wanglab/gogpt-training-data huggingface dataset:
Protein: Probable beta-1,4-xylosyltransferase IRX9 (EC 2.4.2.-) (OsGT43C) (Probable glucuronosyltransferase Os07g0694400) (Protein IRREGULAR XYLEM 9 homolog) (OsIRX9) (Q6Z3Y6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable beta-1,4-xylosyltransferase involved in xylan biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASAGGCKKKTGNSRSRSPRSPVVLRRAMLHSSLCFLVGLLAGLAAPSDWPAAAGAAVFLRTLRASNVIFSRSSNRPQQPQLVVVVTTTEQSDDSERRAAGLTRTAHALRLVSPPLLWLVVEEAPAEKHAAPPTARLLRRTGVVHRHLLMKQGDDDFSMQISMRREQQRNVALRHIEDHRIAGVVLFGGLADIYDLRLLHHLRDIRTFGAWPVATVSAYERKVMVQGPLCINTSSSSVITRGWFDMDMDMAAGGERRAAADRPPPETLMEVGGFAFSSWMLWDPHRWDRFPLSDPDASQESVKFVQRVAVEEYNQSTTRGMPDSDCSQIMLWRIQTTL
Protein: (S)-8-oxocitronellyl enol synthase (EC 1.3.1.122) (Iridoid synthase) (ISY) (K7WDL7)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Iridoid synthase that catalyzes the first step in generation of the iridoid ring scaffold using the linear monoterpene (6E)-8-oxogeranial as substrate. Iridoids comprise a large family of distinctive bicyclic monoterpenes that possess a wide range of pharmacological activities, including anticancer, anti-inflammatory, antifungal and antibacterial activities.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23172143}.
Interaction partners:
Sequence:
MSWWWKRSIGAGKNLPNQNKENGVCKSYKSVALVVGVTGIVGSSLAEVLKLPDTPGGPWKVYGVARRPCPVWLAKKPVEYIQCDVSDNQETISKLSPLKDITHIFYVSWIGSEDCQTNATMFKNILNSVIPNASNLQHVCLQTGIKHYFGIFEEGSKVVPHDSPFTEDLPRLNVPNFYHDLEDILYEETGKNNLTWSVHRPALVFGFSPCSMMNIVSTLCVYATICKHENKALVYPGSKNSWNCYADAVDADLVAEHEIWAAVDPKAKNQVLNCNNGDVFKWKHIWKKLAEEFGIEMVGYVEGKEQVSLAELMKDKDQVWDEIVKKNNLVPTKLKEIAAFWFADIAFCSENLISSMNKSKELGFLGFRNSMKSFVSCIDKMRDYRFIP
Protein: Nicalin (Q9M292)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- BOS complex subunit TMEM147
- At4g24330
- Uncharacterized protein At5g49945
- Calcium load-activated calcium channel
- Calcium load-activated calcium channel
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL38z/eL38y
- Carbohydrate-binding-like fold
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein uL4y
Sequence:
MAEEKKSKQRHRVMVFESMYPILALMLILVACVELCDAATVVDVYRLIQYDISGVPFGSRFSSLNHHAASLSFQRGADLSRSVLILPLRELDIAFVQDYISQKQSLGGLLILLPQTFRPGNVGGGSLSSENDGFRSLLGQLEKLLVHGNIPFPVYFAFENEETDAMLADVKKNDALGQQATATTGGYKLVISVSEPRKIASPTITNIQGWLPGLRAEGDSSQLPTIAVVASYDTFGAAPALSVGSDSNGSGVVALLEVARLFSVLYSNPKTRGKYNLLFALTSGGPYNYEGTQKWLKSLDQRMRESIDYAICLNSVGSWDSELLIHVSKPPDNAYIKQIFEGFSNVAEDLGFQVALKHKKINISNSRVAWEHEQFSRLRVTAATLSELSTPPELLENAGSLSDTRQLVNEDAIIKGVKLVAESLAKHIYGHQGKDIKIFADDSSLAVNPFYVRSWLDLLSQTPRVAPFLSKNEPLIMALKKELEDYTAEVSVQHESLDGSFTFYDSTKASLNIYQVASVTFDLLLLLVLGSYLIVLFSFLVITTRGLDDLISLFRRPPSRKVKMG
Protein: U6 snRNA-associated Sm-like protein LSm4 (Q382E1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365049}.
Interaction partners:
- Sm protein B
- Small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm8p
- U6 snRNA-associated Sm-like protein LSm7p
- Uncharacterized protein
- Small nuclear ribonucleoprotein E
- Sm protein G
- PRP1 splicing factor N-terminal domain-containing protein
- Small nuclear ribonucleoprotein SmD1
- U5 small nuclear ribonucleoprotein component, putative
Sequence:
MSVRKPITPLDVLRNCRAKVVSVELAGGETINGTVVRVDRAMNMVLKQCIRTSADGEAFWRSRESLIRGASVRNVRMDERAVIIADAQLREVTSKSKNKNRVKAKSNDKQQGERKATLSGEKRNRGK
Protein: Adenosine 5'-monophosphoramidase HNT1 (EC 3.-.-.-) (Histidine triad nucleotide-binding protein HNT1) (HINT) (Hit family protein 1) (Q04344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Plays a role in the regulation of kinase KIN28 function. Essential for growth on galactose media at elevated temperatures.
Interaction partners:
- Serine/threonine-protein kinase KIN28
- Aprataxin-like protein
- Protein-lysine N-methyltransferase EFM5
Sequence:
MEPLISAPYLTTTKMSAPATLDAACIFCKIIKSEIPSFKLIETKYSYAFLDIQPTAEGHALIIPKYHGAKLHDIPDEFLTDAMPIAKRLAKAMKLDTYNVLQNNGKIAHQEVDHVHFHLIPKRDEKSGLIVGWPAQETDFDKLGKLHKELLAKLEGSD
Protein: Rab proteins geranylgeranyltransferase (Q5ADQ8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Rab family GTPase
- Rab family GTPase
- Ras-related protein SEC4
- Rab family GTPase
- Geranylgeranyl transferase type-2 subunit beta
- Rab family GTPase
- Ypt7p
- Geranylgeranyl transferase type-2 subunit alpha
- Zinc-coordinating transcription factor
Sequence:
MNFARTERRKSMAERRPSTVYTPPVIPHLAGLEKPQDQYLKMDNCDVLIIGTGLQESILAAALSWQGTQVLHIDSNTYYGDSCSTLTIEQLKKWCGDVNSGKIHQFQDAQIYIPGGKQSNQYTSKDYGIDLTPKIMFCQSDLLSLLIKSRVYRYLEFQSLSNFHVFENDDFQQKVNATTKQDIFTDKSLSLMTKRYLMKFLKFLLLDPDYKQRVKPYADTPIQVFLQQEFKLEEPQINELVYSIGLSYKEQTSTKQALIRMKRFLSSFDVYGKFPCMVSKFGGPGELSQGFCRSAAVAGTTYKLNTNLTDFDPISKIAHFNDGSHIKINEKIIISPTQLPKFLQSSYNKVVENLQPYYVTRLVTVVRRDCKEWMSGNESSAIVVFPPHSLPTDNQHSVQVIIQNGNSGVCPDGQAIWFSSTVEQDLSRAKVDLESAFEKMETSLLRESSEEIVNDILGDNNNNNNNDFVMNAQGTTTPVLVNSFKLGSSLINFVPKDKLEIVCKLGYVEKTFINPDLSNIFKPTKTNNIVYKDVEDANNEIIFTNMPSSELSYDGIITDVKSIYQRITGTTDDFFDVDFEDEEDEYDRNNQPVVQPKRSSVVGGIVGGGSITSLTALREQHNENNHSDNAIDSDEDEDEDINDMNDMNDNEEEDDHGRGPEPFGADEMEL
Protein: Peroxisomal acyl-coenzyme A oxidase 2 (EC 1.17.99.3) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCA-CoA oxidase) (THCCox) (P97562)
Organism: Rattus norvegicus (Rat)
Function: Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycoprostanic acids. Capable of oxidizing short as well as long chain 2-methyl branched fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:8947475}.
Interaction partners:
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal acyl-coenzyme A oxidase 3
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Enoyl-CoA delta isomerase 2
- Peroxisomal acyl-coenzyme A oxidase 1
- Bile acid-CoA:amino acid N-acyltransferase
- Peroxisomal bifunctional enzyme
- Alpha-methylacyl-CoA racemase
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Peroxisomal targeting signal 1 receptor
Sequence:
MGSPMHRVSLGDHWSWQVHPDIDSERHSPSFSVERLTNILDGGLPNTVLRRKVESIIQSDPVFNLKKLYFMTREELYEDAIQKRFHLEKLAWSLGWSEDGPERIYANRVLDGNVNLSLHGVAMNAIRSLGSDEQIAKWGQLCKNFQIITTYAQTELGHGTYLQGLETEATYDEARQELVIHSPTMTSTKWWPGDLGWSVTHAVVLAQLTCLGVRHGMHAFIVPIRSLEDHTPLPGITVGDIGPKMGLEHIDNGFLQLNHVRVPRENMLSRFAEVLPDGTYQRLGTPQSNYLGMLVTRVQLLCKGILPSLQKACIIATRYSVIRHQSRLRPSDPEAKILEYQTQQQKLLPQLAVSYAFHFTATSLSEFFHSSYSAILKRDFSLLPELHALSTGMKATFADFCAQGAEICRRACGGHGYSKLSGLPTLVARATASCTYEGENTVLYLQVARFLMKSYLQAQASPGATPQKPLPQSVMYIATQRPARCSAQTAADFRCPDVYTTAWAYVSTRLIRDAAHRTQTLMKSGVDQHDAWNQTTVIHLQAAKAHCYFITVKNFKEAVEKLDKEPEIQRVLQRLCDLYALHGVLTNSGDFLHDGFLSGAQVDMAREAFLDLLPLIRKDAILLTDAFDFSDHCLNSALGCYDGHVYERLFEWAQKYPANTQENPAYKKYIRPLMLGWRHKM
Protein: Bidirectional sugar transporter SWEET6 (AtSWEET6) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 6) (Q9C9M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8L9J7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8L9J7}.
Interaction partners:
- Ankyrin repeat protein
- Actin-related protein 2/3 complex subunit 2B
- Pentatricopeptide repeat-containing protein At3g12770
Sequence:
MVHEQLNLIRKIVGILGNFISLCLFLSPTPTFIHIVKKKSVEKYSPLPYLATLLNCLVRALYGLPMVHPDSTLLVTISGIGITIEIVFLTIFFVFCGRQQHRLVISAVLTVQVVFVATLAVLVLTLEHTTDQRTISVGIVSCVFNAMMYASPLSVMKMVIKTKSLEFMPFLLSVVGFLNAGVWTIYGFVPFDPFLAIPNGIGCVFGLVQLILYGTYYKSTKGIMEERKNRLGYVGEVGLSNAIAQTEPENIPYLNKRVSGV
Protein: Ceramide synthase 2 (CerS2) (LAG1 longevity assurance homolog 2) (SP260) (Sphingosine N-acyltransferase CERS2) (EC 2.3.1.24) (Tumor metastasis-suppressor gene 1 protein) (Very-long-chain ceramide synthase CERS2) (EC 2.3.1.297) (Q96G23)
Organism: Homo sapiens (Human)
Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (By similarity). Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18165233}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acid ceramidase
- 3-ketodihydrosphingosine reductase
- Sphingolipid delta
- Ceramide glucosyltransferase
- Sphingomyelin phosphodiesterase
- Ceramide kinase
- Sphingomyelin phosphodiesterase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Sphingolipid delta
- Alkaline ceramidase 2
Sequence:
MLQTLYDYFWWERLWLPVNLTWADLEDRDGRVYAKASDLYITLPLALLFLIVRYFFELYVATPLAALLNIKEKTRLRAPPNATLEHFYLTSGKQPKQVEVELLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTFYLIAFIAGMAVIVDKPWFYDMKKVWEGYPIQSTIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILISFSWFANYIRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNIFIVFAIVFIITRLVILPFWILHCTLVYPLELYPAFFGYYFFNSMMGVLQLLHIFWAYLILRMAHKFITGKLVEDERSDREETESSEGEEAAAGGGAKSRPLANGHPILNNNHRKND
Protein: Zgc:109927 (tRNA-splicing endonuclease subunit Sen54) (Q504E6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGFSERGKQYLQPEEALYLMECGNVQVFYRDLPLSIQDGYERFLSSDTVTLHQYQVFGHLKRLGYVVNRFDPSSVSSTYERQLNLPASDKQKKQLKRKRSQSPVSSDKHGISTEEKTTSEAHNELAETSKLPADLQEPVHLADAPERTWWMEEDVQQKHPKTQTAAPRWDFSSISFPDLGSRRRSERLASPHRSLLPENVDVGECDVSRWLGRLNMKQEKLSRRDMERQRERDRYRWDVNSDREVRRCRNWAEYSELMGERRRRRRKHRPEHLWEREETPLTQPGQCTSHRELLDQIGIIKSSTFSEGLSRLSPSDQWKISFDVYQPDTVAEFKKSHPGKPYTRMCVCSFAGPVPDLHAVKQLSFQSQDVPVTFAVVDHGDISFYCFKDFKLPTDVY
Protein: Hereditary hemochromatosis protein homolog (P70387)
Organism: Mus musculus (Mouse)
Function: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q30201}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q30201}.
Interaction partners:
- Transferrin receptor protein 2
- Transferrin receptor protein 1
- Beta-2-microglobulin
- Hemojuvelin
- Hepcidin
- Hepcidin-2
- Transmembrane protease serine 6
- Bone morphogenetic protein 6
- Ferroportin
- Serotransferrin
Sequence:
MSLSAGLPVRPLLLLLLLLWSVAPQALPPRSHSLRYLFMGASEPDLGLPLFEARGYVDDQLFVSYNHESRRAEPRAPWILEQTSSQLWLHLSQSLKGWDYMFIVDFWTIMGNYNHSKVTKLGVVSESHILQVVLGCEVHEDNSTSGFWRYGYDGQDHLEFCPKTLNWSAAEPGAWATKVEWDEHKIRAKQNRDYLEKDCPEQLKRLLELGRGVLGQQVPTLVKVTRHWASTGTSLRCQALDFFPQNITMRWLKDNQPLDAKDVNPEKVLPNGDETYQGWLTLAVAPGDETRFTCQVEHPGLDQPLTASWEPLQSQAMIIGIISGVTVCAIFLVGILFLILRKRKASGGTMGGYVLTDCE
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial (Complex I-SGDH) (CI-SGDH) (NADH-ubiquinone oxidoreductase SGDH subunit) (O43674)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase flavoprotein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 1
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 6
Sequence:
MAAMSLLRRVSVTAVAALSGRPLGTRLGFGGFLTRGFPKAAAPVRHSGDHGKRLFVIRPSRFYDRRFLKLLRFYIALTGIPVAIFITLVNVFIGQAELAEIPEGYVPEHWEYYKHPISRWIARNFYDSPEKIYERTMAVLQIEAEKAELRVKELEVRKLMHVRGDGPWYYYETIDKELIDHSPKATPDN
Protein: Fatty acid binding protein 11a (Fatty acid binding protein 4a) (Fatty acid-binding protein H6-isoform) (Q66I80)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Fatty acid binding protein 1-B.1
- Fatty acid binding protein 1-A, liver
- Gastrotropin
- Brain-type fatty acid-binding protein b
- Fatty acid-binding protein 2, intestinal
- Brain-type fatty acid-binding protein
- Fatty acid-binding protein 3, muscle and heart
- Adipocyte fatty acid-binding protein
- Peroxisome proliferator-activated receptor gamma
- Adiponectin, C1Q and collagen domain-containing, b.
Sequence:
MVDKFVGTWKMTTSDNFDEYMKAIGVGFATRQVGNRTKPNLVVCVDEQGLICMKSQSTFKTTEIKFKLNEPFEETTADDRKTTTVMTIENGKLVQKQTWDGKESTIEREVSDGKLIAKCKMGDVVAVRTYVKEA
Protein: G-protein coupled receptor 39 (O43194)
Organism: Homo sapiens (Human)
Function: Zn(2+) acts as an agonist. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone secretion and cell death (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26365466}; Multi-pass membrane protein.
Interaction partners:
- Appetite-regulating hormone
- Ly6/PLAUR domain-containing protein 1
- Promotilin
- Membrane-bound ghrelin O-acyltransferase MBOAT4
Sequence:
MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFRAYMILLPFSETFFYLSSVINPLLYTVSSQQFRRVFVQVLCCRLSLQHANHEKRLRVHAHSTTDSARFVQRPLLFASRRQSSARRTEKIFLSTFQSEAEPQSKSQSLSLESLEPNSGAKPANSAAENGFQEHEV
Protein: Pumilio homolog 4 (APUM-4) (AtPUM4) (Q9SS47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- La-related protein 1A
- Oligouridylate-binding protein 1C
- Pumilio homolog 26
- Eukaryotic translation initiation factor isoform 4G-2
- Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
- Eukaryotic translation initiation factor isoform 4G-1
- Glycine-rich RNA-binding protein RZ1A
- Varicose-related protein
- Ribonuclease TUDOR 2
Sequence:
MVTNSYMDTRSNLTSVNRGSNVDLEDRFQRELESLLQQHRNQQSFGRERERDIDVHRSGSAPPTVEGLLRAMDNQYLNNNNSDHRDVGNISSITTSNGVELLSDDELRWHPEYLSYYYSNEHSNPRLPPPLLSREDWRVAQRFHNSESVFDPVGEWRKKTVEVDNSSSLFSVQPGVPVEQAENDLMELRNAVAQGRSQKVQRLDQGREDLIGLSGYSGLGPRRKSFADILQEGLERDAALGSQLSRPASCNTFRDMKDAAVLSNFSAGGFDSPLAFHDSLHSTAKNSPNTMLGSTMSSPVPRNRTPDSHLVGRSTASGLPPIGTRVGPVEKKNTFGTAIQNCESYTAADVADTLSRLNMSEMSQVKENHMQSQLQVELENQSDVMRYIPNGHKKALRQQNTAETKDHLFSANYGGMSGYGASLGASTVGSHGQVNIPKRTSSSASLYSTSDHSRLGSVGLSDVNIRNGNINGTDFSTAGGYMAKNKLNSLAEHYSAEGSHLTGDGDRQSLNRLINQVASELHSPVMDPHYSQYLHTASSTAAPIDHSLIRNNFGTSNGDTANEYLAMLLAQNRQQLGNLNAANSRFFESPSYDLGNMYLGNHLPSPSKNSRNFQNMRMSQSASMMKVPFGGLQGSSHVDIGSTAEASLLEGFKNNKTRSLELSEIVGHVIEFSMDQYGSRFIQQKLETATDEEKNAIFPEILPYGRTLMTDVFGNYVIQKFFEHGTTKQRKELAEQVTGHVLALSLQMYGCRVIQKALEVVELEQQARMVKELDGSVMKCVHDQNGNHVIQKCIERLPQDWIQFIISSFYGKVLALSTHPYGCRVIQRVLEHIDDIETQRIIMEEIMDSVCTLAQDQYGNYVIQHIIQHGKPHERSEIINKLAGQIVKMSQQKFASNVVEKCLTFGGPEERQVLVNEMLGYTDENEPLQAMMKDPFGNYVVQKVLETCDDQSLALILSRIKVHLNALKRYTYGKHIVARVEKLITTGERRIGLSSSLAANTTP
Protein: Prickle planar cell polarity protein 3 (LIM domain only protein 6) (LMO-6) (Prickle-like protein 3) (Pk3) (Triple LIM domain protein 6) (Q80VL3)
Organism: Mus musculus (Mouse)
Function: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A8WH69}. Cell membrane {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side {ECO:0000250|UniProtKB:A8WH69}. Mitochondrion {ECO:0000269|PubMed:32516135}. Note=Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity). WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}.
Interaction partners:
- Vang-like protein 2
- Segment polarity protein dishevelled homolog DVL-1
- Vang-like protein 1
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Ankyrin repeat domain-containing protein 6
- Cadherin EGF LAG seven-pass G-type receptor 1
- Rho GTPase-activating protein 21
- Inversin
Sequence:
MFARGSRRRRSGRAPPEAEDPARGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVRTVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRATVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHAGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMGHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCSRPLLGRPFLPRRGLIFCSRACSLGSETTAPGPGRRSWSAGTVTTPLTTSTASFSATEGTSETASKGTCTKAEPAAGPEEPSHFLRGAPHRHSMPELGLRSAPEPPTESPGHPAPHPDDNAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRTPSCHHHHHHRRRRQRHRRRGSHHHHHHPGRHGHHRCDLGSGSDSGSCSSSPSSPSSESSEDDGFFLGERIPLPPHLCRPRTTQDTSTETFNSPAQPLVQESHPVMPRQTRDKNCIVA
Protein: Endo-1,4-beta-xylanase A (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase A) (C6CRV0)
Organism: Paenibacillus sp. (strain JDR-2)
Function: Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues, which is predominant in hemicellulose fractions of hardwood and crop residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the predominant products of MeGAXn hydrolysis; these products are then directly assimilated by the bacterium for subsequent metabolism. Thus, allows the bacterium to efficiently use polymeric MeGAXn as a growth substrate.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:16461704}.
Interaction partners:
- Xylan alpha-1,2-glucuronidase
- PFAM: glycoside hydrolase family 8
Sequence:
MSRSLKKFVSILLAAALLIPIGRLAPVAEAAENPTIVYHEDFAIDKGKAIQSGGASLTQVTGKVFDGNNDGSALYVSNRANTWDAADFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYGFLASANFAAGTAFTLTKEFTVDTSVSTQLRVQSSEEGKAVPFYIGDILITANPTTTTNTVYHEDFATDKGKAVQSGGANLAQVADKVFDGNDDGKALYVSNRANTWDAADFKFADIGLQNGKTYTVTVKGYVDQDATVPSGAQAFLQAVDSNNYGFLASANFAARSAFTLTKEFTVDTSVSTQLRVQSSEEGKAVPFYIGDILITETVNSGGGQEDPPRPPALPFNTITFEDQTAGGFTGRAGTETLTVTNESNHTADGSYSLKVEGRTTSWHGPSLRVEKYVDKGYEYKVTAWVKLLSPETSTKLELASQVGDGGSANYPSLASKTITAADGWVQLQGNYRYNSVGGEYLTIYVQSSNATASYYIDDISFESTGSGPVGIQKDLAPLKDVYKNDFLIGNAISAEDLEGTRLELLKMHHDVVTAGNAMKPDALQPTKGNFTFTAADAMIDKVLAEGMKMHGHVLVWHQQSPAWLNTKKDDNNNTVPLGRDEALDNLRTHIQTVMKHFGNKVISWDVVNEAMNDNPSNPADYKASLRQTPWYQAIGSDYVEQAFLAAREVLDENPSWNIKLYYNDYNEDNQNKATAIYNMVKDINDRYAAAHNGKLLIDGVGMQGHYNINTNPDNVKLSLEKFISLGVEVSVSELDVTAGNNYTLPENLAVGQAYLYAQLFKLYKEHADHIARVTFWGMDDNTSWRAENNPLLFDKNLQAKPAYYGVIDPDKYMEEHAPESKDANQAEAQYGTPVIDGTVDSIWSNAQAMPVNRYQMAWQGATGTAKALWDDQNLYVLIQVSDSQLNKANENAWEQDSVEVFLDQNNGKTTFYQNDDGQYRVNFDNETSFSPASIAAGFESQTKKTANSYTVELKIPLTAVTPANQKKLGFDVQINDATDGARTSVAAWNDTTGNGYQDTSVYGELTLAGKGTGGTGTVGTTVPQTGNVVKNPDGSTTLKPEVKTTNGNAVGTVTGDDLKKALDQAAPAAGGKKQVIIDVPLQANAATYAVQLPTQSLKSQDGYQLTAKIANAFIQIPSNMLANTNVTTDQVSIRVAKASLDNVDAATRELIGNRPVIDLSLVAGGNVIAWNNPTAPVTVAVPYAPTAEELKHPEHILIWYIDGSGKATPVPNSRYDAALGAVVFQTTHFSTYAAVSVFTTFGDLAKVPWAKEAIDAMASRGVIKGTGENTFSPAASIKRADFIALLVRALELHGTGTTDTAMFSDVPANAYYYNELAVAKQLGIATGFEDNTFKPDSSISRQDMMVLTTRALAVLGKQLPAGGSLNAFSDAASVAGYAQDSVAALVKAGVVQGSGSKLAPNDQLTRAEAAVILYRIWKLQ
Protein: Caldesmon 1 (F6ZAW1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XKEEKEEEEQEKLKGGSLGENQVEKMVEEKTPEIQEEAVLMVLENGQEKEEEKGVKGQAQRQKPRDDKPAFRKEEIKDEKIKKDKEPKEEVKSFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKRLEELRRRRGETENEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKARE
Protein: Zinc finger protein 1 homolog (Zfp-1) (Zinc finger protein 475) (Q6P2D0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P08042}. Note=Shows widespread expression throughout the nucleus, but appears to be excluded from nucleoli. {ECO:0000250|UniProtKB:P08042}.
Interaction partners:
- Zinc finger protein castor homolog 1
- Transcription intermediary factor 1-beta
- Myc proto-oncogene protein
Sequence:
MNKSQGSVSFTDVTVDFTQEEWEQLDPSQRILYMDVMLENYSNLLSVEVWKADDQMERDHRNPDEQARQFLILKNQTPIEERGDLFGKALNLNTDFVSLRQVPYKYDLYEKTLKYNSDLLNSNRSYAGKQTDECNEFGKALLYLKQEKTHSGVEYSEYNKSGKALSHKAAIFKHQKIKNLVQPFICTYCDKAFSFKSLLISHKRIHTGEKPYECNVCKKTFSHKANLIKHQRIHTGEKPFECPECGKAFTHQSNLIVHQRAHMEKKPYECSECGKTFAQKFELTTHQRIHTGERPYECNECAKTFFKKSNLIIHQKIHTGEKRYECSECGKSFIQNSQLIIHMRTHTGEKPYECTECGKTFSQRSTLRLHLRIHTGEKPYECSECGKAFSRKSRLSVHQRVHIGEKP
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Nucleosome-remodeling factor 38 kDa subunit) (Pyrophosphate phospho-hydrolase) (PPase) (O77460)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis. Inorganic pyrophosphatase (PPase), hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential for driving critical biosynthetic reactions including transcription, replication, and DNA repair.
Subcellular location: Cytoplasm. Nucleus {ECO:0000269|PubMed:9784495}.
Interaction partners:
- Chromatin-remodeling complex ATPase chain Iswi
- Nucleosome-remodeling factor subunit NURF301
- Chromatin assembly factor 1 p55 subunit
- Eukaryotic translation initiation factor 5A
- ATP-dependent chromatin assembly factor large subunit
- ATP synthase subunit alpha, mitochondrial
- C-terminal-binding protein
- Toutatis, isoform E
- DNA polymerase epsilon subunit 3
- Chromatin accessibility complex 16kD protein
Sequence:
MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGGQVEEVSDTVDTWHFIHLK