wanglab/gogpt-training-data huggingface dataset:
Protein: Transient receptor potential cation channel subfamily V member 5 (TrpV5) (Epithelial calcium channel 1) (ECaC1) (Osm-9-like TRP channel 3) (OTRPC3) (Q9XSM3)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine. Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification. A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay. Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10085067, ECO:0000269|PubMed:11035011, ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:29323279}; Multi-pass membrane protein {ECO:0000269|PubMed:29323279}. Apical cell membrane {ECO:0000269|PubMed:10085067}; Multi-pass membrane protein {ECO:0000269|PubMed:29323279}. Note=Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells (By similarity). The expression of the glycosylated form in the cell membrane is increased in the presence of WNK3 (By similarity). {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9NQA5}.
Interaction partners:
- Calmodulin
- cAMP-dependent protein kinase
- Protein kinase C beta type
- non-specific serine/threonine protein kinase
- Protein S100-A10
- Transient receptor potential cation channel subfamily M member 8
- non-specific serine/threonine protein kinase
- Extracellular calcium-sensing receptor
- Parathyroid hormone
- Serine/threonine-protein kinase WNK4
Sequence:
MGACPPKAKGPWAQLQKLLISWPVGEQDWEQYRDRVNMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLKLRDDNRTDPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQEQLSEKRPSTVESGMLSRASVAFQTPSLSRTTSQSSNSHRGWEILRRNTLGHLNLGLDLGEGDGEEVYHF
Protein: Transcription factor 20 (TCF-20) (Nuclear factor SPBP) (Stromelysin-1 PDGF-responsive element-binding protein) (SPRE-binding protein) (Q9EPQ8)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.
Subcellular location: Nucleus {ECO:0000305|PubMed:7760812}.
Interaction partners:
Sequence:
MQSFREQSSYHGNQQSYPQEVHSSSRIEEFSPRQAQMFQNFGGAGGGSSGTGSSSSGRRGTAAAAAAMASETSGHQGYQGFRKEAGDFYYMAGNKDTVAAGTPQPPQRRPSGPVQSYGPPQGSSFGNQYASEGHVSQFQAQHSALGGVSHYQQDYTGPFSPGSAQYQQQASSQQQQQQQQQQQQQQQQQQQQVQQLRQQLYQSHQPLPQTTGQPASGSSHLQPMQRPSTLPSSAGYQLRVGQFGQHYQSSASSSSSSSFPSPQRFSQSGQSYDGSYSVNAGSQYEGHNVGSNAQAYGTQSNYSYQPQSMKNFEQAKIPPGNQQGQQQQQQQPQPQQQQPQQQQQQQQQQQHPPQHVMQYTNAATKMPLQSQVGQYNQPEVPVRSPMQFHQNFSPISNPSPAASVVQSPSCSSTPSPLMQSGENLQCGQGNVPMSSRNRILQLMPQLSPTPSMMPSPNSHAAGFKGFGLEGVPEKRLTDPGLSSLSALSSQVANLPNTVQHMLLSDALTPQKKTSKRPSSSSKKADSCTNSEGSSQPEEQLKSPMAESLDGGCSSSSEDQGERVRQLSGQSTSSDTTYKCGASEKAGSSPTQGAQNEAPRLSTSPATRDEAASPGAKDTSLSSEGNTKVNEKTVGVIVSREAMTGRVEKSGGQDKGSQEDDPAASQRPPSNSGVKEISHTSLPQPDPPGGGSKGNKNGDNNSSNHNGEGNGPSSHSAVGPSFTGRTEPSKSPGSLRYSYKESFGSAVPRNVSGYPQYPSGQEKGDFGSHGERKGRNEKFPSLLQEVLQGYHHHPDRRYPRSAQEHQGMASGLEGTARPNILVSQTNELASRGLLNKSIGSLLENPHWGPWERKSSSTAPEMKQINLSDYPIPRKFEIEPPSSAHEPGGSLSERRSVICDISPLRQIVRDPGAHSLGHMGTDARIGRNERLNPSLSQSVILPGGLVSMETKLKSQSGQIKEEDFEQSKSQASFNKKSGDHCHPTSIKHETYRGNASPGAAAHDSISDYGPQDSRSTPMRRVPGRVGSRETMRGRSSSQYHDFAEKLKMSPGRSRGPGGDPHHMNPHMTFSERANRSSLHAPFSPNSESLASAYHTNTRAHAYGDPNTGLNSQLHYKRQMYQQQQEEYKDWASSSAQGVIAAAQHRQEGPRKSPRQQQFLDRVRSPLKNDKDGMMYGPPVGTYHDPSTQEAGRCLMSSDGLPAKSMELKHSSQKLQESCWDLSRQTSPAKSSGPPGMSNQKRYGPPHEPDGHGLAESAQSSKPSNVMLRLPGQEDHSSQNPLIMRRRVRSFISPIPSKRQSQDVKNSNADDKGRLLHPSKEGADKAYNSYSHLSHSQDIKSIPKRDSSKDLPNPDNRNCPAVTLTSPAKTKILPPRKGRGLKLEAIVQKITSPNIRRSASANSAEAGGDTVTLDDILSLKSGPPEGGTVATQEAEMEKRKCEVVSDLVSVTNQESNVEKPLPGPSEEWRGSGDDKVKTEAHVETASTGKEPSGTMTSTASQKPGGNQGRPDGSLGGAAPLIFPDSKNVAPVGILAPEANPKAEEKENDTVMISPKQESFPPKGYFPSGKKKGRPIGSVNKQKKQQQQPPPPPQPPQMPEGSADGEPKPKKQRQRRERRKPGAQPRKRKTKQAVPIVEPQEPEIKLKYATQPLDKTDAKNKSFFPYIHVVNKCELGAVCTIINAEEEEQTKLVRSRKGQRSLTPPPSSTESKVLPASSFMLQGPVVTESSVMGHLVCCLCGKWASYRNMGDLFGPFYPQDYAATLPKNPPPKRSSEMQSKVKVRHKSASNGSKTDTEEEEEQQQQKEQRSLAAHPRFKRRHRSEDCGGGPRSLSRGLPCKKAATEGSSEKTVSDTKPSVPTTSEGGPELELQIPELPLDSNEFWVHEGCILWANGIYLVCGRLYGLQEALEIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLHEENFSVRCPKHKPPLPCPLPPLQNKTAKGSLSTEQSERG
Protein: Zinc finger SWIM domain-containing protein 8 (A7E2V4)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex that promotes target-directed microRNA degradation (TDMD), a process that mediates degradation of microRNAs (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by catalyzing ubiquitination and subsequent degradation of AGO proteins (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for degradation. Specifically recognizes and binds AGO proteins when they are engaged with a TDMD target. May also act as a regulator of axon guidance: specifically recognizes misfolded ROBO3 and promotes its ubiquitination and subsequent degradation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3UHH1}. Note=Translocates together with its substrate into stress granules (SGs) under proteostatic stress. {ECO:0000250|UniProtKB:Q3UHH1}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Leucine-zipper-like transcriptional regulator 1
- Elongin-B
- Kelch-like protein 21
- Kelch-like protein 22
- Kelch-like protein 9
- Kelch-like protein 13
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
Sequence:
MELMFAEWEDGERFSFEDSDRFEEDSLCSFISEAESLCQNWRGWRKQSAGPNSPTGGGGGGGSGGTRMRDGLVIPLVELSAKQVAFHIPFEVVEKVYPPVPEQLQLRIAFWSFPENEEDIRLYSCLANGSADEFQRGDQLFRMRAVKDPLQIGFHLSATVVPPQMVPPKGAYNVAVMFDRCRVTSCSCTCGAGAKWCTHVVALCLFRIHNASAVCLRAPVSESLSRLQRDQLQKFAQYLISELPQQILPTAQRLLDELLSSQSTAINTVCGAPDPTAGPSASDQSTWYLDESTLTDNIKKTLHKFCGPSPVVFSDVNSMYLSSTEPPAAAEWACLLRPLRGREPEGVWNLLSIVREMFKRRDSNAAPLLEILTDQCLTYEQITGWWYSVRTSASHSSASGHTGRSNGQSEVAAHACASMCDEMVTLWRLAVLDPALSPQRRRELCTQLRQWQLKVIENVKRGQHKKTLERLFPGFRPAVEACYFNWEEAYPLPGVTYSGTDRKLALCWARALPSRPGASRSGGLEESRDRPRPLPTEPAVRPKEPGTKRKGLGEGVPSSQRGPRRLSAEGGDKALHKMGPGGGKAKALGGAGSGSKGSAGGGSKRRLSSEDSSLEPDLAEMSLDDSSLALGAEASTFGGFPESPPPCPLHGGSRGPSTFLPEPPDTYEEDGGVYFSEGPEPPTASVGPPGLLPGDVCTQDDLPSTDESGNGLPKTKEAAPAVGEEDDDYQAYYLNAQDGAGGEEEKAEGGAGEEHDLFAGLKPLEQESRMEVLFACAEALHAHGYSSEASRLTVELAQDLLANPPDLKVEPPPAKGKKNKVSTSRQTWVATNTLSKAAFLLTVLSERPEHHNLAFRVGMFALELQRPPASTKALEVKLAYQESEVAALLKKIPLGPSEMSTMRCRAEELREGTLCDYRPVLPLMLASFIFDVLCAPGSRPPSRNWNSETPGDEELGFEAAVAALGMKTTVSEAEHPLLCEGTRREKGDLALALMITYKDDQAKLKKILDKLLDRESQTHKPQTLSSFYSSSRPTTASQRSPSKHGGPSAPGALQPLTSGSAGPAQPGSVAGAGPGPTEGFTEKNVPESSPHSPCEGLPSEAALTPRPEGKVPSRLALGSRGGYNGRGWGSPGRPKKKHTGMASIDSSAPETTSDSSPTLSRRPLRGGWAPTSWGRGQDSDSISSSSSDSLGSSSSSGSRRASASGGARAKTVEVGRYKGRRPESHAPHVPNQPSEAAAHFYFELAKTVLIKAGGNSSTSIFTHPSSSGGHQGPHRNLHLCAFEIGLYALGLHNFVSPNWLSRTYSSHVSWITGQAMEIGSAALTILVECWDGHLTPPEVASLADRASRARDSNMVRAAAELALSCLPHAHALNPNEIQRALVQCKEQDNLMLEKACMAVEEAAKGGGVYPEVLFEVAHQWFWLYEQTAGGSSTAREGATSCSASGIRAGGEAGRGMPEGRGGPGTEPVTVAAAAVTAAATVVPVISVGSSLYPGPGLGHGHSPGLHPYTALQPHLPCSPQYLTHPAHPAHPMPHMPRPAVFPVPSSAYPQGVHPAFLGAQYPYSVTPPSLAATAVSFPVPSMAPITVHPYHTEPGLPLPTSVACELWGQGTVSSVHPASTFPAIQGASLPALTTQPSPLVSGGFPPPEEETHSQPVNPHSLHHLHAAYRVGMLALEMLGRRAHNDHPNNFSRSPPYTDDVKWLLGLAAKLGVNYVHQFCVGAAKGVLSPFVLQEIVMETLQRLSPAHAHNHLRAPAFHQLVQRCQQAYMQYIHHRLIHLTPADYDDFVNAIRSARSAFCLTPMGMMQFNDILQNLKRSKQTKELWQRVSLEMATFSP
Protein: Emerin (O08579)
Organism: Mus musculus (Mouse)
Function: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Prelamin-A/C
- Barrier-to-autointegration factor
- Barrier-to-autointegration factor-like protein
- SUN domain-containing protein 1
- LIM domain only 7
- Nesprin-1
- Nesprin-2
- Lamin-B1
- Catenin beta-1
- SUN domain-containing protein 2
Sequence:
MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFLLFVYYSIQAEEGNPFWMDP
Protein: Mitoferrin-1 (Mitochondrial iron transporter 1) (Mitochondrial solute carrier protein) (Solute carrier family 25 member 37) (Q920G8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q287T7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family B member 10, mitochondrial
- Ferrochelatase, mitochondrial
- Asparaginyl-tRNA synthetase
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Frataxin, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Natural resistance-associated macrophage protein 2
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Ferritin, mitochondrial
- Glutaredoxin-related protein 5, mitochondrial
Sequence:
MELRRGGVGNQAAGRRMDGDCRDGGCGSKDAGSEDYENLPTSASVSTHMTAGAMAGILEHSIMYPVDSVKTRMQSLNPDPKARYTSIYGALKRIMHTEGFWRPLRGLNVMMMGAGPAHAMYFACYENMKRTLNDVFSHQGNSHLANGVAGSMATLLHDAVMNPAEVVKQRLQMYNSQHQSAFSCIRTVWRTEGLGAFYRSYTTQLTMNIPFQSIHFITYEFLQEQVNPRRDYNPQSHIISGGLAGALAAAATTPLDVCKTLLNTQENMALSLANVSGRLSGMANAFRTVYQLNGLAGYFKGIQARVIYQMPSTAISWSVYEFFKYILTKRQLENRTLY
Protein: Protein phosphatase 1F (PP2C domain containing) (Q6IPC0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSGAPQKSSPMASGAEETPGFLDTLLQDFPALLNPEDPLPWKAPGTVLSQEEVEGELAELAMGFLGSRKAPPPLAAALAHEAVSQLLQTDLSEFRKLPREEEEEEEDDDEEKAPVTLLDAQSLAQSFFNRLWEVAGQWQKQVPLAARASQRQWLVSIHAIRNTRRKMEDRHVSLPSFNQLFGLSDPVNRAYFAVFDGHGGVDAARYAAVHVHTNAARQPELPTDPEGALREAFRRTDQMFLRKAKRERLQSGTTGVCALIAGATLHVAWLGDSQVILVQQGQVVKLMEPHRPERQDEKARIEALGGFVSHMDCWRVNGTLAVSRAIGDVFQKPYVSGEADAASRALTGSEDYLLLACDGFFDVVPHQEVVGLVQSHLTRQQGSGLRVAEELVAAARERGSHDNITVMVVFLRDPQELLEGGNQGEGDPQAEGRRQDLPSSLPEPETQAPPRS
Protein: Macrophage-capping protein (Actin regulatory protein CAP-G) (P40121)
Organism: Homo sapiens (Human)
Function: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:18266911}. Cytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P24452}. Cell projection, ruffle {ECO:0000250|UniProtKB:P24452}. Note=In macrophages, may be predominantly cytoplasmic. Nuclear localization was observed in fibroblasts. In macrophages, present at the membrane-cytoplasm interface. In activated macrophages, concentrated in the ruffles of the leading lamellipodia. {ECO:0000250|UniProtKB:P24452}.
Interaction partners:
- Myotrophin
- Beta-adducin
- Alpha-adducin
Sequence:
MYTAIPQSGSPFPGSVQDPGLHVWRVEKLKPVPVAQENQGVFFSGDSYLVLHNGPEEVSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREVQGNESDLFMSYFPRGLKYQEGGVESAFHKTSTGAPAAIKKLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQVEIVTDGEEPAEMIQVLGPKPALKEGNPEEDLTADKANAQAAALYKVSDATGQMNLTKVADSSPFALELLISDDCFVLDNGLCGKIYIWKGRKANEKERQAALQVAEGFISRMQYAPNTQVEILPQGHESPIFKQFFKDWK
Protein: Casein kinase II subunit beta (CK II beta) (Phosvitin) (P67874)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Participates in Wnt signaling (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P67870}.
Interaction partners:
- Casein kinase II subunit alpha
- Casein kinase II subunit alpha
- Catenin beta-1
- FUN14 domain-containing protein 1
- NF-kappa-B inhibitor alpha
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Dishevelled segment polarity protein 2
- Dishevelled segment polarity protein 3
- Major prion protein
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPRLYGFKIHPMAYQLQLQAASNFKSPVKTIR
Protein: Leucine carboxyl methyltransferase 1 (Q9D963)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
RCVLVYMTPEQSANLLKWAASSFETAMFINYEQVNMDDRFGQIMIENLRRRSCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDEMELLEQLMRHYCLCWATRGGQELGLKEITY
Protein: Integrin subunit alpha D (G3V8L7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
TTMPFPPQSFLTLCHGFNLDTENPMTFQENARGFGQSVIQLGETRVVVAAPQEVKAVNQTGALYQCDYSTNRCDPIPLQVPPEAVNMSLGLSLAATTVPPQLLACGPTVHQNCKENTYVNGLCYLFGSNLLRKPQQFPEALRGCPQQESDIAFLIDGSGSINSIDFQKMKEFVSTVMDQFQKSKTLFSLMQYSDEFRTHFTFNDFKRNPDPKSHVRPIRQLNGRTKTASGIRKVVRELFQKINGARDNAAKILVVITDGEKFGDPLNYEDVIPEAEEAGIIRYVIGVGNAFHKPQSRRELDTIASKPAGDHVFQVDNFEALNTIRNQLQEKIFAIEGTQTGSTSSFEHEMSQEGFSAAITSNGPLLGSVGSFDWAGGAFLYPSKDKATFINTTRIDSDMNDAYLGYASAVISRNRVQSLVLGAPRYQHIGLVVMFKQNFGAWEPHTDIKGSQIGSYFGASLCSVDMDADGNTNLILIGAPHHYEKTRGGQVSVCPLPRGRARWQCEAILHGDQGHPWGRFGAALTVLGDVNGDKLTDVAIGAPGEQENQGAVYIFHGASVASISTPHSQRIAGARFSPGLQYFGQSLSGGKDLTMDGLMDLAVGAQGRLLLIRAQPVLRLEATMEFSPKNLARSVFACQEEVVKNKDAGEVRVCLHVRKNTKDRLREGDIQSTVTYDLALDPGRSVVRAFFDETKNGILRRIRVFGLTQKCETLKLILPDCVDNSVSPIILRLNYTLVGEPLRSSRDLRPVLAMEAQRIFTAMFPFEKNCGNDTICQDDLSITVSSIRVNTLVVGDSRDFDVSVTLRNDGEDSYGTKVTCYYPSGLSYRKVSASQNQFSKKPWRVIAEPSSSEGQGVLKSTIWDINHPIFPANSEVTFNVTFDVDSDASLGNKLLLKVVVTSENNVSRTDKTESQLELPVKYAIYMVVTSGESSIKYLNFTASEMTSKVIQHQYQFNNLGQRSFPVSVVFWIPVQINKVTIWDPPQVTFSQNLSSVCRTEQKSPSHSKFQDELERTPVLNCSVAVCKRIQCDIPSFNSKEIFNVTLQGNLLFDWYIETSHDHLLLVSTAEILFNDSAFALLPGQETFVKAQTETKVEPYKVHNPVPLIVGSSVGGLVLLALITAGLYKLGFFKRQYKDMMNEAAPQDGPPQ
Protein: P-type Na(+) transporter (EC 7.2.2.3) (Q6FM06)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MTNGQIDFEFSDYHALSVEDTCARLVTDSSKGISPEEFQARLAQCGENSLGDDAKIDYKAMLIHQICNAMILVLIISMIISFAIRDWITGGVICFVIGINVIIGLIQEYKASKTMNALRALSSPNAHVIRNGNSEVVDSTDVVPGDLVVVKVGDTIPADLRLVSQQNFETDEALLTGESLPVSKDANEIFDDETPVGDRINLAFSSSTVVKGRAQGIAIKTGLNTEIGKIAKSLRGGNELISRDPAKTWYQNAWISTKRTVGAFLGTTQGTPLHRKLSKLAVLLFWIAVVFAIVVMASQKFDVDRGVAIYAVCVALSMIPSSLVVVLTITMSVGAAVMASRNVIIRKLDSLEALGAVNDICSDKTGTLTQGKMIAKQIWVPKFGTLQVVGSNEPLNPEKGDINFIPNLSPYEYSHNETEDVGIMQNFKDKYEGKSIPGNCQYQLFDKWLETASLANIASVFTDPETKEWKAHGDPTEIAIQVFATRMDLPRHVLTGERDDMDEDEIMSSVSLSEKDATAANAKFRHAAEFPFDSTIKRMSSVYESRDYKTYEIYTKGAFESVLNCCTHWYGRDPNTATVMTDADVDTIKENIDSMSSEGLRVLAFANKSYPKSDVNEEKLQKILKERDYAETGLTFLGLIGIYDPPREETAGAVKKFHQAGINVRMLTGDFPGTAKAIAQEVGILPTNLYHYSKEVVDIMVMTGKQFDNLSEDEIDNLPVLPLVIARCSPQTKVRMIEALHRREKFCAMTGDGVNDSPSLKMANVGIAMGINGSDVAKDASDIVLSDDNFASILNAVEEGRRMSDNIQKFVLQLLAENVAQALYLIVGLAFQDKEGKSVFPLAPVEVLWIIVVTSCFPAMGLGLEKAAHDLMDRPPNDSKAGIFTWEIIVDMFVYGVWMAASCMATFVTIIYGRDHGNLGQNCNRDYSESCHDVFRARSAAFATMTWCALILAWEVIDLRRSFFRMHPDTDAPVKQFFKDIYGNKFLFYSVVFGFASVFPVVYIPVINTDVFLHKPIGWEWGIAIAFSVCFWIGCELHKYFKRIYYRNKSRAINPENDLENKAGTHPFDAYSTSTTLQTEVVFNGKA
Protein: Centrosomal protein of 41 kDa (Cep41) (Testis-specific gene A14 protein) (Q99NF3)
Organism: Mus musculus (Mouse)
Function: Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, cilium {ECO:0000269|PubMed:22246503}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:22246503}. Note=Localizes mainly to the cilium basal body and in primary cilia.
Interaction partners:
- Tubulin polyglutamylase TTLL6
- Serine/threonine-protein kinase PLK1
- Transmembrane protein 237
Sequence:
MSARRHIGNPEYLTRRIPQNPRYQHVKSRLDTGNSMTKYIEKLEEIKKNYRYKKDELFKRLKVTTFAQLVIQVASLSDQTLEVTAEEIQRLEDNDSATSEADAEIAAKTNGKGSPEEQSPSPVQFINSTGAGDSSRSTLQSVISGVGELDVDKGLVKKEEPNGKDKPYPDCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKNAHGKIIILYDEDERLASQAATTMCERGFENLFMLSGGLKVLAQKFPEGLVTGSLPASCQQALPFGSVRKRRGPKMPALPAENKWRFTPEDLKKIECYLEEDQGPADNPSRLNQNNSAGKDSKVAACRGGQNLPTSCPASHSSPRTLTSGHLQGKPWK
Protein: Retrotransposon Gag-like protein 4 (Mammalian retrotransposon-derived protein 4) (Zinc finger CCHC domain-containing protein 16) (Q6ZR62)
Organism: Homo sapiens (Human)
Function: Involved in cognitive function in the brain, possibly via the noradrenergic system.
Interaction partners:
- Retrotransposon Gag-like protein 6
- Retrotransposon Gag-like protein 9
Sequence:
MEKCTKSSSTMQVEPSFLQAENLILRLQMQHPTTENTAKRGQVMPALATTVMPVPYSLEHLTQFHGDPANCSEFLTQVTTYLTALQISNPANDAQIKLFFDYLSQQLESCGIISGPDKSTLLKQYENLILEFQQSFGKPTKQEINPLMNAKFDKGDNSSQQDPATFHLLAQNLICNETNQSGQFEKALADPNQDEESVTDMMDNLPDLITQCIQLDKKHSDRPELLQSETQLPLLASLIQHQALFSPTDPPPKKGPIQLREGQLPLTPAKRARQQETQLCLYCSQSGHFTRDCLAKRSRAPATTNNTAHQ
Protein: very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (EC 4.2.1.134) (Q389R7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Putative enoyl-CoA reductase
- Short-chain dehydrogenase, putative
- Fatty acid desaturase, putative
- Fatty acid desaturase, putative
- Fatty acid elongase 1
- Short-chain dehydrogenase, putative
- S-phase kinase-associated protein, putative
- SKP1 component dimerisation domain-containing protein
Sequence:
MVLFFFFCLSSGRMVVKLKLSLYSCSTTFLTLVHPLLMLSKVYLLAYNGVLLAGWSTILMKIVQHLSTGGRFADVYSLIAPLLVVSQSAAVLEVLHALFGLVRSPVGTTLLQVLSRLLVLYGALEIGPTAARMSPFATQMIVAWSLAEVIRYTFYASNLAGVKLKPVTWLRYSAFTVLYPMGITGEIACFISALPYIREKKPWTVELPNRLNFSFSWYYTVLLLLAVVYPAGSYVMYTYMLQQRRKALKATDDASQTDVSNKKKAS
Protein: Quaking related 54B, isoform A (Quaking related 54B, isoform B) (Quaking related 54B, isoform D) (RE34120p) (Sam50) (Q7KNS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEKYDGNGDFSAFNDDDNDFGGKPRKPGGSIGAPGGAHNGDASAHDHGHHGGDPGGNVQINEKANEYIRDCMAERNRMDRKFPIAEKLLEGEIEKVQTTGRIPSREQKYADIYREKPLRISQRVLVPIREHPKFNFVGKLLGPKGNSLRRLQEETLCKMTVLGRNSMRDRVKEEELRSSKDPKYAHLNSDLHVEISTIAPPAEAYARIAYAMAELRKYLIPDSNDIIRQEQLRELMDSTSLNDNDNAKSGYKKTSHMQGGNNVLGGGSINPIGGVKNTPHHSYRSSQPSSFSKNVLAPKQKVMSILEKARTAMDETYGRGYDDGLGYDPHQSYDSYSYGTHGHGPHGPPANILGGVGGISGGGGRGGHYESSDYEPDYGRREYYQHSPGYSAGGGGGVGLGTGGASQSNAIGGSGLSSNHNRSHVNR
Protein: Selenoprotein S (E9PN30)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
Sequence:
MMGGSSAAAPGAGAWEAWERSGVGAYADLGQQARTLRGGFSGAALPWAARLSLVCASLFCEPSPSLGSLLATYGWYIVFSCILLYVVFQKLSARLRALRQRQLDRAAAAVEPDVVVKRQEALAAARLKMQEELNAQVEKHKEKLKQLEEEKRRQKIEMWDSMQEGKSYKGNAKKPQEEDSPGPSTSSVLKRKSDRKPLRGGGYNPLSGEGGGACSWRP
Protein: Zinc finger FYVE domain-containing protein 21 (ZF21) (Q9BQ24)
Organism: Homo sapiens (Human)
Function: Plays a role in cell adhesion, and thereby in cell motility which requires repeated formation and disassembly of focal adhesions. Regulates microtubule-induced PTK2/FAK1 dephosphorylation, an event important for focal adhesion disassembly, as well as integrin beta-1/ITGB1 cell surface expression.
Subcellular location: Cell junction, focal adhesion. Cytoplasmic vesicle. Endosome. Note=Within cytoplasmic vesicles, partially colocalizes with EEA1, an endosomal marker.
Interaction partners:
Sequence:
MSSEVSARRDAKKLVRSPSGLRMVPEHRAFGSPFGLEEPQWVPDKECRRCMQCDAKFDFLTRKHHCRRCGKCFCDRCCSQKVPLRRMCFVDPVRQCAECALVSLKEAEFYDKQLKVLLSGATFLVTFGNSEKPETMTCRLSNNQRYLFLDGDSHYEIEIVHISTVQILTEGFPPGGGNARATGMFLQYTVPGTEGVTQLKLTVVEDVTVGRRQAVAWLVAMHKAAKLLYESRDQ
Protein: FGFR1 oncogene partner 2 homolog (Q9VM65)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Connector of kinase to AP-1, isoform E
- AT25231p
- Cerebral cavernous malformation 3
- Sarcolemmal membrane-associated protein
- MOB kinase activator-like 4
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- CTTNBP2 N-terminal-like protein
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MSNLSVGQIIMDAQRMASRVKDLDALGTALLEEAENNNRLVESLRQYQDDIESLNRISNNKTNADMVNRIQQQNINSSEILKENRELKIFIEDYERAMELMMQKYREHTVSKVLDSKFSFKELYNERMWQVIREQREKINEMAAVMQLAASVDDGVVQRELQTISQLRLENETLRELLQISKQYGSSQRPIRESDHLLEEKAVQTDSTADDSADDLSISGASVENMNNNSVIQMYSSPEQPAKVAGTTNSFNTAPVHSQSETQAPSVTLETAPPGEEPLANDNNNGPAVNTTSAPPPATTSNESVEDQATVAPAT
Protein: Bnip3l protein (Q66HQ4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
VLRPCRFQPPDHVSLSRAAAAPAQQQQQLRGRGAVPAAARWPQQRLWLLFEASQNSYLNPAYGHLWHRRDFGPAVVLTYYLSRPTGSWVELPMNSSNGNGNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVDGEKEVEALKKSADWVSDWSSRPENIPPKEFLFRHPKRAASLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY