wanglab/gogpt-training-data huggingface dataset:
Protein: SSD domain-containing protein (B6VQ56)
Organism: Caenorhabditis elegans
Interaction partners:
- Ground-like domain-containing protein
Sequence:
MCQWATRAELGEPPPSNSSASSTKNTPYSVIVYLKSSKFSDISSSLLLQMTVAVENVKKSAKIGKKMILGPSLGHLGSIVGSRPWLWITLSLFIGIASFTTLIIKPPKKEFGFDTGYTTSDAPSIREMKAQRDFFTGGKKGTPWYQALFFEPRNNEKSMHKGREYDEMKQFYRTVKNMIIRYDETLEKNITYYDLCGSTCDLNELLFTTVTMSFWSGLTYPIASIFGYESNIGKHFYEIETSETGEFLSAKKAMLVYMAFYETKHVKADLKLYEELMQNAVDVHNANKDNSVIVTLHGERGMSIAVEAGMKHAFNYLGFGVLLSLFVLFGVLFFFSRLFCQFTIFRIVFLWIVAIIAPILSFITSFAIYNFFGYSITPLIIFTPFLALIHGYYTVIMLTHTWLSDSELRRDSRDEHLLEVFATCMPSLIVTASPAIALLLCSVYPIENYGAVSILLGLIMTFDIVFAIFFFSPFMLIICPTQDFSPLPTNSKKIVKTTLKSVENMRDYYCNYVDKSLLVEIVAVAGIIALLIIPVYKGCTSVEGNLDYRQLLKQDSNRNHGVHLMSDVVWPTWFSIMFFVNKPPNFSNVREYGRFKSMMAEIDAIENKLPNNTDMVWINDFCRFTNSKPTDDALNMTRFKSFIEDAIYKSWKDGVKFIFLNDTHPVITSMLHIVSFEKTTSLADKAKLFEKCRAVTNKYPEFKTTPFDTEIGFADIILQVPLVVAVIPLVGTVAMFIVSTIIIGNLSVAVLNFIAVCILYASTIGTVSLYDVTINPFNAAFFLIIAALAPSCTTHYCYYYQQAMRIKLRAKKVDRMNEMLRKCFFPCIASVICSIAVFVPTMFCHINIFESVAFTNNVFCLLGIVIAFFVQVMLNMLPDMFTGTHWFCSPQS
Protein: Eyes absent homolog (EC 3.1.3.48) (E7EQM5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLFPQVAVKTEPMSSSETASTTADGSLNNFSGSAIGSSSFSPRPTHQFSPPQIYPSKPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGALWAGIKTEGGLSQSQSPGQTGFLSYGTSFSTPQPGQAPYSYQMQGSSFTTSSGIYTGNNSLTNSSGFNSSQQDYPSYPSFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGITSQAVTDPTAEYSTIHSPSTPIKDSDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRISSHSDLMALHHALELEYL
Protein: Serine/threonine-protein kinase MAK (EC 2.7.11.1) (Male germ cell-associated kinase) (Protein kinase RCK) (Q04859)
Organism: Mus musculus (Mouse)
Function: Essential for the regulation of ciliary length and required for the long-term survival of photoreceptors. Could have an important function in sensory cells and in spermatogenesis. May participate in signaling pathways used in visual and olfactory sensory transduction. Phosphorylates FZR1 in a cell cycle-dependent manner. Plays a role in the transcriptional coactivation of AR (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:21148103}. Photoreceptor inner segment {ECO:0000250}. Note=Localizes in both the connecting cilia and the outer segment axonemes.
Interaction partners:
- DNA replication licensing factor MCM2
- Cell division control protein 6 homolog
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication factor Cdt1
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 2
Sequence:
MNRYTTMKQLGDGTYGSVLMGKSNESGELVAIKRMKRKFYSWDECMNLREVKSLKKLNHANVIKLKEVIRENDHLYFVFEYMKENLYQLMKDRNKLFPESVIRNIMYQILQGLAFIHKHGFFHRDMKPENLLCMGPELVKIADFGLARELRSQPPYTDYVSTRWYRAPEVLLRSSVYSSPIDVWAVGSIMAELYTFRPLFPGTSEVDEIFKICQVLGTPKKSDWPEGYQLASSMNFRFPQCIPINLKTLIPNASSEAIQLMTEMLNWDPKKRPTASQALKHPYFQVGQVLGSSAHHLDTKQTLHKQLQPLEPKPSSSERDPKPLPNILDQPAGQPQPKQGHQPLQTIQPPQNTVTHPPPKQQGHQKPPQTMFPSIIKTIPVNSVSTLGHKGARRRWGQTVFKSGDSCDDIEDDLGASHSKKPSMEACKEKKKESPFRFPDSGLPVSNHFKGENRNLHASVSLKSDPNLSTASTAKQYYLKQSRYLPGVNPKNVSLVAGGKDINSHSWNNQLFPKSLGSMGADLSFKRSNAAGNLGSYTTYNQTGYMPSFLKKEVGSAGQRIQLAPLGASASDYTWSTKTGRGQFSGRTYNPTAKNLNIVNRTQPVPSVHGRTDWVAKYGGHR
Protein: Protein YchQ (Protein SirB2) (Q46755)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- UPF0162 protein YchA
- Release factor glutamine methyltransferase
- Peptide chain release factor RF1
- Uncharacterized fimbrial-like protein YdeR
- Glutamyl-tRNA reductase
Sequence:
MTSFSTLLSVHLISIALSVGLLTLRFWLRYQKHPQAFARWTRIVPPVVDTLLLLSGIALMAKAHILPFSGQAQWLTEKLFGVIIYIVLGFIALDYRRMHSQQARIIAFPLALVVLYIIIKLATTKVPLLG
Protein: LINE-1 retrotransposable element ORF1 protein (L1ORF1p) (LINE retrotransposable element 1) (LINE1 retrotransposable element 1) (Q9UN81)
Organism: Homo sapiens (Human)
Function: Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17562864}. Cytoplasm {ECO:0000269|PubMed:27428332}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:16183655, ECO:0000269|PubMed:30122351}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17562864, ECO:0000269|PubMed:23093941}. Note=Colocalizes with its encoding RNA in cytoplasmic ribonucleoprotein particle (PubMed:16183655). Mainly cytoplasmic, rarely detected in the nucleus, possibly within the nucleolus (PubMed:17562864). {ECO:0000269|PubMed:16183655, ECO:0000269|PubMed:17562864}.
Interaction partners:
Sequence:
MGKKQNRKTGNSKTQSASPPPKERSSSPATEQSWMENDFDELREEGFRRSNYSELREDIQTKGKEVENFEKNLEECITRITNTEKCLKELMELKTKARELREECRSLRSRCDQLEERVSAMEDEMNEMKREGKFREKRIKRNEQSLQEIWDYVKRPNLRLIGVPESDVENGTKLENTLQDIIQENFPNLARQANVQIQEIQRTPQRYSSRRATPRHIIVRFTKVEMKEKMLRAAREKGRVTLKGKPIRLTADLSAETLQARREWGPIFNILKEKNFQPRISYPAKLSFISEGEIKYFIDKQMLRDFVTTRPALKELLKEALNMERNNRYQPLQNHAKM
Protein: DNA polymerase epsilon subunit 4 (DNA polymerase II subunit 4) (DNA polymerase epsilon subunit p12) (Q9NR33)
Organism: Homo sapiens (Human)
Function: Accessory component of the DNA polymerase epsilon complex. Participates in DNA repair and in chromosomal DNA replication (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit 2
- DNA polymerase epsilon subunit 3
- DNA polymerase alpha catalytic subunit
- DNA polymerase delta subunit 2
- DNA polymerase delta catalytic subunit
- DNA polymerase alpha subunit B
- DNA polymerase zeta catalytic subunit
- DNA primase large subunit
- DNA polymerase delta subunit 3
Sequence:
MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLDNAIEAVDEFAFLEGTLD
Protein: Nuclear RNA export factor 3 (B1AUS0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRCRRIFQQRFLNSPAHVSDTVHTSFYQQPAMSNPPMHTRRYTPYGIPSRYQRVSVQKWNQTDVNMEGGSKPPERKMQRDKQDDTSENWFKVTIPFGIKYDKK
Protein: Protein LSM14 homolog (RNA-associated protein of 55 kDa) (RAP55) (Q9YH12)
Organism: Pleurodeles waltl (Iberian ribbed newt)
Function: Does not appear to bind RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9851867}.
Interaction partners:
Sequence:
MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVVLAKFALLGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSTSFQSVSSYGPFSRMPTYSQFNQKSFRSTKFGRGRFRQLNKILRTFETTTSASLSQSSAVGSSFTSDARSLKTQLSQGRSSPHLDTLRKSPTMEQSVQTTPASHLPPPGPVGRRSPPPARPLPSVNQRTIESQEQKRVEAHRLSRPEADQLRNENKDANKRQAAPGAPPARRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFTKEEIDREFHNKLKLKDDKPEKVEKPVNGEDKGDSGIDTQNSEGNADEEEALASNCYYDKTKSFFDNISCDDNRERRQTWAEERRINAETFGLPLRSNRGRGGYRGRGSGMGFRGARGRGGQRGGFGAPRGFRGGFRGTRGGREFADFEYRKDNKVAA
Protein: Cystathionine gamma-synthase (EC 2.5.1.48) (O-succinylhomoserine (thiol)-lyase) (Sulfur transfer protein 2) (P47164)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cystathionine beta-lyase
- Cystathionine beta-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Putative mitochondrial cysteine synthase
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Adenosylhomocysteinase
- Sulfite reductase subunit beta
- Homoserine O-acetyltransferase
- Homoserine dehydrogenase
Sequence:
MISRTIGESIPPNTKHAVSVCLPTWEATVGYEEGESSIINSLTTGYPRFFIHKSIKKLCEILSAKYSMEDEACLCFPSYKVANRCREFIKVKTGLSTKVRILQLCTPKPMNQEEKLWRRECKITVVFVDQEIFPVMKQYWQHSGEIVSSRMAEYILHELQVKDNLKKMETVDNGKKFMTEDENRVNEEYIETRFGRNLNFLAADKAKYLIRKRIATKVVEKIDSEGLSDLFSFEHYNESNGPFNVGSGEALDDDQLNSDIPAETITSMGESGSNSTFENTATDDLKFHVNPNTDVYLFPSGMASIFTAHRLLLNFDAKRLSRSSSRQDKLIGYGPPFKKTVMFGFPYTDTLSILRKFNHTHFLGQGDSTSMNALKNILHSGEQILAVFIEAPSNPLLKMGDLQELKRLSDLYSFYIVVDETVGGFVNIDVLPYADIVCSSLTKIFSGDSNVIAGSLVLNPRGKIYEFARKFMKTEDGYEDCLWCEDALCLERNSRDFVERTIKVNTNTDILLKRVLLPQVGKLFKKIYYPSLTSEDTKRNYDSVMSTKDGGYGGLFSLTFFNIEEAKKFFNNLELCKGPSLGTNFTLACPYAIIAHYQELDEVAQYGVETNLVRVSVGLENSDVLCNVFQRAIEKALGE
Protein: Four-jointed box protein 1 (Four-jointed protein homolog) (Q86VR8)
Organism: Homo sapiens (Human)
Function: Acts as an inhibitor of dendrite extension and branching.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protocadherin Fat 4
- COMM domain-containing protein 9
- Tripartite motif-containing protein 44
- Protocadherin Fat 1
- Protocadherin Fat 3
- Vang-like protein 2
- Protocadherin Fat 2
Sequence:
MGRRMRGAAATAGLWLLALGSLLALWGGLLPPRTELPASRPPEDRLPRRPARSGGPAPAPRFPLPPPLAWDARGGSLKTFRALLTLAAGADGPPRQSRSEPRWHVSARQPRPEESAAVHGGVFWSRGLEEQVPPGFSEAQAAAWLEAARGARMVALERGGCGRSSNRLARFADGTRACVRYGINPEQIQGEALSYYLARLLGLQRHVPPLALARVEARGAQWAQVQEELRAAHWTEGSVVSLTRWLPNLTDVVVPAPWRSEDGRLRPLRDAGGELANLSQAELVDLVQWTDLILFDYLTANFDRLVSNLFSLQWDPRVMQRATSNLHRGPGGALVFLDNEAGLVHGYRVAGMWDKYNEPLLQSVCVFRERTARRVLELHRGQDAAARLLRLYRRHEPRFPELAALADPHAQLLQRRLDFLAKHILHCKAKYGRRSGT
Protein: Metallothionein zym1 (Q9UTC0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Metallothionein involved in tolerance to zinc and cadmium. Binds four zinc ions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Zinc homeostasis factor 1
- Zinc-regulated transporter 1
- Zinc finger protein C25B8.19c
- Probable zinc transporter zrg17
- Low-affinity iron/zinc ion transport protein fet4
- VEL1-related protein SPBC1348.06c
Sequence:
MEHTTQCKSKQGKPCDCQSKCGCQDCKESCGCKSSAVDNCKCSSCKCASK
Protein: NAD-dependent protein deacylase SIR2rp2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (SIR2-related protein 2) (Q57YZ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:17214740}.
Interaction partners:
- NAD-specific glutamate dehydrogenase
- Uncharacterized protein
- NAD-dependent protein deacetylase SIR2rp1
Sequence:
MADRLAIFIKQCGLQRCVILTGAGCSTESGVPDYRGPNGLYRRPNFVPLTRQVFLSGSEHRKRYWARSMFGYNTVSGASCNDTHMGLYELYRAGVVNRLLTQNVDGLHHLAAHGGTGSKTVEAYAKYTSSNSGVLELHGNIHQVCCMQCGDVSPRRRLQQRLCEANYQLCRDYEAEFSEVRPDGDYEVPDRVVQAMQLVCCEHCGGLLKPHVVLFGENVPKECVREAYTAVRAASCLICLGTSLQVFSALRFVLAARESGVPIAIVTAGRTRADGLEELKVDTNSTAATMRGVVKQLLGFELGGTK
Protein: Stearoyl-[acyl-carrier-protein] 9-desaturase 3, chloroplastic (Stearoyl-ACP desaturase 3) (EC 1.14.19.2) (Acyl-[acyl-carrier-protein] desaturase 3) (Q9LF05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Also able to convert palmitoyl-ACP to palmitoleoyl-ACP at the C9 position. Exhibits delta-9 palmitoyl-[acyl-carrier-protein] desaturase (PAD) activity. Involved in omega-7 monounsaturated fatty acid biosynthesis, especially in the endosperm oil.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Delta
- sn-2 acyl-lipid omega-3 desaturase
- Temperature-sensitive sn-2 acyl-lipid omega-3 desaturase
- Transcription factor MYB115
- Transcription factor MYB118
Sequence:
MSMALLLTSPAMKQKPAVITSPRRGSSPSRRLRVSCVTTNPARKKNETCNHFRPIKEVNNQLTHTIPQEKLEIFKSMENWAEQKLLPYLKPVEDSWQPQDFLPAPENDDEFYDRVKEIRERTKEIPDDYFVVLVGDMITEEALPTYQTTLNTLDGVKDETGGSLSPWAVWIRAWTAEENRHGDLLNKYLYLTGRVDMRHVEKTIQYLIGSGMDSKFENNPYNGFIYTSFQERATFISHGNTARLATTYGDVTLAKICGTIAADEKRHETAYTKIVEKLFEIDPDGSVQALASMMKKRITMPAHLMHDGRDNDLFDHYAAVAQRIGVYTAADYAGILEFLLRRWKVESLGLGLSGEGRRAQEYLCTLPQRIKRLEERANDRVKLVSKPSVSFSWVFGRDVKL
Protein: Trimeric intracellular cation channel type A (TRIC-A) (TRICA) (Transmembrane protein 38A) (Q9H6F2)
Organism: Homo sapiens (Human)
Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:A5A6S6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A5A6S6}. Nucleus membrane {ECO:0000250|UniProtKB:A5A6S6}.
Interaction partners:
- Inactive phospholipid phosphatase 7
Sequence:
MELLSALSLGELALSFSRVPLFPVFDLSYFIVSILYLKYEPGAVELSRRHPIASWLCAMLHCFGSYILADLLLGEPLIDYFSNNSSILLASAVWYLIFFCPLDLFYKCVCFLPVKLIFVAMKEVVRVRKIAVGIHHAHHHYHHGWFVMIATGWVKGSGVALMSNFEQLLRGVWKPETNEILHMSFPTKASLYGAILFTLQQTRWLPVSKASLIFIFTLFMVSCKVFLTATHSHSSPFDALEGYICPVLFGSACGGDHHHDNHGGSHSGGGPGAQHSAMPAKSKEELSEGSRKKKAKKAD
Protein: SAM-dependent MTase RsmB/NOP-type domain-containing protein (Q384A7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Nucleolar complex protein 2
- RNA-binding protein, putative
- Peter pan protein, putative
- Methionyl-trna formyltransferase
Sequence:
MDVYRQASEIVRAVREGTGTAKALCLRKEMQKKRQTYAVVCETLRHYDLLQDVLEQAEFFQYYPRANRDFAICMAYDAVLGKGVNTNRDTTAQAIQKSVSYLQEAYERVKKHHVIPPRAGELLTDEEAGPCARTGDHNNDGGRVKHNGVDGGSLGKHFVSDGEGAGDNTQGLGCLIPRYARVNTLKIDVDSLVERLRRASAKRERNNTENCTGNDHSRRDHRHRAAGIRVLPPFTLDPVVPSLLVFPPGTDLHAHPAVRSGQLVLQDRASCLPVCVLLNAVEVITSFSASGEGEGDSKPAEPLEYVVDACAAPGNKTTQLAALGAPHVKIMAIERDDKRAELLRHRVQSLGAADYTNVVNMDFLKMAQDDREVTEGILLDPSCSASGVLTRVDVALLRKQCVAVDGSGIYTNDVVRQETAEEGVSETAVGGEVGTITAEAQGVGFASNMERVMGLARLQRKLLAHSLLSFDNCRTVVYSTCSVHEAENEEVVRQVLQDERVQARGWALSNIMPTTWRTRGWRNDSDTFPLEYTIRCDPEVDATNGFFVARFDRVVATPQKRSKKKR
Protein: Cilia- and flagella-associated protein 73 (Flagella-associated protein 73) (Modifier of inner arms 2 protein) (Mia2p) (M1V4Y8)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of inner dynein arm.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23569216}. Note=Localizes to the outer doublet microtubules of the axoneme. {ECO:0000269|PubMed:23569216}.
Interaction partners:
Sequence:
MDEEGSATARAKMMPQTLVLDHVSPATRLLEKRRQMFEVQEALEAQKQDFNRKEEVFKRREEALKLKDLELQESLIRFSKFLQENDSKRARAEKKANDEIKARIQKEKEIEQLTEVLEELKSEKERILEVLEKNMRYQHYLESVLEVADEYQEVADLLLRHATLSATNADLKDHQRKCSELAEKVRTELQIYVKQKTDEILNLNNQVAKLKTELEGYEAEAMVQEAKKDSSLQIASQRTLEYGQVVLSADNIFNRCRSKSSIGHPAESNPLHQLDVIGNFVSDLGSIIKQFKQEQAKRASLASRAEIE
Protein: ARM-like helical domain-containing protein (Q4GZ52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ferric reductase, putative
Sequence:
MLTGDILLQEIESLGRVERYERVVEVGRAARAGGDVCKERLALIELSRSCVPYERLTAALGLWQSGCSSETLRLLKDPCGRVSRLAMLPAAEALPDADLLKVFGELPVQRLAMFCGYLERKGRVTGLVDRYVAAVTPVLQKGPGLTLLCWASVSMLAAQPTSTFYLLRKSEWGTLVRRNPNFAATLVKANINSGTEANPSAITQAHTVLAQLRRFHPSVGSQLLGCVLPRVRVSNECIEAYAKMYPVEVTQMLLKHKLEETLDVSHFFKKLDPDTLLTLFSAGVFRGKDFKECFAYAPHNLRMILYKRYRKELLDPDGSMDISMIELIPNREEREREALRALNESESLRLDPKRWVSFLSPLPLSQAVEVGKQYLKEKDVHVRAELIAAIAYGGQYHRECLDDILDFCIARGNDNDVVRRKFLMRLSMISRSKWEERHIPKLAEIVKAALDARDSSSSSLDTCMSLVLGTAHLSTKVIESSFLPLVRRVGPPFNLGKYHLPKSALLCIWSCLEPVMKKEAQSDQHMKERIMWMFSSRLRDIGDVVIPYLKGLCESEDDLVFCGISTLLKHFPTIGSQMLPNLVVKRPDVISVPEVCFKVSNSIQGELLERCLMREALEDIVCRGRFPHSALSGRYWTAAKQQMYANSTVEILLEKEEEWFEAQCLLKPLESLYSVDVAKIASVLLGEDSKPPLLRDRLIELLGRAENPESLQFLLSALNDNRSRVAIHAISKRAGALSTAQVLQIVDKAMHSKLVAVQKVAVRLGALNGDEASYNFLMQLRKGGRMNADVEAVWVQAMFNFLGKEDVWVFFHNAAQDERRAVALAVVDIPSGTLEACWQLTALCKLFVLLLNHDDAYVTVQALKKLSKSKLPSYDEELISCLFHLLDTRRQSDYFPDILLALANSSADARELAQRLVDVDLDSVLSVNAHTHCGSMASHGERFRNIVSSMVELLVEEGRQPAIVCHLICWLHPTVAGEYLMKLCEKGHLHPGCVYAIVEAAGNFGSETDGVSALEEQLRGHSNPIMQRIGLELLRRMASSAGWDGTLCEALEVYRSASDPWVRDTAKVISAEDLNESCSSY
Protein: Calcium homeostasis modulator protein 1 (Protein FAM26C) (Q8IU99)
Organism: Homo sapiens (Human)
Function: Pore-forming subunit of a voltage-gated ion channel required for sensory perception of sweet, bitter and umami tastes (By similarity). Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways (By similarity). Together with CALHM3, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs) (By similarity). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions. Acts as an activator of the ERK1 and ERK2 cascade. Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum. May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23300080}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18585350}; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:D3Z291}. Note=Colocalizes with HSPA5 at the endoplasmic reticulum (PubMed:18585350). Localizes to the basolateral membrane of epithelial cells including taste cells (By similarity). {ECO:0000250|UniProtKB:D3Z291, ECO:0000269|PubMed:18585350}.
Interaction partners:
- Calcium homeostasis modulator protein 3
- Sodium channel protein type 9 subunit alpha
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Transient receptor potential cation channel subfamily M member 5
- Catenin alpha-3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Pannexin-1
- Taste receptor type 1 member 2
Sequence:
MMDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNAAYSAGILLAPPLVLFLLGLVMNNNVSMLAEEWKRPLGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVSALGNGSLAPGLPAPELARLLARVPCPEIYDGDWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQAAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGTLATAPASAAAPTTPDGAEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEEPPLMGNGWAGGGPRPPRKEVATYFSKV
Protein: Cyclin-T1 (CycT1) (Cyclin-T) (Q9QWV9)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60563}.
Interaction partners:
- Bromodomain-containing protein 4
- AF4/FMR2 family member 4
- Cyclin-dependent kinase 9
- AF4/FMR2 family member 1
- Protein HEXIM1
- Btk-PH-domain binding protein translocated to, 1)
- RNA polymerase II elongation factor ELL
- RNA polymerase II elongation factor ELL2
- Cyclin-dependent kinase 7
- Cyclin-H
Sequence:
MEGERKNNNKRWYFTREQLENSPSRRFGVDSDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFHRYSMAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPSRLKRIRNWRAYQAAMKTKPDDRGADENTSEQTILNMISQTSSDTTIAGLMSMSTASTSAVPSLPSSEESSSSLTSVDMLQGERWLSSQPPFKLEAAQGHRTSESLALIGVDHSLQQDGSSAFGSQKQASKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHDSHSSVILKMPIESSENPERPFLDKADKSALKMRLPVASGDKAVSSKPEEIKMRIKVHSAGDKHNSIEDSVTKSREHKEKQRTHPSNHHHHHNHHSHRHSHLQLPAGPVSKRPSDPKHSSQTSTLAHKTYSLSSTLSSSSSTRKRGPPEETGAAVFDHPAKIAKSTKSSLNFPFPPLPTMTQLPGHSSDTSGLPFSQPSCKTRVPHMKLDKGPPGANGHNATQSIDYQDTVNMLHSLLSAQGVQPTQAPAFEFVHSYGEYMNPRAGAISSRSGTTDKPRPPPLPSEPPPPLPPLPK
Protein: E3 ubiquitin-protein ligase TRIM8a (EC 2.3.2.27) (Tripartite motif containing protein 8) (J9UF94)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAESWRNCFEEELICPICLHVFVEPVQLPCKHNFCRGCISEAWAKDAANVRCPECNHAYSQKPNLEKNIKLNNIVEKFNALNVEKAPAVLHCILCRRGPPLQAQKVCLRCNAPCCQSHIQTHLQQPCPAPGHLLVATEEVRAWSCPHHDEYRLYHCDVEQVSVCKYCCFSRCAPNHGHAVCDVEVRRNDIRHMLMKQQDRIDDRVKDIEEQLYKLESDKLLVEDKVRQLKEEVRVQYHKMHQLLEDDLGRTLEVLDKAHSKYCQESSTQTLQLNERRQEAKKLLSSVQVVFDKAEDINIMKNTKPVKILMDRSQSCTGSVLPPYKVGHLNSKIFLSEVSKKEKNLRKVLEAPFSTPAHFLQSISVHPSSVNPTGGEKRKHSTAFPESSTSLLESSTGPMSKQQFLAPGSSDGATAQTTIAPCSSAQHIVGLSSGTGGGAAQSVHHSSSVFTSADYSNPSSSQQAMLPQYGGRKILMCTMDNCYCSSVPSISNHRTHPPYSRSGSFPWTQDYSHPLPSTPSMSQPLQGLSMHDWIDASQSHRHPDFYGLYGQSSTKPYVTS