGGHNDVVRQGFICPFCMEDFGEYERLICHVENDHPEEDSSDLAGMFVSNVKGFFDKAKRGIQKLDAKKSIADLASNVETEFTETTEKLVERAPLPRIPKPLPPDEILPGTRRSKTREFLSTRELNINEVAVRTNMLIIRLDRLINGGPKDKDPVKRKEFEREVVPWLDDAEAVCCPLCASRFGLTRRRHHCRLCGRVLCHSCSKFLSFDTAKTLTSSSNPLGDTHIIVEEPNTVENEQELLQPEENGRRSFFSLSQKSMDKMKRAMAGAVQKVHSAATGEEIIAGALNEQDLSEHMRVCNLCLRDLHFRESQMDKKEPPEFVQQYDLMKVMIEEVKNLVPTYVRVVTSLKNGESVYSHKHGEELRSKCLEIQKSIDYVSKKIAEGANDKPNSAKEQQLRKNIRLYAVQALQGLIGQMESLPTAEECSNLIIKRKERRAKDFARVNRTVMKMSSSMPQLQEQHSHLNSTSSVSSFGGPSSIDDGWSAEDNDLVFEPSSIEDDTIQTDHPLYEQREQLRKFLFQASATGKLDEMDILERNLKEIEEEMMRLGLSC
Protein: Orf16 (Type III secretion system LEE needle length regulator EscP) (O52142)
Organism: Escherichia coli
Interaction partners:
Sequence:
MTRVSLKRNLIEPVSFRPSDDWPQGEESFNDIFYHIKKRSPDTLFIRMASLWKRLFYSSGRRRRYFEEGEHSFSILCGRLRGVVLTIKCSNGIIYLSIKISQNNRNHVFLYHKKDYVFDKLKEIFPDEAIEFTIEYEN
Protein: Ankyrin repeat and SOCS box protein 15 (ASB-15) (Q8VHS6)
Organism: Mus musculus (Mouse)
Function: May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Ankyrin repeat and SOCS box protein 4
Sequence:
MDINDDSNDDHLASYDIQLCIQESIEASQAIFHPKRLVQLSDQNRKLVEAIRQGRIFELQEYVQYKYALEEADEKGWFPLHEAVVQPIQQILETVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVKTLLDKGVWPNTKNDKGETPLLIAIKRGSYDMVSALIKYNTSLDQPCVKRWSAMHEAAKQGRKDIITLLLNHRGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVFALADDGASVLFEAAGGGNPDCISLLLKYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKHAIQKSGLTPIHSAAEGQNAQCLELLIENGFDVNALLADHISQSYDDERKTALYFAVSNNDIHCTEVLLAAGADPNLDPLNCLLVAVRANRHEIVRLLLSYGANVNCYFMHVNDTRFPSAIQYALNDEIMLRLLLNNGYQVELCFDCMHGNIFGNSFVWSETEEEGLPGWTSCIIKDNPFCEFITVPWMKHLVGGIVRILIDYMDYVPLCAKLKSVLEVQREWPEIRQIIENPCSLKHLCRLKIRRVMGLQRLCQPASIQMLPLPAAMRRYLLFKEFDLYGQ
Protein: Zinc-finger homeodomain protein 12 (AtZHD12) (Homeobox protein 26) (AtHB-26) (Q9FKJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pathogenesis-related homeodomain protein
Sequence:
MSSLSKPNRQFLSPTTNNQDTGREQTIACARDMVVLYNECLKNHAVSLGGHALDGCGEFTPKSTTILTDPPSLRCDACGCHRNFHRRSPSDGFSQHRSPPSPLQLQPLAPVPNLLLSLSSGFFGPSDQEVKNKFTVERDVRKTAMIKKHKRTKFTAEQKVKMRGFAERAGWKINGWDEKWVREFCSEVGIERKVLKVWIHNNKYFNNGRSRDTTSSMSLNLKL