wanglab/gogpt-training-data huggingface dataset:
Protein: Retinitis pigmentosa 1-like 1 protein (Q8IWN7)
Organism: Homo sapiens (Human)
Function: Required for the differentiation of photoreceptor cells. Plays a role in the organization of outer segment of rod and cone photoreceptors (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, cilium, photoreceptor outer segment {ECO:0000250}. Note=Localized to the axoneme of outer segments and connecting cilia in rod photoreceptors. {ECO:0000250}.
Interaction partners:
- Mitochondrial peptide methionine sulfoxide reductase
- Transcription factor SOX-7
Sequence:
MNSTPRNAQAPSHRECFLPSVARTPSVTKVTPAKKITFLKRGDPRFAGVRLAVHQRAFKTFSALMDELSQRVPLSFGVRSVTTPRGLHSLSALEQLEDGGCYLCSDKKPPKTPSGPGRPQERNPTAQQLRDVEGQREAPGTSSSRKSLKTPRRILLIKNMDPRLQQTVVLSHRNTRNLAAFLGKASDLLRFPVKQLYTTSGKKVDSLQALLHSPSVLVCAGHEAFRTPAMKNARRSEAETLSGLTSRNKNGSWGPKTKPSVIHSRSPPGSTPRLPERPGPSNPPVGPAPGRHPQDTPAQSGPLVAGDDMKKKVRMNEDGSLSVEMKVRFHLVGEDTLLWSRRMGRASALTAASGEDPVLGEVDPLCCVWEGYPWGFSEPGVWGPRPCRVGCREVFGRGGQPGPKYEIWTNPLHASQGERVAARKRWGLAQHVRCSGLWGHGTAGRERCSQDSASPASSTGLPEGSEPESSCCPRTPEDGVDSASPSAQIGAERKAGGSLGEDPGLCIDGAGLGGPEQGGRLTPRARSEEGASSDSSASTGSHEGSSEWGGRPQGCPGKARAETSQQEASEGGDPASPALSLSSLRSDDLQAETQGQGTEQATGAAVTREPLVLGLSCSWDSEGASSTPSTCTSSQQGQRRHRSRASAMSSPSSPGLGRVAPRGHPRHSHYRKDTHSPLDSSVTKQVPRPPERRRACQDGSVPRYSGSSSSTRTQASGNLRPPSSGSLPSQDLLGTSSATVTPAVHSDFVSGVSPHNAPSAGWAGDAGSRTCSPAPIPPHTSDSCSKSGAASLGEEARDTPQPSSPLVLQVGRPEQGAVGPHRSHCCSQPGTQPAQEAQRGPSPEASWLCGRYCPTPPRGRPCPQRRSSSCGSTGSSHQSTARGPGGSPQEGTRQPGPTPSPGPNSGASRRSSASQGAGSRGLSEEKTLRSGGGPQGQEEASGVSPSSLPRSSPEAVVREWLDNIPEEPILMTYELADETTGAAGGGLRGPEVDPGDDHSLEGLGEPAQAGQQSLEGDPGQDPEPEGALLGSSDTGPQSGEGVPQGAAPEGVSEAPAEAGADREAPAGCRVSLRALPGRVSASTQIMRALMGSKQGRPSSVPEVSRPMARRLSCSAGALITCLASLQLFEEDLGSPASKVRFKDSPRYQELLSISKDLWPGCDVGEDQLDSGLWELTWSQALPDLGSHAMTENFTPTSSSGVDISSGSGGSGESSVPCAMDGTLVTQGTELPLKTSNQRPDSRTYESPGDLENQQQCCFPTFLNARACACATNEDEAERDSEEQRASSNLEQLAENTVQEEVQLEETKEGTEGEGLQEEAVQLEETKTEEGLQEEGVQLEETKETEGEGQQEEEAQLEEIEETGGEGLQEEGVQLEEVKEGPEGGLQGEALEEGLKEEGLPEEGSVHGQELSEASSPDGKGSQEDDPVQEEEAGRASASAEPCPAEGTEEPTEPPSHLSETDPSASERQSGSQLEPGLEKPPGATMMGQEHTQAQPTQGAAERSSSVACSAALDCDPIWVSVLLKKTEKAFLAHLASAVAELRARWGLQDNDLLDQMAAELQQDVAQRLQDSTKRELQKLQGRAGRMVLEPPREALTGELLLQTQQRRHRLRGLRNLSAFSERTLGLGPLSFTLEDEPALSTALGSQLGEEAEGEEFCPCEACVRKKVSPMSPKATMGATRGPIKEAFDLQQILQRKRGEHTDGEAAEVAPGKTHTDPTSTRTVQGAEGGLGPGLSQGPGVDEGEDGEGSQRLNRDKDPKLGEAEGDAMAQEREGKTHNSETSAGSELGEAEQEGEGISERGETGGQGSGHEDNLQGEAAAGGDQDPGQSDGAEGIEAPEAEGEAQPESEGVEAPEAEGDAQEAEGEAQPESEDVEAPEAEGEAQPESEDVETPEAEWEVQPESEGAEAPEAEKEAQPETESVEALETEGEDEPESEGAEAQEAEEAAQEAEGQTQPESEVIESQEAEEEAQPESEDVEALEVEVETQEAEGEAQPESEDVEAPEAEGEMQEAEEEAQPESDGVEAQPKSEGEEAQEVEGETQKTEGDAQPESDGVEAPEAEEEAQEAEGEVQEAEGEAHPESEDVDAQEAEGEAQPESEGVEAPEAEGEAQKAEGIEAPETEGEAQPESEGIEAPEAEGEAQPESEGVEAQDAEGEAQPESEGIEAQEAEEEAQPELEGVEAPEAEGEAQPESEGIEAPEAEGEAQPELEGVEAPEAEEEAQPEPEGVETPEAEGEAQPESEGETQGEKKGSPQVSLGDGQSEEASESSSPVPEDRPTPPPSPGGDTPHQRPGSQTGPSSSRASSWGNCWQKDSENDHVLGDTRSPDAKSTGTPHAERKATRMYPESSTSEQEEAPLGSRTPEQGASEGYDLQEDQALGSLAPTEAVGRADGFGQDDLDF
Protein: Ankyrin repeat domain-containing protein 7 (Testis-specific protein TSA806) (Q92527)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNKLFSFWKRKNETRSQGYNLREKDLKKLHRAASVGDLKKLKEYLQIKKYDVNMQDKKYRTPLHLACANGHTDVVLFLIEQQCKINVRDSENKSPLIKAVQCQNEDCATILLNFGADPDLRDIRYNTVLHYAVCGQSLSLVEKLLEYEADLEAKNKDGYTPLLVAVINNNPKMVKFLLEKGADVNASDNYQRTALILAVSGEPPCLVKLLLQQGVELCYEGIVDSQLRNMFISMVLLHRYPQFTASHGKKKHAK
Protein: Replication factor C subunit 5 (Replication factor C5) (O94697)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication factor C subunit 1
- Replication factor C subunit 2
- Telomere length regulation protein elg1
- Replication factor C subunit 3
- Replication factor C subunit 4
- Checkpoint protein rad17
- Chromosome transmission fidelity protein 18
- Sister chromatid cohesion protein dcc1
- Proliferating cell nuclear antigen
- Checkpoint protein hus1
Sequence:
MLWLDQYRPKTLASLDYHKQLSERLISLSSTNEFPHLLVYGPSGAGKKTRVVAILRELYGPGSEKLKIDQRTFLTPSSKKLQINIVSSLHHLEITPSDVGNYDRVIMQELLKDVAQSAQVDLQAKKIFKVVVINVADELTRDAQAALRRTMEKYSNNIRLILIANSTSKIIEPIRSRTLMVRVAAPTPEEIILVMSKILTAQGLEAPDSLLNNIANNCDRNLRKAILLLETVHAKSPGNKQLIDTGAQLPLPDWQTFIQQVGDSMLQEQSPARILAVRSMLYDLLSHCIPPTTILKELLSFFLSKVDTKLHPYLIQAAANYEHRTRMGNKSIFHLEAFVAYFMKVYAMLQLGMELPSY
Protein: Nuclear receptor subfamily 2 group F member 1-B (COUP transcription factor 1-B) (COUP-TFalpha-B) (Q6PH18)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Putative transcription factor that is required in photoreceptor cells precursors during eye development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Alpha-tocopherol transfer protein-like
- Macrophage mannose receptor 1
- Coiled-coil domain containing 85A, like isoform X3
Sequence:
MAMVVSAWRDPQEELAAVDDQSAAGREHLQHRHSPKSAEEKAQIAAQNQQHVECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPVDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPNQPNPSHYALTNGDHLNGQCYLSGYISLLLRAEPYPASRYGNQCMQSGNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQSSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRFFQEQVEKLKALQVDSAEYSCAKAIVLFTSDACGLSDIPHIEGLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPALRMVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMPIQ
Protein: Geminin (Q7SXL0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSIRRPKNAENPSENIKKFLVAPTSGAGMGRRTLQVLQPSAVNKNLGRIIENGKAMPKRKMWSAEQVKGSKRVKAEVAVKSTNAENENQPEGVTQEAYELMIKETPGSSYWKEVAEERGKALFSVLQENEKLHKDIEAKDEQIAQLKTENEELQELAQHVQHMADMIERLTGKSPDNLEELREIAFDAEDEELENENEDEEEHEDEDQEHDCEGEADESQDTEENPERSIKHNDSATEES
Protein: U2-myrmicitoxin-Tb1a (U2-MYRTX-Tb1a) (A0A6M3Z4R4)
Organism: Tetramorium bicarinatum (Tramp ant)
Subcellular location: Secreted {ECO:0000305|PubMed:30149710}.
Interaction partners:
Sequence:
AEAMAEAMADAMADAMADAMADAMAEAAADPPPGFIGVRG
Protein: Calcium-activated potassium channel subunit alpha-1 (BK channel) (BKCA alpha) (Calcium-activated potassium channel, subfamily M subunit alpha-1) (K(VCA)alpha) (KCa1.1) (Maxi K channel) (MaxiK) (Slo-alpha) (Slo1) (Slowpoke homolog) (Slo homolog) (cSlo) (Q8AYS8)
Organism: Gallus gallus (Chicken)
Function: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-activated potassium channel beta subunit
- Uncharacterized protein.
- Uncharacterized protein.
Sequence:
MSNNINANNLNTDSSSSPVNVPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGVKNKEAQKINGGGDTQADGACKPTDEKEENVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLCSIFISTWLTAAGFIHLVENSGDPWENFQNNQQLTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAPGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVANEMYTEYLSSAFVGLSFPAVCELVFAKLKLLMIAIEYKSEKRESSILINPGNHVKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNSSPKLMRHDPLLIPGNEQIDNMDANVKKYDSTGMFHWCPAKDIEKVILTRSEAAMTVLSGHVVVCIFGDVKSALIGLRNLVMPLRASNFHYHELKHIVFVGSLEYLRREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDASLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGLLRQPSITTGANIPIITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALYDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSYSSSKKSSSVHSIPSTANRPNRTKTRDSREKQKYVQEDRL
Protein: Isocitrate lyase (ICL) (Isocitrase) (Isocitratase) (EC 4.1.3.1) (Methylisocitrate lyase) (MICA) (EC 4.1.3.30) (Threo-D(S)-isocitrate glyoxylate-lyase) (P28298)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.
Subcellular location: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
Interaction partners:
- Malate synthase, glyoxysomal
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- alanine--glyoxylate transaminase
- FMN-dependent dehydrogenase family protein
- Hypothetical D-isomer specific 2-hydroxyacid dehydrogenase
- Hydroxyisocaproate dehydrogenase, putative
- D-isomer specific 2-hydroxyacid dehydrogenase family protein
- Methylisocitrate lyase, mitochondrial
- Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
Sequence:
MSYIEEEDQRYWDEVAAVKNWWKDSRWRYTKRPFTAEQIVAKRGNLKIEYPSNVQAKKLWGILERNFKNKEASFTYGCLDPTMVTQMAKYLDTVYVSGWQSSSTASSTDEPSPDLADYPMNTVPNKVNHLWMAQLFHDRKQREERMTTPKDQRHKVANVDYLRPIIADADTGHGGLTAVMKLTKLFVERGAAGIHIEDQAPGTKKCGHMAGKVLVPISEHINRLVAIRAQADIMGTDLLAIARTDSEAATLITSTIDHRDHPFIIGSTNPDIQPLNDLMVMAEQAGKNGAELQAIEDEWLAKAGLKLFNDAVVDAINNSPLPNKKAAIEKYLTQSKGKSNLEARAIAKEIAGTDIYFDWEAPRTREGYYRYQGGTQCAINRAVAYAPFADLIWMESKLPDYKQAKEFADGVHAVWPEQKLAYNLSPSFNWKKAMPRDEQETYIKRLGALGYAWQFITLAGLHTTALISDTFAKAYAKQGMRAYGELVQEPEMANGVDVVTHQKWSGANYVDNMLKMITGGVSSTAAMGKGVTEDQFKS
Protein: Serine/threonine-protein phosphatase PP1 isozyme 1 (EC 3.1.3.16) (Type one protein phosphatase 1) (P30366)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro. Acts as negative regulator of abscisic acid (ABA) signaling. In vitro, can dephosphorylate and inhibit the kinase activity of SRK2E/SNRK2.6, an activator of ABA signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm {ECO:0000269|PubMed:19329567}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit INH3
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Flowering time control protein FY
- Transducin/WD40 repeat-like superfamily protein
- Protein ANTHESIS POMOTING FACTOR 1
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3-I
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein kinase BLUS1
- 30-kDa cleavage and polyadenylation specificity factor 30
Sequence:
MAEKPAQEQEQKRAMEPAVLDDIIRRLVEFRNTRPGSGKQVHLSEGEIRQLCAVSKEIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHESASINRIYGFYDECKRRFNVRLWKIFTDCFNCLPVAALIDDRILCMHGGISPELKSLDQIRNIARPMDIPESGLVCDLLWSDPSGDVGWGMNDRGVSYTFGADKVAEFLEKHDMDLICRAHQVVEDGYEFFAERQLVTVFSAPNYCGEFDNAGAMMSIDESLMCSFQILKPSEKKSPFL
Protein: EvC complex member EVC (DWF-1) (Ellis-van Creveld syndrome protein) (P57679)
Organism: Homo sapiens (Human)
Function: Component of the EvC complex that positively regulates ciliary Hedgehog (Hh) signaling. Involved in endochondral growth and skeletal development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P57680}; Single-pass membrane protein {ECO:0000250|UniProtKB:P57680}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P57680}. Cell projection, cilium {ECO:0000250|UniProtKB:P57680}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:P57680}. Note=EVC2 is required for the localization of EVC at the base of primary cilia. The EvC complex localizes at the base of cilia in the EvC zone of primary cilia in a EFCAB7-dependent manner. {ECO:0000250|UniProtKB:P57680}.
Interaction partners:
- Limbin
- Protein smoothened
- Delta
- Cytoplasmic dynein 2 heavy chain 1
- Suppressor of fused homolog
- EF-hand calcium-binding domain-containing protein 7
- IQ domain-containing protein E
Sequence:
MARGGAACKSDARLLLGRDALRPAPALLAPAVLLGAALGLGLGLWLGCRAGRQRTRHQKDDTQNLLKNLESNAQTPSETGSPSRRRKREVQMSKDKEAVDECEPPSNSNITAFALKAKVIYPINQKFRPLADGSSNPSLHENLKQAVLPHQPVEASPSSSLGSLSQGEKDDCSSSSSVHSATSDDRFLSRTFLRVNAFPEVLACESVDVDLCIYSLHLKDLLHLDTALRQEKHMMFIQIFKMCLLDLLPKKKSDDELYQKILSKQEKDLEELEKGLQVKLSNTEMSGAGDSEYITLADVEKKEREYSEQLIDNMEAFWKQMANIQHFLVDQFKCSSSKARQLMMTLTERMIAAEGLLCDSQELQALDALERTMGRAHMAKVIEFLKLQVQEETRCRLAAISHGLELLAGEGKLSGRQKEELLTQQHKAFWQEAERFSREFVQRGKDLVTASLAHQVEGTAKLTLAQEEEQRSFLAEAQPTADPEKFLEAFHEVLERQRLMQCDLEEEENVRATEAVVALCQELYFSTVDTFQKFVDALFLQTLPGMTGLPPEECDYLRQEVQENAAWQLGKSNRFRRQQWKLFQELLEQDQQVWMEECALSSVLQTHLREDHEGTIRGVLGRLGGLTEESTRCVLQGHDLLLRSALRRLALRGNALATLTQMRLSGKKHLLQELREQRALEQGSSQCLDEHQWQLLRALEARVLEEASRLEEEAQQTRLQLQQRLLAEAQEVGQLLQQHMECAIGQALLVHARNAATKSRAKDRDDFKRTLMEAAVESVYVTSAGVSRLVQAYYQQIGRIMEDHEERKLQHLKTLQGERMENYKLRKKQELSNPSSGSRTAGGAHETSQAVHQRMLSQQKRFLAQFPVHQQMRLHAQQQQAGVMDLLEAQLETQLQEAEQNFISELAALARVPLAESKLLPAKRGLLEKPLRTKRKKPLPQERGDLGVPNNEDLASGDQTSGSLSSKRLSQQESEAGDSGNSKKMLKRRSNL
Protein: Muc10 protein (Q80XS5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKNEMFILGLLALTSYFMPGESHHKSRSSQFPVRKYLEDPRYPRYPRPHYSYGFIPSSPKFPKDNQWYKMCPPGTTLMLISRRSPKFLCIPKRQIISDKTKPNATTPAPTTKPTTNATTPAPTNRTTTNAITPAPTPKPTTNATTPAPTNRTTTNATTPAPTLKPTTNVTTPATTTNVTTPATTTNATTPATTTNATTPATTTKSTTKEPTTSPKPSTSTAIPTTTKSANSTSSTTTSTTIQTTAPTFAEVFWKFFQQIFRLKK
Protein: Alkane hydroxylase MAH1 (EC 1.14.-.-) (Cytochrome P450 96A15) (Protein MID-CHAIN ALKANE HYDROXYLASE 1) (Q9FVS9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the formation of secondary alcohols and ketones in stem cuticular wax. Catalyzes the hydroxylation of a methylene unit in the middle of alkane molecules to form secondary alcohols and possibly also a second hydroxylation leading to the corresponding ketones.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17905869}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Very-long-chain aldehyde decarbonylase CER1
- Fatty acyl-CoA reductase 3
- Wax ester synthase/diacylglycerol acyltransferase 1
- Protein CER1-like 1
- Protein CER1-like 2
- Very-long-chain enoyl-CoA reductase
- Protein ECERIFERUM 2
- 3-ketoacyl-CoA synthase 6
- ABC transporter G family member 12
- Very-long-chain 3-oxoacyl-CoA reductase 1
Sequence:
MAMLGFYVTFIFFLVCLFTYFFLQKKPQGQPILKNWPFLRMLPGMLHQIPRIYDWTVEVLEATNLTFYFKGPWLSGTDMLFTADPRNIHHILSSNFGNYPKGPEFKKIFDVLGEGILTVDFELWEEMRKSNHALFHNQDFIELSVSSNKSKLKEGLVPFLDNAAQKNIIIELQDVFQRFMFDTSSILMTGYDPMSLSIEMLEVEFGEAADIGEEAIYYRHFKPVILWRLQNWIGIGLERKMRTALATVNRMFAKIISSRRKEEISRAKTEPYSKDALTYYMNVDTSKYKLLKPNKDKFIRDVIFSLVLAGRDTTSSVLTWFFWLLSKHPQVMAKLRHEINTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKSPAKPDVLPSGHKVDANSKIVICIYALGRMRSVWGEDALDFKPERWISDNGGLRHEPSYKFMAFNSGPRTCLGKNLALLQMKMVALEIIRNYDFKVIEGHKVEPIPSILLRMKHGLKVTVTKKI
Protein: Nonsense-mediated mRNA decay protein 5 (Karyopherin-119) (P46970)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Active in protein import into the nucleus. Its major import substrate is transcription elongation factor TFIIS.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Importin subunit beta-1
- Importin subunit beta-2
- Importin subunit beta-4
- Importin subunit beta-3
- Importin subunit beta-5
- mRNA transport regulator MTR10
- GTP-binding nuclear protein GSP1/CNR1
- Importin beta-like protein KAP122
- Importin beta-like protein KAP120
- Exportin-1
Sequence:
MDITELLQCFACTLDHNAAVRTNAETHLKNASKVPGFLGACLDIIAADEVPENIKLSASLYFKNKITYGWSAGARQGSNELLDSHVDPDEKPVVKDMLIKTMVSVSKTSPRCIRVLKSALTVIISEDYPSKKWGNLLPNSLELLANEDITVTYVGLLCLAEIFRTYRWKNNDERQDLEELILNYFPALLNYGANVLFQDGKYMNNEQIGELVKLIIKIYKFVSYHDLPFTLQRSESFTPWACFFVSIIQQPLPQEVLAISDIEVRSKNPWVKCKKWALANLYRLFQRYASTSLTRKFQYDEFKQMYCEEFLTQFLQVVFDQIEKWGTGQLWLSDECLYYILNFVEQCVVQKTTWKLVGPHYNVILQHVIFPLLKPTAETLEAFDNDPQEYINRNMDFWDVGYSPDLAALALLTTCVTKRGKTTLQPTLEFMVSTLQSAVGDYNNIMLDNALQIESCLRIFSSIIDRLITKDSPFASEMEKFILTYVLPFFKSQYGFLQSRVCDICSKLGSMDFKDPVITSTIYEGVMNCLNNSSNSLPVELTAALALQTFISDDQFNMKLSEHVVPTMQKLLSLSNDFESDVISGVMQDFVEQFAEQLQPFGVELMNTLVQQFLKLAIDLHETSNLDPDSFTNVDSIPDESDKQMAALGILSTTISILLSFENSPEILKNLEQSFYPAAEFILKNDIEDFYRECCEFVENSTFLLRDITPISWKILELIGECNRKPDSMVSYYLSDFMLALNNILIYGRNELKKNEFYTKIIFEIYQKAVTAEDNSLDDLRVVFDLSQELVLALDDSLPQQYRERLLADVVGSILTQKNELKTNVVFSVTAFNVVISNMITEPLITLQYLKQQGCLEIFFQTWITDYIPNYKRCYDIKLSVLALLKIILKLESNDYSVLNLENLVPQLGSIVTQLASRLPTALRQLANQRKEFSSSGFEEDTKWDENFLDVGDDDENDDEGDLTEKYLELIKNRADSLDFVDGYDAKETFDDLEEDPLTGSILDTVDVYKVFKESIANLQHVDSNRYQGILRHLTPADQELFMGIMNA
Protein: Natriuretic peptide receptor 3 (A0A2R8RSJ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSCFMPLCLSIWAVLMVPGRTSALNDNIEVMVMLPRNNTYLFSYTRVFPAIEYAKKALREADAYAGLRFNVRFENSACGMDALYALVDRQKDERPDLVLGPVCEYAASSVTRVASHWNIPVISAGALATGFNSKTPEYSHLTRIAPTYLKMAETFQAIFGHFGWRTAYLIYDDDKDERNCYFTMEGVFTVLSEYHISTDFAVLNSNEERVDPDGIITSVYGSEVVIMCSKADIVRDLMLAAHRRKLTSDSHIFFNIELFNSSSYGDGSWRRRDKYDDEARAAYSFLNTVTLLRSTKPEFEDFSIEMKKSLQQSNIPICEDCSAVNMFMEGFHDALLLYAIALREVKSKGLTKKNGLEITHSMWNRTFEGIAGQVSLDANGDRNGDFSVVRMTDPESGKHETVMNYFGTNGSFQILPGFKREWFSLRTIPPPKPLDPSSGGLGVSAVTGIIVGGILGTALLLAFYFFRKNYRITIERRTLREECDIGKHRQLREDSIRSNFSAA
Protein: Sugar ABC transporter, ATP-binding protein (P71620)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MANVQYSAVTQRYPGADAPTVDNLDLDIADGEFLVLVGPSGCGKSTTLRVLAGLEPIESGRISIGDVDVTHLPPRARDVAMVFQNYALYPNMTVAANMGFALRNAGMSRADTRRRVLEVADMLELTDLLDRKPAKLSGGQRQRVAMGRAIVRRPRVFCMDEPLSNLDAKLRVSTRSQISGLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKDGVLQQVDTPRALYDDPVNTFVATFIGAPAMNLIDAAVAHGVVRAPDLAIPVPDPAAERVLVGVRPESWDVASIGTPGSLTVHVELVEELGFESFVYATPVDQRGWSSRAPRIVFRTDRRTAVRVGESLAIVPHSQEVRLFNSRTETRLR
Protein: Testin (TESS) (Q9UGI8)
Organism: Homo sapiens (Human)
Function: Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth.
Subcellular location: Cytoplasm. Cell junction, focal adhesion. Note=Detected along actin stress fibers.
Interaction partners:
- Protein enabled homolog
- Actin-like protein 7A
- Vasodilator-stimulated phosphoprotein
- Zyxin
- Spectrin alpha chain, non-erythrocytic 1
Sequence:
MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS
Protein: Cadherin FAT1 isoform +32 (A7ISQ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
SWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNASIVTVIHLVNAVVDTVNKEESLAAPDLSKPRGYHWDTSDWMPSVPLPD
Protein: Methylsterol monooxygenase 1 (EC 1.14.18.9) (C-4 methylsterol oxidase) (Sterol-C4-methyl oxidase) (Q15800)
Organism: Homo sapiens (Human)
Function: Catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be subsequently metabolized to cholesterol. Also involved in drug metabolism, as it can metabolize eldecalcitol (ED-71 or 1alpha,25-dihydroxy-2beta-(3-hydroxypropoxy)-cholecalciferol), a second-generation vitamin D analog, into 1alpha,2beta,25-trihydroxy vitamin D3; this reaction occurs via enzymatic hydroxylation and spontaneous O-dehydroxypropylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Lanosterol 14-alpha demethylase
- Ergosterol biosynthetic protein 28 homolog
- Squalene monooxygenase
- Lathosterol oxidase
- Squalene synthase
- Delta
- Delta
- Delta
Sequence:
MATNESVSIFSSASLAVEYVDSLLPENPLQEPFKNAWNYMLNNYTKFQIATWGSLIVHEALYFLFCLPGFLFQFIPYMKKYKIQKDKPETWENQWKCFKVLLFNHFCIQLPLICGTYYFTEYFNIPYDWERMPRWYFLLARCFGCAVIEDTWHYFLHRLLHHKRIYKYIHKVHHEFQAPFGMEAEYAHPLETLILGTGFFIGIVLLCDHVILLWAWVTIRLLETIDVHSGYDIPLNPLNLIPFYAGSRHHDFHHMNFIGNYASTFTWWDRIFGTDSQYNAYNEKRKKFEKKTE
Protein: LOB domain-containing protein 41 (ASYMMETRIC LEAVES 2-like protein 38) (AS2-like protein 38) (Q9M886)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Sequence-specific DNA binding transcription factor
- Plant cysteine oxidase 1
- Rhodanese-like domain-containing protein 17
- Anaerobic nitrite reductase AHB1
- At5g66985
- Plant cysteine oxidase 2
- Pyruvate decarboxylase 1
- At5g10040
- LOB domain-containing protein 24
- At5g02550
Sequence:
MRMSCNGCRVLRKGCSEDCSIRPCLAWIKSPEAQANATVFLAKFYGRAGLMNLINAGPNHLRPGIFRSLLHEACGRIVNPIYGSVGLLWSGNWQLCQDAVEAVMKGEPVKEIATDAATIGQGPPLKIYDIRHISKDDNSAAAATGSTDLKLAKTRRAKRVSTVAIQAESEGKSDEASHDSSLSHQSEIVAAHEGESKESESNVSEVLAFSPPAVKGSGEIKLDLTLRLEPVSRAYHVVPVKKRRIGVFGTCQKESTCKTELML
Protein: MIF4G domain containing (J3QRZ6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQAREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAA
Protein: U6 snRNA-associated Sm-like protein LSm3 (A0A1D8PTG5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365046}.
Interaction partners:
- Sm-like protein
- RNA-binding protein
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm6
- mRNA decay factor PAT1 domain-containing protein
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm4
- Sm protein B
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MSTIQAEQQQDQQPLDLIRFQLDEYVLVKLRGARELKGKLQGYDSHCNMVLSDAEETIYTSNEDDDSENTSEEPIVKKTAMVFVRGDSVILISPIQ
Protein: Nuclear receptor-binding factor 2 (NRBF-2) (Q8VCQ3)
Organism: Mus musculus (Mouse)
Function: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9QYK3}. Cytoplasm {ECO:0000269|PubMed:18619852}. Cytoplasmic vesicle, autophagosome {ECO:0000305}.
Interaction partners:
- Beclin 1-associated autophagy-related key regulator
- Beclin-1
- Phosphoinositide 3-kinase regulatory subunit 4
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- RB1-inducible coiled-coil protein 1
- Activating molecule in BECN1-regulated autophagy protein 1
- UV radiation resistance-associated protein
- Autophagy-related protein 101
- Serine/threonine-protein kinase ULK2
- Serine/threonine-protein kinase ULK1
Sequence:
MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHRKATTYLSEAMKLTESEQAHLSLELQRDSHMKQLLLIQERWKRAKREERLKAQQSTERDGAPHLQAPPRPSEDAEGQSPLLSQPYIPSTERRLPEVQGVFDRDPDTLLFLLQQKNEPSEPCIGSKAPKDDKTIIEEQATKIADLKRHVEFLVAENERLRKENKQLKAEKARLLKGTAEKELDVDADFVEKSELWGLPSHSESAAASSTWQKFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGFMND