wanglab/gogpt-training-data huggingface dataset:
Protein: Lipase LipC (Q9HUZ7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Lipase chaperone
- Triacylglycerol lipase
- Diacylglycerol kinase
- Long-chain-fatty-acid--CoA ligase
- Long-chain-fatty-acid--CoA ligase
- Esterase EstA
Sequence:
MNKNKTFLAAALVALAASFPVHAATDYTRTRYPIVLSHGLFGFKSVGPVDYWHAIVPALEKDGAKVFATSQSPVNSNEVRGEQLLAQVEEVLALTGAEKVNLIGHSQGGMTVRYVAGVAPQLVASVTTMGTPHKGTPVADAVTGFSEFLGPIGTEVIASAVEALFSVVDIVDGGEWVKGDALAALNSLNTPGTARFNQRFPQAIPASACGQGAETVAGVRYYSMSGTGSLTNALDPSSAGLAVTGLLFGEANDGLVGQCSSHLGSVVKDNYRMDHLDEVNQLLGLVSLFESDPTQVYRQHANRLRNVGL
Protein: Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (O09010)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1. Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity. Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors. May play a role in boundary formation of the enamel knot.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16385447}. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Beta-1,3-N-acetylglucosaminyltransferase manic fringe
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- Protein jagged-1
- Mesoderm posterior 2
- Delta-like protein 1
- GDP-fucose protein O-fucosyltransferase 1
Sequence:
MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTTELHEQVTLSYGMFENKRNAVHIKGPFSVEADPSRFRSVHCHLYPDTPWCPRSAIF
Protein: Ubiquitin fusion degradation protein 4 (UB fusion protein 4) (EC 2.3.2.-) (HECT-type E3 ubiquitin transferase UFD4) (EC 2.3.2.26) (P33202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Interaction partners:
- E3 ubiquitin-protein ligase UBR1
- E4 ubiquitin-protein ligase UFD2
- Ubiquitin carboxyl-terminal hydrolase 15
- Ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin-conjugating enzyme E2 4
- E3 ubiquitin-protein ligase UBR2
- GID complex subunit 7
- Transcriptional regulatory protein SAP30
- Polyubiquitin
- E3 ubiquitin-protein ligase HUL5
Sequence:
MSENNSHNLDEHESHSENSDYMMDTQVEDDYDEDGHVQGEYSYYPDEDEDEHMLSSVGSFEADDGEDDDNDYHHEDDSGLLYGYHRTQNGSDEDRNEEEDGLERSHDNNEFGSNPLHLPDILETFAQRLEQRRQTSEGLGQHPVGRTLPEILSMIGGRMERSAESSARNERISKLIENTGNASEDPYIAMESLKELSENILMMNQMVVDRIIPMETLIGNIAAILSDKILREELELQMQACRCMYNLFEVCPESISIAVDEHVIPILQGKLVEISYIDLAEQVLETVEYISRVHGRDILKTGQLSIYVQFFDFLTIHAQRKAIAIVSNACSSIRTDDFKTIVEVLPTLKPIFSNATDQPILTRLVNAMYGICGALHGVDKFETLFSLDLIERIVQLVSIQDTPLENKLKCLDILTVLAMSSDVLSRELREKTDIVDMATRSFQHYSKSPNAGLHETLIYVPNSLLISISRFIVVLFPPEDERILSADKYTGNSDRGVISNQEKFDSLVQCLIPILVEIYTNAADFDVRRYVLIALLRVVSCINNSTAKAINDQLIKLIGSILAQKETASNANGTYSSEAGTLLVGGLSLLDLICKKFSELFFPSIKREGIFDLVKDLSVDFNNIDLKEDGNENISLSDEEGDLHSSIEECDEGDEEYDYEFTDMEIPDSVKPKKISIHIFRTLSLAYIKNKGVNLVNRVLSQMNVEQEAITEELHQIEGVVSILENPSTPDKTEEDWKGIWSVLKKCIFHEDFDVSGFEFTSTGLASSITKRITSSTVSHFILAKSFLEVFEDCIDRFLEILQSALTRLENFSIVDCGLHDGGGVSSLAKEIKIKLVYDGDASKDNIGTDLSSTIVSVHCIASFTSLNEFLRHRMVRMRFLNSLIPNLTSSSTEADREEEENCLDHMRKKNFDFFYDNEKVDMESTVFGVIFNTFVRRNRDLKTLWDDTHTIKFCKSLEGNNRESEAAEEANEGKKLRDFYKKREFAQVDTGSSADILTLLDFLHSCGVKSDSFINSKLSAKLARQLDEPLVVASGALPDWSLFLTRRFPFLFPFDTRMLFLQCTSFGYGRLIQLWKNKSKGSKDLRNDEALQQLGRITRRKLRISRKTIFATGLKILSKYGSSPDVLEIEYQEEAGTGLGPTLEFYSVVSKYFARKSLNMWRCNSYSYRSEMDVDTTDDYITTLLFPEPLNPFSNNEKVIELFGYLGTFVARSLLDNRILDFRFSKVFFELLHRMSTPNVTTVPSDVETCLLMIELVDPLLAKSLKYIVANKDDNMTLESLSLTFTVPGNDDIELIPGGCNKSLNSSNVEEYIHGVIDQILGKGIEKQLKAFIEGFSKVFSYERMLILFPDELVDIFGRVEEDWSMATLYTNLNAEHGYTMDSSIIHDFISIISAFGKHERRLFLQFLTGSPKLPIGGFKSLNPKFTVVLKHAEDGLTADEYLPSVMTCANYLKLPKYTSKDIMRSRLCQAIEEGAGAFLLS
Protein: Palmitoyltransferase ZDHHC15B (EC 2.3.1.225) (Acyltransferase ZDHHC15B) (EC 2.3.1.-) (Zinc finger DHHC domain-containing protein 15B) (F1QXD3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). May thereby regulate target proteins association and localization to membranes (By similarity). In the nervous system, probably catalyzes the palmitoylation of synaptic proteins and is involved in the differentiation of dopaminergic neurons and the development of the diencephalon.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein {ECO:0000269|PubMed:29326245}. Postsynaptic density {ECO:0000250|UniProtKB:Q2TGJ4}.
Interaction partners:
- Palmitoyltransferase
- Ankyrin repeat and SOCS box protein 12
Sequence:
MALSRALRCCQRIFSWIPVIIISSVVLWSYYAYVFELCFVTLSNNLERVTYLLIFHVCFIMFCWTYWKAIFTPPSTPTKKFHLSYTDKERYEMEERPEVQKQILVDIAKKLPIFTRAQSGAIRFCDRCQVIKPDRCHHCSVCETCVLKMDHHCPWVNNCVGFSNYKFFLLFLSYSMIYCVFIASTVFQYFLKFWVGDLPNGPAKFHVLFLLFVALMFFVSLMFLFGYHCWLVAKNRSTLEAFSPPVFQNGPDRNGFNVGLSKNLRQVFGEHKKLWFIPVFTSQGDGHYFPLRTLRESENPLLANEEKWVEDGGSDEESADENGSSLLIRTES
Protein: Protein phosphatase EYA3 (EC 3.1.3.48) (Eyes absent homolog 3) (Q99504)
Organism: Homo sapiens (Human)
Function: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. Coactivates SIX1, and seems to coactivate SIX2, SIX4 and SIX5. The repression of precursor cell proliferation in myoblasts by SIX1 is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex and seems to be dependent on EYA3 phosphatase activity (By similarity). May be involved in development of the eye.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P97480}. Nucleus {ECO:0000269|PubMed:19234442}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:19234442). With decreasing efficiency, translocalized to the nucleus by SIX2 and SIX5, and SIX4, respectively (By similarity). {ECO:0000250|UniProtKB:P97480, ECO:0000269|PubMed:19234442}.
Interaction partners:
- Homeobox protein SIX1
- Homeobox protein SIX2
- Homeobox protein SIX5
- Histone H2AX
- Homeobox protein SIX4
- Dachshund homolog 1
Sequence:
MEEEQDLPEQPVKKAKMQESGEQTISQVSNPDVSDQKPETSSLASNLPMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETAYPGQTQYQTLQQTQPYAVYPQATQTYGLPPFGALWPGMKPESGLIQTPSPSQHSVLTCTTGLTTSQPSPAHYSYPIQASSTNASLISTSSTIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDAESTTLAATTYQSEKPSVMAPAPAAQRLSSGDPSTSPSLSQTTPSKDTDDQSRKNMTSKNRGKRKADATSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL
Protein: BCL11 transcription factor A (A0A0G2K4M7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKGVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIAGKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVLHTPPFGVVPRELKMCGSFRMEAQEPLSSEKL
Protein: Short stature homeobox (B0S5T0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEELTAFVSKSFDQKTKESSKESITYREVLESGLARARELGNSETNLQEITETNNNHCPVHLYKEHVELEKEKLKEFSVTRASDGIYDCKDKKEDVKSEDEDAQSKLKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQMHKGVILGTASHLDACRVAPYVNMGALRMPFQQVQAQLQLEGVGTHSHPHLHPHLAAHAPYLMFPPPPFGLPIASLADSASAAAAVVAAAKSNSKNSSIADLRLKARKHAEALGL
Protein: Protein transport protein SEC22 (Suppressor of loss of YPT1 protein 2) (P22214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Nonessential SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Syntaxin VAM3
- Synaptobrevin homolog YKT6
- Protein transport protein BET1
- t-SNARE affecting a late Golgi compartment protein 1
- Protein transport protein BOS1
- Protein transport protein SEC20
- t-SNARE VTI1
- Syntaxin PEP12
- Syntaxin UFE1
- Vacuolar morphogenesis protein 7
Sequence:
MIKSTLIYREDGLPLCTSVDNENDPSLFEQKQKVKIVVSRLTPQSATEATLESGSFEIHYLKKSMVYYFVICESGYPRNLAFSYLNDIAQEFEHSFANEYPKPTVRPYQFVNFDNFLQMTKKSYSDKKVQDNLDQLNQELVGVKQIMSKNIEDLLYRGDSLDKMSDMSSSLKETSKRYRKSAQKINFDLLISQYAPIVIVAFFFVFLFWWIFLK
Protein: Uncharacterized protein (Q38FL2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDLGSDEDRSLAGTLSGTKIPTGPPTRKGSRAGSPRQRRRRSKSKSKTKRRGGRRSKSKGRRRRSSRRSSRRSRTGSRRGKRRGSVRKVSKAGMTSSESGTNSPEGAISPVPVLGEGESSLISSHVTELEITLYRPLPEDGKPLLFFDTTACLFREHGRQIDYVGVGRRMTNDKGLLHRAHDVVSVDTACKVSDNFLEPAGGPKVVAGDTVVANLKKVSMCAGFSLCSTLFTKEVPLCEATGVYYAVKKANERLPLAIVPVQVTTVGHNSCIVLMVRKRKNCSESAWELVRLGETLVQQDVKGVVKALQSRGLVDPANYTFDFLRFLSHSAADHDSESMDSFDDYIDDADHLREKSPTPFTDSLAPDDLLRNIPRVKREGRRQYSVGRSAVNLFVAEGDSSDDDEVTEDALRAVVPKYTDTLPVRYDDKTYNIGSCSDRLTHHYVDRREEYGLISADVLGNGSTNLPPIVNPTSLDLRRFSFGTMGFLRPPIPPELSSTFPHMGRRRPTLCSRGTRLGSPSRKKRRKGKPRRKRKSRSRSRSHSRRKRRSSSRKSSCKSRGGTEKQ
Protein: Selenoprotein M (SelM) (Q8WWX9)
Organism: Homo sapiens (Human)
Function: May function as a thiol-disulfide oxidoreductase that participates in disulfide bond formation.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum {ECO:0000305|PubMed:11839807}. Golgi apparatus {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures corresponding to Golgi and endoplasmic reticulum.
Interaction partners:
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein F
- Selenoprotein K
- Selenoprotein S
- Selenoprotein N
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein H
- Selenide, water dikinase 2
- Ethanolaminephosphotransferase 1
- Selenoprotein V
Sequence:
MSLLLPPLALLLLLAALVAPATAATAYRPDWNRLSGLTRARVETCGGUQLNRLKEVKAFVTQDIPFYHNLVMKHLPGADPELVLLGRRYEELERIPLSEMTREEINALVQELGFYRKAAPDAQVPPEYVWAPAKPPEETSDHADL
Protein: Calcium homeostasis endoplasmic reticulum protein (ERPROT 213-21) (SR-related CTD-associated factor 6) (Q8IWX8)
Organism: Homo sapiens (Human)
Function: Involved in calcium homeostasis, growth and proliferation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Endoplasmic reticulum {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Note=Distributed throughout the cytoplasm and also localizes to the perinuclear region of both human erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1. {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}.
Interaction partners:
- U2 snRNP-associated SURP motif-containing protein
- Splicing factor 45
- ATP-dependent RNA helicase DHX15
- Splicing factor 3A subunit 2
- Splicing factor 1
- PHD finger-like domain-containing protein 5A
- Poly
- U2 small nuclear ribonucleoprotein A'
- ATP-dependent RNA helicase DHX8
- Splicing factor U2AF 65 kDa subunit
Sequence:
MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQTPELEPAATMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQEQHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQTLKTQHEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAPPPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDPAAAGPRGPGPHDQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSRSRSRSRSRSSRSRSRSQSRSRSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDECK
Protein: Large ribosomal subunit protein eL14 (60S ribosomal protein L14) (Q9CR57)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS12
Sequence:
MVFRRYVEVGRVAYISFGPHAGKLVAIVDVIDQNRALVDGPCTRVRRQAMPFKCMQLTDFILKFPHSARQKYVRKAWEKADINTKWAATRWAKKIDARERKAKMTDFDRFKVMKAKKMRNRIIKTEVKKLQRAAILKASPKKAAVAKAAIAAAAAAAAAKAKVPAKKATGPGKKAAGQKAPAQKAAGQKAAPPAKGQKGQKTPAQKAPAPKAAGKKA
Protein: IL-13 receptor-alpha-1-a (E6ZCC8)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MYKCWGVFVLYYFVSFVATQPETELPSPRNVTFSWTNEFCWELSWSLLENVDSQRCKYHINISRIGKNNIIRTKKETRLEECFPLMGGVRFFIQTQCNKTQMSQTVVHTIPAPTELVTNFKWFLYTPKAMNCSWLLANQVPEDLQLYYGLKNMSKVSECNEYLYNGNQRTGCHLRGDSHTRIFFQVNGTLNGSSVRNTFKVNPEDHVQPIPLDLKITEEGSNLNISWISPDIRHPHCWKYAINYTRCKIPESMSLEDKTWIMVNYDPHCQYRARTKPIFLQLCGMGEGDWTEEEIYGKDGNRDWHLHVAAVFISVIAVIVSILVCFCIRKHKDKILPKVPKPTNLISDMFNNNNEMGINENLYIPAQEEVDCKITLVQSPLPQQPEP
Protein: Jouberin (Abelson helper integration site 1 protein homolog) (AHI-1) (Q6DTM3)
Organism: Rattus norvegicus (Rat)
Function: Involved in vesicle trafficking and required for ciliogenesis, formation of primary non-motile cilium, and recruitment of RAB8A to the basal body of primary cilium. Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in neuronal differentiation. As a positive modulator of classical Wnt signaling, may play a crucial role in ciliary signaling during cerebellum embryonic development.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8K3E5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8K3E5}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8N157}. Note=In the retinal photoreceptor cell layer, localizes at the connecting cilium. {ECO:0000250|UniProtKB:Q8K3E5}.
Interaction partners:
- Coiled-coil and C2 domain containing 2A
- Tectonic family member 1
- Meckelin
- B9 domain-containing protein 1
- Transmembrane protein 216
- Centrosomal protein 290
- B9 domain-containing protein 2
- Transmembrane protein 231
- Tectonic-like complex member MKS1
- Nephrocystin-1
Sequence:
MEQETPEKVDSAQEKVRGKSQPADDSEDSREKAGTEGTGELTEAYELQVAEEMAKEIKKKIRRKLKEQLTYFPPDTLLHDDKLGSEKRKKKKKKKVPVPAKPETSPSDVCDSAAEGEQKKEGAPEGSHHREGGCSTEQNADASVPENTKPKPKKMKKKPKAVSEDNEETNGDGVHEITGRDSPVHPKCLLDDDLVMGVYIHRTDRLKSDFMISHPMVKIHVVDEHTGQYVKKDDSERPVSSYYEKDNVDYILPIMTQPYDFKKLKSRLPEWEEQVIFNENFPYLLREFDECPKVILFFEILDFLSMDEIKNNSEFQNQECGFRKIAWAFLKLLGANGNANINSKLRLQLYYPPTKPRSQPNVVEVFEWWSKCPRNRYPSTLYVTVRGLKVPDCIKPSYRSMMALQEERGTPVYCERHRETSSVDTEPGLEDSKEEVKWKRLPGQACRIPNKHLFSLNAGERGCFCLDFSHNGRILAAACASRDGYPIILYEIPSGRFMRELCGHLNIIYDLDWSKDDRYLVTSSSDGTARVWKNEINSTSTFRVLPHPSFVYTARFHPATRELVVTGCYDSMIRIWKVDAREDAAILVRQLDVHKSFVNSICFDDEGHHMYSGDCIGVIAVWDTYVKVTDVQHSVRHWTINKEIKETEFRGVPVSYLEVHPNGKRLLIHTKDSTLRIMDLRILAARKFVGAANYREKIHSTLTPCGTLLFSGSEDGIVYVWNPETGEQVAMYSELPFKSTIRDISYHPFENMVAFCAFGQSEPILLYIYDFQVAQQEAEMLKRYSGTVPLPGIHLSEDALCTCPKLPQQGSFQIDEFVNTENNSSRKIQLVKQRLETVTEVIRSCAAKVNKNLSITSPPPGPAKKPRVKQSFVLTTDQIIHQFGVPQTAFISIERRPFMRPVDPPPMVVALYDYTASRSDELTIHRGDIIRVFFKDNEDWWYGSLGKGQEGFFPANHVASETLYRDSPPKVKERSPPLTPKEKAKMEKPPASRKSLIKDRFLDSRLGSKPMGHSEKGRDQNFEERGHKSDMEMKKSEPTVRKVTLIE
Protein: Serine/threonine-protein phosphatase 2A catalytic subunit A (EC 3.1.3.16) (Protein phosphatase 2A 37 kDa catalytic subunit) (Q9XZE5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a role in activating the myosin contractile function. Dephosphorylates threonine at 'Thr-1823', 'Thr-1833' and 'Thr-2029' in the C-terminal tail region of myosin II heavy chain (mhcA). Drives the assembly of dephosphorylated myosin II filaments to allow myosin recruitment into the cytoskeleton.
Subcellular location: Cytoplasm, cytosol. Nucleus speckle.
Interaction partners:
- TAP42-like family protein
- Serine/threonine-protein phosphatase 2A regulatory subunit psrA
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- Serine/threonine-protein phosphatase 2A regulatory subunit phr2AB
- EF-hand domain-containing protein
- Probable serine/threonine-protein phosphatase 2A activator 1
- Protein phosphatase 2A scaffold subunit
- Probable protein phosphatase methylesterase 1
- Uncharacterized protein
- Probable serine/threonine-protein phosphatase 2A activator 2
Sequence:
MGEFQDVDKYISILKECKPLSESEVRDLCEKAREILSKESNVQPVRCPVTVCGDIHGQFHDLMELFKIGGNCPDTNYLFMGDYVDRGFYSVETVTLLVALKVRYKDRVTILRGNHESRQITQVYGFYDECLRKYGNPNVWKLFTDLFDYLPLTALIENQVFCLHGGLSPSIDTLDHIENLDRVQEVPHEGAMCDLLWSDPDDRLGFGYSPRGAGYTFGKDISEQFNHNNGLTLVARAHQLVMEGYNWCHDQNVVTIFSAPNYCYRCGNLAAIMEIDEKMKHTFLQFDPAPRRGEPHVTRRTPDYFL
Protein: Probable esterase D14L (Protein DWARF-14-like) (Protein D14-like) (Protein HEBIBA D14L) (Q10J20)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May be involved in strigolactone signaling pathway (By similarity). Essential for plant responses to karrikins, a class of butenolide compounds, structurally similar to strigolactones, released from burning vegetation that stimulate seed germination and enhance seedling photomorphogenesis. Mediates a specific perception of karrikin. Required for the establishment of symbiosis with the arbuscular mycorrhizal fungi (AMF) Rhizophagus irregularis and Gigaspora rosea. Karrikin binding induces a conformational change (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26680197}. Cytoplasm {ECO:0000269|PubMed:26680197}.
Interaction partners:
- 4-coumarate--CoA ligase
- Os02g0276400 protein
- Os02g0276200 protein
Sequence:
MGIVEEAHNLRVVGEGKRGVIVLAHGFGTDQSVWKHLVPHLVADYRVVLFDTMGAGPTNPDYFDFSRYATLEGYALDLLAILQELRVASCIYVGHSVSAVIGAIASISRPDLFSKLVLLSASPRYLNDVDYYGGFEQEDLDELFEAMGSNYKAWCSGFAPLCVGGDMESVAVQEFSRTLFNIRPDIALSVAQTIFQSDVRSLLPLVTVPCHIVQSTKDLAVPVVVSEYLHKHLGGDSIVEVMPSEGHLPQLSSPDIVIPVLLRHIQHDIAV
Protein: Acyl-coenzyme A thioesterase 11 (Acyl-CoA thioesterase 11) (EC 3.1.2.-) (Acyl-CoA thioester hydrolase 11) (Adipose-associated thioesterase) (Brown fat-inducible thioesterase) (BFIT) (Palmitoyl-coenzyme A thioesterase) (EC 3.1.2.2) (Q8WXI4)
Organism: Homo sapiens (Human)
Function: Has an acyl-CoA thioesterase activity with a preference for the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in the mitochondrial beta-oxidation pathway.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:22897136}. Cytoplasm {ECO:0000269|PubMed:22897136}.
Interaction partners:
- Acyl-coenzyme A thioesterase 13
- Solute carrier organic anion transporter family member 1A2
Sequence:
MIQNVGNHLRRGLASVFSNRTSRKSALRAGNDSAMADGEGYRNPTEVQMSQLVLPCHTNQRGELSVGQLLKWIDTTACLSAERHAGCPCVTASMDDIYFEHTISVGQVVNIKAKVNRAFNSSMEVGIQVASEDLCSEKQWNVCKALATFVARREITKVKLKQITPRTEEEKMEHSVAAERRRMRLVYADTIKDLLANCAIQGDLESRDCSRMVPAEKTRVESVELVLPPHANHQGNTFGGQIMAWMENVATIAASRLCRAHPTLKAIEMFHFRGPSQVGDRLVLKAIVNNAFKHSMEVGVCVEAYRQEAETHRRHINSAFMTFVVLDADDQPQLLPWIRPQPGDGERRYREASARKKIRLDRKYIVSCKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKDNWVLSSEISQVRLYTLEDDKFLSFHMEMVVHVDAAQAFLLLSDLRQRPEWDKHYRSVELVQQVDEDDAIYHVTSPALGGHTKPQDFVILASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREGDQLTKCCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVAKINSRFGYLQDT
Protein: BRI1-associated receptor kinase (F4JIX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLSQKVVSPNRCYVILLDEKVFSWRLGCCIIWSILIMSFRKRNQNSILVRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR
Protein: AT-hook motif nuclear-localized protein 4 (Q9FHM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL3 to regulate the formation of tissue boundary between the xylem and procambium in the root meristem. Cell-to-cell movement of AHL4 from the procambium to the xylem is critical for its function in root vascular patterning.
Subcellular location: Nucleus {ECO:0000269|PubMed:23335615}.
Interaction partners:
Sequence:
MEEREGTNINNIPTSFGLKQHETPLPPPGYPPRSENPNLFPVGQSSTSSAAAAVKPSENVAPPFSLTMPVENSSSELKKKRGRPRKYNPDGSLAVTLSPMPISSSVPLTSEFGSRKRGRGRGRGRGRGRGRGQGQGSREPNNNNNDNNWLKNPQMFEFNNNTPTSGGGGPAEIVSPSFTPHVLTVNAGEDVTMKIMTFSQQGSRAICILSANGPISNVTLRQSMTSGGTLTYEGHFEILSLTGSFIPSESGGTRSRAGGMSVSLAGQDGRVFGGGLAGLFIAAGPVQVMVGSFIAGQEESQQQQQQIKKQRRERLGIPTTTQASNISFGGSAEDPKARYGLNKPVVIQPPPVSAPPVSFSHEPSTNTVHGYYANNTANHIKDLFSSLPGEDREEDEDDLEGEDDEEFGGHSESDTEVPS