wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor E2-alpha (Transcription factor 3) (A4IIL6)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNQQQRMTAVGTDKELSDLLDFSMMFPLPVANGKTRPTTLASTQFGGSGLEERTGSGPWGTEDHNGSNFDQGRGYGDGSHYGEHRELPSHEGNLSAPFLASGLVGKNERPPYSTFGRDSGMAMNQTGFLPGDLAMNSPSALSPNAGKAGSQYYTYPNNSRRRPGDSNLDAQPKKVRKVPPGLPSSVYPANSGDEYCGDRGSYANPKAPNSVYPGAFYMTDGLHSSSDIWASSGGIGQGGYSSVLNSSQSSVSQTTGFSSLHPHERMGFPMHSGEVNPSVTSSFSTTPAQYGVSSHTPPISSGDTMIGNRGTATGSSGDALGKALASIYSPDHSSTNFSSTPSTPVGSPQGITGSGQWPRASGPGALSPSYDGTLHTLQNKMEDRLDEAIHVLRSHAVGQTGSLPGGHEDIHSLLSATASVLGSGFPAAVLSLANRHSMLNSHTEEALPSASNMLHSQVTVPAQPGSLPDLTRPQDSYSGLPGLGRAVPPGRAPEIKRESKEDEENRSVGDLSDDEKKESKTQRSRTRCSINSGGSSKEESNSVEEKDSRDRDRRMSNNARERVRVRDINEAFKELGRMVQMHMKADKAQTKLIILQQAVQVIMTLEQQVRERNLNPKAACLKRREEEKVSGVDPQMGLSGGHPGVGDSHNPVGHM
Protein: EH domain-containing protein 1 (Q5E9R3)
Organism: Bos taurus (Bovine)
Function: ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth. Plays a role in myoblast fusion. Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing. Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis. Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis.
Subcellular location: Recycling endosome membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially associates with tubular recycling endosomes (By similarity). Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes (By similarity). Localizes to the ciliary pocket from where the cilium protrudes (By similarity). Colocalizes with BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta proteins in hippocampal mossy fiber terminals (By similarity). {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4}.
Interaction partners:
- Rabenosyn, RAB effector.
- Rab11 family-interacting protein 2
- Rab11 family-interacting protein 1
- Rab11 family-interacting protein 5
- EH domain binding protein 1.
- ADP ribosylation factor 6
- Vacuolar protein sorting-associated protein 45
- Ras-related protein Rab-35
Sequence:
MFSWVSKDARRKKEPELFQTVSEGLRQLYAQKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCAQLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNKADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISPGDFPNLRKMQELLQTQDFSKFQALKPKLLDTVDDMLANDIARLMVMVRQEESLMPAQVVKGGAFDGTMNGPFGHGYGEGAGEGIDDVEWVVGKDKPTYDEIFYTLSPVNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDRDGLLDDEEFALANHLIKVKLEGHELPADLPPHLVPPSKRRHE
Protein: Keratin, type II cytoskeletal 7 (Cytokeratin-7) (CK-7) (Keratin-7) (K7) (Type-II keratin Kb7) (Q9DCV7)
Organism: Mus musculus (Mouse)
Function: Blocks interferon-dependent interphase and stimulates DNA synthesis in cells.
Interaction partners:
- Keratin, type II cytoskeletal 8
- Keratin, type I cytoskeletal 19
- Epithelial cell adhesion molecule
- Napsin-A
Sequence:
MSIHFSSRSTAYPGRGAQVRLSSGRASFGSRSLYGLGSSRPRVAVRSAYGGPVGAGIREITINQSLLAPLSVDIDPTIQQVRQEEREQIKTLNNKFASFIDKVRFLEQQNKMLETKWALLQEQKSAKSSQLPRIFEAQIAGLRQQLETLQLDGGRLEVELRNMQDVVEDFKNKYEEEINRRTAAENEFVLLKKDVDAAYTNKVELEAKADSLQDEINFLKTLHETELAELQSQISDTSVVLSMDNSRSLDLDGIIADVKAQYEEMANHSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEIAEMNRSIQRLQAEIDTLKNQRAKLESSIAEAEEQGELAIKDAHAKQGELEAALQKAKQDVARQLREYQELLNTKLALDIEIATYRKLLEGEESRLSGDGMGPVNISVVNSTGGNGGKLIFGGTMGSNALSFSGGPGALRAYSIKTTSTTRRGTHN
Protein: Polyprenol dehydrogenase (EC 1.3.-.-) (DHRSXY) (Dehydrogenase/reductase SDR family member on chromosome X) (Dolichal reductase) (EC 1.3.-.-) (Q8N5I4)
Organism: Homo sapiens (Human)
Function: Involved in the positive regulation of starvation-induced autophagy.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:38821050}. Secreted {ECO:0000269|PubMed:25076851}. Note=Secreted in a non-classical form; a signal peptide sequence at position 1-31 is predicted. {ECO:0000305|PubMed:25076851}.
Interaction partners:
- E3 SUMO-protein ligase ZBED1
- Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein
- PI-PLC X domain-containing protein 1
Sequence:
MSPLSAARAALRVYAVGAAVILAQLLRRCRGGFLEPVFPPRPDRVAIVTGGTDGIGYSTAKHLARLGMHVIIAGNNDSKAKQVVSKIKEETLNDKVEFLYCDLASMTSIRQFVQKFKMKKIPLHVLINNAGVMMVPQRKTRDGFEEHFGLNYLGHFLLTNLLLDTLKESGSPGHSARVVTVSSATHYVAELNMDDLQSSACYSPHAAYAQSKLALVLFTYHLQRLLAAEGSHVTANVVDPGVVNTDVYKHVFWATRLAKKLLGWLLFKTPDEGAWTSIYAAVTPELEGVGGHYLYNEKETKSLHVTYNQKLQQQLWSKSCEMTGVLDVTL
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] (EC 1.1.1.8) (Q59XU9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Dihydroxyacetone kinase
- Lysophosphatidic acid acyltransferase
- Dpp1p
- Phosphatidate phosphatase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
Sequence:
MYTTANNRLTQLTQILSPIVNDADSSFAQYLLQNPTFAPNPESSLNPEKPFKIAVVGSGNWGTTIAKIVAENALARPHLFSHYVNMWVFEEKINGENLTQIINQRHENIKYLPGVKLPNNLIAQPDIVTAVKGADLIIFNLPHQFLPKILKQLKGNVPKTTRAISCLKGLEVSKDGCKLLSTYITEELGIVCGALSGANLAPEIARGKWSETTVAYKLPNDYRGAGKDIDKLVLKACFHRPYFHVNVIEDVAGVSVAGALKNIVALAVGFVEGLGWGDNAKAAIMRVGLLETIKFSETFFPQSQADTFTAESAGVADLITTCAGGRNVKVGRYMAETGVSAEEAEKKLLNGQSSQGIVTAKEVHELLTYVNKLEEFPLFEATYQIAFGSESIENLPNLLNTTA
Protein: LP12095p (Phosphatidylethanolamine-binding protein 1) (Q9VD01)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Jonah 25Biii
- Jonah 25Bi
- Peptidoglycan-recognition protein SC2
- Venom allergen-1
- Acyl-CoA binding protein 3, isoform A
- Acyl-CoA binding protein 5
- Jonah 25Bii, isoform A
- trypsin
- RE65433p
- Uncharacterized protein, isoform A
Sequence:
MDTAGIIPDIIDVKPASKATITYPSGVQVELGKELTPTQVKDQPTVVFDAEPNSLYTILLVDPDAPSREDPKFRELLHWLVINIPGNKVSEGQTIAEYIGAGPREGTGLHRYVFLVFKQNDKITTEKFVSKTSRTGRINVKARDYIQKYSFGGPVAGNFFQAQYDDYVKTLIETVQ
Protein: CUB_2 domain-containing protein (Q9XUF6)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- VWFA domain-containing protein
- Uncharacterized protein
- Serpentine Receptor, class R
- Fatty Acid/Retinol binding protein
- C-type LECtin
- C-type lectin domain-containing protein
Sequence:
MFHLIRSFLVLFIVFKFSIAQECSSQAVSFDATNTSFNILSDPNDLASKNCKYTFTVPKYFVPSISFIGIHLNGVNKITTTQYSDFGGSKSFDISEDLLLNLAPVNFTIELNLPQKTAGVTFQITITVKDSTPAVTGQTFTVAQDVGTLLDWGSIQGNSSVIQTFDNQNPQANSYSINLALFTEGVLVYNLLSNFFIYDGGVYKGHLLDVLVAQNMFQSCTGSQFAIVNSNYGSIGIFTISISQVKDWSASQIIIVPSVYVNNTSTYTATNGLTVFYDIANPLLNTVGTTYRNISFRGDGEVTIYAGCVTGEEEDKKIATISPSNSVNYEDILIYGTCKTYVLTRGVLQWSTVQYQTGNYRHRIGRKGVIMSNTYPYRSTQNVRFANHLIQAPKDDFKENIIVTYEVVHIGANVKLNIDQDIKANQDVNKTLSSSDTGTTFTSVSTYQQYITYSIPSGSEGFLVRYTVTSSGNISTFFGAIFLCCAFLLSL
Protein: Photosystem II reaction center protein J (PSII-J) (P0C414)
Organism: Oryza sativa (Rice)
Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01305}.
Interaction partners:
Sequence:
MADTTGRIPLWLIGTVTGIAVIGLIGVFFYGSYSGLGSSL
Protein: Importin N-terminal domain-containing protein (Q388L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMDQMNIGVLSQLAEEMLKAPDKTVRDRAATRLRTMSCYDNYEALKLLLPQATSNYLRFIIGKALRYIVSNELGPQERRDMQSYVLSYLNRIREQEEALPSYVRNELYAIYAAAFYINWRLTVVTLDAGSKGIGDHIIEELTGHFPTEDVLECALVVINHIAEQESKGTLGYLRTAFVHDILPSFFQLGVGHIAEHGRTALEVCCAVLESIPSSPAEPLITVRLTTHDSVFLEDASGWFPALTVAAQSCGRALLADPTMELGGQCAQLLRVVSAIVCLDPEWFSARNALNDMFLELTGDLLTLYTSTGLTHLLQLSCTLLVNVFDRDEGKVSVYLYNRPQLIEMWAGAAQGLLDRWDDDEEEIRREVMHLFYLFGDRVIPRVVALNGQGCEDPRALPLASTLLRVGQCYFENVVSKAHLQEDSNELRSDVGVMLHNEKTLLPIAEMFFCEQIDLYSLIVERLVTTIEQYEACVELRGSGDKERLGELMLSLAINQDALPCALKETNVFLFITHVCLSRLSVIIAAVAIAMLNDTARNGDKVIDIIGQFAQGLVTATDTLTTAFLEGLSFMDMDSGDVDGASVGNVCEGDFNSDVTDWGVSNSKIHVGVLRSLFFYCGCVYESQHEGYREFYEILASLVRYVYMYHSDKAVLVSDANNLLMKVLGQGVRGCFLSSGKMTSLLTAVKEDRIFLLRTTGGDFPKEERAARSGLFTALTFFVESRHYAGFPTFDLFPRIVANIIEGARQVSNSHILIGDLIAVAEGIHQPEPLYWLLDAVSESHAIFEDLLCADATIVPLLVELCARLCDLAKGLLHDDKACEAHYSLFSFATFALRAGVGSYGITETNSELFLQSPPFSQSNELLVYNMSSIMSSLIDGEWCNLGVVLVYNEEFLSRFYQFLVAVISTPVELIMSHTKRRKTVFNTITAALSSKGYFGAQIRAQLNAGNCWTLLLTYLVRCLGNTFLLEILATVDTVLNHEDDYDGSVPLIEEQTIGDIFHEVAVHVAGCPSMEESESELCFKMLTTCFEWSPSLCSARMGALLDFCSAYHRVRLRHIHTLLRSGRGDVLHSYVQVFGLTSKVQTLSAW
Protein: Defective proboscis extension response 13, isoform B (IP04317p) (A1ZB15)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein epsilon
- Dpr-interacting protein zeta, isoform A
Sequence:
MPASSGLYRIKNGRVLDRLQKPAALIFIIAYIAACGICDHTASASPGGGKTVAATMTTPASEPSVRHINQNLIMSQSKEGEPVPVPQPYAQSAASAGGSSITSFDSTNVIDGQSQPTPTHLQEAVLQTHSHSRIQAKDTAGPYPIPVHRPEPVENHLEANNGIEGGMESLFGTPMYFGTENSTVVTTQIGATAHVPCTVHHIGEGVVSWIRKKDYHLLTVGLTTYSSDERFSATHLKHSEDWTLQIKFVQLRDAGVYECQVSTHPPTSIFLHLSVVEARAEITGPPIRYLTPGSTLRLQCRVVQNTEASEYIFWYHDNRMINYDIDRGINVSTEPDFQSSELTIQRTRREHSGNFTCVASNTQPASVLVHIFKGDNPAAMYHGHVGGSTKTTQSQLHMIMIIIASGYRIFHTSVYMKIV
Protein: Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 28) (Cell division protein kinase 2) (P43063)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles (By similarity). May drive the G1-S transition. Plays a role in mitotic exit. Plays a role in the expression of morphology-related transcription factors, and especially hyphae-specific genes. Binds distinct cyclin subunits as cells progress through the division cycle or flamentous growth. The CDC28-CLB2 complex regulates cytokinesis partly by phosphorylating the actomyosin ring component IQG1. The CDC28-CLN3 complex phosphorylates SLA1 which regulates cortical actin patch dynamics. The CDC28-CCN1 complex phosphorylates CDC11 and SEC2 upon induction of filamentous growth. The CDC28-HGC1 complex also phosphorylates SEC2 and maintains CDC11 phosphorylation throughout hyphal growth. Moreover, the CDC28-HGC1 complex phosphorylates and prevents RGA2 from localizing to hyphal tips, leading to localized CDC42 activation for hyphal extension. CDC28-HGC1 phosphorylation of EFG1 represses cell separation genes during hyphal growth. Additional substrates for CDC28 are RFA2 in G1-phase; MOB2, which is required for the maintenance of polarisome components and for inhibition of cell separation in hyphae; and GIN4 to regulate its association to SEP7 and subsequent septin ring assembly.
Interaction partners:
- Hypha-specific G1 cyclin-related protein 1
- G1/S-specific cyclin CLN3
- G2/mitotic-specific cyclin CLB2
- Cell division control protein
- Pho81p
- Cyclin-dependent kinases regulatory subunit
- Mitosis inhibitor protein kinase SWE1
- M-phase inducer phosphatase
- Serine/threonine-protein kinase MEC1
- Anaphase promoting complex subunit
Sequence:
MVELSDYQRQEKVGEGTYGVVYKALDTKHNNRVVALKKIRLESEDEGVPSTAIREISLLKEMKDDNIVRLYDIIHSDSHKLYLVFEFLDLDLKKYMESIPQGVGLGANMIKRFMNQLIRGIKHCHSHRVLHRDLKPQNLLIDKEGNLKLADFGLARAFGVPLRAYTHEVVTLWYRAPEILLGGKQYSTGVDMWSVGCIFAEMCNRKPLFPGDSEIDEIFRIFRILGTPNEEIWPDVNYLPDFKSSFPQWKKKPLSEAVPSLDANGIDLLDQMLVYDPSRRISAKRALIHPYFNDNDDRDHNNYNEDNIGIDKHQNMQ
Protein: GCN5-related N-acetyltransferase 4, chloroplastic (EC 2.3.1.255) (EC 2.3.1.48) (N-alpha-acetyltransferase 70) (AtNAA70) (Q9ZV08)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:25951519, ECO:0000269|PubMed:32633465}.
Interaction partners:
- GCN5-related N-acetyltransferase 10, chloroplastic
- GCN5-related N-acetyltransferase 7, chloroplastic
- GCN5-related N-acetyltransferase 6, chloroplastic
- GCN5-related N-acetyltransferase 5, chloroplastic
- GCN5-related N-acetyltransferase 8
- GCN5-related N-acetyltransferase 9
- Acyl-CoA N-acyltransferases
- GCN5-related N-acetyltransferase 1, chloroplastic
- N-terminal acetyltransferase A complex catalytic subunit NAA10
- N-terminal acetyltransferase B complex catalytic subunit NAA20
Sequence:
MRSTPLGTTAVSPASIKHNSYGYGRFVSSSGVSNFSIHRRRRHSSFSISQAPSQINSGACNASQIVDLFPAVSPEIVVREARLEDCWEVAETHCSSFFPGYSFPLDVVLRVDRLMAMVMGFSIPPGCQRTCLVAVIGSSVDETICFGSDDFKIGAFDAKISLNKGYVAGILTVDTVADYLPRKGPLRQRRTGIAYVSNVAVRENFRRKGIAKRLIWKAEALAKNWGCRAIGLHCDLNNLGATKLYKDQGFRSIKIPEGATWPQPKTSPDTRFTFMMKLVNNNNTQALEQFR
Protein: Cytochrome P450 302a1, mitochondrial (EC 1.14.15.44) (Protein disembodied) (Q9NGX9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for CNS development; negatively regulates glial cell division in the embryonic midline. Involved in the metabolism of insect hormones; responsible for ecdysteroid C22-hydroxylase activity. May be involved in the breakdown of synthetic insecticides.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14610274}.
Interaction partners:
- Cytochrome P450 306a1
- Spookier
- Cytochrome P450 315a1, mitochondrial
- Cholesterol 7-desaturase nvd
- Short-chain dehydrogenase/reductase)
- Prothoracicotropic hormone, isoform F
- Glutathione S-transferase E14
- Cytochrome P450 307a1
- Ecdysone receptor
Sequence:
MLTKLLKISCTSRQCTFAKPYQAIPGPRGPFGMGNLYNYLPGIGSYSWLRLHQAGQDKYEKYGAIVRETIVPGQDIVWLYDPKDIALLLNERDCPQRRSHLALAQYRKSRPDVYKTTGLLPTNGPEWWRIRAQVQKELSAPKSVRNFVRQVDGVTKEFIRFLQESRNGGAIDMLPKLTRLNLELTCLLTFGARLQSFTAQEQDPRSRSTRLMDAAETTNSCILPTDQGLQLWRFLETPSFRKLSQAQSYMESVALELVEENVRNGSVGSSLISAYVKNPELDRSDVVGTAADLLLAGIDTTSYASAFLLYHIARNPEVQQKLHEEARRVLPSAKDELSMDALRTDITYTRAVLKESLRLNPIAVGVGRILNQDAIFSGYFVPKGTTVVTQNMVACRLEQHFQDPLRFQPDRWLQHRSALNPYLVLPFGHGMRACIARRLAEQNMHILLLRLLREYELIWSGSDDEMGVKTLLINKPDAPVLIDLRLRRE
Protein: Suppressor of activated egl-4 protein 2 (Q03615)
Organism: Caenorhabditis elegans
Function: As a likely component of a histone deacetylase complex, together with saeg-1 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and foraging.
Subcellular location: Nucleus {ECO:0000269|PubMed:21573134}.
Interaction partners:
- Suppressor of activated egl-4 protein 1
- Putative histone deacetylase 2
- UPF0375 protein Y45F10C.2
- Prion-like-
- Transposase
Sequence:
MRIVILDELLSREMDGSNDGSSARVNSLKHVIKRNKMDMADDAPSSLDLMRRIFQAEISREIHQIMERHTRTTLLPAIENLRKNGHVVDESVLNGLYCNILEAAKKPYQKDPEPMPPICTNGNGFLDINSQEHENNLKRGYESDSSDVSGVSHCSDAKRRRGRPRKDEEAYRLEMTPPTMNEVIRWNPDRIDVNTRFITATKIAQVMGMPPSILFNKYPRMFRYSCDEDDKNILHEQNLLIRAPGRCYLLVAEDARQLVPSTYFQDVLNVSFLISEPLLSKIRQKAASTYEKYKVFLPTQPNNYL
Protein: Catenin alpha-1 (102 kDa cadherin-associated protein) (CAP102) (Alpha E-catenin) (P26231)
Organism: Mus musculus (Mouse)
Function: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation. May play a crucial role in cell differentiation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16325583}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P35221}. Cell membrane {ECO:0000269|PubMed:1924379}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:16325583}. Cell junction {ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:1924379}. Cytoplasm {ECO:0000250|UniProtKB:Q9PVF8}. Nucleus {ECO:0000250|UniProtKB:P35221}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. {ECO:0000269|PubMed:1924379}.
Interaction partners:
- Catenin beta-1
- Cadherin-1
- Catenin delta-1
- Vinculin
- Junction plakoglobin
- Tight junction protein 1
- Actin, cytoplasmic 1
- Afadin
- Alpha-actinin-1
- Cadherin-2
Sequence:
MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVVAVEDVRKQGDLMKSAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGNRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDAAQHQGGSGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
Protein: Catenin beta 1 (A0A2R8Y5A3)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}.
Interaction partners:
Sequence:
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVAGKNIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
Protein: Rhino (Q49BL8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMNQKKGKNIKKTEGKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIQSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPDWKFPEMTKPFGVNRGLDLDKILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK
Protein: Putidaredoxin (PDX) (P00259)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
Interaction partners:
Sequence:
MSKVVYVSHDGTRRELDVADGVSLMQAAVSNGIYDIVGDCGGSASCATCHVYVNEAFTDKVPAANEREIGMLECVTAELKPNSRLCCQIIMTPELDGIVVDVPDRQW
Protein: Kinase-like protein (Protein kinase superfamily protein) (Q9LUI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat
- TOM1-like protein 3
Sequence:
METRNETKASPENNLRNRGADGNNSKKDMIFRADKIDLKNLDIQLEKHLSRVWSRSIEKHPKPKEEWEIELAKLEMRNVIARGAYGIVYKGIYDGQDVAVKVLDWGEDGYATTAETSALRASFRQEVAVWHKLDHPNVTRFVGASMGTANLKIPSSAETENSLPQRACCVVVEYIPGGTLKQYLFRNRRKKLAFKVVVQLALDLSRGLSYLHSERIVHRDVKTENMLLDYQRNLKIADFGVARVEAQNPKDMTGETGTLGYMAPEVLDGKPYNRRCDVYSFGICLWEIYCCDMPYPDLSFADVSSAVVRQNLRPDIPRCCPTALATIMKRCWEANPEKRPEMEEVVSLLEAVDTTKGGGMIPEDQRPGCFCFVSGRGP
Protein: LD24110p (Q8SY43)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIVKMEPDELITFRVQYLVDSDPLSACTAFPIPVRAPTYAFATTMPLANQLGTILRLLNAPQSIDDAAIQVYKDGDYGAYLDLESSLAEQAEEIEGVNVSRKNSLVVRTQLNVRVQAIIEKLLSAQGSDLRRALFSLKQVFQEDKDLVHAFVALGGLNCLVRVGNCADQNYQNYILRALGQVMLYVDGMNGVMKHEPTMQWLYSLIASNYRSVVKTALKLLLVFVEYAESNCYVLVSAIHAVDASQGTLPWSNIMRLLKDYDNADAELVIYATSLINKTLAGLNDQDSFYDESDLLEQQGMETVIQRYMSKPGTDLDLLDQLQLYEAVLKFEDGESDGQRLPQNSMRKTQRYRPGANTTERRKSRRHSTDNSPASLTKVLPTTVLRMTPTQATVDEDSSGSTNSTEFSGGLFNEKKPRDGAGVTPGLRRRRERAERHKSFLKEQQEAAANGIFAALEQREGLGQIVTAIPATIQTGDSPPQSLQHEVPPCNNISGITNISNNNVSNLSCNDTPNNSLLVMSPSKQLLTGSHSISIINNSFDKASNNNQSEFLTKKNLFRERNSTVINGIMKNIQQTDSAYKKYENEANRLNNYYSQSPKHQIHQPIQPTPEVLLSPKKTLNASGFDFTPAPLSSTPVKCDVPPEPEPLSPVKKPAAAPPPPPPPPPPPPPPPGWWHAPIYNSPQARTLTSTNPELLPHPVDPSDMESEDQQLLLQLKRDHTVKDLTQKLSNLPMSPTQDSANRALVGDMSGLISKAKEGLAKSKSKGEISRSSSVDQDVKKSEPKKSENELHWEELVRNMTRPLNLCDLDFTDLRDDDEKDVLAPRSLGAGIPPPPPLLGGAIAPPPMMPPSLAPPPMYGYGGSLTNSVNSLNGSINGELVNGNNTIKKNKKTVKLFWKEVREDMIPQVVGKTIWDELPDANVDTQKLEHLFESRAKDLMTKKQQELNKSKEIIVLDHKRSNAINIAITKLPPPRAIKTAILKMDATVVTREGIDKLLNMLPTDEERGKIQEAQLSNPELPLGSAEQFLLTLASISELEARLKLWAFRLDFDNSEKEIAEPLMDLKQGIEILRQNRTFRSILSTLLSVGIFLNGAPVKGFQIEYLAKVPEVKDTVHKHSLLHHLCHMVMESSSDTSDLYSEIGPITRASKADFTDLAHNLNQLEAECKACWDRLKLIAKHDCPPPLKQKLVDFLADCAERIIILQIVHRRVMNRYRKFLLWLGMPQHSVAESRPNEFCRTLSEFALEYRTTRERVQQQLEKKANHRERNKTRGKLIIDMAKFKTKDDVADDELK
Protein: Cullin 3, isoform C (Cullin 3, isoform D) (Cullin 3, isoform E) (LD10516p) (Q9V475)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLRGNPPKKEGKMRIRAFPASMDEKYVETIWASLKNAIQEIQKKNNSGLSFEQLYRNAYNMVLHKHGNRLYYGLREVVSEHLEHKVRADVLEALHSNFLPKLNQAWTDHQTSMVMIRDILMYMDRVYVQQREVDNVYNLGLILFRDQVVRYSEIQKALREKLLGMVMEERHGEAINHLAIKNACSMLITLGINSRTVYEEDFEKPFLAQSAAFYKFESQNFLAENNAGVYIKKVEARITEESSRAALYLDKDTEPRIVRVVEEELIKKHMRPIVEMENSGVVYMIKNSKTEDLACTYKLFSRLKEEGLKVIADTMSAYLREQGRMLVKEEENGNTNPITFVQNLLDLKDRFDQFLVHSFANDRIFKNVISSDFEHFLNLNNKSPEYLSLFIDDKLKKGGKGMSEQEIESILDKTMVLFRFLLEKDVFERYYKTHLAKRLLLNKSVSDDFEKNMISKLKTECGCQFTSKLEGMFKDMSVSNTIMDEFKNFVNNNNLSLGGVELTVRILTTGFWPTQTATPNCNIPAAPREAFDIFKNFYLNKHSGRQLTLQPQMGTAYINAVFYGRKAVESEKDKDAPSSSSSGCGVPTTTRKHILQVSTYQMCVLLLFNNRDVLTYDDIHQETDIPERELVRALQSLSMGKPAQRLLVRNSKTKTKDIEPTDEFYVNDAFNSKFHRVKIQTVAAKGESEPERKETRGKVDEDRKHEIEAAIVRIMKARKRLAHNLLVSDVTSQLKSRFLPSPVFIKKRIEGLIEREYLQRSPEDRKVYNYLA