wanglab/gogpt-training-data huggingface dataset:
Protein: Ribosome quality control complex subunit 2 (Translation-associated element 2) (Q12532)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As part of the ribosome quality control complex (RQC), a ribosome-associated complex, mediates the extraction of incompletely synthesized nascent chains from stalled ribosomes as well as their ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes from the stalled translation complex and prevents the accumulation of nascent polypeptide chains that are potentially toxic for the cell. RQC2 is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. RQC2 is important for the stable association of the E3 ubiquitin-protein ligase RKR1/LTN1 to the complex. RQC2 is also able to recruit alanine- and threonine-charged tRNA to the A site and directs the elongation of stalled nascent chains independently of mRNA or 40S subunits, leading to non-templated C-terminal Ala and Thr extensions (CAT tails). CAT tails induce a HSF1-dependent heat shock response. CAT tails also promote the RKR1/LTN1-mediated ubiquitination of incompletely synthesized nascent polypeptides and their subsequent proteasomal degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 48
- Ribosome quality control complex subunit 1
- E3 ubiquitin-protein ligase listerin
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- tRNA endonuclease VMS1
- Protein DOM34
- RQC trigger complex subunit RQT4
- E3 ubiquitin-protein ligase HEL2
- Threonylcarbamoyl-AMP synthase
Sequence:
MKQRISALDLLLLARELKQDLEGYRLSNIYNIADSSKQFLLKFNKPDSKLNVVVDCGLRIYLTEFSRPIPPTPSGFVVKLRKHLKAKRLTALKQVDQDRILVLQFADGHFYLVLEFFSAGNVILLDENRRIMALQRVVLEHENKVGQIYEMFDESLFTTNNESADESIEKNRKAEYTSELVNEWIKAVQAKYESDITVIKQLNIQGKEGAKKKKVKVPSIHKLLLSKVPHLSSDLLSKNLKVFNIDPSESCLNLLEETDSLAELLNSTQLEYNQLLTTTDRKGYILAKRNENYISEKDTADLEFIYDTFHPFKPYINGGDTDSSCIIEVEGPYNRTLDKFFSTIESSKYALRIQNQESQAQKKIDDARAENDRKIQALLDVQELNERKGHLIIENAPLIEEVKLAVQGLIDQQMDWNTIEKLIKSEQKKGNRIAQLLNLPLNLKQNKISVKLDLSSKELNTSSDEDNESEGNTTDSSSDSDSEDMESSKERSTKSMKRKSNEKINVTIDLGLSAYANATEYFNIKKTSAQKQKKVEKNVGKAMKNIEVKIDQQLKKKLKDSHSVLKKIRTPYFFEKYSWFISSEGFLVMMGKSPAETDQIYSKYIEDDDIYMSNSFNSHVWIKNPEKTEVPPNTLMQAGILCMSSSEAWSKKISSSPWWCFAKNVSKFDGSDNSILPEGAFRLKNENDQNHLPPAQLVMGFGFLWKVKTSGNEDNGDDDEEEEEEEEEEEEEEEEEEEEEEEEKEEEEKEEEQQQDEDDSNEVNGLEKGGDSNDSTKNNSFEHDNLEKDIEKHCTISSDTDSDSGNAKAKNDNSSTQRILDEPGVPISLIENINSNVRGKRGKLKKIQKKYADQDETERLLRLEALGTLKGIEKQQQRKKEEIMKREVREDRKNKREKQRRLQALKFTKKEKARVNYDKHKSELKPSLDKGDVVDDIIPVFAPWPALLKYKYKVKIQPGSAKKTKTLTEILHYFKSRPLDGSSTDNEMDWPQEHEMIKGLKEQDLVLLLCVDKLKVTIAGQKSTKNGGNSSKKGKKKR
Protein: Sodium channel subunit beta-1 isoform X1 (Sodium channel, voltage-gated, type I, beta a) (Voltage-gated sodium channel beta 1 subunit splice variant A) (Q06W35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MSALRLLWVPALLCLTHAWLCYGACVEVDSDTEAVAGKGFKLTCISCKMRGEVVASATVDWWFMAKGESEFTHIYTYAEMTASITDERFEDRLAWNGSKKTDDVQDGSIYILNVTFNDTGTFRCFFDRILIFPNYEYHTNATKFITISVVGHATRGMASILSEVMMYVSIIGLQLWLVVEMVYCYRKIAAAGEEALRESESKKSLKPKA
Protein: Single-pass membrane and coiled-coil domain-containing protein 3 (A2RU48)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAQSDFLYPENPKRREEVNRLHQQLLDCLSDSFDVTNKLTEVLNMHLGCRLASIEMKRDGTIKENCDLIIQAIMKIQKELQKVDEALKDKLEPTLYRKLQDIKEKETDKIAIVQKVISVILGEATSAASAVAVKLVGSNVTTGIINKLVTVLAQIGASLLGSIGVAVLGLGIDMIVRAILGAVEKTQLQAAIKSYEKHLVEFKSASEKYNHAITEVINTVKHQMK
Protein: Phospholipase A2 (EC 3.1.1.4) (Group IB phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 1B) (P04055)
Organism: Rattus norvegicus (Rat)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. May act in an autocrine and paracrine manner (By similarity). Has anti-helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}.
Interaction partners:
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Phospholipase A2, group III
- Group 10 secretory phospholipase A2
- Cytochrome P450 2E1
- Group IIC secretory phospholipase A2
- Phospholipase A2, membrane associated
- Phospholipase A and acyltransferase 3
- Phospholipase A2
- Phospholipase A2 group V
Sequence:
MKLLLLAALLTAGVTAHSISTRAVWQFRNMIKCTIPGSDPLREYNNYGCYCGLGGSGTPVDDLDRCCQTHDHCYNQAKKLESCKFLIDNPYTNTYSYKCSGNVITCSDKNNDCESFICNCDRQAAICFSKVPYNKEYKDLDTKKHC
Protein: Serine/threonine-protein phosphatase PP2A-3 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 3) (Q07100)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions redundantly with PP2A4, and is involved in establishing auxin gradients, apical-basal axis of polarity and root and shoot apical meristem during embryogenesis. May dephosphorylate PIN1 and regulate its subcellular distribution for polar auxin transport. Involved in the regulation of formative cell division in roots by dephosphorylating ACR4 protein kinase.
Subcellular location: Cytoplasm.
Interaction partners:
- PP2A regulatory subunit TAP46
- Protein phosphatase methylesterase 1
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- Leucine carboxyl methyltransferase 1 homolog
Sequence:
MGANSIPTDATIDLDEQISQLMQCKPLSEQQVRALCEKAKEILMDESNVQPVKSPVTICGDIHGQFHDLAELFRIGGMCPDTNYLFMGDYVDRGYYSVETVTLLVALKMRYPQRITILRGNHESRQITQVYGFYDECLRKYGNANVWKIFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNIRNFDRVQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDISEQFNHTNNLKLIARAHQLVMDGYNWAHEQKVVTIFSAPNYCYRCGNMASILEVDDCRNHTFIQFEPAPRRGEPDVTRRTPDYFL
Protein: Hemagglutinin component of the neurotoxin complex (A5HZZ5)
Organism: Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Interaction partners:
Sequence:
MSVERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQKWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSNRCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILSQPLLLLPNFDIYNSNQMFKLEKI
Protein: Glypican-1 [Cleaved into: Secreted glypican-1] (F1QCC6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cell surface proteoglycan that bears heparan sulfate.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Adducin 3
- Syndecan
- Slit homolog 2
Sequence:
MDLTAVALLVSLVSVSLSAENAGGKARSCTDVRQFYSGKGFTLNGVPQSEISGEHLRICPQGYTCCTSAMEETLSNLSRREFEGLVREAGRSIQALLNAQYRTFDTYFLELLNGSERWLEEAFVAALGELYRLNAGVFRDLYAELHRYYSGASLNLEEALDEFWMKLLERLLKASDPETASLLSDDFLDCASKQTETLRPFGDAPRELKAKLVRAFIAARAFVQGLNAAGEIVRKVSQVPLSPECNRAIMKLVYCPHCRGLGSVKPCINYCKNVMKGCLANQADLDTEWQSLIETMLQVASSFGAEPSMDTVIYSIPVRISEAVLAMQENMEIYTSKVFKACGDRGEEGTPSSISEEPKKKERTVTALEYKPSPKSAARLEVQVTDVYSKLKEMQLYWIQLPSALCSGKTASSTTGDKCWNGITKASYLPEVMGDGLANQINNPEVEIDITKPDRTIRQQIMLLKIMSNRLKNALEGNDVDFQDTSDDFSGSGSGMCADHLCVRGRPPVFGPKTDRPKLYATGPENKRVKGSGNQIQPSFILLIVFFVSLLLRR
Protein: Rhea, isoform I (M9PF06)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTLSLRIQLEGGRVTKTIQFQPNTTVFDACKVIRDKFAEAVQGQPSEYGLFISDEQNQQGVWLEPGRTLGYYILHNQDTLEYRRKTRTLRVRMLDGAVKTILVDDSQPVSQLMVVICTKIGITNHEEYGLVREDNEAQNENLPDNKFGTLTLKRKIMEKDRDAKMESLRKKLKTDDEMNWVDVSRTLREQGIDEAETVLLRRRFFFSDQNIDSRDPVQLNLLYVQARDAILDGTHPVTQDKACEFAGIQVHIQFGPHNEAKHKTGFLDLKDFLPQSYVRTKGIEKKIFSEHRKHVDLSEIDAKVLYTKTARELPTYGVTFFLVKEKMNGKNKLVPRLLGVTKDSVLRLDEHTKEILISWPLTTVRRWGASPNTFTLDFGDYANQYYSVQTTEAEQIVQLIAGYIDIILKKKQTKDHFGIEGDEGSTMVEESVAPSKATFLQHETNRMEQLNVESLAHPGIMRPYDGERSYMENEVQTVQYGAFVGQVNHAHQPPTPVVIQCFTKLRKFALVL
Protein: Zinc transporter ZIP10 (Solute carrier family 39 member 10) (Zrt- and Irt-like protein 10) (ZIP-10) (Q6P5F6)
Organism: Mus musculus (Mouse)
Function: May act as a zinc-influx transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21738690, ECO:0000269|PubMed:25074919}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:30520657}; Multi-pass membrane protein {ECO:0000255}. Note=Expressed at the apical membranes of proximal tubules in the kidney. {ECO:0000269|PubMed:30520657}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A1
- Zinc transporter ZIP1
- Zinc transporter ZIP9
- Proton-coupled zinc antiporter SLC30A5
- Probable proton-coupled zinc antiporter SLC30A4
- Zinc transporter 6
- Zinc transporter ZIP11
- Zinc transporter 7
- Proton-coupled zinc antiporter SLC30A2
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MKVHIHTKFCLICLLTFIFHHCNHCHEDHDHGPEELHRHHRGMTESESSKFSVQDAENEKKYYIEKLFDRYGENGRLSFFGLEKLLTNLGLGEIKVVEINHEDLGHDHVSHLDILAVQEGKHFHSHTHQHFHNHLNAENHTTTSVTSKRNHKCDPEKEAAELPIKADDKHLHDRNHRFHHRHRLHHHLDHNTTRHVHNDSVAHSEHGEPGHSPSPETNKTQEQSEVKSVKVRRKEKGKRKKENSEVNTPGFLPNHDHSEQYEHNRVHKLDRVHSPGHPHAHLPEHSGHELGHGHQELDPDNEGELRHTRKREAPHVRKSAIYSTPSHKDQSEDDRQHECLNVTQLLKHFGLGPNSPISPDLFTYLCPALLYQIDSRLCIEHFDKLLVEDLNKDKTLVPEDKTNIGASAWICGIISITVISLLSLLGVILVPIINQGCFKFLLTFLVALAVGTMSGDALLHLLPHSQGGHDHSHQHTHGHGHSHGHESKEFLEEYDAVLKGLVALGGIYLLFIIEHCIRMFKHYKQQRGKQKWFMKQSTEESTIGRKLSDHKLNSTPDADWLQLKPLAGTDDSVVSEDRLNETELTDLEAQQESPPKNYLGVEEEKIMDHSHSDGLHTIHEHEVHVTSHNHHDEDKAVLRKHSHQWHHRHAHHSHGPCHSGSDLKETGIANIAWMVIMGDGIHNFSDGLAIGAAFSAGLTGGISTSIAVFCHELPHELGDFAVLLKAGMTVKQAIVYNLLSAMMAYIGMLIGTAVGQYANNITLWIFAITAGMFLYVALVDMLPEMLHGDGDHEEHGFCPVGQFILQNLGLLFGFAIMLVIALYEDKIVFDIQF
Protein: Myogenic factor 6 (Myf-6) (Herculin) (Muscle-specific regulatory factor 4) (P15375)
Organism: Mus musculus (Mouse)
Function: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein.
Subcellular location: Nucleus.
Interaction partners:
- Myogenic factor 5
- Myoblast determination protein 1
- Paired box protein Pax-7
- Myocyte-specific enhancer factor 2C
- Paired box protein Pax-3
- Myogenin
- Myocyte-specific enhancer factor 2D
- Myocyte-specific enhancer factor 2A
- Transcription factor E2-alpha
- Myozenin-1
Sequence:
MMMDLFETGSYFFYLDGENVTLQPLEVAEGSPLYPGSDGTLSPCQDQMPQEAGSDSSGEEHVLAPPGLQPPHCPGQCLIWACKTCKRKSAPTDRRKAATLRERRRLKKINEAFEALKRRTVANPNQRLPKVEILRSAISYIERLQDLLHRLDQQEKMQELGVDPYSYKPKQEILEGADFLRTCSPQWPSVSDHSRGLVITAKEGGANVDASASSSLQRLSSIVDSISSEERKLPSVEEVVEK
Protein: Coiled-coil domain-containing 28B (Coiled-coil domain-containing protein 28B) (B8A4M8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Bardet-Biedl syndrome 1.
- Bardet-Biedl syndrome 10.
- Bardet-Biedl syndrome 12
- Bardet-Biedl syndrome 7 protein homolog
- BBSome complex member BBS2
- Reticulon 4 receptor-like 1a.
- MKS transition zone complex subunit 1
- Tetratricopeptide repeat domain 8.
Sequence:
MEDKRKKRSPKVSLPQPPPPPINPRKLTVLPASKSATFSLGLPQPPSPKPRGKYKRSVGAMGPSKEALAVPVVPPKNTRPHREKPRAPQPAGPSRVSQSSSPLQHTFLTDVSDVREMEGGLLNLLNDFHSGKLQAFGKVCSFEQLEHVREMQERLARLHFSLDSHVEELSEDQRKNASDRNLEHLLSNLEELSTSIQKLHLAENQDLPKTSNT
Protein: Probable ATP synthase subunit g 2, mitochondrial (ATPase subunit g 2) (Q18803)
Organism: Caenorhabditis elegans
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion membrane {ECO:0000250}.
Interaction partners:
- ATP synthase subunit d
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase subunit delta, mitochondrial
- ATP synthase-coupling factor 6
- Oligomycin sensitivity conferral protein
- Putative ATP synthase subunit f
- ATP synthase c subunit
- F-ATPase gamma subunit
Sequence:
MAAPKLGFFEKIANLTGALYRHQHAQFPRRFAILKAVGKHELAPPRQADWPAIKADWAKVQSFIQTGGYKNLSIREGLVYTAVTLEVVFWFFVGEMIGRRYIFGYLVPADYVSKSTKKTVKEQEALAALEN
Protein: Protein transport protein BET1 (Suppressor of loss of YPT1 protein 12) (Protein SLY12) (P22804)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Protein transport protein SEC22
- Integral membrane protein SED5
- Golgi SNAP receptor complex member 1
- Protein SLY1
- Synaptobrevin homolog YKT6
- Protein transport protein BOS1
- Vacuolar v-SNARE NYV1
- Intracellular protein transport protein USO1
- GTP-binding protein YPT1
- Protein transport protein SFT1
Sequence:
MSSRFAGGNAYQRDTGRTQLFGPADGSNSLDDNVSSALGSTDKLDYSQSTLASLESQSEEQMGAMGQRIKALKSLSLKMGDEIRGSNQTIDQLGDTFHNTSVKLKRTFGNMMEMARRSGISIKTWLIIFFMVGVLFFWVWIT
Protein: Class V chitinase CHIT5a (MtCHIT5a) (EC 3.2.1.14) (A0A072VEP0)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5. Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules. Has the capacity to inhibit hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay.
Interaction partners:
- Beta-hexosaminidase
- Beta-hexosaminidase
- Beta-hexosaminidase
Sequence:
MAVQKIIITPILVFLVTIFFNVSSSSSSNNSQYQFLNHGVRSAYWPAGDDFSPSLIDTNYFTHILLAFIQPEPISFKLEITKSGIKWGQNFIKALRHRSPPVKTLLSIGGGGSNSTLFSEIASTKQNREIFINSTIEVARKYRFDGVDLDWEFPETQQDMFNLGLLYEEWYNALFAEAKVRRKPRLLLTSAVYYNSTVRLIGKHGPRSYPTQAINKYLDWASPMCFDYHGTWDNNTDFNAALYDSKSEISTNFGLHSWIKSGVRPEKLVMGLALYGRAWELKDPNVNGVGAEAVGPATDTDGSMNYNEILKFNKQSGANVVYDKVAISFYSYAGTTWIGYDDGPSITTKVRFAKSLGLKGYFFWALGKDKDWSISKQASNAWGH
Protein: Large ribosomal subunit protein uL4m (54S ribosomal protein yml6, mitochondrial) (O74801)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL15m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL3m
- mRNA export factor elf1
- Elongation factor 3
- Large ribosomal subunit protein uL11m
Sequence:
MTAKMLHLVRYKFPSLEPASLFLIPGSFLQERFRRDILHRAVIYEADNDRQGTASSKRRNEITCSGRKLYRQKGTGHARVGDASSPIRRGGAKSHGPKPRDFSTKLQTQVYNLAMRIALSTRFINNELTILENPINLSQPKTRILLEVLKQHKLGHEYGKALFVLNDNYFEDESLKNNNLLLASRQLGYHCSFIPVGEFQVRDALKFGKLFIDSEAMSLIVEKFAQRNTLSDMDQPASLTAYVDANSSSFTKSKPEPSLSL
Protein: Transmembrane protein 254 (Q8TBM7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MATAAGATYFQRGSLFWFTVITLSFGYYTWVVFWPQSIPYQNLGPLGPFTQYLVDHHHTLLCNGYWLAWLIHVGESLYAIVLCKHKGITSGRAQLLWFLQTFFFGIASLTILIAYKRKRQKQT
Protein: Actin cross-linking protein, putative (DUF569) (Q8GXC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Fimbrin-5
- LIM domain-containing protein PLIM2c
- LIM domain-containing protein PLIM2b
- LIM domain-containing protein PLIM2a
- Formin-like protein 3
- TNF receptor-associated factor homolog 1a
- TNF receptor-associated factor homolog 1b
- Actin-depolymerizing factor 7
- Fimbrin-3
Sequence:
MIFNPILGGKIAAVAIKRSLFQIFVILYKRTIMEIFKKAETVRLRSYHDKYLLAEEDEESVSQDRDGRSMNARWTVEVVEKADVIRLKSCFGKYLTASNIPMFLGMTGKRVTQTLPRRLDSSTEWEPVREGVQVRLKTRYGQYLRANGGLPPWRNSITHDIPHRSTTQDWVLWDIDILESRKKKAPPVAEPAYTPLPPPPPPPELLQVRKDDHQEPNSPKGFSLRSPRFSKSESDDTVSSPVKADGRLIYYRIGDEDGNVDETAKEELFCFKGMGLEELKEKLIEETGLSDISICSKNPLNGKLYPLRLHLPPNNTKMHVVLIPSPSKGDAASTS
Protein: Beta-alanine degradation protein BauB (Q9I701)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the degradation of beta-alanine.
Interaction partners:
- Beta-alanine--pyruvate aminotransferase
- Malonate-semialdehyde dehydrogenase
- Probable GABA permease
Sequence:
MSGRPQAVPTVQVDNAEVIVTEWRFAPGAETGRHRHGHDYVVVPLTDGTLLLETPEGDRHAPLVAGQAYFRKAGVEHNVINASAHEVVFVETEIK
Protein: Zinc transporter 7 (Solute carrier family 30 member 7) (Q5BJM8)
Organism: Rattus norvegicus (Rat)
Function: Seems to facilitate zinc transport from the cytoplasm into the Golgi apparatus. Partly regulates cellular zinc homeostasis. Required with ZNT5 for the activation of zinc-requiring enzymes, alkaline phosphatases (ALPs). Transports zinc into the lumens of the Golgi apparatus and the vesicular compartments where ALPs locate, thus, converting apoALPs to holoALPs. Required with ZNT5 and ZNT6 for the activation of TNAP (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:28232492}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9JKN1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9JKN1}. Sarcoplasmic reticulum {ECO:0000269|PubMed:28232492}. Mitochondrion {ECO:0000269|PubMed:29307859}.
Interaction partners:
- Zinc transporter ZIP9
- Zinc transporter ZIP11
- Zinc transporter ZIP13
- Metal cation symporter ZIP8
- Zinc transporter ZIP6
- Zinc transporter SLC39A7
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
Sequence:
MLPLSIKDDEYKPPKFNLFGKISGWFRSILSDKTSRNLFFFLCLNLSFAFVELLYGIWSNCLGLISDSFHMFFDSTAILAGLAASVISKWRDNDAFSYGYVRAEVLAGFVNGLFLIFTAFFIFSEGVERALAPPDVHHERLLLVSILGFVVNLVGIFVFNHGGHGHSHGSGHGHSHSLFNGALDHSHGHEDHCHSHGAKHGGAHSHDHDHAHGHGHLHSHDGPSFKETAGPSRQILQGVFLHILADTLGSIGVIASAIMMQNFGLMIADPICSILIAILIVVSVIPLLRESIGILMQRTPPSLENVLPQCYQRVQQLQGVYNLQEQHFWTLCSDVYVGTLKLVVAPDADARWILSQTHNIFTQAGVRQLYVQIDFAAM
Protein: Alcohol O-acetyltransferase 1 (AATase 1) (EC 2.3.1.84) (EC 3.1.2.20) (P40353)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Major alcohol O-acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate. The alcohol acyltransferase activity is promiscuous with regard to alcohol but relatively specific for acetyl-CoA since ATF1 does not use any other acyl-CoAs (C3, C4, C5, C6, C8, C10, C12). Acts also as an efficient thioesterase in vitro with specificity towards medium-chain-length acyl-CoAs. In natural environments, the production of aromatic volatile metabolites promotes dispersal through insect vectors.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:15042596, ECO:0000269|PubMed:25093817, ECO:0000269|PubMed:28497697}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25093817}; Peripheral membrane protein {ECO:0000269|PubMed:25093817}. Note=Traffics to lipid droplets during the stationary phase (PubMed:25093817). {ECO:0000269|PubMed:25093817}.
Interaction partners:
- Ethanol acetyltransferase 1
- Medium-chain fatty acid ethyl ester synthase/esterase 1
- Medium-chain fatty acid ethyl ester synthase/esterase 2
- Isoamyl acetate-hydrolyzing esterase
- Monoacylglycerol lipase
- Branched-chain-amino-acid aminotransferase, cytosolic
Sequence:
MNEIDEKNQAPVQQECLKEMIQNGHARRMGSVEDLYVALNRQNLYRNFCTYGELSDYCTRDQLTLALREICLKNPTLLHIVLPTRWPNHENYYRSSEYYSRPHPVHDYISVLQELKLSGVVLNEQPEYSAVMKQILEEFKNSKGSYTAKIFKLTTTLTIPYFGPTGPSWRLICLPEEHTEKWKKFIFVSNHCMSDGRSSIHFFHDLRDELNNIKTPPKKLDYIFKYEEDYQLLRKLPEPIEKVIDFRPPYLFIPKSLLSGFIYNHLRFSSKGVCMRMDDVEKTDDVVTEIINISPTEFQAIKANIKSNIQGKCTITPFLHVCWFVSLHKWGKFFKPLNFEWLTDIFIPADCRSQLPDDDEMRQMYRYGANVGFIDFTPWISEFDMNDNKENFWPLIEHYHEVISEALRNKKHLHGLGFNIQGFVQKYVNIDKVMCDRAIGKRRGGTLLSNVGLFNQLEEPDAKYSICDLAFGQFQGSWHQAFSLGVCSTNVKGMNIVVASTKNVVGSQESLEELCSIYKALLLGP
Protein: Inner membrane transport protein RhmT (P76470)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- L-rhamnonate dehydratase
- 2-keto-3-deoxy-L-rhamnonate aldolase
- Uncharacterized HTH-type transcriptional regulator RhmR
- Probable galactarate/D-glucarate transporter GarP
Sequence:
MSTALLDAVVKKNRVRLIPFMLALYVLAFLDRSNIGFAKQTYQIDTGLSNEAYALGAGIFFVVYAFLGVPANLLMRKLGARTWIGTTTLLWGFLSAAMAWADTEAKFLIVRTLLRAAEAGFFPGMIYLTSQWFPQRNRASIMGLFYMGAPLALTLGSPLSGALLEMHGFMGHPGWFWMFVIEGLLAVGAGVFTFFWLDDTPEQARFLSKQEKTLLINQLASEEQQKVTSRLSDALRNGRVWQLAIIYLTIQVAVYGLIFFLPTQVAALLGTKVGFTASVVTAIPWVAALFGTWLIPRYSDKTGERRNVAALTLLAAGIGIGLSGLLSPVMAIVALCVAAIGFIAVQPVFWTMPTQLLSGTALAAGIGFVNLFGAVGGFIAPILRVKAETLFASDAAGLLTLAAVAVIGSLIIFTLRVNRTVAQTDVAHH
Protein: Keratin-associated protein 17-1 (Keratin-associated protein 16.1) (Q9BYP8)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 9-8
- Keratin-associated protein 9-3
- Keratin-associated protein 9-4
- Keratin-associated protein 4-3
- Keratin-associated protein 11-1
- Keratin-associated protein 4-8
- Keratin-associated protein 4-5
- Keratin-associated protein 3-1
- Keratin, type I cytoskeletal 27
- Keratin-associated protein 4-1
Sequence:
MGCCPGDCFTCCTQEQNCCEECCCQPGCCGCCGSCCGCGGSGCGGSGCGGSCCGSSCCGSGCGGCGGCGGCGGGCCGSSCCGSSCCGSGCCGPVCCQPTPICDTK