wanglab/gogpt-training-data huggingface dataset:
Protein: Slc5a4b protein (Q2VPB3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASTLSPSITPQTEEPPVVPVRIQNAADISVIVIYFIVVLAVGLWSMVRSNRGTVGGFFLAGHDMAWWPMGASLFASNIGSNHFVGLAGTGAASGIAIAAVEWNALLMVLVLGWVFLPIYIKAGVLTMPEYLRKRFGGKRLQIYLSVLSLFIMVALQTSSIIFSGAIFIQLALGLNLYLAVFILLAITAFYTVAGGLASVIYTDSVQTFIMLLGSLILMGFAFAEVGGYESFTEKYMNAIPSVVEGDNLTISPKCYTPQPDSFHVFRDPVTGDIPWPGLIFGMTILAIWYWCADQVIVQRCLCGKNMSHVKAACILCGYLKLLPMFLMVMPGMISRILYTDKVACVVPSECEKQCGTAVGCTNYAYPTLVLELMPDGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKIRKKASERELMIAGRIFGMVLIAVSILWVPLVQVSQNGQLFHYIGSVSSYLGPPLGAVFMLAIFFKRVNEQGAFWGLMVGLVVGLIRLIAEFVYGTGSCVAPSNCPKIICGVHYMYFAIILFFVSIIVILGVSFLTEPIPDVHLYRLCWSLWNNTEERIDLDAEELETQEEAGGALEEDSEQSRGCLKRACCLLCGLQNTGPKLTKEEEAALRQKFSDTSEKPLWRTVMNINAVLLLGVAVFVHA
Protein: Peroxisome biogenesis factor 2 (EC 2.3.2.27) (EC 2.3.2.36) (Peroxin-2) (Peroxisomal membrane protein 3) (Peroxisome assembly factor 1) (PAF-1) (Q06438)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase. PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-11', a modification that acts as a signal for PEX5 extraction into the cytosol (By similarity). Required for pexophagy in response to starvation by mediating ubiquitination of peroxisomal proteins, such as PEX5 and ABCD3/PMP70. Also involved in the response to reactive oxygen species (ROS) by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of PNPLA2/ATGL, thereby regulating lipolysis (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P28328}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAGREKTKSANRVLRISQLDALELNKALEQLVWSQFTQCFHGFKPGLLARFEPEVKACLWLFLWRFTIYSKNATVGQSVLNIQYKNDFSSNSRYQPPSKNQKLWYAVCTIGGRWLEERCYDLFRNRHLASFGKVKQCMNVMVGLLKLGELINFLIFLQKGKFATLTERLLGIHSVFCKPQNIREVGFDYMNRELLWHGFAEFLIFLLPLINIQKFKAKLSSWCIPLTGAASSDSALASSGKECALCGEWPTMPHTIGCEHVFCYYCVKSSFLFDMYFTCPKCGIEVHSVQPLKSGIEMSEVNAL
Protein: N(5)-(carboxyethyl)ornithine synthase (CEOS) (EC 1.5.1.24) (N(5)-(L-1-carboxyethyl)-L-ornithine:NADP(+) oxidoreductase) (A5HZ59)
Organism: Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Function: Catalyzes the NADPH-dependent reductive condensation between pyruvic acid and the side chain amino group of L-ornithine to form N(5)-(L-1-carboxyethyl)-L-ornithine. To a lesser extent, can also use L-lysine as substrate (yielding N(6)-(L-1-carboxyethyl)-L-lysine), and the D-isomers of the 2 basic amino acids. Can use alpha-keto acids other than pyruvate, e.g. glyoxylate.
Interaction partners:
Sequence:
MKLGFLIPNHPNEKRVALLPEHVKGFNNELVIETGFGETLGISDAEYVKVGCTIASREEIFKTCEGIFSLKVLKPQDYKHIREGQIIVGWTHPEGSGKIFMEEQGIPKNLIIVDLDNIHPSIYYKDYVIPMEWIPSNFVRKNSYIAGYASTMHAVMNYGSIPTSETKVAILGSGNVSQGAFSAISKFNPDIRMFYRKTMNQLKDELEEFDIIINGIEMDNPNKHILTLEDQMRLKKNCLIIDAAANLGKAIEGARHTTASDPIYNKDGKYYYAVNNSPSIFYRQSSKAISEAFSKHVYSKELEFYLDVIAEVEEMIV
Protein: COMM domain-containing protein 5 (Hypertension-related calcium-regulated gene protein) (HCaRG) (Q9GZQ3)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Negatively regulates cell proliferation. Negatively regulates cell cycle G2/M phase transition probably by transactivating p21/CDKN1A through the p53/TP53-independent signaling pathway. Involved in kidney proximal tubule morphogenesis (By similarity). Down-regulates activation of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 2
- COMM domain-containing protein 10
- COMM domain-containing protein 1
- COMM domain-containing protein 4
- Ubiquitin-like protein FUBI
- COMM domain-containing protein 8
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 6
- COMM domain-containing protein 9
- COMM domain-containing protein 3
Sequence:
MSAVGAATPYLHHPGDSHSGRVSFLGAQLPPEVAAMARLLGDLDRSTFRKLLKFVVSSLQGEDCREAVQRLGVSANLPEEQLGALLAGMHTLLQQALRLPPTSLKPDTFRDQLQELCIPQDLVGDLASVVFGSQRPLLDSVAQQQGAWLPHVADFRWRVDVAISTSALARSLQPSVLMQLKLSDGSAYRFEVPTAKFQELRYSVALVLKEMADLEKRCERRLQD
Protein: Uronyl 2-sulfotransferase homolog pip (UST) (EC 2.8.2.-) (Heparan sulfate 2-O-sulfotransferase pipe) (Protein pipe) (Q86BJ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sulfotransferase involved in dorsoventral axis patterning in early embryos. Required for the specific ventral activation of a series of proteases acting in the perivitelline space between the embryonic membrane and the eggshell. Probably acts by mediating the sulfation of some glycoprotein or glycosaminoglycan stably deposited in the egg, whose ventrally localized modification leads to spatially restricted activation of the protease cascade.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11076773, ECO:0000269|PubMed:12941941}; Single-pass type II membrane protein {ECO:0000269|PubMed:11076773}. Note=Wbl/windbeutel is required for targeting to the Golgi. {ECO:0000269|PubMed:11076773, ECO:0000269|PubMed:12941941}.
Interaction partners:
Sequence:
MSLNAERSYKMKLRDVENAFKYRRIPYPKRSVELIALLAISCTFFLFMHTNKLNSRLKEMEVKLQPSEFSALGLTGNHISGHDAGKHDDINTLHGTYQYLKSTGQKVGYNVHDRRSSEEQLRTPTAHGHHHDHHSHHHHMHQQEKIDGHKHKASHDKQLAVPDNKHKEDEVHYEDDEDEVEENDDDLANDVGTTDSEGFNFKADLLNNTKYAEVDFVFFNRVPKVGSQSLMELMARLGKINGFTHARNKGSAHETIVMNKQRQNDLIADLLTRPKPHIYSQHIAYINFTRFHLPKPIYINLIRDPIDRIISWHYYIRAPWYYRDMQAKLGENAIPMPSEEFMNLDLDTCVRNHDPHCTFTQMQIKNPVGDHRRQTLFFCGMNQKLCMPFNSEAAMQKAKRTVETEYAVVGTWEDTNITLSVLEAYIPRYFRNAKVAYYLGKDRLSRVNRNNVTRIVSDETRLILRKNLTNEIEFYEFCKQRLYLQYAALSHGKRFGEDDYLLVPEQQNEYNEDY
Protein: Glutamine synthetase (EC 6.3.1.2) (Q8JI31)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Aldehyde dehydrogenase domain-containing protein
- Uncharacterized protein
- Delta-1-pyrroline-5-carboxylate synthase
- Delta-1-pyrroline-5-carboxylate synthase
- Serine hydroxymethyltransferase
- Lengsin
- Succinate-semialdehyde dehydrogenase
- glutamate--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- glutamate--tRNA ligase
Sequence:
MATSSSAELSKAVKQQYMDLPQGDKVQIMYVWIDGTGEGLRCKTRTLDSEPKCIEELPEWNFDGSSTYQSEGSNSDMYLIPSAMFRDPFRKDPNKLVLCEVLKYNRKPAETNLRLTCNKVMDMVENQVPWFGMEQEYTILGTDGHPFGWPNNGFPGPQGPYYCGVGSDKAYGRDIVEAHYKACLYAGVMICGTNAEVMPAQWEFQVGPCEGISMGDHLWAARFILHRVCEDFGVVASFDPKPIPGNWNGAGCHTNFSTKEMREEGGLKAIEESIERLGKRHSYHIRAYDPKGGLDNARRLTGHHETSNIHEFSAGVANRGASIRIPRTVGQEKKGYFEDRRPSANCDPYAVTEAIIRTCLLSEEGDEPVNY
Protein: EF-hand domain-containing protein (Q57YA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Calcium uniporter protein C-terminal domain-containing protein
- Prohibitin
Sequence:
MAGIRFAATGAFFAAVGYFSVDRFINSASWWALLRSSGEASAEDGGSGGCIRRRLGSAGSVWQRFNQYSTPGAAGVQVLRFLDFVACVCLLDEEDRQRLHSRLCGAPTEGREDLCSLFKLVDTNASGTITYDEFCVLITLLSACQRHLKIAFGAFDVTEEDSLSRDGFRRIINTLMVDPTVQIVERTGHESDVHSHGGGRRDGGLTSSEFLSSNLVKLFFGVDEDARISFDDFWTVVRRIQWMVRRVEFQLYDTQNTGRIKLHQLQKILFPDRYCSTQCEEGHSDEESRYVSSRLNCLKDKFVSWDLYMKVFDVLCETESIVRGMNLALNARDPEGRNDHTSCLCHRDDSMTPIVSVLADTAAGLTTSHSGRDRELDYVEFHRVLQSCDHLKHLTKSDAEEIVEIFDIDGSGKLSPDEFGKMSRMCTSFFMRSTPLFLEPRRNTIQRFVYCMQQLR
Protein: Atrial natriuretic peptide receptor 3 (Atrial natriuretic peptide clearance receptor) (Atrial natriuretic peptide receptor type C) (ANP-C) (ANPR-C) (NPR-C) (P41740)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P17342}; Single-pass type I membrane protein.
Interaction partners:
- Natriuretic peptides A
- C-type natriuretic peptide
- Natriuretic peptides B
- Neuronal pentraxin receptor
- Osteocrin
Sequence:
MRSLLLFTFSACVLLARALLAGGASSGGGDTGPGNRRREREALAAQKIEVLVLLPRDDSYLFSLARVRPAIEYALRSVEGNGTGRKLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDTEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALLYSDDKLERNCYFTLEGVHEVFQEEGLHTSAYNFDETKDLDLDDIVRYIQGSERVVIMCASGDTIRRIMLAVHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQTVTLLRTAKPEFEKFSMEVKSSVEKQGLNEEDYVNMFVEGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVVAMTDTEAGTQEVIGDYFGKEGRFKMRSNVKYPWGSLKLRIDETRIVEHTNSSPCKSCGLEESAVTGIVVGALLGAGLLMAFYFFRKKYRITIERRNHQEESNIGKHRELREDSIRSHFSVA
Protein: Phosphatase Rv3376 (EC 3.1.-.-) (P9WMS5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Able to hydrolyze geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) to respectively yield geraniol, farnesol and geranylgeraniol.
Interaction partners:
- Tuberculosinyl adenosine transferase
- Type B diterpene cyclase
- Putative amidase AmiD
- Probable enoyl-CoA hydratase EchA18
- Cyclo
- Esterase Rv1288
Sequence:
MSISAVVFDRDGVLTSFDWTRAEEDVRRITGLPLEEIERRWGGWLNGLTIDDAFVETQPISEFLSSLARELELGSKARDELVRLDYMAFAQGYPDARPALEEARRRGLKVGVLTNNSLLVSARSLLQCAALHDLVDVVLSSQMIGAAKPDPRAYQAIAEALGVSTTSCLFFDDIADWVEGARCAGMRAYLVDRSGQTRDGVVRDLSSLGAILDGAGP
Protein: Cyclin-dependent kinase inhibitor 3 (EC 3.1.3.16) (EC 3.1.3.48) (CDK2-associated dual-specificity phosphatase) (Kinase-associated phosphatase) (Q810P3)
Organism: Mus musculus (Mouse)
Function: May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q16667}.
Interaction partners:
- Cyclin-dependent kinase 2
- Disks large-associated protein 5
- Cyclin-dependent kinase 1
- Cyclin-A2
- Baculoviral IAP repeat-containing protein 5
- Kinesin-like protein KIF11
- Cell division cycle protein 20 homolog
- Lymphokine-activated killer T-cell-originated protein kinase
- G2/mitotic-specific cyclin-B2
- Cell division cycle-associated protein 3
Sequence:
MKPPISIQASEFDSSDEEPVDEEQTPIQISWLPLSRVNCSQFLGLCALPGCKFKDVRRNIQKDTEELKSYGIQDVFVFCTRGELSKYRVPNLLDLYQQYGIVTHHHPIPDGGTPDIGSCWEIMEELATCLKNNRKTLIHCYGGLGRSCLAACLLLYLSDSISPQQAIDSLRDVRGSGAIQTIKQYNYLHEFRDKLAAYLSSRDSLSRSVSR
Protein: Coiled-coil domain-containing protein 39 (Q9D5Y1)
Organism: Mus musculus (Mouse)
Function: Required for assembly of dynein regulatory complex (DRC) and inner dynein arm (IDA) complexes, which are responsible for ciliary beat regulation, thereby playing a central role in motility in cilia and flagella. Probably acts together with CCDC40 to form a molecular ruler that determines the 96 nanometer (nm) repeat length and arrangements of components in cilia and flagella. Not required for outer dynein arm complexes assembly.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UFE4}. Note=CCDC40 is required for localization to axonemes. {ECO:0000250|UniProtKB:Q9UFE4}.
Interaction partners:
- Dynein regulatory complex subunit 2
- Dynein regulatory complex protein 1
- Radial spoke head protein 4 homolog A
- Axonemal dynein light intermediate polypeptide 1
- Radial spoke head protein 9 homolog
- Dynein axonemal intermediate chain 2
- Cilia- and flagella-associated protein 43
- Dynein axonemal heavy chain 5
- Outer dynein arm-docking complex subunit 2
- Dynein axonemal assembly factor 3
Sequence:
MCSEFLSELHWEDGFAIPVANQENKILEDQLAKLREEKSNLQDQLHDYEERINSMTSHLKNVNQEFLFTQSLYKARESEIESEEHFKAIAERELGRVKNETQLLEKEMAIIRERKSQMENNIFKTTQKLDDLKCQMNWDQQALEAWLEESAHKDSDSLTLQKYSQQDDNKIRALTLQLEKLTMEYNEKRKLLDSELTETLSAQLELDKAAQDFRKIHLERQELIQQWENTIEQMQRRDQEIDNCALALSRIKQEAREKEGVVKEKIKFLENEVENNIEYERKISVAERKVSKCRMDYQRHEGNRSQLKDELDTLKTTLNRTSSDLQALRKNISKVKKDIFDETLRLQKLKHHNEVVKHKLKMITEKTLSIEEKATNMEDMLKEEEKGLKEVEVQLGIVKDVLFKKVQELQNEIAKEKALVSEIEGTRSSLKHLNKQLHKLDFETLKQQEIMYSQDFYIQQVERRMSRLKGEINSEEKQALEAKILELKKTMDEKKSTLSLLESQIKKLHNDLYFIKKSNGKNNDEKESLMNKISELNLFIDRSEKELSKAKAVKEDMMIEDNLLKLQVKRARELLYSKAEEVLSLEKRKQQLGKDMEERAEEIKVHKAMLTSQIRCVEQQRKTMSSEFHERLSKIDKLKNRYEILTVVMLPPEGEEEKTQSYYVIKAAQEKEELQREGDSLDAKINKAEKEIYALQNTLQVLNSCNSNYKQSFKKVTPSSDEYALKIQLEEQKRTADERYRCKQRQIRELQEDIQSMENTFEVIGHLANNAKEKLTEKQTLAFQLRKETEEQKPKLQRITKQCGRLRREIRILKQTDNETLEEQDIQLREIIQFHKDIDQMLVNAMENAEIHAIFKTYFEQNGLELPTARGPSSRSSSQSSSLSSFRSLEDVTLQSPPTAKVIQLRFPEPPPATNDSSRSASSGSNSNIPKEKKLSK
Protein: V-type proton ATPase subunit c' (V-ATPase subunit c') (Proteolipid protein VMA11) (Trifluoperazine resistance protein 3) (V-ATPase 16 kDa proteolipid subunit 2) (Vacuolar proton pump c' subunit) (P32842)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:9030535}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit B
Sequence:
MSTQLASNIYAPLYAPFFGFAGCAAAMVLSCLGAAIGTAKSGIGIAGIGTFKPELIMKSLIPVVMSGILAIYGLVVAVLIAGNLSPTEDYTLFNGFMHLSCGLCVGFACLSSGYAIGMVGDVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIVALILNTRGSE
Protein: Transmembrane protein (F4I924)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Rhomboid-like protein 18
- Rhomboid-like protein 20
- Protein transport protein Sec61 subunit beta
- At3g63160
- Outer envelope protein 64, chloroplastic
- ATG8-interacting protein 1
- Peroxisomal and mitochondrial division factor 1
Sequence:
MNRNSKGRAWYDKIYRKLASQGNVSSGLDSVKDEPEKLREEQMEGDGFKEKLSDSVLIDEKLEEYSDCDRTATTSRSHTDPVSSQSTHQTPESFRTPITCDDDTFVSVSGISRDVSNLIPFATETPASPVQEKMANTRSFSNNSVKGNQDEFFIEDFDVGPMDTIDLYDMTFREDPSDFDDNLLYAMRDRTKQLRSFKRKIMDAIKSKRRREKEYEQLAIWFGDADMGCDLVNDKEQSTTSIDSKSSQTNVPVVSEDSEWEIL
Protein: Anaphase-promoting complex subunit 13 (Cyclosome subunit 13) (A8K3Z6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSEVQRDGRILDLIDDAWREDKLPYEDVAIPLNELPEPEQDNGGTTESVKEQEMKWTDLALQYLHENVPPIGN
Protein: Small ribosomal subunit protein uS4A (40S ribosomal protein S9-A) (Q09757)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS15
- Elongation factor 3
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS8B
Sequence:
MPSAPRKQSKTYKVPRRPFESARLDAELKLAGEYGLRNKHEIWRVALTLSKIRRAARELLTLDEKDPKRLFEGNAIIRRLVRLGILDETRMKLDYVLALRIEDFLERRLQTQVFKLGLAKSIHHARVLIFQRHIRVGKQIVNVPSFVVRLDTQKHIDFALSSPYGGGRPGRCKRKRLRSQEGGEGEEAEEE
Protein: Enoyl-CoA hydratase domain-containing protein 3, mitochondrial (Q3MIE0)
Organism: Rattus norvegicus (Rat)
Function: May play a role in fatty acid biosynthesis and insulin sensitivity.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MALVAGLRAFGAKWPSWLRRSPWAPLSAGFCSPGSARPAGPESEPRLTSTRQQDGIRNIVLSNPRRRNALSLAMLKSLRSDILHEAESEDLKVIIISAEGPVFSSGHDLKELTGAQGRDYHTEVFQTCSEVMMLIRNHPVPIVAMVNGLATAAGCQLVASCDIAVASDKSSFATPGVNVGLFCSTPAVALGRAVPRKVALEMLFTGEPISAQEALRHGLISKVVPEEQLEEEATRIAKKIASLSRSVVALGKATFYKQLPQDLSTAYFLASQAMVDNLTLKDGQEGIEAFIQKRRPVWSH
Protein: Methionine-R-sulfoxide reductase B1 (EC 1.8.4.12) (Selenoprotein R) (Q8INK9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Methionine-sulfoxide reductase that specifically reduces methionine (R)-sulfoxide back to methionine. While in many cases methionine oxidation is the result of random oxidation following oxidative stress, methionine oxidation is also a post-translational modification that takes place on specific residues. Acts as a regulator of actin assembly by reducing methionine (R)-sulfoxide mediated by Mical on actin thereby promoting filament repolymerization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9JLC3}. Nucleus {ECO:0000250|UniProtKB:Q9JLC3}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9JLC3}.
Interaction partners:
- Peptide methionine sulfoxide reductase
- Thioredoxin reductase-like selenoprotein T homolog CG3887
- Selenoprotein F
- HDC12925
- Thioredoxin-2
- Large ribosomal subunit protein bL20m
- [F-actin]-monooxygenase Mical
- Thioredoxin reductase 2, mitochondrial
- Glutathione peroxidase
- catalase
Sequence:
MFALSARHALRRTRIFAIPRFFADSRQDSDNPDKRYSGPAATMDNKSEKVTVNKEELRKRLTPVQYQVTQEAGTERPFTGCYNKHYEKGVYQCIVCHQDLFSSETKYDSGCGWPAFNDVLDKGKVTLHRDASIPGGNILLLIAHPERIRTEVRCARCNAHMGHVFEDGPKPTRKRYCINSASIEFVNADPATSSPPVATPTAAPIAQQ
Protein: Non-selective voltage-gated ion channel VDAC3 (E5RHZ6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSVGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLS
Protein: Heavy metal-associated isoprenylated plant protein 3 (AtHIP03) (AtHIPP3) (Q9FJH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein. Binds high amounts of zinc. May act as an upstream regulator of the salicylate-dependent pathogen response. Involved in abiotic stress responses, and seed and flower development.
Subcellular location: Nucleus {ECO:0000269|PubMed:25913773}. Nucleus, nucleolus {ECO:0000269|PubMed:25913773}. Cytoplasm {ECO:0000269|PubMed:25913773}. Note=Weakly expressed in the cytoplasm. {ECO:0000269|PubMed:25913773}.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 39
- Heavy metal-associated isoprenylated plant protein 20
- Heavy metal-associated isoprenylated plant protein 31
- Heavy metal-associated isoprenylated plant protein 21
- Defensin-like protein 18
- Heavy metal-associated isoprenylated plant protein 10
- Heavy metal-associated isoprenylated plant protein 27
- Heavy metal-associated isoprenylated plant protein 12
- Heavy metal-associated isoprenylated plant protein 22
- Heavy metal-associated isoprenylated plant protein 30
Sequence:
MGEKKNEGDNKKKGGDNKKKNETPSITVVLKVDMHCEGCASRIVKCVRSFQGVETVKSESATGKLTVTGALDPVKLREKLEEKTKKKVDLVSPQPKKEKEKENKNKNDEDKKKSEEKKKPDNNDKKPKETPVTTAVLKLNFHCQGCIGKIQKTVTKTKGVNGLTMDKEKNLLTVKGTMDVKKLVEILSEKLKRAVEIVPPKKEKDKENGNENGEKKKGGGGDGGGKEKTGNKGGGEGVNMMEYMAAQPAYGYGYYPGGPYGYPIQAHAPQIFSDENPNACVVM
Protein: Small exported membrane protein 1 (Q8IC43)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSQPQKQQNEEGAATAANTQEKKFNPTRNPSQSGPYRHHGPQGRTPYMQLHKNQNNNMVNKISNYLGIENKELVEFGLNLFTYIIAIFLALQIYDYVTHRKCGYYKDMLAKIVRFQASLQNAK
Protein: Chromatin assembly factor-1 p105 subunit (Q9BII5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKCKIPEISWHNRDPVLSVDIQQNGLGLRSPTICRLASGGSDAHVLIWYVNRSDDAEGVDVELAADLSRHQRAVNAVRWSPNGELLASGDDESVVFIWKQKADHEVVNIVDADGCSEQDKEVWLTLKVLRGHREDIYDLSWAPNSQFLVSGSVDNTAMLWDVHSGKSLAILDDHKGYVQGVAWDPCNQYIATMSTDRQMRIFDANTKRVLHRVSKCVLPVKEDHEMHGKSMRLYQDGTLQTFFRRLCFTPDGKLLLTPSGITDYDGVVKPINTSYGFSRYDLSKPAFVLPFPNEYAVAVRCSPVLYRLRPYNAEKNPPIISLPYRMIYAVATKNAVFFYDTQQPVPFAIVSNIHYSRLTDLAWSSDGTVLIVSSTDGYCSLITFEPTELGDCYEDMETVLSVVLKSSENATVLKKKRQKLRKVSLDEPRKPLQEKSKPNTIRRASEAGITEVGEPELDAENDSSTHSVSSNKTNSPKTKASEEEKPTPIAIRRSPRKNSTAPMPIAIRRAPRKPEDKGNSESSKPKDEMEVTHTKTTQVQKTVASPVKRKVSTEAVPPAETSQPALAVIPVFEKEIISSDDKFESPEKKSRPATPIQVRRQPRTPGSSSQFNLTPKSQPAKQATPIAVRRTPRVLIEMPVNSPVVPMEEAMDAWPLDESITPLPATKKDSRKPLPETVKTETKPAVIEASEATCERTEDIRLVYEDTQEETPKNPTESGPSTPNNKTPRRVSLRTISTPKSKKKLLE
Protein: Serine/threonine-protein kinase STY46 (EC 2.7.11.1) (Serine/threonine/tyrosine-protein kinase 46) (F4JTP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs. Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21799034}.
Interaction partners:
- AT4g30010/F6G3_40
- Probable protein phosphatase 2C 8
- F18K10.11 protein
- At1g65370/T8F5_15
- Hyperosmolality-gated Ca2+ permeable channel 2.1
- Expressed protein
Sequence:
MVMEDNESCASRVIFDALPTSQATMDRRERIKMEVFDEVLRRLRQSDIEDAHLPGFEDDLWNHFNRLPARYALDVNVERAEDVLMHKRLLHSAYDPQNRPAIEVHLVQVQPAGISADLDSTSNDAGHSSPTRKSIHPPPAFGSSPNLEALALAASLSQDEDADNSVHNNSLYSRPLHEITFSTEDKPKLLFQLTALLAELGLNIQEAHAFSTTDGYSLDVFVVDGWPYEETERLRISLEKEAAKIELQSQSWPMQQSFSPEKENGQTGARTHVPIPNDGTDVWEINLKHLKFGHKIASGSYGDLYKGTYCSQEVAIKVLKPERLDSDLEKEFAQEVFIMRKVRHKNVVQFIGACTKPPHLCIVTEFMPGGSVYDYLHKQKGVFKLPTLFKVAIDICKGMSYLHQNNIIHRDLKAANLLMDENEVVKVADFGVARVKAQTGVMTAETGTYRWMAPEVIEHKPYDHKADVFSYGIVLWELLTGKLPYEYMTPLQAAVGVVQKGLRPTIPKNTHPKLAELLERLWEHDSTQRPDFSEIIEQLQEIAKEVGEEGEEKKKSSTGLGGGIFAALRRSTTHH
Protein: Growth hormone (B0FPG6)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFALLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Estrogen-related receptor gamma a (F6PD98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
- G-protein coupled estrogen receptor 1
- Peroxisome proliferator-activated receptor gamma, coactivator 1 alpha.
Sequence:
MDSVELSLPECFSLHSDQQMNLSKAQVNSEDKYAKCGAWRTQQQYDIEASHMRDAHALYNQRLLCRMSNKDRHIESSCPSYIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPTLYGPTGALGPSGTGAKRYEDCSSTITEDSQIKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLTVGMMREGVRLDRVRGGRQKYKRRIDAENSPYLNPQLALPPKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVNIGWAKHIPGFSTLSLADQMSLLQSAWMEILILRVVYRSLSFEDKLVYAEDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHVEDPRRAGKLLMTLPLLRQTSTKAVQHFYSIKQDGKVPMHKLFLELLEAKV