wanglab/gogpt-training-data huggingface dataset:
Protein: Cytosol aminopeptidase (EC 3.4.11.1) (Cysteinylglycine-S-conjugate dipeptidase) (EC 3.4.13.23) (Leucine aminopeptidase 3) (LAP-3) (Leucyl aminopeptidase) (Peptidase S) (Proline aminopeptidase) (EC 3.4.11.5) (Prolyl aminopeptidase) (Q9CPY7)
Organism: Mus musculus (Mouse)
Function: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
Interaction partners:
- Aminopeptidase N
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 5 proenzyme
- Glutathione synthetase
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Gamma-glutamylcyclotransferase
- Pyrroline-5-carboxylate reductase 3
Sequence:
MYLLPLPAAARVALRRLGVRGLWDRGLSTADMTKGLVLGIYAKDKDDDLPQFTSAGESFNKLVSGKLREMLNISGPPLKAGKTRTFYGLHQDFPSVVVVGLGKRSAGVDDQENWHEGKENIRAAVAAGCRQVQDLELPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKVAVSAKLHGSGDLEAWEKGVLFASGQNLARHLMESPANEMTPTRFAEIIEKNLKSASSKTKVHIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYMGSPNATEAPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASVETGDRVWRMPLFEHYTRQVIDCQLADVNNLGKYRSAGACTAAAFLREFVTHTKWAHLDIAGVMTNKDEIPYLRKGMSGRPTRTLIEFLLRFSKDSS
Protein: Oxysterol-binding protein 2 (Q5QNQ6)
Organism: Mus musculus (Mouse)
Function: Binds 7-ketocholesterol.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q969R2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q969R2}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:24245814}. Note=Localizes to the equatorial segment of the acrosome following cytoplasmic removal in the developing spermatid. {ECO:0000269|PubMed:24245814}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein A
Sequence:
MGKAAALSRGGGCAGRSRGLSSLFTVVPCLSCHTAAPGMNSSAFGSGPASKPQLQPVQAPERELLSKQVCQPISEPASRSEPGSQTTSVPRPSGVGQESELQGLWPGSENGTRSVSIIKASPELAMPSPLQSTVGSLPVTKPESKLVPKTQSFLRQGQAKISVGTPVSGIGVQMVSPPLDSYKGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRATINLASTHFETEDSCGILLCNGARTYHLKASSEVDRQHWITALELAKAKAIRVMKTQSDDSGDDDEEPAAPADNSELHHTLKTLSLKLNDLSTCNDLIAKHGAALQRSLNELDSLKIPSECGEKLKVVNERATLFRITSNAMINACRDFLELAETHSRKWQRALNYEQEQRVHLEETIEQLAKQHNSLERAFCNTPGGPASSSKSFSEGSFLTSKGENSEEDEDTEYFDAMEDSTSFITVVTEAKEDRKPESGPGTTTVDWTSADNVLDGASFMPKNSCKVKRRVRIPDKPNYSLNLWSIMKNCIGRELSRIPMPVNFNEPLSMLQRLTEDLEYHHLLDKAVNCTSSVEQMCLVAAFSVSSYSTTVHRIAKPFNPMLGETFELDRMEDMGLRSLCEQVSHHPPSAAHHVFSKHGWSLWQEITIASKFRGKYISIMPLGAIHLEFQASGNHYVWRKSTSTVHNIIVGKLWIDQSGDIEIVNHKTKDRCQLKFVPYSYFSKEAARKVTGVVSDSQGKAHYVLSGSWDDQMECSKIVHSSPSSDGRQKTVYQTLPAKLLWRKYPLPENAENMYYFSELALTLNEQEDGVAPTDSRLRPDQRLMERGRWDEANTEKQRLEEKQRLSRRRRLESCTAGCGGEEEKESDGYVPLWFEKRLDPLTGEMACMYKGGYWEAKEKKDWHMCPNIF
Protein: Metal transporter (A2ATX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU369091}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369091}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Transient receptor potential cation channel, subfamily M, member 6.
- Potassium voltage-gated channel subfamily A member 1
- FXYD domain-containing ion transport regulator
- 5'-nucleotidase, cytosolic IIb
- Solute carrier family 12 member 3
Sequence:
MAEQWTAVPTSNMAALNRAGSLTVIFLIVSSCLIKSIDGKDPSEETVIIGLRLEDTDEVSFMDRGFLRVSERSRVRLRVYGQNINNETWSKLAFTEHRSNAPAESLSPGDAPASHPCGIRSSDIIILPTMEVNRKTSGIIELEVKPLRKTEKSKTYYLCTAIGTPGAQDSWSEHTWVYHEGHDTKVIVVEEKKFLLPFWLQVIFIAMLLCLSGMFSGLNLGLMALDPMELRIVQNCGTEKEKHYAKAIEPVRSQGNYLLCSLLLGNVLVNTTLTILLDDIAGSGLIAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMILTFPASYPVSKLLDHVLGQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMISGDAILDFATMSEIMESGYTRIPVYEGERCHIVDLLFVKDLAFVDPDDCTPLKTITKFYSHPLHFVFNDTKLDAMLEEFKKGKSHLAIVQRVNNEGEGDPFYEVLGIVTLEDVIEEIIKSEILDETDLYTDNKTKKKIAHREKKQDFSAFKPTENELRVKISPQLLLATLRFLATEVESFSATQMSEKILLRLLKHPNVIQELKYDDKDKKMSEHYLFHRNKPVDYFILILQGKVEVEAGKEGMKFEAGAFSYYGVLSLTSSPVPLSLSRTFVVSRAESLAGSPENKSPPRPFGLNHSDSLNRSDRMEAVTPTLGSSNNQLNSFLQVYVPDYSVRAVSDLLYIKVTRQQYQNALMASRMDKTPQSTDSEFTKIELTFTEHQDGPLEESATLLTTNSHKPNHTAHNDGVV
Protein: Dehydrodolichyl diphosphate synthase complex subunit SRT1 (EC 2.5.1.87) (Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific)) (Q03175)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular location: Lipid droplet {ECO:0000269|PubMed:11442630}.
Interaction partners:
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- Farnesyl pyrophosphate synthase
- Dolichol-phosphate mannosyltransferase
- Dehydrodolichyl diphosphate synthase complex subunit RER2
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Geranylgeranyl pyrophosphate synthase BTS1
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Squalene synthase ERG9
- Polyprenal reductase
Sequence:
MKMPSIIQIQFVALKRLLVETKEQMCFAVKSIFQRVFAWVMSLSLFSWFYVNLQNILIKALRVGPVPEHVSFIMDGNRRYAKSRRLPVKKGHEAGGLTLLTLLYICKRLGVKCVSAYAFSIENFNRPKEEVDTLMNLFTVKLDEFAKRAKDYKDPLYGSKIRIVGDQSLLSPEMRKKIKKVEEITQDGDDFTLFICFPYTSRNDMLHTIRDSVEDHLENKSPRINIRKFTNKMYMGFHSNKCELLIRTSGHRRLSDYMLWQVHENATIEFSDTLWPNFSFFAMYLMILKWSFFSTIQKYNEKNHSLFEKIHESVPSIFKKKKTAMSLYNFPNPPISVSVTGDE
Protein: CD274 molecule (D4AE25)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Programmed cell death protein 1
- T-lymphocyte activation antigen CD80
- Programmed cell death 1 ligand 2
- Hepatitis A virus cellular receptor 2 homolog
- T-lymphocyte activation antigen CD86
- Tyrosine-protein phosphatase non-receptor type 11
- Inducible T-cell costimulator
- Signal transducer and activator of transcription 3
- Lymphocyte activation gene 3 protein
- T-cell immunoreceptor with Ig and ITIM domains
Sequence:
MRIFAVLIVTACSHVLAAFTITAPKDLYVVEYGSNVTMECRFPVEQKLDLLALVVYWEKEDKEVIQFVEGEEDLKPQHSSFRGRAFLPKDQLLKGNAVLQITDVKLQDAGVYCCMISYGGADYKRITLKVNAPYRKINQRISMDPATSEHELMCQAEGYPEAEVIWTNSDHQSLSGETTVTTSQTEEKLLNVTSVLRVNATANDVFHCTFWRVHSGENHTAELIIPELPVPRLPHNRTHWVLLGSVLLFLIVGFTVFFCLRKQVRMLDVEKCGFEDRNSKNRNDTQFEET
Protein: Mitochondrial intermembrane space cysteine motif-containing protein MIX17 (Mitochondrial intermembrane space CX(n)C motif protein of 17 kDa) (Q03667)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:17095012, ECO:0000269|PubMed:22984289}. Note=Imported into mitochondrion intermembrane space through the MIA pathway.
Interaction partners:
- Mitochondrial intermembrane space cysteine motif-containing protein MIX14C motif protein of 14 kDa)
- Mitochondrial intermembrane space import and assembly protein 40
- Cytochrome c oxidase assembly protein COX19
- Cytochrome c oxidase copper chaperone
- Mitochondrial distribution and morphology protein 35
- Mitochondrial protein PET191
- Cytochrome c oxidase subunit 12, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM13
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
Sequence:
MARSRGSSRPISRSRPTQTRSASTMAAPVHPQQQQQPNAYSHPPAAGAQTRQPGMFAQMASTAAGVAVGSTIGHTLGAGITGMFSGSGSDSAPVEQQQQNMANTSGQTQTDQQLGRTCEIDARNFTRCLDENNGNFQICDYYLQQLKACQEAARQY
Protein: BZIP domain-containing protein (G5EAS5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAATISAASVARQITAYLDISPHSFSDSDFLFSSNSSLSSSSTPALFPDLSAAFPPVDLDPNAPQLFYDPLLVPSVFPGDPASSSGSDQFNDLTTAAGYPSITTTTADDIDWTALGCLPQSEHPANSLGSQSQGLTPSVDSPDPPFNSTQPRILTTDLSTTHITTTKPIQPQPMPSVTSLSTSRESSPKEKEHLSRITKRQLNTLAARRYRQRKLDKVAQLEEELAAVKRERDELKMRVSKLEGETEVLRSMVKDKN
Protein: Sodium/potassium/calcium exchanger 3 (Na(+)/K(+)/Ca(2+)-exchange protein 3) (Solute carrier family 24 member 3) (Q9HC58)
Organism: Homo sapiens (Human)
Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26631410}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRPSGDEDRARRRRRRRRRRDLLLSQLCFLASVALLLWSLSSLREQKELDLMDLVGEDRKWMMARKLMQVNDTLTSEDAGLRNSKNCTEPALHEFPNDIFTNEDRRQGAVVLHVLCAIYMFYALAIVCDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVALSSWCLLRDSIYYTLSVIALIVFIYDEKVSWWESLVLVLMYLIYIVIMKYNACIHQCFERRTKGAGNMVNGLANNAEIDDSSNCDATVVLLKKANFHRKASVIMVDELLSAYPHQLSFSEAGLRIMITSHFPPKTRLSMASRMLINERQRLINSRAYTNGESEVAIKIPIKHTVENGTGPSSAPDRGVNGTRRDDVVAEAGNETENENEDNENDEEEEEDEDDDEGPYTPFDTPSGKLETVKWAFTWPLSFVLYFTVPNCNKPRWEKWFMVTFASSTLWIAAFSYMMVWMVTIIGYTLGIPDVIMGITFLAAGTSVPDCMASLIVARQGMGDMAVSNSIGSNVFDILIGLGLPWALQTLAVDYGSYIRLNSRGLIYSVGLLLASVFVTVFGVHLNKWQLDKKLGCGCLLLYGVFLCFSIMTEFNVFTFVNLPMCGDH
Protein: Lengsin (Glutamate-ammonia ligase domain-containing protein 1) (Lens glutamine synthase-like) (Q8CIX8)
Organism: Mus musculus (Mouse)
Function: May act as a component of the cytoskeleton or as a chaperone for the reorganization of intermediate filament proteins during terminal differentiation in the lens. Does not seem to have enzymatic activity.
Interaction partners:
- Glutamate dehydrogenase 1, mitochondrial
Sequence:
MTDEGDLAQEDTAKDEGNVTEGSRMSKLRRARRKVTKPHLCSMDGEEIAKANSSEMSRNQIADLSKPGSAESWSSHSAKDAYHPTPVVKPSLPSALAGAPDAEFSPNTDPTRYNAQSFNPPQLSARMKHIKQEMAKNHLQFVRFEATDLHGVSRSKSIPAQFFQEKVIHGVFMPRGYLELMPNPKDNEVNHIRATCFNSDIVLMPELSTFRVLPWAERTARVICDTFTVTGEPLLTSPRYIAKRQLRQLQDAGFCLLSAFIYDFCIFGVPEVINSKTISFPASTLLSNHDQPFMQELVEGLYQTGANVESFSSSTRPGQMEICFLPEFGISSADNAFTLRTGLQEVARRYNYIASLVIETGFCNSGILSHSIWDVGGKTNMFCSGSGVERLTLTGKKWLAGLLKHSAALSCLMAPAVNCRKRYCKDSRDLKDSVPTTWGYNDNSCALNIKCHGEKGTQIENKLGSATANPYLVLAATVAAGLDGLQSSDGAAAGSDESQDLYQPEPSEIPLKMEDALAALEQDECLKQALGETFIRYFVAMKKYELENEETDAEGNKFLEYFI
Protein: Mediator of RNA polymerase II transcription subunit 6 (Mediator complex subunit 6) (A0A8I6GLU7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR023869}.
Interaction partners:
Sequence:
MAAVDIRDNLLGISWVDSSWIPILNSGSVLDYFSERSNPFYDRTCNNEVVKMQRLTLEHLNQMVGIEYILLHAQEPILFIIRKQQRQSPAQVIPLADYYIIAGVIYQAPDLGSVINSRVLTAVHGIQSAFDEAMSYCRYHPSKGYWWHFKDHEEQDKVKPKAKRKEEPSSIFQRQRVDALLIDLRQKFPPRFVQVIRMCLDQAKKEAEPLPETVKSEEKESAKSAQQTVSTKGPPEKRMRLQ
Protein: Uncharacterized protein (F4K1C7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein NPGR1
- Protein NPGR2
- Hyccin
- At5g64090
- Phosphatidylinositol 4-kinase alpha 1
- Protein NPG1
- Phosphatidylinositol 4-kinase alpha 2
Sequence:
MGFISRNVFPACESMCICCPALRSRSRQPVKRYKKLLGEIFPKSPDGGPNERKIVKLCEYAAKNPIRIPKIAKFLEERCYKDLRSEQMKFINIVTEAYNKMLCHCKDQMAYFATSLLNVVTELLDNSKQDTPTILGCQTLTRFIYSQVDGTYTHSIEKFALKVCSLAREEGEEHQKQCLRASGLQCLSAMVWYMGEFSHIFATVDEIVHAILDNYEADMIVQTNEDREEQNCNWVNEVIRCEGRGTTICNSPSYMIVRPRTARKDPTLLTKEETEMPKVWAQICLQRMVDLAKESTTLRQILDPMFSYFNSRRQWTPPNGLAMIVLSDAVYLMETSGSQQLVLSTVVRHLDNKHVANDPELKAYIIQVAGCLAKLIRTSSYLRDISFVNDLCRHLRKSFQATARSIGDEELNLNVMIQNSIEDCLREIAKGIVNTQPLFDMMAVSVEGLPSSGIVSRAAVGSLLILAHAMSSALSPSMRSQQVFPDTLLDALLKAMLHPNVETRVGAHEIFSVILLQSSGQSQAGLASVRASGYLNESRNWRSDTTSAFTSVTARLDKLRKEKDGVKIEKNGYNNTHEDLKNYKSSPKFHKLNSIIDRTAGFINLADMLPSMMKFTEDQIGQLLSAFWIQSALPDILPSNIEAIAHSFSLVLLSLRLKNPDDGLVVRAFQLLFSLRTLSLDLNNGTLPSVCKRLILALSTSMLMFAAKIYQIPHICEMLKAQLPGDVDPYLFIGDDLQLHVRPQANMKDFGSSSDSQMATSMLFEMRSKVELSNTIITDIVAKNLPKLSKLEEADVKMQILEQFTPDDAFMFGSRPNIEPQPNQSISKESLSFDEDIPAGSMVEDEVTSELSVRFPPRGSPSPSIPQVISIGQLMESALEVAGQVVGSSVSTSPLPYDTMTNRCETFGTGTREKLSRWLATENRQMNGLYGNSLEESSALEKVVEDGNIYGRESGMLQDSWSMMRLPPASPFDNFLKAAGAGR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VEN3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cerebral cavernous malformation 3
- Connector of kinase to AP-1, isoform E
- Protein Mo25
- MOB kinase activator-like 4
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- AT25231p
- FGFR1 oncogene partner 2 homolog
- CTTNBP2 N-terminal-like protein
- Serine/threonine-protein kinase tricornered
Sequence:
MSWTEKVDPELIFTKQERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDEIDDIQQEIMVLSQCDSPYVTKYYGSFLKGTKLWIIMEYLGGGSALDLMKAGSFEEMHIGIILREVLKGLDYLHSERKLHRDIKAANVLLSEQGDVKLADFGVAGQLTNTTSKRNTFVGTPFWMAPEVIKQSQYDAKADIWSLGITAIELAKGEPPNSELHPMRVLFLIPKNNPPQLTGSYTKSFKDFVEACLNKDPENRPTAKELLKYPFIKKAKKNAYLIDLIDRFKKWKVSKGDESETESENSDSDSDAKQGGSSQDEPWIMTVKGLHINSAPRAGVNSFQLQEHELTMQKLMQTTHSPAGGGGVQASPAANALSSSVSAVAASASSVSVITANEGVSSASALPPQNSHVHNHNHNNINNNNIRNLSNKHATTTMLNAAPPPSSVTSSSSASELQQKRSSSKPELRQSRSAAPLDQVEDRRASLGLPLQSSVPTPSTAEQQQQRRSSQRESFHANNAALVASCSSSSNNHSHEEHVATNHASHVKHSGAGQRLVQTNSACLNNFLFPVLSDIQRKYSGGGSAGSGGSGGRNIGVGSDIGDLKSVFELAERSSPGVSDLFMKELIHMLVPGYSETRINTIMDRAIRNRK
Protein: Centromere protein I (CENP-I) (FSH primary response protein 1) (Follicle-stimulating hormone primary response protein) (Leucine-rich primary response protein 1) (Q63517)
Organism: Rattus norvegicus (Rat)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Required for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to kinetochores. Involved in the response of gonadal tissues to follicle-stimulating hormone (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). {ECO:0000250}.
Interaction partners:
- Centromere protein K
- Centromere protein H
- Centromere protein M
- Centromere protein N.
- Centromere protein O
- Centromere protein P
- Centromere protein T
- Centromere protein Q
- Centromere protein L
- Centromere protein R
Sequence:
MATPRLTRNSQQQNRISQGSNSRQTTLLDWKVKDKAGNSKSVLEESSSLEDSNHADDQTEDALQTAVEYFQKGPKKASLSKDSVLEKHLKTVENVAWNNGLAPEAIDILLNVALSGKFGNALSTRILKCMIPETHISEDSVVKAVSWLCVGKCSGNTKVLFYRWLVAMFDFIDHKKQINSLYGFFFVSLQDDTLCPYVCHLLYLLTKKENVKPFRARKLLDLQAKMGMQPHLQALLSLYKFFAPTLISVSLPVRKKIFFNNSKNLWTPALLAVKLRNQGIFPEPLKLQLGPTSGRSLKRKWNYHSVIPAVNSAKKECREKMSLFDYLSNDRSLPVEQLQSFPQLLENIHCLELPSQMSSVLNSSLLLHYVNCVKDESILLRLSYWLSQTLQEECVWYNMNDYQQEKEFINFLDMVIRVQCFLQEGFYSCEAFLYKSLPLWDGFSCRSQFLKLLAWIPFSSFSEIKPLLLDHLAPLFFTSSIYFKCSLLQCLKDLLQNWLLWLSTEAQVQPMTDSPLETTLGGSMDSVSQLIEYIGWLSMVAIRLESSSTLLVHFILDFYEKVCDIYINYDLPLVVLFPPVVFHSAFLSLDATILNQLCYIMYRYRDNLTAAKKKDLVQKAKSEFSISSKICKEFNYYLTALVHCLWSSRPFETGVYIDPQIIENTGETQYKHNLNFVHHPCLLNYAASFLLQESPEEMPVHLSSIRGKKWNWYLDHLYSEGFQGLNLFIKSSIDHSSVSKTEKNT
Protein: Olfactory receptor 960 (Olfactory receptor MOR224-12) (Olfactory receptor family 10 subfamily D member 4B) (Q8VET5)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MNMTNNTMVTEFTLLGIPETEGLENVLLFLFSTLYACALLGNLLLLTAVTSSPRLHTPMYFFLSNLSISDMGFCSTTAPKMLSYLSGRGGGISFQGCVVQHFFYHCIGCVLCFLYTVMAYDRFVAICFPLRYTIIMNHRVCCVLATGTWMSGCVHATILTCLTFQLPYCGPSEVSYYFCDMPAVLLLACEDSSLAQRVGFTNVGLLSLICFFLIVVSYTRIGISISKIRSTEGRQRAFSTCSAHLTAIMCVYGPVIVIYLQPNPSPLLSAIIQIFNNLVTPTINPLIYSLRNKDVKAALRHVFLKRCLSLEVNENI
Protein: Cell division cycle protein 48 (EC 3.6.4.6) (Transitional endoplasmic reticulum ATPase homolog) (Q9P3A7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates. By recruiting and promoting the degradation of ubiquitinated proteins, plays a role in the ubiquitin fusion degradation (UFD) pathway. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway which mediates the cytoplasmic elimination of misfolded proteins exported from the ER. Involved in spindle disassembly. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. CDC48 may provide the mechanical force that dislodges the polyubiquitinated nascent peptides from the exit channel. Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- UBX domain-containing protein 3
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- Uncharacterized derlin-like protein C365.08c
- Putative ubiquitin thioesterase otu1
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- ERAD-associated E3 ubiquitin-protein ligase doa10
- Protein OS-9 homolog
- Ubiquitin conjugation factor E4
- Ubiquitin homeostasis protein lub1
Sequence:
MNAPSTMTDKKPEVEHLQGENPPKDTYSAEDTATAILRKKRKPNSLVVDDATNDDNSVITLSSNTMETLQLFRGDTVVVKGKRRKDTVLIVLTDEEMEDGVARINRVVRNNLRVRLGDIVTINPCPDIKYAERISVLPLADTVEGLTGSLFDVYLKPYFVEAYRPIRKGDLFVVRGSMRQVEFKVVDVAPDEFGIVSQDTIIHWEGEPINREDEESSLAEVGYDDIGGCRRQMAQIRELVELPLRHPQLFKSIGIKPPRGILMYGPPGTGKTLMARAVANETGAFFFLINGPEIMSKMAGESESNLRKAFEEAEKNSPAIIFIDEIDSIAPKREKTNGEVERRVVSQLLTLMDGMKARSNVVVMAATNRPNSIDPALRRFGRFDREVDVGIPDPTGRLEILRIHTKNMKLADDVDLEQIAAETHGYVGSDLASLCSEAAMQQIREKMDMIDLDEDEIDAEVLDSLGVTMDNFRFALGSSNPSALRETVVEVPNVRWEDIGGLEEVKRELRETVQMPVMYAEKFLRFGVTPSKGVLFFGPPGTGKTLLAKAIANECSANFISVKGPELLSMWFGESESNVRDIFDKARAAAPCVVFLDELDSIAKARGASAGDSGGGDRVVNQLLTEMDGVNSKKNVFVIGATNRPDQIDPALMRPGRLDQLIYVPLPDEEARFSILQTQLRHTPVAEDVDLRAVAKATHGFSGADLEFVVQRAVKLAIKDSIEEDIKRENETGEAPADDVVMDEDASVSQVQRHHVEEAMKMARRSVSDAEVRRYEAYAHQLLTSRGLTGFQFDSADSNTNGPSFGNDGADDLYA
Protein: Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (hSPP1) (hSPPase1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1) (Sphingosine-1-phosphate phosphohydrolase 1) (SPP-1) (Q9BX95)
Organism: Homo sapiens (Human)
Function: Specifically dephosphorylates sphingosine 1-phosphate (S1P), dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate, lysophosphatidic acid or phosphatidic acid. Sphingosine-1-phosphate phosphatase activity is needed for efficient recycling of sphingosine into the sphingolipid synthesis pathway. Regulates the intracellular levels of the bioactive sphingolipid metabolite S1P that regulates diverse biological processes acting both as an extracellular receptor ligand or as an intracellular second messenger. Involved in efficient ceramide synthesis from exogenous sphingoid bases. Converts S1P to sphingosine, which is readily metabolized to ceramide via ceramide synthase. In concert with sphingosine kinase 2 (SphK2), recycles sphingosine into ceramide through a phosphorylation/dephosphorylation cycle (By similarity). Regulates endoplasmic-to-Golgi trafficking of ceramides, resulting in the regulation of ceramide levels in the endoplasmic reticulum, preferentially long-chain ceramide species, and influences the anterograde membrane transport of both ceramide and proteins from the endoplasmic reticulum to the Golgi apparatus. The modulation of intracellular ceramide levels in turn regulates apoptosis (By similarity). Via S1P levels, modulates resting tone, intracellular Ca(2+) and myogenic vasoconstriction in resistance arteries. Also involved in unfolded protein response (UPR) and ER stress-induced autophagy via regulation of intracellular S1P levels. Involved in the regulation of epidermal homeostasis and keratinocyte differentiation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12815058}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9JI99}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingosine kinase 2
- Sphingosine-1-phosphate lyase 1
- Sphingosine kinase 1
- Ceramide synthase 4
- Acid ceramidase
- Ceramide synthase 6
- Ceramide synthase 2
- Alkaline ceramidase 3
- Ceramide glucosyltransferase
- Ceramide synthase 5
Sequence:
MSLRQRLAQLVGRLQDPQKVARFQRLCGVEAPPRRSADRREDEKAEAPLAGDPRLRGRQPGAPGGPQPPGSDRNQCPAKPDGGGAPNGVRNGLAAELGPASPRRAGALRRNSLTGEEGQLARVSNWPLYCLFCFGTELGNELFYILFFPFWIWNLDPLVGRRLVVIWVLVMYLGQCTKDIIRWPRPASPPVVKLEVFYNSEYSMPSTHAMSGTAIPISMVLLTYGRWQYPLIYGLILIPCWCSLVCLSRIYMGMHSILDIIAGFLYTILILAVFYPFVDLIDNFNQTHKYAPFIIIGLHLALGIFSFTLDTWSTSRGDTAEILGSGAGIACGSHVTYNMGLVLDPSLDTLPLAGPPITVTLFGKAILRILIGMVFVLIIRDVMKKITIPLACKIFNIPCDDIRKARQHMEVELPYRYITYGMVGFSITFFVPYIFFFIGIS
Protein: 23S rRNA (uracil(747)-C(5))-methyltransferase RlmC (EC 2.1.1.189) (23S rRNA(m5U747)-methyltransferase) (P75817)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase F
- Inner membrane protein YbjO
Sequence:
MQCALYDAGRCRSCQWIMQPIPEQLSAKTADLKNLLADFPVEEWCAPVSGPEQGFRNKAKMVVSGSVEKPLLGMLHRDGTPEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDTKLAQLRKALPWLHEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDVPELVLVNPPRRGIGKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELPGFRIERVQLFDMFPHTAHYEVLTLLVKQ