wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 595 (Q8IYB9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MELVTFRDVAIEFSPEEWKCLDPAQQNLYRDVMLENYRNLVSLGFVISNPDLVTCLEQIKEPCNLKIHETAAKPPAICSPFSQDLSPVQGIEDSFHKLILKRYEKCGHENLQLRKGCKRVNECKVQKGVNNGVYQCLSTTQSKIFQCNTCVKVFSKFSNSNKHKIRHTGEKPFKCTECGRSFYMSHLTQHTGIHAGEKPYKCEKCGKAFNRSTSLSKHKRIHTGEKPYTCEECGKAFRRSTVLNEHKKIHTGEKPYKCEECGKAFTRSTTLNEHKKIHTGEKPYKCKECGKAFRWSTSLNEHKNIHTGEKPYKCKECGKAFRQSRSLNEHKNIHTGEKPYTCEKCGKAFNQSSSLIIHRSIHSEQKLYKCEECGKAFTWSSSLNKHKRIHTGEKPYTCEECGKAFYRSSHLAKHKRIHTGEKPYTCEECGKAFNQSSTLILHKRIHSGQKPYKCEECGKAFTRSTTLNEHKKIHTGEKPYKCEECGKAFIWSASLNEHKNIHTGEKPYKCKECGKAFNQSSGLIIHRSIHSEQKLYKCEECGKAFTRSTALNEHKKIHSGEKPYKCKECGKAYNLSSTLTKHKRIHTGEKPFTCEECGKAFNWSSSLTKHKIIHTGEKSYKCEECGKAFNRPSTLTVHKRIHTGKEHS
Protein: 1-aminocyclopropane-1-carboxylate oxidase (ACC oxidase) (Ddaco) (EC 1.14.17.4) (Ethylene-forming enzyme) (EFE) (Q76NT9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in ethylene biosynthesis. Overexpression induces overproduction of ethylene.
Interaction partners:
- Nitrilase homolog 2
- Probable serine/threonine-protein kinase kinX
Sequence:
MEIDIEKLPIIDISSFQNNENDKNQVAKEINKACKEYGFFYIKNHGVDQELIENLQNVIKKFFSLPLEIKMKWKMGLTNREWLGFFKVGQEITYGQVDWKEGCYYSSEMDGDINTIHNVPLYPTAEQEEQYEIQGFKSTIHTYIEKLTHLSQQIIEAISLSLNLPQDYFFKNYTYDPFILMGLLHYPSFHHQEQEEEQEDDESNNGGKKSPNPDESKKPEVEKFGTGQHTDWGLLTVLYQDDVGGLQVKSKNSEEYIDAPPIPGTFICNIGDMLDKMTGGYYLSNLHRVKYNKSGRDRFSIPFFLDPSLNSIPKLIPNYDQLSQFADKPERWDKQNIHEFDGTYGQYFIKKIGRVFPDYVYKKSGELV
Protein: Aquaporin-3 (Aquaglyceroporin-3) (D3TI80)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}.
Interaction partners:
- Uncharacterized protein.
Sequence:
MGRQKVILEKMARIFQIRNMLMRQALAECLGTLILVMFGCGALAQHILSGGSHGMFLTVNFAFGFAATLGILVCGQVSGGHINPTVTFSLCLLGREPWRKFPVYFLAQTVGAFLGAGIIFGMYFDAIWKFGQGSLDVDGVNATAGIFATYPSKHLTLLNGFFDQMIGTAALIVCILAIVDPYNNPIPQGLEAFTVGFVVLVIGLSMGFNSGYAVNPARDLGPRIFTAIAGWGSKVFSAESYWSFVPVFAPFIGAVFGVMVYQLMVGCHVKGEERDKREAVEREEKERLKLSAVSDKDAA
Protein: EXPERA domain-containing protein (A0A494C0F3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVERPHQQKALTRCDSLTMDFPASRTKCESFLPPEFRSFAVDPQITSLDVLQHILIRAFDLSGKKNFGISYLGRDRLGQEVYLSLLSDWDLSTAFATASKPYLQLRVDIRPSEDSEYSVPPGALLWNPFTP
Protein: Sphingomyelin phosphodiesterase (EC 3.1.4.12) (EC 3.1.4.3) (Acid sphingomyelinase) (aSMase) [Cleaved into: Sphingomyelin phosphodiesterase, processed form] (Q0VD19)
Organism: Bos taurus (Bovine)
Function: Converts sphingomyelin to ceramide. Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly. However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P17405}. Lipid droplet {ECO:0000250|UniProtKB:P17405}. Secreted {ECO:0000250|UniProtKB:P17405}. Note=The secreted form is induced in a time- and dose-dependent by IL1B and TNF as well as stress and viral infection. This increase of the secreted form seems to be due to exocytosis of the lysosomal form and is Ca(2+)-dependent. Secretion is dependent of phosphorylation at Ser-504. Secretion is induced by inflammatory mediators such as IL1B, IFNG or TNF as well as infection with bacteria and viruses. {ECO:0000250|UniProtKB:P17405}.; SUBCELLULAR LOCATION: [Sphingomyelin phosphodiesterase, processed form]: Secreted, extracellular space {ECO:0000250|UniProtKB:Q04519}. Note=This form is generated following cleavage by CASP7. {ECO:0000250|UniProtKB:Q04519}.
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Sphingomyelin synthase 2
- Lysosomal acid glucosylceramidase
- Ceramide glucosyltransferase
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase 3
- sphingosine N-acyltransferase
- sphingosine N-acyltransferase
- Sphingolipid delta
Sequence:
MPRHGVSPGQGLPRSGREQASDRSLGAPCLRLLWLGLALALALPNSPVLWSPAEARPLPTQGHPAKFIRIAPQLQEAFGWWNLTCPTCKGLFTAIDFGLRNQASVAWVGSVAIKLCVLLKIAPPAVCQSAVQLFEDDMVEVWTRSVLSPSEACGLLLGSSCGHWDIFSSWNISLPAVPKPPPQPPKPPAPGSPVSRVLFLTDLHWDHDYLEGTDPNCENPLCCRRDSGPPPASQPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHNIWQQSRQDQLRALTTITALVKKFLGPVPVYPAVGNHESTPVNGFPPPFIKGNQSSHWLYEAMAEAWEPWLPAEALRTLRIGGFYALSPRPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVERYENTLAGQFFGHTHVDEFEVFYDEETLSRPLSVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYIMNLTEANEPGATPHWYLLYRARETYGLPNALPTAWHDLVYRMRKDTQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARSDSPALCRHLVPDASLPDVQSLWSMPLLC
Protein: Pumilio domain-containing protein C6G9.14 (Q92359)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Pumilio homology domain family member 6
Sequence:
MTEQSSKSHPSFMSTEYSLPVFSSQYSDIENKDVLKSNSWDPYAANAPIALSEIPSSSKSGKTNGSKAAVESGLASGAFGNRTGNMNRNTSMSGYTFGSSNFVPYNLLSNTPSFTTSHSSSTTFVPPATMGGGLNNLSSPSSSLYLPGSASYQRSNSKNSSASILQMNTTLDDIPILLRRPGLSSYTPGPSTSRRSISSSSNLGGNPGLIANNPSASKNFAFTSGSSSTNNSTTSSSSMANGLQSISKHSAAFPLLSNATSFFGENLTPSLAASTASTGSTDSSGSNIANTLIAPTPTISPPSANTVGNPSPADTPGFNVPSLISDDPSVSSSLSSSVASLSLQNSNILSFCKDQHGCRYLQRLLEKKNQSHIDAVFAETHPYLAVLMVDAFGNYLCQKLFEHASEAQRSTFIQIIAPKLVPISFNMHGTRALQKIIDLVSSPDQISCIVNALRPNVVLLTKDLNGNHVIQKCLNKFSQEDCQFIFDAICEDPLDVSTHRHGCCVVQRCFDHASPAQIEQLVEHIVPHALTLVQDAFGNYVLQYVLELNNPNHTEAIISYFLYKVRALSTQKFSSNVMEKCIFFAPAAIKEKLISELMDEKHLPKLLRDSFANYVIQTALDNASVKQRAELVERIKPLIPSIKNTPCGRRILSKLERRHPSSKEKPIVYSNSERVNTSSSA
Protein: Nodulin-like domain-containing protein (Q57VL1)
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:
Sequence:
MSAPVDNVVVERLSTANQKPVSEPRRFATLVLGVFCCMCTSFMYAFNLISGAMQERYDLTQRDLSTITTVGIVVGYFLLPYGFIYDYLGPRPVFVISMTVFCLGTLLLALTFQEVIEGSVVRLSVYNGLMVLGCMLFDLGAVVTVLSVFPSNRGAVMAIMKTFTGLGSAIVGCIRLGFLSQSTSAYFYFLMSFALAAGILAIAFLRLPPFHLTGYQEKHLDEEEKAQLRVTKGVYLKQKAPMWRFVYGFAILLILIVFLPLQGSLSAYLKLGSNFRVGFALVVIALIVIFPFMAFPLTTFDGKRPHDDSDSKAKEHVGAGDEVSAAEDKVVETDVDYIAPQFQETFIAGLKTARLWCLLWSVFCCVGVHYVVIYNARFIYTALTGEAPEDALNTLLTVLNGVGSAVGRLCMSYFEIWSQKRRAEDRVPITIALFIPSVCIITMLTLFLTLPKAALPLPYFIAAFSNGFTAAIIALVTRTIFAKDPAKHYNFCYLASVLSAIFLNRLLYGEWYTQQADKLGQDVCKKRVCVVMPLAFMLGLAFPAFATSTYLHLQYRRLCTLALEERQRIREEERVLNELPSNPIEPTGNAGEPAHQLK
Protein: Defence against restriction A N-terminal domain-containing protein (O21969)
Organism: Punavirus P1
Interaction partners:
Sequence:
MCQMTKNKYATVDFDQVNEKGLKSLITAINKTGVTVIEVDSSNRATTKDGVKVKTAKLVLSDGQILAIQVNDTGDISSVKLNGKAIPNAQSPDIKTLGTVMGQAARKNSAKFQKSLIAKAKRVANPVDKKPAVKSNFQRLQEAKQRNAQVVAAYKSAQNSVSFNQQQITDLRAKLDKETGRLNNEKARNGELKRRLKQLKAGN
Protein: Ubiquitin-activating enzyme E1, putative (Q38DE8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-conjugating enzyme E2, putative
- Polyubiquitin, putative
- Ubiquitin-activating enzyme E1, putative
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin-conjugating enzyme E2, putative
- E2 ubiquitin-conjugating enzyme
- Ubiquitin-conjugating enzyme E2, putative
- Ubiquitin/ribosomal protein S27a, putative
- Ubiquitin-like protein, putative
Sequence:
MPKHQRDRFSNCPAFCSHTSNKLFRTELTHYSSDTTRNVNINGFTKMSKMAGATADSSDASSAIDSKFLDQQSRTIGTYGLETMAKLISFKVLVVGCGGVGIETAKNLALAGVHTITLCDPKKAELKDMGVNFAVTETTIKAGLTRAEASKRLVAELNPNVRVRTVDAIDEAVVSEVNCVVYTSAAADWSSKTLLKWDQFCRTRTPAISFIFAFQGGSLASVFADHAPNFTVKDADGRPMLQKLIVEVLTKRDKSGVEYTRVRYETPEGQTPGAFRDYTEVKFSEVKGLCKANGESINGNVFKGVVCTGDPPNTVRIYPSLESQGYSAYETAGFLHEMKESQQLKFRALSEALSCPGQFVPVSSMMDGSEESQSHLTFTALLRFFDKHGRLPELHNLSEANEVVSLAKAVNEENKAADAKLEKVDHPMFLQHENKEFPSRLAPPPPPTPLCVETLDEGFVCSQALVSAAELQPLCAVWGAVLAQEIVKITGKYTPICQWLHVGYSSILASNASYTKSPQEYKVVDHRYKHLISLFGKTFVEKLNNLKLFMVGCGALGCENIKNFALCGMSCGPRGSFVVTDNDRIEVSNLSRQFLFREENVGQPKSAVAVSRMKSINKDVKADARQDYVGSNTEHIYHDVFWNGLDAVVNALDNMETRLYVDQKCVNFHKILVEAGTMGTGGNVDIVVPGKTTSYSDGGAADTTGGIPMCTLRNFPYTSDHCTEWARAQFDDLFVSPMQTVRQLLENPAAFTERIKNEVNNAQSAGERLSLVEKNLGILQGIQKTVTTLSAGVSMEKCVQCAWETMFHLFRDRILDLQRSFPKDAKKKNGEKFWSGHRKYPTPLEVNIKALSSDPDVVEFLISAANLFACMYGIHPQKHEPRLNDPKKRWMQQYRTLDWLNGVMKNCTVPEYKPGSVEGLDDDLLQSMEKQEVSKDETTKEQTLNNLLSSVVALAQKCHNMNTVPLDFEKDDDDNFHIDFVAATSNLRARNYDIPTQDRFKVKLVAGKIIPAIATTTAAVTGLALIEYFKALLSNDVSCLRNGMLDIGTNNYVLFERDAPLKHRTRVDKTYLPEQDYTYKKKVICLPEGYTKYDMIEVPITKATTVQQFATELEKKLNTLLPTGMNAGCEVSAIGVGKGSLWNGLPKHANTNCSLMDIIEKQKLSEAGGKLPRPFWENRTHFHDLSVTVSIDDDDANVDEVDVETATILLRIQQ
Protein: CMP-N,N'-diacetyllegionaminic acid synthase (EC 2.7.7.82) (Q5ZXI0)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates such as lipopolysaccharide (LPS) which could be a key determinant in the ability of L.pneumophila to inhibit the fusion of phagosomes with lysosomes. LPS contains a majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the conversion of N,N'-diacetyllegionaminic acid (Leg5Ac7Ac) and CTP into CMP-N,N'-diacetyllegionaminic acid (CMP-Leg5Ac7Ac).
Interaction partners:
- N,N'-diacetyllegionaminic acid synthase
- UDP-N,N'-diacetylbacillosamine 2-epimerase
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
- Spore coat polysaccharide biosynthesis protein E
- LPS biosynthesis protein, PseA-like
- GDP-perosamine synthase
- Acetyltransferase
- Imidazole glycerol phosphate synthase subunit HisH 1
- imidazole glycerol-phosphate synthase
- dTDP-glucose 4,6-dehydratase
Sequence:
MRILAVIPARAGSKRLPGKNTRLLAGKPLIAHTIVAALQSSCCEEIVVSTDSKQIADVAVQYGASVPWLRSEDLATDTSDVIHTVIDLLFKFQQMDVFFDSVLLLQPTSPFRKPETIRHAVEIHKVTGKSVVSVSPISLKPSWCRSIDSQGNLVKPELFQDLEIYCNENPIYKLNGSIYIATAKQIIENKSFYSEPTKPLLLNSISESIDIDTPIDWALTEKLMELNQEALV
Protein: Transcription factor SOX-15 (SRY-box transcription factor 15) (P43267)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to DNA at the 5'-AACAATG-3' consensus sequence. Acts as a transcriptional activator and repressor. Binds synergistically with POU5F1 (OCT3/4) to gene promoters. Binds to the FOXK1 promoter and recruits FHL3, resulting in transcriptional activation of FOXK1 which leads to myoblast proliferation. Acts as an inhibitor of myoblast differentiation via transcriptional repression which leads to down-regulation of the muscle-specific genes MYOD and MYOG. Involved in trophoblast giant cell differentiation via enhancement of HAND1 transcriptional activity. Regulates transcription of HRC via binding to its proximal enhancer region. Involved in skeletal muscle regeneration. Also plays a role in the development of myogenic precursor cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:10821863, ECO:0000269|PubMed:15367664, ECO:0000269|PubMed:17363903}.
Interaction partners:
- POU domain, class 5, transcription factor 1
Sequence:
MALTSSSQAETWSLHPRASTASLPLGPQEQEAGGSPGASGGLPLEKVKRPMNAFMVWSSVQRRQMAQQNPKMHNSEISKRLGAQWKLLGDEEKRPFVEEAKRLRARHLRDYPDYKYRPRRKSKNSSTGSVPFSQEGGGLACGGSHWGPGYTTTQGSRGFGYQPPNYSTAYLPGSYTSSHCRPEAPLPCTFPQSDPRLQGELRPSFSPYLSPDSSTPYNTSLAGAPMPVTHL
Protein: Glutathione/L-cysteine transport system ATP-binding/permease protein CydC (EC 7.4.2.-) (P23886)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in periplasmic and secreted proteins (Probable). CydC contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Required for the assembly of functional cytochrome bd-type quinol oxidases and periplasmic c-type cytochromes. Overexpression of CydDC under anaerobic conditions also results in the formation of a heme biosynthesis-derived pigment, P-574. CydDC binds heme b, but heme is probably not transported by the complex and instead has a role in regulating ATPase activity.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15470119, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15470119}.
Interaction partners:
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Cytochrome bd-I ubiquinol oxidase subunit 2
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Spermidine/putrescine import ATP-binding protein PotA
- Sulfate/thiosulfate import ATP-binding protein CysA
- Fe
- Cytochrome bd-II ubiquinol oxidase subunit 2
- ATP-dependent lipid A-core flippase
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Vitamin B12 import ATP-binding protein BtuD
Sequence:
MRALLPYLALYKRHKWMLSLGIVLAIVTLLASIGLLTLSGWFLSASAVAGVAGLYSFNYMLPAAGVRGAAITRTAGRYFERLVSHDATFRVLQHLRIYTFSKLLPLSPAGLARYRQGELLNRVVADVDTLDHLYLRVISPLVGAFVVIMVVTIGLSFLDFTLAFTLGGIMLLTLFLMPPLFYRAGKSTGQNLTHLRGQYRQQLTAWLQGQAELTIFGASDRYRTQLENTEIQWLEAQRRQSELTALSQAIMLLIGALAVILMLWMASGGVGGNAQPGALIALFVFCALAAFEALAPVTGAFQHLGQVIASAVRISDLTDQKPEVTFPDTQTRVADRVSLTLRDVQFTYPEQSQQALKGISLQVNAGEHIAILGRTGCGKSTLLQQLTRAWDPQQGEILLNDSPIASLNEAALRQTISVVPQRVHLFSATLRDNLLLASPGSSDEALSEILRRVGLEKLLEDAGLNSWLGEGGRQLSGGELRRLAIARALLHDAPLVLLDEPTEGLDATTESQILELLAEMMREKTVLMVTHRLRGLSRFQQIIVMDNGQIIEQGTHAELLARQGRYYQFKQGL
Protein: E3 ubiquitin-protein ligase TRIM38 (EC 2.3.2.27) (E3 SUMO-protein ligase TRIM38) (EC 2.3.2.-) (Tripartite motif-containing protein 38) (Q5SZ99)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity. Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation. Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling. Acts as positive regulator of the cGAS-STING pathway by acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and STING, preventing their degradation and thereby activating the innate immune response to DNA virus. Also acts as a negative regulator of NF-kappa-B signaling independently of its E3 protein ligase activity by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22539786}.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM56
Sequence:
MGSDFSTVKIRKVTSCSICKAMMSHPVSINCGHSYCKSCIQSYYCNVSPKTGWKMLGCPLCSSPFSLENLRPNKELETIIDMIKGMEEQDQDMVCEEHEEKFNRFCEDDGQLLCWRCYWEDRHKGHTLAHVKDVYQNYKEKLQNTMTKLRELQENHEVQIHFITHQINAWKDAVEDRRQTIKSNFKNLQSFLQEEEKFYLWRLENEEKEMLVQLEGSEANLQQTFERAQCQIQELEAKCQGSAQKLLQDVKNTLSRCEAMKRNPLKADPLKVHTKCNVSELYFDVKTILRRHQVSVILDPSTAHLDLALTKGGRLVTYKRCPRDLQARSSAKRFYGLPCVLGCEGFTSGRYYFEVSVENATSWDLGVCVENVHRGFNMKKEPESGFWTIKMSEEDGLEALTSTPTPPLHLIEKPQILGVFLDYEAGAVSFYSVTTGSHIFTFPKASFQDTLRPFFQVYQYSPLFLPAINNQ
Protein: Probable protein phosphatase 2C 46 (AtPP2C46) (EC 3.1.3.16) (Q9SD12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May dephosphorylate and repress plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness.
Interaction partners:
- Probable protein phosphatase 2C 5
- E3 ubiquitin-protein ligase APD4
- E3 ubiquitin-protein ligase APD3
- E3 ubiquitin-protein ligase APD2
- E3 ubiquitin-protein ligase APD1
- Protein SMALL AUXIN UP-REGULATED RNA 9
- Auxin-responsive protein SAUR19
Sequence:
MLSTLMKLLSACLWPSSSSGKSSDSTGKQDGLLWYKDFGQHLVGEFSMAVVQANNLLEDQSQVESGPLSTLDSGPYGTFIGIYDGHGGPETSRFVNDHLFQHLKRFAAEQASMSVDVIKKAYEATEEGFLGVVTKQWPTKPQIAAVGSCCLVGVICGGMLYIANVGDSRAVLGRAMKATGEVIALQLSAEHNVSIESVRQEMHSLHPDDSHIVMLKHNVWRVKGLIQISRSIGDVYLKKAEFNKEPLYTKYRIREPFKRPILSGEPTITEHEIQPQDKFLIFASDGLWEQMSNQEAVDIVQNHPRNGIARRLVKMALQEAAKKREMRYSDLKKIERGVRRHFHDDITVVIIFLDTNQVSSVKGPPLSIRGGGMTFPKKI
Protein: Transient receptor potential cation channel subfamily C member 5 (Transient receptor potential cation channel, subfamily C, member 5) (Transient receptor potential protein 5) (Q8VD38)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLSAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRKPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRHNLRSFTERHADSLIQNQHYQEVIRNLVKRYVAAMIRNSKTNEGLTEENFKELKQDISSFRYEVLDLLGNRKHPRRSFSTSSAEFSQRDDTNDGSGGARAKSKSVSFNLGCKKKACQGAPLIRTMPRASGAQGKPKAESSGKRSFMGPSFKKLGLLFSKFNGQTSEPTSEPMYTISDGIAQQHSMWQDIRYSQMEKGKAEACSQSEMNLSEVELGEIRGAARSSECPLACSSSLHCASGICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL
Protein: Ubiquitin-conjugating enzyme E2 1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 1) (Ubiquitin carrier protein 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase 1) (P25865)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase PRT6
- E3 ubiquitin-protein ligase BRE1-like 1
- E3 ubiquitin-protein ligase BRE1-like 2
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-activating enzyme E1 2
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 3
- Histone H2B.6
- E3 ubiquitin-protein ligase UPL4
- Ubiquitin-ribosomal protein eS31y fusion protein
Sequence:
MSTPARKRLMRDFKRLQQDPPAGISGAPQDNNIMLWNAVIFGPDDTPWDGGTFKLSLQFSEDYPNKPPTVRFVSRMFHPNIYADGSICLDILQNQWSPIYDVAAILTSIQSLLCDPNPNSPANSEAARMYSESKREYNRRVRDVVEQSWTAD
Protein: Olfactory receptor 51D1 (Olfactory receptor OR11-14) (Q8NGF3)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MQKPQLLVPIIATSNGNLVHAAYFLLVGIPGLGPTIHFWLAFPLCFMYALATLGNLTIVLIIRVERRLHEPMYLFLAMLSTIDLVLSSITMPKMASLFLMGIQEIEFNICLAQMFLIHALSAVESAVLLAMAFDRFVAICHPLRHASVLTGCTVAKIGLSALTRGFVFFFPLPFILKWLSYCQTHTVTHSFCLHQDIMKLSCTDTRVNVVYGLFIILSVMGVDSLFIGFSYILILWAVLELSSRRAALKAFNTCISHLCAVLVFYVPLIGLSVVHRLGGPTSLLHVVMANTYLLLPPVVNPLVYGAKTKEICSRVLCMFSQGGK
Protein: Zinc finger protein 473 (Zinc finger protein 100 homolog) (Zfp-100) (Q8WTR7)
Organism: Homo sapiens (Human)
Function: Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases.
Subcellular location: Nucleus {ECO:0000269|PubMed:16714279}. Note=Stable component of Cajal bodies (CBs). Colocalizes with SMN, coilin and U7 snRNA.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm11
- Histone RNA hairpin-binding protein
- U7 snRNA-associated Sm-like protein LSm10
- Small nuclear ribonucleoprotein F
Sequence:
MAEEFVTLKDVGMDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETKNSPLMEDFFEEGFSQEIIEMLSKDGFWNSNFGEACIEDTWLDSLLGDPESLLRSDIATNGESPTECKSHELKRGLSPVSTVSTGEDSMVHNVSEKTLTPAKSKEYRGEFFSYSDHSQQDSVQEGEKPYQCSECGKSFSGSYRLTQHWITHTREKPTVHQECEQGFDRNASLSVYPKTHTGYKFYVCNEYGTTFSQSTYLWHQKTHTGEKPCKSQDSDHPPSHDTQPGEHQKTHTDSKSYNCNECGKAFTRIFHLTRHQKIHTRKRYECSKCQATFNLRKHLIQHQKTHAAKTTSECQECGKIFRHSSLLIEHQALHAGEEPYKCNERGKSFRHNSTLKIHQRVHSGEKPYKCSECGKAFHRHTHLNEHRRIHTGYRPHKCQECVRSFSRPSHLMRHQAIHTAEKPYSCAECKETFSDNNRLVQHQKMHTVKTPYECQECGERFICGSTLKCHESVHAREKQGFFVSGKILDQNPEQKEKCFKCNKCEKTFSCSKYLTQHERIHTRGVKPFECDQCGKAFGQSTRLIHHQRIHSRVRLYKWGEQGKAISSASLIKLQSFHTKEHPFKCNECGKTFSHSAHLSKHQLIHAGENPFKCSKCDRVFTQRNYLVQHERTHARKKPLVCNECGKTFRQSSCLSKHQRIHSGEKPYVCDYCGKAFGLSAELVRHQRIHTGEKPYVCQECGKAFTQSSCLSIHRRVHTGEKPYRCGECGKAFAQKANLTQHQRIHTGEKPYSCNVCGKAFVLSAHLNQHLRVHTQETLYQCQRCQKAFRCHSSLSRHQRVHNKQQYCL
Protein: Stromal interaction molecule 2 (Q9P246)
Organism: Homo sapiens (Human)
Function: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041}; Single-pass type I membrane protein {ECO:0000269|PubMed:16860747, ECO:0000269|PubMed:17905723, ECO:0000269|PubMed:18160041}. Note=Dynamically translocates from a uniform endoplasmic reticulum distribution to punctual endoplasmic reticulum-plasma membrane junctions in response to decrease in endoplasmic reticulum Ca(2+) concentration.
Interaction partners:
- Protein orai-2
- Protein orai-3
- Calcium release-activated calcium channel protein 1
- Stromal interaction molecule 1
- Short transient receptor potential channel 1
- Short transient receptor potential channel 6
- Short transient receptor potential channel 3
- Short transient receptor potential channel 4
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit beta-2
Sequence:
MLVLGLLVAGAADGCELVPRHLRGRRATGSAATAASSPAAAAGDSPALMTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVEESDEFIREDMKYKDATNKHSHLHREDKHITIEDLWKRWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTVSIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTMAKPPGSLARSSSLCRSRRSIVPSSPQPQRAQLAPHAPHPSHPRHPHHPQHTPHSLPSPDPDILSVSSCPALYRNEEEEEAIYFSAEKQWEVPDTASECDSLNSSIGRKQSPPLSLEIYQTLSPRKISRDEVSLEDSSRGDSPVTVDVSWGSPDCVGLTETKSMIFSPASKVYNGILEKSCSMNQLSSGIPVPKPRHTSCSSAGNDSKPVQEAPSVARISSIPHDLCHNGEKSKKPSKIKSLFKKKSK