wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized MFS-type transporter YdeE (P31126)
Organism: Escherichia coli (strain K12)
Function: A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth. Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inner membrane protein YbcI
- Uncharacterized MFS-type transporter YfcJ
- Probable amino-acid metabolite efflux pump
Sequence:
MNLSLRRSTSALLASSLLLTIGRGATLPFMTIYLSRQYSLSVDLIGYAMTIALTIGVVFSLGFGILADKFDKKRYMLLAITAFASGFIAITLVNNVTLVVLFFALINCAYSVFATVLKAWFADNLSSTSKTKIFSINYTMLNIGWTIGPPLGTLLVMQSINLPFWLAAICSAFPMLFIQIWVKRSEKIIATETGSVWSPKVLLQDKALLWFTCSGFLASFVSGAFASCISQYVMVIADGDFAEKVVAVVLPVNAAMVVTLQYSVGRRLNPANIRALMTAGTLCFVIGLVGFIFSGNSLLLWGMSAAVFTVGEIIYAPGEYMLIDHIAPPEMKASYFSAQSLGWLGAAINPLVSGVVLTSLPPSSLFVILALVIIAAWVLMLKGIRARPWGQPALC
Protein: threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (Q8IP94)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKKEKKEKPSGGGDTRKELSPLPKYIEERNVFWEKCKAEYEAELAAKKREPIKVTLPDGKQVDATSWETTPYEVARGISQGLADNTVISKVNGEVWDLDRVLEGNCTLQLLKFDDPEAQAVFWHSSAHIMGEAMERIYGGHLCYGPPIENGFYYDMHLEGEGISTNDYGAMEGLVKQIVKEKQNFERLEMKKSDLLEMFKYNEFKVRILNEKVTTDRTTVYKCGSLIDLCRGPHVRHTGKVKALKITKNSSTYWEGKADAETLQRVYGISFPDPKQLKEWEKLQEEAAKRDHRKIGREQELFFFHELSPGSCFFQPRGAHIYNTLMGFIKAEYRKRGFQEVISPNIYNAKLWMTSGHWQHYAENMFSFEAEKEKFALKPMNCPGHCLIFDNRNRSWRELPLRMADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAPEQIKSEMKGCLEFLKYVYTIFGFSFQLVLSTRPDNYLGELEQWNDAEKALAESLNEFGMPWKENPGDGAFYGPKIDITIMDALKRAHQCATIQLDFQLPIRFNLSYIADDGEKKRPVIIHRAILGSVERMIAILTENFAGKWPFWLSPRQVMVVPVGPAYDQYAQSVRDQLHDAGFMSEADCDAGDTMNKKIRNAQLAQFNFILVVGDKERSSNTVNVRTRDNKVHGEVSVAELITKLQKIRDEFIANEDSF
Protein: SAGA-associated factor 29 (29 kDa SAGA-associated factor) (SAGA histone acetyltransferase complex 29 kDa subunit) (P25554)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Chromatin reader component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. In the SAGA complex, SGF29 specifically recognizes and binds methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3). SGF29 is also required for heterochromatin boundary formation function. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit TAF6
- SAGA complex/transcription factor TFIID complex subunit TAF5
- SAGA complex subunit HFI1
- SAGA complex subunit SUS1
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF10
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex subunit SGF73
- Histone acetyltransferase GCN5
- SAGA complex subunit NGG1
Sequence:
MDGYWDVVVSSLQDIYNANEVIPFDDELQTKKLNFLNMSKDQLQLHLNTFQEHMENVNRVHRILDNVRSNLSLMLNQSREEKSEENTEDAEEGEGTRMALSQGKKAVGKVGRSYWTSEYNPNAPILVGSEVAYKPRRGSADGEWIQCEVLKVVADGTRFEVRDPEPDELGNSGKVYKCNRKELLLIPPGFPTKNYPPGTKVLARYPETTTFYPAIVIGTKRDGTCRLRFDGEEEVDKETEVTRRLVLPSPTALANLARK
Protein: Transcription factor atoh8 (Atonal bHLH transcription factor 8) (Protein atonal homolog 8) (D2CLZ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). During development, is required for heart looping and swim bladder formation by acting in concert with GATA4 and ZFPM1. During the development of both the retina and skeletal muscles is required for neural retinal cell through modulating PAX6 and NEUROG3 expression and myogenic differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99NA2}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q99NA2}.
Interaction partners:
Sequence:
MKNPHLNSPCKILNTVSGDKKMKRKAREPIKHVSEDHYPYFKLYKNPHLMAETLGDGSPQETHRSEIITSRDDSVRNDVLNTAVDMRINTITAAEVPDSKLRSVSEKTVNSKIVQASPQVSVLSAPQVFPLERVVLSQRAASQAPAGGSERAESPRKRAGEPSGVVTEIKAIQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLAQLADLDYTPDHRNMSFRECVEQCTRTLQAEGRSKKRKE
Protein: Probable serine/threonine-protein kinase dyrk1 (EC 2.7.12.1) (Dual specificity tyrosine-phosphorylation regulated kinase 1) (Q76NV1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DDB1- and CUL4-associated factor 7 homolog
- Small GTPase
Sequence:
MDSDAKSRNDAPIIKLSIDLIKTYKHINQVYYTAKAKKKQQAQQQAQQQAQQLQQQAQQQQHQLQQQQQLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQYQQQHNNNINNNNNNSNINNKNNNNNNTNFNTSNNNNNTNNNSNNNSNNNNSNNNNNNNNINNINNININNKNNNNNNNNNNNINNINNNNNKNNNNNNNNNNNDDNNNINNNNSNNNNNNNNNNNNNNNNNNNNNNNNNSNNNNNNNNLNNNNSNNNYNNNTTTTSSSNNNNNNKQSKYNDGYDDENADYIVRIGEVFVDRFEIISSLGKGSFGQVVKAFDSVLKEYVAIKIIKNKVPFYNQALIEIRLLELMNNKDPEDQYKIIKLKHHFKFRNHLCIVTELLSYNLYDLLRNTHFHGVSLNLIKKFAHQILTALFFMSTPEVDVIHCDLKPENILLRNPKRSAIKIIDFGSSCHSNERMYKYIQSRFYRSPEILLELEYSFSIDMWSLGCILVEMHVGEPLFSGQNEQDQLTKIIEVLDLPPSHMIDSSPKAKKFFTKDPINSTYQLKKNEKLKTNVEFCKKKLSEIIGVETGGPQSRRKNEPGHALVDYLKFLDLIEKMLIYDPQKRITPLEALQHSFFLTDETSQPPQQQSQQQSQQQSQQQSQQQSQQQSQQRRQSNTDNNFSNNNPINNYNSPSSKSPHQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQTYSPTTQQSNHKLVDQMKKASMKDKSPHSNISNILNDSEEDNSKVHINSNTSDNMQARINFQVENQSNIYNNNNNNNNNNNNNNNNNNSNNYNNSNELSPNPPILPNLKDLLPHNNNNI
Protein: Lipase member I (A0A2Q2TCK2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCTYYFVLSIIVPDKTMMDGSFSFKLLNQLGMIEEPRLYEKNKPFYKLQEVKILAQFYNDFVNISSIGLTYFQSSNLQCSTCTYKIQSLMLKSLTYPERPPLCRYNIVLKDREEVFLNPNTCTPKNT
Protein: Tip elongation aberrant protein 1 (Altered polarity protein 8) (Cell polarity protein tea1) (P87061)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cell polarity protein. Acts as an end marker, directing the growth machinery to the cell poles. Involved in the regulation of microtubular organization, affecting the maintenance of a single central axis. Prevents the curling of microtubule tips around the cell ends and is required for the retention of polarity factors such as pom1, tip1 and tea2 at the cell ends, necessary for the cell to grow in a straight line. Links tip1 and tea4 in a common complex.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12034771, ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9200612}. Note=Present at both poles of the cell throughout the cell cycle whether they are growing or not. Located at the ends of microtubules growing towards the cell poles. An intact microtubular skeleton is required to maintain the location at the cell tips; on the other hand, a normally organized actin cytoskeleton is not required.
Interaction partners:
- Tip elongation aberrant protein Tea4
- Tip elongation protein 1
- Formin-3
- Kinesin-like protein tea2
- Actin-interacting protein 3 homolog
- DYRK-family kinase pom1
- Microtubule integrity protein mal3
- Cell division control protein 42 homolog
- Actin
- Tip elongation aberrant protein 3
Sequence:
MSFLFKRNKGSAHKPTKPNFSKTSTTPSTSQLKHSHESNVKMSTSTVTEHRKKPTGSGSHITASPWSKLTVRGSSNVLPRYSHASHLYAEGGQEIYIFGGVASDSQPKNDLWVLNLATSQFTSLRSLGETPSPRLGHASILIGNAFIVFGGLTNHDVADRQDNSLYLLNTSSLVWQKANASGARPSGRYGHTISCLGSKICLFGGRLLDYYFNDLVCFDLNNLNTSDSRWELASVVNDPPPARAGHVAFTFSDKLYIFGGTDGANFFNDLWCYHPKQSAWSKVETFGVAPNPRAGHAASVVEGILYVFGGRASDGTFLNDLYAFRLSSKHWYKLSDLPFTPSPRSSHTLSCSGLTLVLIGGKQGKGASDSNVYMLDTSRFRLGSVPTTSGRQRNTSFFSNSTGNTNPSAFNGLLTSSRIPSYNGSKVRSTSHPSRQQYIGSSNSRFNTRHQTISTPVSGRASNDLPSPVVPTRSNSSSILQPSYNLNSHSSDRRNTNDDDQSSLNSQQLSNQAKAQGEVSPTLSFVPSSHSMEQGNGSVASANNAQSEAATRSINSISEVSEVRFPEQSSVKTVDERKSLDGRITSVTLETLVEKYSELSKQQIVEWFKSKLYEILRDSASKIDSLTEKLKVANAEKNAALCEAALEKVPLAKHNKLSDGTFSTPDKENVQSTNDAHIMQENFSLHKALEVMRETSSDLDKQLKDATASQKELIVQTSSFQKELVEERERHNAISKRLQEIESLYRDRELLVTNLEDQLVDQTVTINKFAFERDQFRERSMGFENTIKDLTRKMEATDMLNVSLHESLRSVQTENSELVTEMALLKAELVKKQAIIDANANIYDKLTADHTNYETVSADINQNLKETLDKLLNGSSDFKNNEIELLHDQIRITNAKLEKREKLINASKYIEDTLRSEIQEAAEKVSNLEFSNFNLKEENSNMQLQLMKALEQRNTGAKQLVNLRMQLSTATSELDMLKLKLRTTALALEESPDDYSDILSILRADMSPFHDLHKQCGVLIDTLNGVKRGFGIFEKKFTDYHKFLENISDKLKSEEDTSLETPIHENQSIQSDQIKEVGEVLSAIKSLSDSVMLLKNQIDDLAKEKLPLSSSDDEKVNIKEKTDFMKLLVKSGLSNPPAKEPVHDNEN
Protein: Myocyte enhancer factor 2cb (Myocyte-specific enhancer factor 2C isoform X4) (A2BGA7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESKDKYREINDDIDLHMISRQRICAVPSSTYDMTIPVNNQIYPGNHNLLPLAHHGLQRNSMSPGVTHRPPSAGGLMGTDLSTGAGTSAGNGYGNHRNSPGLLVSSGGMNKSMQAKSPPPVNLGMNSRKPDLRVLIPPGAKNNMPSISEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTSYGTEYSLSSADLSSISGFNSANTLHLGSMSGWQQHQIQNMQHSALSQLGNCSSSHLCQGSNLSLPSTQSLHIKSEPVSPPRDRSSSTTPGGYGQLPSHQQHQGPTSQGRQDSGRSPADSLSSCGSSHEGSDRDEHRPDFHSPLGLGRPGLDDQDSPSIKRIRLSEGWAT
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) (Isovaleryl-CoA dehydrogenase 2) (St-IVD2) (Q9FS87)
Organism: Solanum tuberosum (Potato)
Function: Involved in the catabolism of amino acids. Uses isovaleryl-CoA as substrate. Minor activity detected with 2-methylpalmitoyl-CoA or 2-methylbutanoyl-CoA, but no activity with short- and medium-straight chain acyl-CoA esters or with 2-methylhexanoyl-CoA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11231285}.
Interaction partners:
- methylcrotonoyl-CoA carboxylase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Biotin-containing subunit of methylcrotonyl-CoA carboxylase
- Peroxisomal enoyl-CoA hydratase/isomerase family protein
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- 2-methylacyl-CoA dehydrogenase, mitochondrial
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
- AMP dependent ligase
Sequence:
MHKLFVARSVKSALFRIKNHQKPQFAAFSTSLLFDDTQKQFKESVAQFAQENIAPHAEKIDRTNYFPQDVNLWKLMGNFNLLGITVPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHTNLCINQLVRNGTHEQKQKYLPKLISGEHVGALAMSEPNAGSDVVSMKCKADRVEGGYVLNGNKMWCTNGPTAQTLVVYAKTDVTAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQVGRGVYVLMSGLDLERLVLASGPVGIMQACLDVVLPYVKQREQFGRPIGEFQFVQGKVADMYTSMQSSRSYLYSVARECDSGTINTKDCAGVILSAAERATQVALQAIQCLGGNGYVNEYPTGRFLRDAKLYEIGAGTSEIRRMIIGRELFKEQ
Protein: Large ribosomal subunit protein uL14A (60S ribosomal protein L23-A) (L17a) (YL32) (P0CX41)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL24A
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
Sequence:
MSGNGAQGTKFRISLGLPVGAIMNCADNSGARNLYIIAVKGSGSRLNRLPAASLGDMVMATVKKGKPELRKKVMPAIVVRQAKSWRRRDGVFLYFEDNAGVIANPKGEMKGSAITGPVGKECADLWPRVASNSGVVV
Protein: Polypyrimidine tract-binding protein homolog 1 (Q9MAC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in pre-mRNA splicing. Binds to the polypyrimidine tract of introns. May promote the binding of U2 snRNP to pre-mRNA (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SUPPRESSOR OF ABI3-5
- Nuclear cap-binding protein subunit 2
- Serine/arginine-rich splicing factor SC35
- RNA-binding
- E3 ubiquitin-protein ligase UPL7
- At3g02555
- Pentatricopeptide repeat-containing protein At5g55840
- Nuclear cap-binding protein subunit 1
- AP-2 complex subunit mu
- Vacuolar fusion protein MON1 homolog
Sequence:
MSSSGQTQFRYTQTPSKVVHLRNLPWECVEEELIDLCKRFGKIVNTKSNVGANRNQAFVEFADLNQAISMVSYYASSSEPAQIRGKTVYIQYSNRHEIVNNQSPGDVPGNVLLVTFEGVESHEVSIDVIHLVFSAFGFVHKIATFEKAAGFQALVQFTDVETASAARSALDGRSIPRYLLSAHVGSCSLRMSYSAHTDLNIKFQSHRSRDYTNPYLPVNQTAMDGSMQPALGADGKKVESQSNVLLGLIENMQYAVTVDVLHTVFSAYGTVQKIAIFEKNGSTQALIQYSDIPTAAMAKEALEGHCIYDGGYCKLRLSYSRHTDLNVKAFSDKSRDYTLPDLSLLVAQKGPAVSGSAPPAGWQNPQAQSQYSGYGGSPYMYPSSDPNGASPSGQPPYYG
Protein: AT1G22750 protein (Transmembrane protein) (O64379)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable WRKY transcription factor 14
- Berberine bridge enzyme-like 6
- Endoglucanase 4
- Isopentenyl phosphate kinase
- CBL-interacting serine/threonine-protein kinase 18
- NAC domain-containing protein 1
Sequence:
MATTSLVTGLKVVLPVMFCLMLATLVYTIITDGLPLPDRQDVFTPWFVTTILDFYINLVPIAVWIVYKESTWSGSILWTILLIIFGSLTTCVYLFLQLLKLTNQEASEDPMYYLLLRDSIKDGVGLRDKNSLVVTARFVFGALGCVMLGALVYTCFTYGSPFHMELLYPWMVVLLVNFYIDVAVLSVWVVYKESSLIIGILWVALLIGLGSVGTSAVIVVQLFRLSPLDPLYLVLVNNSNRAGDMYERTHSAALRIM
Protein: Reticulon-1-A (RTN1.1) (xRTN1) (XRTN1-C.1) (Q6IFY7)
Organism: Xenopus laevis (African clawed frog)
Function: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17969151}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:17969151}. Note=Mainly localized to the endoplasmic reticulum with some expression in the nucleus and polysome fractions. {ECO:0000269|PubMed:17969151}.
Interaction partners:
Sequence:
MQASADSTRMECLWSNWKCQAIDLLYWRDIKQTGIVFGSVLLMLFSLIQFSVVSVMAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKSYLDMEISLSQEQIQKYTDCLQVYTNSIAKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLIMAVVSMFSLPVVYDKYQAQIDQYLGLVRTNMNTIMTKIQAKIPGTKQKE
Protein: Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) (Q54DF9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protoporphyrinogen oxidase
- Oxygen-dependent coproporphyrinogen-III oxidase
- Porphobilinogen deaminase
- Ferrochelatase, mitochondrial
- CDK5RAP1-like protein
- JmjC domain-containing protein B
- Molybdenum cofactor biosynthesis protein 1
Sequence:
MSEENINKNEFPELKNDTFLKACRGEEVPYVPVWIMRQAGRYLPEFKSVRADVDFFSVCRTPELACKVTLQPLDRFPLDAAIIFSDILVVPQAMGIEVQMIPGKGPFFPNPIRTIEDLSRVQFPVDVNKELGYVFDALTLTRKRLEGRVPLIGFTGAPWTLMTYCIEGSGGTTMSNSKSWLYKHPAESHKFLSMLTRVCIDYLLGQIKAGAQALQIFDSWSNELSPAMFKEYCLPYLVQIGKEVKAVHPEIPLICFAKGSNFALEDLSKSGAYDVLGIDWTIEPSVAREMVADRVSLQGNLDPCVLYCGDQVIRDQTQKMLQSFGTTKRLIANLGHGMHPTHPIEGPESYVKAVHELSKQMINK
Protein: Golgi SNARE protein-like (Q383Q2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004409}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004409}.
Interaction partners:
- SNARE protein, putative
- Syntaxin 5
- Vesicle-associated membrane protein, putative
- Sec1 family transport protein, putative
- Vesicle tethering protein Uso1/P115-like head domain-containing protein
- Golgi vesicular membrane trafficking protein, putative
- t-SNARE coiled-coil homology domain-containing protein
- Longin domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Gamma-soluble NSF attachment protein
Sequence:
MDSKQRIWDSLRNDARQADNLIERKLAALEDIARRVDDETSGVSFGAKGTAPTTGFNQYNNPSSSSSTTFGNTAVVHFPSESHVRSVQREFEHSQSEVEVVLQRFETLLETMAETARELPLESAAMTHMERFQQLAVEKRRTLFRVAADFKRRCERVELLPNISRELDVHREDVGTQLLLKEQESLRHTQRMLNNIIDRGEQAHLQLREQRDTFSSVSDRLLEITQRVPFVKNVLNRIDSRRRREAVIVGALIGLCMTIFVLFLF
Protein: S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase beta chain; S-adenosylmethionine decarboxylase alpha chain] (Q9UWY8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. Has no arginine decarboxylase (ArgDC) activity.
Interaction partners:
- Polyamine aminopropyltransferase
- S-adenosylmethionine synthase
- Arginine decarboxylase proenzyme
- DNA
- NAD
Sequence:
MMMGVELAFPKVVGKQVYGSLYECDEDVLKDTKRLEQIIKEAADIGNMNILDIKSWKIGEGVSVVAIILESHITIHTWPEYRFATVDVYSCGPHTSPLNAFRYIVEKLGAKRYTINEADRSSEF
Protein: Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' (EC 3.1.4.35) (cGMP phosphodiesterase 6C) (Q91ZQ1)
Organism: Mus musculus (Mouse)
Function: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanylate kinase
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Adenine phosphoribosyltransferase
- Cyclic nucleotide-gated channel beta-3
- GMP synthase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Cyclic nucleotide-gated channel alpha-3
- Retinal guanylyl cyclase 2
Sequence:
MGEISQEAVERYLEKNPCFAKEYFDKKLRVEALGVIFKNSHAGVQTGLSLPEMTQVEESAVCLELLQCMQDEAGSAEQMAHRALQRLAQLLQADCCSMFSCRARNGIPEVASRLLNVTPTSKFEDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVKKNSHFSDFMDKQTGYVTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYLYSVESRRSQILMWSANKVFEELTDVERQFHKALYTIRTYLNCDRYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREIIFYKIIDYILHGKEEINVIPSPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEHITETLTQFLGWSLLNTDTYERVNKLESRKDIAQEMVMNLTKATPDEISSILKFKEKLNVEVIEECEERQLLAILKEDLPDPRTADLYEFCFSDFPITEHELVKCGLRLFLEINVVEKFKVPVEVLTRWMYTVRKGYRPVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGTSILERHHLEYSKTLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDTCEQMQSEEETIKYVTSDPTKKEVIMAMMMTACDLSAITKPWEVQSQVALLVANEFWEQGDLERTVLQQQPIPMMDRSKKDELPKLQVGFIDFVCTFVYKEFSRFHGEITPMLNGLQNNRVEWKSLAEEYEAKVKVTEEEAGKQEEEASDGKAATDLGGSAEDKKSKTCLML
Protein: GPI transamidase component PIG-T (Phosphatidylinositol-glycan biosynthesis class T protein) (Q969N2)
Organism: Homo sapiens (Human)
Function: Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Single-pass type I membrane protein {ECO:0000269|PubMed:11483512}.
Interaction partners:
- GPI-anchor transamidase
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGU
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase, stabilizing subunit
- GPI alpha-1,6-mannosyltransferase 2
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
Sequence:
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQREGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTVTDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREVVCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQTLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPPTTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSGYGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQDRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVAAKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCYGSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
Protein: ATP-dependent RNA helicase DHH1 (EC 3.6.4.13) (DExD/H-box helicase 1) (P39517)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs. May also have a role in translation and mRNA nuclear export. Required for sporulation. Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15706350}.
Interaction partners:
- m7GpppN-mRNA hydrolase
- General negative regulator of transcription subunit 5
- LSM1-LSM7 complex subunit LSM1
- General negative regulator of transcription subunit 3
- Protein SCD6
- Poly
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 1
- mRNA-decapping enzyme subunit 1
- Enhancer of mRNA-decapping protein 3
Sequence:
MGSINNNFNTNNNSNTDLDRDWKTALNIPKKDTRPQTDDVLNTKGNTFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKVKPKLNKIQALIMVPTRELALQTSQVVRTLGKHCGISCMVTTGGTNLRDDILRLNETVHILVGTPGRVLDLASRKVADLSDCSLFIMDEADKMLSRDFKTIIEQILSFLPPTHQSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTLKGITQYYAFVEERQKLHCLNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQERNKVFHEFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIAAIPATIDKSLYVAENDETVPVPFPIEQQSYHQQAIPQQQLPSQQQFAIPPQQHHPQFMVPPSHQQQQAYPPPQMPSQQGYPPQQEHFMAMPPGQSQPQY