wanglab/gogpt-training-data huggingface dataset:
Protein: Muscarinic acetylcholine receptor M3 (P20309)
Organism: Homo sapiens (Human)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21056967}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15870063}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21056967}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with TMEM147 in the endoplasmic reticulum (ER) membrane. TMEM147 impairs its trafficking to the cell membrane leading to its retention in the ER membrane. {ECO:0000269|PubMed:21056967}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Muscarinic acetylcholine receptor M5
- Metabotropic glutamate receptor 5
- Guanine nucleotide-binding protein G
- Muscarinic acetylcholine receptor M1
- Guanine nucleotide-binding protein subunit alpha-11
- Kininogen-1
- Guanine nucleotide-binding protein subunit alpha-15
- Type-1 angiotensin II receptor-associated protein
Sequence:
MTLHNNSTTSPLFPNISSSWIHSPSDAGLPPGTVTHFGSYNVSRAAGNFSSPDGTTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPTGSSRSCSSYELQQQSMKRSNRRKYGRCHFWFTTKSWKPSSEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGMVDLERKADKLQAQKSVDDGGSFPKSFSKLPIQLESAVDTAKTSDVNSSVGKSTATLPLSFKEATLAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQAL
Protein: Zinc finger protein HER (O61373)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSADRDSVEEEYGSCSAWKFRCSVDRCPYRTNRPYNLARHEESHIGITQSKLYGCPVCVYNTDKASNLKRHVSIKHPGCKKRPPEAQHKDRNAKLQCLVMGCRYETNRPYDLKRHLMVHNNPEKSHRTFKCSLCTYSSDRKANLKRHHELRHSGIEEAIQTAEELRQEMLLEKQMLKEHKLKYQITEKQDLKNLKLKDQKQKVQMLRDQQPKQRQKKEQLLEDQSPVLNKQLEHGNIPLKEALVGSMKYDEESLEFVYEELQDEEQPPIITISNPQILHGDIRDKHVIAVNVDGQLRWFQSIDPPPGAPTKLELPIKSTSISVQQQMDELDDELAMSLAEEDQQDEFLVPMLSGEEPVKIKQSSLTDLAWSWSTPDAVHHISPKAELKKDLKAGDADTDFPDWWDDGKYTKMQKNQTFAKHSKKPSQENVQRILRIIYDIYYKPFKEDRKQFEAFQIKDSWLCATRMTRMQIIKDMYSKQGTLSQT
Protein: Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic (PPIase CYP28) (EC 5.2.1.8) (Cyclophilin of 28 kDa) (Cyclophilin-28) (O65220)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:11719511}.
Interaction partners:
- UPF0235 protein At5g63440
- Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic
- Large ribosomal subunit protein uL3c
- Inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Peptidyl-prolyl cis-trans isomerase FKBP17-2, chloroplastic
- ENHANCED DISEASE RESISTANCE protein
- Adenylate kinase 5, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP16-4, chloroplastic
- Putative methyl-CpG-binding domain protein 12
- Thylakoid lumenal protein TL20.3
Sequence:
MASSSILIPPILTRRNLLLSTTIATVTPPPPAKPPSPDITITDRVFLDFSLCPTYFRSDPSATLSSTTPCSDSTPLGRVVLGLYGRHVPITVSTFKRMCTSSSTSYKNTPVHKIFPGQYFLAGRQGGGRRDTAEVGYSLRDLPRNTDVVNSKAFLLPHARAGVVSLCLSENDDDDDIRLDPDYRNVEFLITTGPGPSPQLDGGNIVFGTVLEGLDVVTSISSIPTYKPSENIKQFNDFAEFLGDERAQNARSLWNRPLKTVFISGCGELKVTNPSLSPTLP
Protein: Zinc finger CCHC domain-containing protein 24 (Q8N2G6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLLSAIDTSAASVYQPAQLLNWVYLSLQDTHQASAFDAFRPEPTAGAAPPELAFGKGRPEQLGSPLHSSYLNSFFQLQRGEALSNSVYKGASPYGSLNNIADGLSSLTEHFSDLTLTSEARKPSKRPPPNYLCHLCFNKGHYIKDCPQARPKGEGLTPYQGKKRCFGEYKCPKCKRKWMSGNSWANMGQECIKCHINVYPHKQRPLEKPDGLDVSDQSKEHPQHLCEKCKVLGYYCRRVQ
Protein: Coiled-coil domain-containing 141 (Q8BLD3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSCKESPHVGASTTTVSSVAVHAGDSKIVIAVVKCGKWVRLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLREADRTAEANKAQSQVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEAFLQNPHEFESTEALQSLLLLHDRHAKELLERSLDLLNKSQQLTDFIEKFKCEGSTMNSELIQGAQSSCLKIDSLLELLQDRRRQLDKYLQQQRQELSQVLQLCLWDQQENQVSSWFQKAIRDLQEQSLGASLSDNRELICKHEDLIVKAKEWDSAVEKLKSQALGILLSKDLAGKEHLQLSNQKLNRLQEEFGRLMVERKAWLSMANDFFTSANKSFDVLGKVEAYLKLLKSEGLSLPVLAAKHEELHREIKDSTATALQKGRTLISQVDSCRSRVTGIHEMMGYIQNRVDCLTEQCTAHEEFTRKRQQLATSVDDYLRKVEMSIQEIRPILATTLDVASSPSESEKILNKYLELDIQVKETAHALEAAAKIMTEKNELELNEVALLPLKVKWLEEELSTLGRSISCRSRILQTYVAFRKSSEEAEEQLQSLKEFYLTEIPWKDEDDAVVKCQSNSAERKWQLFLKKSFLTQDLSLEFLNLINMAKENEILNVKNEMHIMENIMEK
Protein: Tryptophan--tRNA ligase, cytoplasmic (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) (Q9SR15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, chloroplastic/mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, chloroplastic/mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MEVDKKDEREAESSEQVVNPWEVSAKDGGKIDYDKLIDKFGCQRLDESLIDRVQRLTSRQPHVFLRRSVFFAHRDFNEILDAYERGDKFYLYTGRGPSSEALHLGHLIPFMFTKYLQEAFKVPLVIQLTDDEKSIWKNLSVEESQRLARENAKDIIACGFDVTKTFIFSDFDYVGGAFYKNMVKVGKCVTLNKAMGIFGFSGEDPIAKLSFPPVQAVPSFPSSFPHLFPGKDNLRCLIPCAIDQDPYFRMTRDVAPRLGYSKPALIESTFFPALQGENGKMSASDPNSAIYVTDSAKDIKNKINRYAFSGGQDSIEKHRELGANLEVDIPVKYLSFFLEDDSELEHIKKEYGEGRMLTGEVKKRLTEVLTEIVERHRRARAAVTDEMVDAFMAVRPLPSMFE
Protein: Transmembrane emp24 domain-containing protein 3 (p24 family protein gamma-4) (p24gamma4) (Q6AY25)
Organism: Rattus norvegicus (Rat)
Function: Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network (By similarity).
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:11739402}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y3Q3}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:15718469}; Single-pass type I membrane protein {ECO:0000255}. Note=Probably cycles between compartments of the early secretatory pathway. {ECO:0000250|UniProtKB:Q9Y3Q3}.
Interaction partners:
- Coatomer subunit beta
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 2
- Transmembrane emp24 domain-containing protein 9
- Transmembrane emp24 protein transport domain containing 11
- Coatomer subunit zeta
- Mitochondrial ribosomal protein S35
- Coatomer subunit zeta
- Small ribosomal subunit protein mS29
- Coatomer subunit beta'
Sequence:
MGNEVPRASSFQMLMLLLLLLLLRAERLRGAELTFELPDNAKQCFHEEVEQGVKFSLDYQVITGGHYDVDCYVEDPMGNIIYRETKKQYDSFTYKTEVKGVYRFCFSNEFSTFSHKTVYFDFQVGDEPPILPDMGNRVTALTQMESACVTIHEALKTVIDSQTHYRLREAQDRARAEDLNSRVSYWSVGETIALFVVSFSQVLLLKSFFTEKRPINRAVHS
Protein: Prolactin-2B1 (Placental prolactin-like protein K) (PLP-K) (PRL-like protein K) (Q9JKL9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- CEA-related cell adhesion molecule 12
- Cathepsin Q
- Carcinoembryonic antigen-related cell adhesion molecule 11
- Ctsq protein-like
- Trophoblast specific protein alpha
Sequence:
MLLYLPQIFSSRASSLLFLVPYLLFWENVASISTCAERDATIQHSLEKLLTLTTFMSHVMSIETAKLFTEFNNQYAQGKRYNDRIPGTCHTAFFDTPVNKEQSLGSDPKTLLKLVRSLLNSWTNALNHLVNEISAMQGDPSFLFSKAREIQAKFDELTTGVKTILSMIGERDNDTHLAWSGLSSLQSSNEDVRCFSFYTLIRCLLRDSRKVNTYLEVIKYQIFNQNNC
Protein: Large ribosomal subunit protein P1B (60S acidic ribosomal protein P1-B) (CaRP1B) (Q9HFQ6)
Organism: Candida albicans (Yeast)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
Sequence:
MSTEASVSYAALILADAEQEITSEKLLAITKAAGANVDQVWADVFAKAVEGKNLKELLFSFAAAAPASGAAAGSASGAAAGGEAAAEEAAEEEAAEESDDDMGFGLFD
Protein: NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (RL/IF-1) (Q63746)
Organism: Rattus norvegicus (Rat)
Function: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25963}. Nucleus {ECO:0000250|UniProtKB:P25963}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. {ECO:0000250|UniProtKB:P25963}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B inhibitor beta
- NF-kappa-B essential modulator
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- S-phase kinase-associated protein 1
- REL proto-oncogene, NF-kB subunit
- Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, p49/p100, isoform CRA_a.
Sequence:
MFQPAGHGQDWAMEGPRDGLKKERLVDDRHDSGLDSMKDEDYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKTLTMEVIGQVKGDLAFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHLASIHGYLGIVEHLVTLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQTLPESEDEESYDTESEFTEDELPYDDCVFGGQRLTL
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (Q5PPJ6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Glutamine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Sequence:
MAERKGTAKVDFLKKIEKEVQQKWEAEKVFEVSASSLEKQKQSSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKSCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPEEEEEEEESSAKPGDIVMKDKAKGKKSKAAAKAGSSKYQWNIMKSLGLSDEDIAKFSEAEHWLDYFPPLAVQDLKKIGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLVKLKVLDPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETANGDIFICTQRAARNMSYQGFTKHNGVVPVVKELMGEEILGASLSAPLTCYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDFAALRDLKKKQALRAKYAVRDDMVLPFEPVPVLEIPGIGNLPAVTVCDELKIQSQNDREKLAEAKEKLYLRGFYDGVMLVDGFKGQKIQHVKKTIQKNMIDAGDALIYMEPEKQVVSRSADECVVALCDQWYLDYGDENWKKQTFQCLKNMETFCEESRKNFEASLDWLQEHACSRTYGLGTRLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGDLQGQAESPLGIRPQQMTRDVWDYVFFKDAPFPKTQIPKEKLDQLKQEFEFWYPVDLRASGKDLIPNHLSYYIYNHVAMWPEQSDKWPVSVRANGHLLLNSEKMSKSTGNFLTLSQAVDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMLANCSSLRSGPANSFNDRVFASEMNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELATEGMHRELVFRFIEVQTILLTPFCPHLCEHIWTLLGKPDSIMHASWPVAGPVDESLIRSSQYLMEVAHDLRLRLKNYMTPAKGKKTDKQPVQRPSHCTIYVAKNYPVWQHITLTTLRSHFEANNGKLPDNKVIACELGSLPELKKYMKKVMPFVAMIKENMEKKGPRVLDLELEFDEQAVLMENIVYLTNSLELEHIDVKFASEAEDKVREECCPGKPLNVFRTEPGVPVSLVNPQPSSGHFSTKIDIRQGDSCESIIRRLTKMDRGIKDLSKVKLMRFDDPLLGPRRVPVLGREQNEKTLISENAIFHVDLVSKKVHLTENGLRADIGDTIVYLVH
Protein: Uncharacterized protein YibL (P0ADK8)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16980477}. Note=Has been seen to comigrate with the 50S ribosomal subunit in sucrose gradients.
Interaction partners:
- Putative RNA-binding protein YbcJ
- Ribosomal large subunit pseudouridine synthase B
- Mannitol operon repressor
Sequence:
MKEVEKNEIKRLSDRLDAIRHQQADLSLVEAADKYAELEKEKATLEAEIARLREVHSQKLSKEAQKLMKMPFQRAITKKEQADMGKLKKSVRGLVVVHPMTALGREMGLQEMTGFSKTAF
Protein: Syntaxin-71 (AtSYP71) (Q9SF29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway.
Subcellular location: Membrane {ECO:0000269|PubMed:15060130}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
- Novel plant SNARE 11
- Syntaxin-121
- Syntaxin-132
- Vesicle-associated membrane protein 721
- Syntaxin-related protein KNOLLE
- Novel plant SNARE 13
- SNAP25 homologous protein SNAP33
- Novel plant SNARE 12
- Syntaxin-81
- 25.3 kDa vesicle transport protein SEC22-1
Sequence:
MTVIDILTRVDSICKKYDKYDVDKQREANISGDDAFARLYGAFETQIETALEKAELVTKEKNRAAAVAMNAEIRRTKARLSEEVPKLQRLAVKRVKGLTTEELAARNDLVLALPARIEAIPDGTAGGPKSTSAWTPSSTTSRPDIKFDSDGRFDDDYFQESNESSQFRQEYEMRKIKQEQGLDMISEGLDALKNMASDMNEELDRQVPLMDEIDTKVDRATSDLKNTNVRLKDTVNQLRSSRNFCIDIVLLCIVLGIAAYLYNVLK
Protein: M protein (Q6V4L1)
Organism: Streptococcus pyogenes
Subcellular location: Secreted, cell wall {ECO:0000256|PROSITE-ProRule:PRU01372}; Peptidoglycan-anchor {ECO:0000256|PROSITE-ProRule:PRU01372}.
Interaction partners:
Sequence:
RKLKTGTASVAVALTVVGAGLASQTEVKAENHPGYTAAQNGVLSELPGQAQAFSRAFLHEREKNGELRLENEGLKTDLKKKEQELESLKGDVEKLKDEVALERLKNERHVHDEEAELERLKNERYEHDKKEAERKALEDKLADKQEHLNGALRYINEKEAERKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQVSDASRQGLRRDLDASREAKKKVEADLAALTAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAEANSKLQALEKLNKELEEGKKLSEKEKAELQARLEAEAKALKEQLAKQAEELAKLRAGKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT
Protein: Cytohesin-1 (PH, SEC7 and coiled-coil domain-containing protein 1) (SEC7 homolog B2-1) (Q15438)
Organism: Homo sapiens (Human)
Function: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization, through regulation of ARF6 activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17398095}; Peripheral membrane protein {ECO:0000269|PubMed:17398095}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9QX11}. Note=Colocalized with TJP1 during epithelial polarization. {ECO:0000250|UniProtKB:Q9QX11}.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor 6
- Cytohesin-interacting protein
- Cyclin-dependent kinase inhibitor 2A
- Integrin beta-2
- Pleckstrin
- FERM domain-containing protein 4A
- Pleckstrin-2
- Guanine nucleotide exchange factor MSS4
- Cytohesin-2
Sequence:
MEEDDSYVPSDLTAEERQELENIRRRKQELLADIQRLKDEIAEVANEIENLGSTEERKNMQRNKQVAMGRKKFNMDPKKGIQFLIENDLLKNTCEDIAQFLYKGEGLNKTAIGDYLGERDEFNIQVLHAFVELHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCQCNNGVFQSTDTCYVLSFAIIMLNTSLHNPNVKDKPTVERFIAMNRGINDGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDSKKPNCFELYIPDNKDQVIKACKTEADGRVVEGNHTVYRISAPTPEEKEEWIKCIKAAISRDPFYEMLAARKKKVSSTKRH
Protein: Metal transporter cnnm-2 (CNNM family homolog 2) (Q9GYL2)
Organism: Caenorhabditis elegans
Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-3, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cubilin homolog
- Probable GMP synthase
Sequence:
MIIKVFLRLLLLCAHIVCIDGKLEIRPVVSGVRIESDVDASGFLGYGDAGELLVEANTEVDLVIFGHGLENVEMVTFTDSVCVTSEFNVSESTFYIHKDMKIVFKYAFVAWPQPWRICLKSECHGLIQIDDDRTWIQAVQSTHETFMPVWAQCAILCLLFSISALCSGLTLGLMALTPQELSILMKSGSQREKKHAAAIYPIRCHGNRLLCTVIIMNVIVNTGITLLFDDLAEGLIAFVASTVGIVVFGEILPQSICVKYGLAVGANTIFITKFFMFLLFPITWPLGKILDKYAGVDIDVVNRSRMVEMLKMNMENDACDIDLSTLKIAIGAMELTKKSVRDVMTDIDDVFMLSEDQVLNAETMTKISDSGYTRIPVFEGNNRNKVKNLLYVSDLALIGKDNNITVKAVARFNKRRLRIVDESMPLTALMDEFKLGDYHLAMVAKATEVKKHHHGKFADGTVDSFILKSMKLVEATMMPQVENPEDHPVTLVGLITLEDITEELLQAEITDETDCYVTDDAQKKRRTNTSKKSAAELFCSEKKSERLSLHMLEMTEKWLLEKTPLFGNMNPKAFENLIQRNIREVLIVPPKNSTSPGTLNLFEAGVMSKRFLLILEGKATIRFNEKDLIFECGPWTCFGEAILEKMEMCISDRKEPSTGFFFLPDYNLTVSGPCRFLQISTSSLLHSLRITQFVKEIRTPKISITSDDDFGSPTRKASILDSSPNSRKRSSTSVMNSLALPTARLAAKIASVEELKPLME
Protein: Rap guanine nucleotide exchange factor 1 (A0A8I6A6H6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LSSGLGLRRSPEMSGKIEKADSQRSHLSSFTMKLMDKFHSPKIKRTPSKKGKPAEVSKTPEKPVSKEARDRFLPEGYPIPLDLEQQAVEFMSTSAVDSRSQRQKNLCWLEEKEKEVVSALRYFKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQTDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRLTIEKQGRPSPTSPVKPSSPASKPDGQPELPLTEREMEILNKTSVSPSTELLPDSTSEEVAPPKPPLPGIRVVDNSPPALPPKKRQSAPSPTRVAVVAPMSRAVSGSSLPVGINRQDFDVECYTQRRLSGGSRSCGGESPRLSPCSSTGKLSRSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQTPPQAACNLSPLPESMGESGPPFVGYSFQLPLGSCLQQDGQQTDTPPALPEKKRRSAVSQTTDSSGCRVSYERHPSQYDNISEDDLQNPAQPVSYPPFAAILPFQQGASSTPVEFVGDFSVPESAGDPEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQSEHIYQQKNKMLMEVYGFSDSFCGSDSTQELAPPPALPPKQRQLQASYAASSFSVSHCVQQTKVAFTPEDGSAAQGLSVSVSNSFLNRHGSLPVPSYKSVFRSYSQDFMPHHQASVQPFLPPTSSSSPHFPPVHASQSSDLAVPTVSSPPPSTVDGPLSSSQDSSFHGNPVRLPSETSFTDSEPPSGKDGHPRDLSVSSASGKDSRENGERSPKSLDALESAQSEEEVDELSLIDHNEIMARLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQCRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCSGELSLARVLRKNILDKVDQKKLLRCAHSDQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEEKSPNLTQFTEHFNNMSYWVRSVIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQRQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQVHYEIRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: Glutaredoxin (Q5PSJ1)
Organism: Populus tremula x Populus tremuloides (Hybrid aspen)
Interaction partners:
Sequence:
MGSLLSSSIKMSKQELDAALKKAKELASSAPVVVFSKTYCGYCNRVKQLLTQVGASYKVVELDELSDGSQLQSALAHWTGRGTVPNVFIGGKQIGGCDTVVEKHQRNELLPLLQDAAATAKTSAQL
Protein: Very long chain fatty acid elongase 3 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl3) (CIN-2) (Cold-inducible glycoprotein of 30 kDa) (ELOVL fatty acid elongase 3) (ELOVL FA elongase 3) (Elongation of very long chain fatty acids protein 3) (Very long chain 3-ketoacyl-CoA synthase 3) (Very long chain 3-oxoacyl-CoA synthase 3) (O35949)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}.
Interaction partners:
- Very long chain fatty acid elongase 1
- Very long chain fatty acid elongase 5
- Very long chain fatty acid elongase 7
- Very-long-chain 3-oxoacyl-CoA reductase
- Lipid transferase CIDEA
- Mitochondrial brown fat uncoupling protein 1
- Histone-lysine N-methyltransferase PRDM16
- Cytochrome c oxidase subunit 8B, mitochondrial
- Type II iodothyronine deiodinase
- Cytochrome c oxidase subunit 7A1, mitochondrial
Sequence:
MDTSMNFSRGLKMDLMQPYDFETFQDLRPFLEEYWVSSFLIVVVYLLLIVVGQTYMRTRKSFSLQRPLILWSFFLAIFSILGTLRMWKFMATVMFTVGLKQTVCFAIYTDDAVVRFWSFLFLLSKVVELGDTAFIILRKRPLIFVHWYHHSTVLLFTSFGYKNKVPSGGWFMTMNFGVHSVMYTYYTMKAAKLKHPNLLPMVITSLQILQMVLGTIFGILNYIWRQEKGCHTTTEHFFWSFMLYGTYFILFAHFFHRAYLRPKGKVASKSQ
Protein: Myelin basic protein (F8W2M5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Myelin membrane {ECO:0000256|ARBA:ARBA00004392}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004392}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004392}.
Interaction partners:
Sequence:
MATASTSGQNPFGLGRKKKAPGVLDQISRFFGGDKKRKGKGSFRGHLSSSPQRPHHSSTRRRGDVNPVVHFFRSFGESRSRSPPKRWSTIF
Protein: Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (Q582T6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03222}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- 2-oxoglutarate dehydrogenase subunit, putative
- oxoglutarate dehydrogenase
- Citrate synthase
- Acetyl-coenzyme A synthetase
Sequence:
MLSRTVRRLWINQNTKVICQGITGKHGTYHTEQAIAYGTKMVGGVNPKKAGSTYLNLPVFGTVAEAVKNTGADATVIYVPAPHCAAAVEEALVAEVPLVVVITEGIPQWDMLRVKSMLLSQNKTRLIGPNCPGIIRPEECKIGIMPGHIHKKGCIGVVSRSGTLTYEAVAQTTAVNLGQSLCVGIGGDPFNGTNMIDCVKLYLEDPGTEGIILIGEIGGTAEEEAAEFIKNHPIKKPLVTFIGGATAPPGRRMGHAGAVVSGGQGTAKGKMEALEAAGAVVAHSPAQLGALMAELMKKRAI
Protein: Mitochondrial outer membrane protein SLC25A46 (Solute carrier family 25 member 46) (Q6DGU5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transmembrane protein of the mitochondrial outer membrane that controls mitochondrial organization (By similarity). May regulate the biogenesis and dynamics of mitochondrial cristae, the inwards folds of the inner mitochondrial membrane (By similarity). Could regulate mitochondrial lipid homeostasis and thereby mitochondrial fission (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96AG3}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable RNA polymerase II nuclear localization protein SLC7A6OS
- Optic atrophy 3 protein homolog
Sequence:
MTSRRPDSFEGLGYRGREDPAFSGGYSGRSFNNSSSSDLQNWVTTPPDIPGSRNLHFDDRTPQFETAPDEAQSAAPPSEQLNRFAGFGIGLASLFTENVLAHPCIVFRRQCQVNYHARCYHLSPMTAISVMYNVTKTQGPKALWKGMGSTFVVQGVTLGTEGIISECTPLPRELSHKWNPKQVVGHLVLKGLTYVVAMPFYSASLIETVQSEIIRDNPGILDCVKEGLGRVMGMGIPHSKRLLPLWNLVLPTVLHGILHYIISSSIQRLVLYLLRRRNNGSPKHSSPGSGMDTVQSMLDAYFPELMASFAASLCADVLLFPLETVLHRLHIQGTRTIIDNTDLGFEVLPINTQYEGMRDCINAIRREEGTMGFYKGFGSIVVQYSLHATVLQITKMIYSTLLRNA
Protein: FI11563p (Sugar baby, isoform E) (B7Z0G4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKATIDKELLPMKAHYFLFNAGTAPVVPFMPTLAGQLGYSPAVVGTMYTILPIIGMLAKPLFGYIADRYHRHRPLFLGGQVLTGIAFFLIMFVPGMEKPLPKVEFHCHQGVSDIPRFCSEYGECVERNLERYYGNRTLECELNCEAQPFMWDIVCEDWLKNNTENCAANRTNTQMEFGASITMQKIENDGSCMFFMIPHDQGQIAGQNVTLYCPKEKEYFKSNCTMDCREDYLKEQLAESAVINTSSAVTMPQFWLFFGLLIFSWIGMAVVVSIGDAICFGILGDRHHLYGKQRLCGSLGWGVFALLAGLLVDHMSLGEVNKNYTAVFWMALLIMGFDVFASSKLRHTPTHLSSNILKDVGQMFLSVRCVIFFLWCVAIGLGTALIWNFLFIYLEELDKAFEGCDSSIKTLEGLVMGIQCFGGELPFFFLSGWILKKIGHVNAMSVVLFGFGVRFILYSMLQNPWYILPIELMNGVTFGLFYATMASYASIVAPPGTDATMQSLVGAIFEGVGVSMGSLIAGQLFESVTARTTFEIFGIGAFIVFVIHVCIQLYLQRNSNIDENGTVKYFAPTDAMHMLNDQEYSRVS