wanglab/gogpt-training-data huggingface dataset:
Protein: Retinal dehydrogenase 2 (RALDH 2) (RalDH2) (EC 1.2.1.36) (Aldehyde dehydrogenase family 1 member A2) (ALDH1A2) (Retinaldehyde-specific dehydrogenase type 2) (RALDH(II)) (Q62148)
Organism: Mus musculus (Mouse)
Function: Converts retinaldehyde to retinoic acid. Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal (By similarity). Lacks activity with benzaldehyde, acetaldehyde and octanal. Displays complete lack of activity with citral (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Cytochrome P450 26B1
- Cytochrome P450 26C1
- Retinol dehydrogenase 5
- Alcohol dehydrogenase 1
- All-trans-retinol dehydrogenase [NAD
- Short-chain dehydrogenase/reductase 3
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase class-3
Sequence:
MTSSEIAMPGEVKADPAALMASLQLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVCNPATGEQVCEVQEADKVDIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRATLATMESLNGGKPFLQAFYIDLQGVIKTLRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFTWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVVNILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVKRSVERAKRRIVGSPFDPTTEQGPQIDKKQYNKVLELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALMVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
Protein: Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase family 3 member A1) (HTC-ALDH) (Tumor-associated aldehyde dehydrogenase) (P11883)
Organism: Rattus norvegicus (Rat)
Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids. Preferentially oxidizes aromatic aldehyde substrates. Comprises about 50 percent of corneal epithelial soluble proteins (By similarity). May play a role in preventing corneal damage caused by ultraviolet light (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47739}.
Interaction partners:
- Alcohol dehydrogenase class-3
- Cytochrome P450 2E1
- All-trans-retinol dehydrogenase [NAD
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Aldo-keto reductase family 1 member A1
- Transmembrane O-methyltransferase homolog
- 4-aminobutyrate aminotransferase, mitochondrial
- Catechol O-methyltransferase
- Acetyl-coenzyme A synthetase
Sequence:
MSSISDTVKRAREAFNSGKTRSLQFRIQQLEALQRMINENLKSISGALASDLGKNEWTSYYEEVAHVLEELDTTIKELPDWAEDEPVAKTRQTQQDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAVAAGNAVILKPSEVSGHMADLLATLIPQYMDQNLYLVVKGGVPETTELLKERFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKDFYGEDAKQSRDYGRIINDRHFQRVKGLIDNQKVAHGGTWDQSSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLEEAIQFINQREKPLALYVFSNNEKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVKSLLNEEAHKARYPPSPAKMPRH
Protein: Protein IWS1 homolog 1 (AtIWS1) (Interacts with SPT6 protein 1) (Protein HIGH NITROGEN INSENSITIVE 9) (Protein SUPPRESSOR OF BES-1-D 1) (F4ICK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in RNA polymerase II (RNAPII) transcription regulation. Involved in transcription elongation. May function at post-recruitment and elongation steps of transcription. May be recruited by BZR2/BES1 to target genes and promote their expression during transcription elongation process. Required for brassinosteroid (BR)-induced gene expression. Required the for regulation of numerous nitrogen-responsive genes in roots. Acts in roots to repress NRT2.1 transcription in response to high nitrogen supply. This repression is associated with an IWS1-dependent increase of trimethylation on 'Lys-27' H3K27me3 at the NRT2.1 locus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:20139304, ECO:0000269|PubMed:24838002}.
Interaction partners:
- Transcription elongation factor SPT6 homolog
- FACT complex subunit SSRP1
- Transcription elongation factor SPT6-like
- FACT complex subunit SPT16
- FACT complex subunit
- Protein CTR9 homolog
- Transcription elongation factor SPT4 homolog 2
- Protein LEO1 homolog
- Transcription elongation factor 1 homolog
- Protein RTF1 homolog
Sequence:
MGFEDDPYRDVDGEPIVDFDDFGNDREPSTEPLQDFDEDLADDIGDWDGEGSQTPVYDNDKVAKPRKRLVKKSSSERVTIDVPELIDEDVDDAEFDEFMGGRGGGSTDYDDKVGRKRKKEKERSSSGSGKEKRHKFPNRGERKSEEIDEMWKSIAHNPENDEEGVRTMDDDNFIDDTGLDPSERYGGDAGDRSPTHYPQAEEGEDEDEVNNLFKMGKKKKKTERNPAEIALLVENVMAELEVTAEEDAELNRQGKPAINKLKKLSLLTDVLGKKQLQTEFLDHGVLTLLKNWLEPLPDGSLPNINIRAAILRVLTDFPIDLDQYDRREQLKKSGLGKVIMFLSKSDEETNSNRRLAKDLVDKWSRPIFNKSTRFEDMRNLDEDRVPYRRPPVKKPSNKATMESRDGDFDLEIRERKTGLTSGQSSRGDRQMTMRPEATPLDFLIRPQSKIDPDEIIARAKQVSQDQRRVKMNKKLQQLKGTKKKRLQATKVSVEGRGMIKYL
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (O45418)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein 90
- Co-chaperone protein daf-41
- Adenylosuccinate lyase
- Stress-induced-phosphoprotein 1
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
- Serine/threonine-protein phosphatase 5
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase
- Arf-GAP domain-containing protein
Sequence:
MSGEKIDITPKKDGGVLKLIKKEGQGVVKPTTGTTVKVHYVGTLENGTKFDSSRDRGDQFSFNLGRGNVIKGWDLGVATMTKGEVAEFTIRSDYGYGDAGSPPKIPGGATLIFEVELFEWSAEDISPDRDGTILRTIIVEGSKNSFPNDTSKVLAHCVGTYQGTEFYNREVNFHIGEGSEEGLPEGVERALRRFQLGEKSKIEIRGHKYTYGNSPPAGSNIPVNATLEFTIFLKEFEKVPATWEMTAEEKLDAAKQAKDRGTMYLQKGNLKLAYNKYKRAEEVLEYEKSTDPEKMAERETILNGAYLNLSLVCSKQNEQLECIKWCDKVLETKPGNVKALYRKATALLTMNEVRDAMKLFEKIVEVEPENKAAAQQIIVCRNTIREQNERDKKRFKNLFAKISTEEDKPTNTVEDEDEIVASTSGSSTSNA
Protein: Arrestin-C (Cone arrestin) (cArr) (Retinal cone arrestin-3) (Q9EQP6)
Organism: Mus musculus (Mouse)
Function: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins.
Subcellular location: Photoreceptor inner segment {ECO:0000269|PubMed:28151698}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:28151698}.
Interaction partners:
- Rhodopsin
- Short-wave-sensitive opsin 1
- Medium-wave-sensitive opsin 1
- Recoverin
- Guanine nucleotide-binding protein G
- Photoreceptor-specific nuclear receptor
- Cone-rod homeobox protein
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Sequence:
MSTVFKKTSSNGKFSIYLGKRDFVDDVDTVEPIDGVVLVDPEYLEGRKLFVRLTCAFRYGRDDLDVIGLTFRKDLYVQTKQVAPAEPTSIQGPLTALQERLLHKLGVNAYPFTLQMVANLPCSVTLQPGPEDSGKPCGVDFEVKSFCAENLEEKIPKSDSVQLVVRKVQFSALEPGPGPSAQTIRSFFLSSQPLQLQAWMDREVHYHGEAISVHVSINNYTNKVIRRIKIAVVQTTDVVLYSLDKYTKTVFVQEFTETVAANSSFSQTFAVTPLLAANCQKQGLALDGKLKHEDTNLASSTILRPGMNKELLGILVSYKVRVNLVVSYGGILGGLPASDVGVELPVILIHPKPSPGERAVATSSEDIVIEEFMQHNSQTQS
Protein: XIAP-associated factor 1 (BIRC4-binding protein) (Q6GPH4)
Organism: Homo sapiens (Human)
Function: Seems to function as a negative regulator of members of the IAP (inhibitor of apoptosis protein) family. Inhibits anti-caspase activity of BIRC4. Induces cleavage and inactivation of BIRC4 independent of caspase activation. Mediates TNF-alpha-induced apoptosis and is involved in apoptosis in trophoblast cells. May inhibit BIRC4 indirectly by activating the mitochondrial apoptosis pathway. After translocation to mitochondria, promotes translocation of BAX to mitochondria and cytochrome c release from mitochondria. Seems to promote the redistribution of BIRC4 from the cytoplasm to the nucleus, probably independent of BIRC4 inactivation which seems to occur in the cytoplasm. The BIRC4-XAF1 complex mediates down-regulation of BIRC5/survivin; the process requires the E3 ligase activity of BIRC4. Seems to be involved in cellular sensitivity to the proapoptotic actions of TRAIL. May be a tumor suppressor by mediating apoptosis resistance of cancer cells.
Subcellular location: Cytoplasm. Nucleus. Mitochondrion. Note=Found in the cytoplasm and nucleus of placental syncytiotrophoblasts. Translocates to mitochondria upon TNF-alpha treatment.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Interferon-induced protein 44-like
- Interferon-induced protein 44
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon alpha-inducible protein 6
- 2'-5'-oligoadenylate synthase 2
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon-induced GTP-binding protein Mx1
- Antiviral innate immune response effector IFIT1
- Interferon regulatory factor 7
Sequence:
MEGDFSVCRNCKRHVVSANFTLHEAYCLRFLVLCPECEEPVPKETMEEHCKLEHQQVGCTMCQQSMQKSSLEFHKANECQERPVECKFCKLDMQLSKLELHESYCGSRTELCQGCGQFIMHRMLAQHRDVCRSEQAQLGKGERISAPEREIYCHYCNQMIPENKYFHHMGKCCPDSEFKKHFPVGNPEILPSSLPSQAAENQTSTMEKDVRPKTRSINRFPLHSESSSKKAPRSKNKTLDPLLMSEPKPRTSSPRGDKAAYDILRRCSQCGILLPLPILNQHQEKCRWLASSKGKQVRNFS
Protein: Alpha carbonic anhydrase 2 (AtaCA2) (AtalphaCA2) (EC 4.2.1.1) (Alpha carbonate dehydratase 2) (F4IHR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reversible hydration of carbon dioxide.
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}. Note=Targeted to the chloroplast via a protein-targeting pathway that uses the secretory system. {ECO:0000250}.
Interaction partners:
- Cyanate hydratase
- Beta carbonic anhydrase 4
- Calcium-transporting ATPase 3, endoplasmic reticulum-type
- Putative calcium-transporting ATPase 11, plasma membrane-type
- Cation/calcium exchanger 5
- Vacuolar cation/proton exchanger 3
- Beta carbonic anhydrase 5, chloroplastic
- Ribosome production factor 2 homolog
- Vacuolar cation/proton exchanger 1
- Large ribosomal subunit protein uL18y
Sequence:
MDKISIRCFIFLVLTSFVTTVSCLSAATDYREVEDEHEFSYEWNQENGPAKWGKLRPEWKMCGKGEMQSPIDLMNKRVRLVTHLKKLTRHYKPCNATLKNRGHDMMLKFGEEGSGSITVNGTEYKLLQLHWHSPSEHTMNGRRFALELHMVHENINGSLAVVTVLYKIGRPDSFLGLLENKLSAITDQNEAEKYVDVIDPRDIKIGSRKFYRYIGSLTTPPCTQNVIWTVVKKVNTHRYFLLFFT
Protein: Torsin-1B (Torsin ATPase-1B) (EC 3.6.4.-) (Torsin family 1 member B) (O14657)
Organism: Homo sapiens (Human)
Function: May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. Plays a role in non-neural cells nuclear envelope and endoplasmic reticulum integrity. May have a redundant function with TOR1A in non-neural tissues.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15147511}. Nucleus membrane {ECO:0000269|PubMed:15147511}.
Interaction partners:
- Torsin-1A
- Torsin-1A-interacting protein 2
- HLA class II histocompatibility antigen, DQ beta 1 chain
- HLA class II histocompatibility antigen DQ alpha chain
- Tumor necrosis factor receptor superfamily member 25
- Tumor necrosis factor receptor superfamily member 10A
- Dynein light chain Tctex-type 1
- HLA class II histocompatibility antigen, DP beta 1 chain beta chain)
Sequence:
MLRAGWLRGAAALALLLAARVVAAFEPITVGLAIGAASAITGYLSYNDIYCRFAECCREERPLNASALKLDLEEKLFGQHLATEVIFKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLHPKGLKSNFVHLFVSTLHFPHEQKIKLYQDQLQKWIRGNVSACANSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDGVSYRKAIFIFLSNAGGDLITKTALDFWRAGRKREDIQLKDLEPVLSVGVFNNKHSGLWHSGLIDKNLIDYFIPFLPLEYRHVKMCVRAEMRARGSAIDEDIVTRVAEEMTFFPRDEKIYSDKGCKTVQSRLDFH
Protein: GPI transamidase component GAA1 (Q38CL7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GPI inositol-deacylase
- GPI-anchor transamidase subunit 8
- GPI ethanolamine phosphate transferase 3
- GPI transamidase component Tta1
Sequence:
MLQAGTKKFLREYGSTCAPLFLALGVCLICCLPAACPKENFIDENAISVSRVPVITGMLGELHMDTRISQYTRVVRGRRSVGSESIAVYVNAAFESSVVLANHLIYVLREKENMACDTNFYFFNDTSKDWPIPDSFVRAAIVINVTSFHTNNLCFNVFGANGMQPNQDLFNLAVAIAEKWRFNIDVLCQNPYISFSTSRPIYEHYFLALQTALVAPLRYQPWYKMRSRGISLLAISTEKSERRTKSSYGYNMAAAHEQLIATLSYLHERFHHSTSVWIPLSVDQYVEYDVIQFATILFVASLLSTCYSIYEVEGFSFSPCAALVSATGLAALVSTLNFGTAGFFVSSGVLTVGLGAFSWDMSWGAINAVVLCLLIILQPVAGLVMGFGATLQLQFIHVRCRKWHVLLIGAILSWIVLVALTEVMKAKLFDTETTAGVYFSFFLYPNALWISSRLIRSTLGA
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (A0A8I6AEC4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAATVDHSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEASKQS
Protein: Glutathione peroxidase (Q8IRD4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGRSIVHFFLGSVAIALGSYIYFTMQIDMSANGDYKNAASIYEFTVKDTHGNDVSLEKYKGKVVLVVNIASKCGLTKNNYEKLTDLKEKYGERGLVILNFPCNQFGSQMPEADGEAMVCHLRDSKADIGEVFAKVDVNGDNAAPLYKYLKAKQTGTLGSGIKWNFTKFLVNKEGVPINRYAPTTDPMDIAKDIEKLL
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Cyclophilin) (CPH) (Cyclosporin A-binding protein) (Rotamase) (P18253)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- Ran-specific GTPase-activating protein 1
- GTP-binding nuclear protein spi1
- Uncharacterized protein C22E12.19
- Set3 complex subunit hif2
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL13m
- Putative acyl carrier protein, mitochondrial
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL15m
Sequence:
MSNCFFDVIANGQPLGRIVFKLFDDVVPKTAANFRALCTGEKGYGYAGSTFHRVIPQFMLQGGDFTRGNGTGGKSIYGEKFPDENFALKHNKPGLLSMANAGPNTNGSQFFITTVVTPWLDGKHVVFGEVTEGMDVVKKVESLGSNSGATRARIVIDKCGTV
Protein: Packaging protein UL32 (O41969)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Subcellular location: Host cytoplasm {ECO:0000256|RuleBase:RU364029}. Host nucleus {ECO:0000256|RuleBase:RU364029}.
Interaction partners:
Sequence:
MTQEVFNTAILPLKYTGRHRVVKMYVPWSLETVTSHDSIMQMLLSKSYLPATPETGFHDPTLTHISSTLLPTSKCKICNMLFEAVLEHNPPDSFFSEYATLCFYVLHAPVTWSATYITICDMLQIFSNAGLNHLITEKINSSKIMGIDFYLHFFARQCFRHTTPDQVAQLENLHQVRLSLLSNTICNVQSAAHIQGIWSSSLETAHKKGAQSPDPPTGCPVKAVPHREFFSNTNRPSLLKIFSEAWKRSLLLDPDYSEPDTPVETVDTSQGPCLLSFPFSLKCRGNTSSVCVLCECLACHPEAARILQEIKSTILTCLENNTSLLDRTAYTLMMYTTSKLIDDPDLAEIITSRGPNVLHKHLFCDPFCAINSLKTDPLVLFKYPSGPKFQIFTKALASGKYLAENALFDQPETELLVLALKACQLAQFPKKFEAEVLKGISRLGTTLTTVSPVHFFSVYT
Protein: Uncharacterized protein (Q580W3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWKTKGRGVSTSPELRALVQVIRAADKKDFPELVHPGQRHPPIAALQQMVKEITGRVLTSEELQLFSVMYMSVEYRLCGVDPMTLPESLVGDALSLTFRLESACIKAGISLLNVFPCISAAHNYFLEIRGFKFSVKLVPVFYRLSDAICGLLHRALDKVNEYKARGDWRPASPLSRAAKSSLNQFSEGELCDDIVLWEKVTGNVPEDILDVLTDIDGDVDELLAHLKWYVEACRETIYIDTANFTDDIYVRRLWNSYVGKGMPACFAESCSPALSLLPKCLHEPVMDVLNYRDCGVISLYSLKRLLDIWGPFLLLGRNMKDDVAMGVFDFGHSLEYRCKTFARREDAREGDYVLMLSNVPSEVLALVLVQRRGAIEQQDPGECKRRNRTLAVKRIRFTQSSGAWVPDGLTVEEFDSIGAACRAFPEVFQRPCGTQYDVEQCSDARALVDSGIDNDMAHNVSSLHRACFRNNVRYVKTLLSRGVAVIVNTSIIDPVVSSRYCWTPLLCAVNNPNSDPSEVVQMLLNEGADAYICDNAKCTALYYAIANGYAEAARILLKHFPDLRPSPWTESLLVALGAHHFHAHEGDIRRLADLIPSAAMMRVLLPRENNLRFVQLCVDIIAGKLCGVDRLPRPEDDITLWHPDGDVELRTVEEEEYLTKIVFYHGVHCRENVDEVSVAAQLLYHRCYYLSCREHFGLAVETPQNS
Protein: Protein pof5 (O14235)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MQSFPPEIWHHIFDHLISFDKFEAKNFGGLLRICRSSYVGGLHAIYYFPKLNPRNYHKFVDTISRKPTRKLVHHISLNNVSYASKASITSRLLRRCATNLETFSGPQSGLGFTALRAFSQCQKLKKIDLSILSEKIDLQYLFGGIQHLKHLEYIILPYLSIPAPMCTECWPSSLTFVGFSGGLTDDFLAESVFPPSLKSINITQCPLLTDAGIFSLLSKIGPNLSSVCVQYPMPELSRSGLDCIFQLCPNATTISIPANYITSTAFESIPESGHNVRSLEITYSGSLLTNISLIKADDLVGALVDGKLPNLHRLQWSIRLGWREESQDVQDLLELIDDQDGEVFITVK
Protein: NGFI-A-binding protein 2 (EGR-1-binding protein 2) (Q61127)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability.
Subcellular location: Nucleus. Note=Isoform 2 is not localized to the nucleus.
Interaction partners:
- E3 SUMO-protein ligase EGR2
- Chromodomain-helicase-DNA-binding protein 4
- Early growth response protein 1
- Early growth response protein 3
- DNA helicase
- Signal transducer and transcription activator 6
Sequence:
MHRAPSPTAEQPPGRGDNTRRTPQPRFKASAPAMALPRTLGELQLYRVLQRANLLSYYETFIQQGGDDVQQLCEAGEEEFLEIMALVGMATKPLHVRRLQKALREWATNPGLFSQPVPAVPVSSIPLFKISETAGTRKGSMSNGHGSPGEKAGSARSFSPKSPLELGEKLSPLPGGPGAGDPRIWPGQSTPESDVGAGGEEEAGSPPFSPPAGGGVSEGPGVGGVAAGGAGGGPDRLEPEMVRMVVESVERIFRSFPRGDTGEIASLLKLNKKLARSVGHIFEMDDHDAQKEEEIRKYSVIYGRLDSKRREGKQLSLHELTINEAAAQFCMRDNTLLLRRVELFSLSRQVARESTYLSSLKGSRLHSEELGGPPLKKLKQEVGEQSHNEIQQPPPGPESYAPPYRPSLEEDSASLSGESLDGHLQAVGSCPRLTPPPADLPLALPAHGLWSRHILQQTLMDEGLRLARLVSHDRVGRLSPCVPAKPPLAEFEEGLLDRCPAPGPHPALVEGRRSSVKVEAEASRQ
Protein: EvC ciliary complex subunit 1 (A0A8I5Y1H2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004309}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
Sequence:
MTCRRDARLQLGREALQAAPTLLVPAVLLGALLGLGLGLWLGCRARRLRARLQKDDTKHLLRSSEPPAQSLRDTSSKARRRQRETTRDEDAPEVCEPSLSGNITAFALKARVVYPINQKFRPLADGSSHPSLHENLTQAAAILPHLPHQPAEASPASSLGSLSQAGKEDGSSSSSMQSTYSDDRVLQCAFLRVGSFPEILAYESVDIDLCVCSLHLKDLLQVDAALRQEKHLMFLQILKACLLECFPKKKPEEELYQKILSKQEHDLEELEKGLQARLANTEMLGTGDSGYISLADVERKERELSEQLIDNMGAFWKQMESMQPILMDQLKCSSSKARQLMMTLTGRMIVAEGLLHESQDLHVLDTLERTMGRAHMARIVEFLRTQIQEETKCRLAAISRGLELLTVQGQLSGRQKEELLTQQHKAFWEEAECFGREFMQRGKDLVQVSQAHRAEAVAELTRAQEEERRIFLADTQPTSDPEEFLKAFHEVLERQRLTRSDQEGEEDTRITEAMAALCQELYCGTMETFQKFVDTLFLKTLPEVSSLPVAECEALRQQVQEQAARQLGQADRFRRRQWGLLCDLLEQDKRVWLEECTLSTVLQRQLRDHHESTIHGVLSRFSGLSEESTRGILQGHELLLCSALRRLALRGTTITALAQMRLSGKKRLLQELHEQLALEQGVSPCLEEHQWQLLRALEARILEETARLEDEAQQTALRLQQQLLAEAQEAGQLLQLHSERAIGQALLVHARNVASKGRTRDKEDFKRTLVETVVESVYVTSTSVNRLVQVHYQGIGKLLQAHEEQLLQRLKTLQDERINAYKLWKKQEFSDPPSESQTPGGTHGAPQAVQQRMTSQRKKLLDQFTKHQQGRLNSQRQKAQELDQLEAQLETQLQEAEQTLISELATLARVPLAENKPFSNKRGLPEKPVRTKRKKPPPREREDLGLPNDDHPALADHSTGPLRTSRIK
Protein: Inositol monophosphatase ttx-7 (IMP) (IMPase) (EC 3.1.3.25) (Abnormal thermotaxis protein 7) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase) (Q19420)
Organism: Caenorhabditis elegans
Function: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates (By similarity). Required in central interneurons of the mature nervous system for correct localization of synaptic components. Required for thermotaxis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17158747}.
Interaction partners:
- Inositol-3-phosphate synthase
- Putative inositol monophosphatase 3
- Glucose-6-phosphate isomerase
- 3'
- Uncharacterized protein F21D5.5
- transketolase
- Probable DNA-directed RNA polymerases I, II, and III subunit RPABC2
- ATP-dependent 6-phosphofructokinase 1
- ATP-dependent 6-phosphofructokinase 2
- Phosphoglucomutase-2
Sequence:
MVFQPIHEEEQVFVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSLGLHNRVQFGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDVMSRKVLCAGTAELGRDLSACLTHVDFEPEA
Protein: phosphopyruvate hydratase (EC 4.2.1.11) (G8BCT3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase
- Pyruvate kinase
- Pyruvate decarboxylase
- mRNA 3'-end-processing protein RNA14
- Phosphoglycerate mutase
- Transketolase
Sequence:
MAITKIHSRYVYDSRGNPTVEVDLNTEKGSFRAIVPSGASTGVHEALELRDGDKSKWLGKGVLKAVANVNDVIAPALIKANIDVADQAKIDEFLLKLDGTPNKSKLGANAILGVSLAAAKAGAAEKNVPLYKHIADISKAKQGKYVLPVPFQNVLNGGSHAGGDLAFQEFMIVPSGAPTFSEGLRIGSEVYHHLKSLTKKKYGQSAGNVGDEGGVAPDIKTAQEALDLIVSAIEAAGYTGKVDIAMDVASSEFYKDGKYDLDFKNPDSDKSKWLSGPQLAELYGELLQKYPIVSIEDPFAEDDWEAWSHFFSKVGGKVQIVGDDLTVTNPLRIKKAIETKAADALLLKVNQIGTLTESIQAANDSYAAGWGVMVSHRSGETEDTFIADLSVGIRSGQIKTGAPARSERLAKLNQILRIEEELGDNAIYAGKDFHNAQTL
Protein: Salicylate 5-hydroxylase, small oxygenase component (S5H small oxygenase component) (EC 1.14.13.172) (Salicylate 5-hydroxylase, oxygenase component NagH) (Salicylate 5-monooxygenase, hydroxylase small subunit) (O52380)
Organism: Ralstonia sp
Function: Oxygenase component of the salicylate 5-hydroxylase (S5H) multicomponent enzyme system which catalyzes the 5-hydroxylation of salicylate to gentisate. Active only on substrates with a ring-substituted carboxylate group with an adjacent hydroxyl group. Primarily active against salicylate and substituted salicylates, but not against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate or 2-hydroxyacetophenone.
Interaction partners:
Sequence:
MVDFKTYFELLNLYSDYAMVCDSANWEKWPDFFIETGTYRLQPRENFEQGLPLCLLALESKAMIRDRVYGVKETMYHDPYYQRHIVGTPRVLSVERDADGERITAEASYAVIRTKYDGDSTIFNAGYYRDVIVRTPEGLKLKSRLCVYDSEMIPNSVIYPI
Protein: Phospholipid-transporting ATPase accessory subunit mug89 (Meiotically up-regulated gene 89 protein) (Q1MTQ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phospholipid-transporting ATPase C4F10.16c
- Phospholipid-transporting ATPase dnf2
- Phospholipid-transporting ATPase C887.12
- Phospholipid-transporting ATPase accessory subunit ivn1
Sequence:
MPEALNENVSDTASNGPVAKTRAPPNTSFRQQRIKSWQPLLTPKIVLPLFFVLGIIFGPLGGGLLYASSIVQELVVDYTDCETLASYDEFSAVPSKKYTASFDQSGTIGFDKESTYWKLEKILDKDLDMDVNYCIIRFTVPSVLKAPIFIYYRLTNFFQNHRRYAKSVDEKQLQGVALTADEVKGGNCFPLEVNEDDKPYYPCGLIANSLFNDTFSSLRLLDDNSVYTFSTKNIAWASDKRRFLKTNYSPDDVAPPPNWVLRYPDGYTESNMPDLSTMENLQVWMRTAGLPTFSKLAMRNDNDDIFPGTYEIKIGLFFPVKSFDGTKSLVLTTRSVLGGKNPFLGIAYIVVSAVCVVLGTVFTLRHFIRPRKLADHRYLNWDSEENNLAPHLSDRP