wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl carrier protein, mitochondrial (ACP) (NADH-ubiquinone oxidoreductase 9.6 kDa subunit) (P32463)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
Subcellular location: Mitochondrion.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase, mitochondrial
- Bud site selection protein 22
- L-2-aminoadipate reductase
- Protein ISD11
- RNA polymerase I-specific transcription initiation factor RRN11
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Large ribosomal subunit protein bL32m
- Cysteine desulfurase, mitochondrial
Sequence:
MFRSVCRISSRVAPSAYRTIMGRSVMSNTILAQRFYSANLSKDQVSQRVIDVIKAFDKNSPNIANKQISSDTQFHKDLGLDSLDTVELLVAIEEEFDIEIPDKVADELRSVGETVDYIASNPDAN
Protein: D-glutamate cyclase, mitochondrial (EC 4.2.1.48) (Q8BH86)
Organism: Mus musculus (Mouse)
Function: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28266638}.
Interaction partners:
- Glutaminase kidney isoform, mitochondrial
- Glutaminase liver isoform, mitochondrial
Sequence:
MTISFLLRSCLRSAVRSLPKAALIRNTSSMTEGLQPASVVVLPRSLAPAFESFCQGNRGPLPLLGQSEAVKTLPQLSAVSDIRTICPQLQKYKFGTCTGILTSLEEHSEQLKEMVTFIIDCSFSIEEALEQAGIPRRDLTGPSHAGAYKTTVPCATIAGFCCPLVVTMRPIPKDKLERLLQATHAIRGQQGQPIHIGDPGLLGIEALSKPDYGSYVECRPEDVPVFWPSPLTSLEAVISCKAPLAFASPPGCMVMVPKDTASSASCLTPEMVPEVHAISKDPLHYSIVSAPAAQKVRELESTIAVDPGNRGIGHLLLKDELLQAALSLSHARSVLVTTGFPTHFNHEPPEETDGPPGAIALAAFLQALGKETAMVVDQRALNLHMRIVEDAIRQGVLKTPIPILTYQGRSMEDARAFLCKDGDPKSPRFDHLVAIERAGRAADGNYYNARKMNIKHLVDPIDDIFLAAQKIPGISSTGVGDGGNELGMGKVKAAVKKHIRNGDVIACDVEADFAVIAGVSNWGGYALACALYILNSCQVHERYLRRATGPSRRAGEQSWIQALPSVAKEEKMLGILVENQVRSGVSGIVGMEVDGLPFHDVHAEMIRKLVGATTVHM
Protein: Response regulator Rcp1 (Q55169)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Forms a two-component system with Cph1 in which it acts as receiver substrate.
Interaction partners:
- Phytochrome-like protein Cph1
- Circadian input-output histidine kinase CikA
- Circadian input-output histidine kinase CikA
- Circadian input-output histidine kinase CikA
- histidine kinase
- histidine kinase
- histidine kinase
- Circadian input-output histidine kinase CikA
Sequence:
MSDESNPPKVILLVEDSKADSRLVQEVLKTSTIDHELIILRDGLAAMAFLQQQGEYENSPRPNLILLDLNLPKKDGREVLAEIKQNPDLKRIPVVVLTTSHNEDDVIASYELHVNCYLTKSRNLKDLFKMVQGIESFWLETVTLPAA
Protein: Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase) (O35074)
Organism: Mus musculus (Mouse)
Function: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Thromboxane-A synthase
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase 3
- Prostaglandin E synthase 2
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Prostamide/prostaglandin F synthase
- Prostacyclin receptor
Sequence:
MSWAALLGLLAVLLLLLLLLSRRRARRPGEPPLDLGSIPWLGHALEFGRDAASFLTRMKEKHGDIFTVLVGGRYVTVLLDPHSYDTVVWELRTRLDFHPYAIFLMERIFDLQLPNFNPSEEKARMKPTLMHRDLQALTEAMYTNLRTVLLGDSTEAGSGWQETGLLEFSYNALLSAGYLTLYGVEASPRTHESQAQDRVHSADVFHTFRQLDLLLPKLARGSLSAGDKDHACSVKNRLWKLLSPARLASRADRSSWLESYLRHLEEMGVSEEMQARALVLQLWATQGNMGPTAFWLLLFLLKNPEALAAVRAELKHTVWQAEQPVSQMTTLPQKILDSMPVLDSVLNETLRLTAAPFITREVMADLALPMADGREFSLRRGDRLLLFPFLSPQKDPEIYTEPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNQCLGKSYAINSIKQFVVLLLTHFDLELGSEDTEVPEFDLSRYGFGLMQPEEDVPIRYRARL
Protein: Chymotrypsin inhibitor WCI (Chloroform/methanol-soluble protein WCI) (P83207)
Organism: Triticum aestivum (Wheat)
Function: Inhibits bovine, insect and wheat chymotrypsins. Inhibits bovine chymotrypsin with Ki of 0.6 nM. Does not inhibit human or wheat alpha-amylases, bovine pancreatic trypsin, or trypsin-like activity isolated from wheat.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01087}.
Interaction partners:
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- Protein kinase domain-containing protein
- Uncharacterized protein
- Pectinesterase inhibitor domain-containing protein
- Uncharacterized protein
- Pectinesterase inhibitor domain-containing protein
- Uncharacterized protein
- Pectinesterase inhibitor domain-containing protein
Sequence:
TSIYTCYEGVGLPVDPLQGCHYYVTSQTCGFVPLLPIEVMKDRCCRELAAISSNCRCEGLRVFIDRAFPPSQSQGGGPPQPPLAPRCPTEVKRDFARTLALPGQCNLPTIHGGPYCVFP
Protein: Homocysteine S-methyltransferase 1 (EC 2.1.1.10) (S-methylmethionine:homocysteine methyltransferase 1) (AtHMT-1) (SMM:Hcy S-methyltransferase 1) (Q9SDL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level.
Interaction partners:
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Cystathionine beta-lyase, chloroplastic
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- Methionine gamma-lyase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- Adenosylhomocysteinase 2
- Adenosylhomocysteinase 1
- S-adenosylmethionine synthase 4
Sequence:
MVLEKKSALLEDLIKKCGGCAVVDGGFATQLEIHGAAINDPLWSAVSLIKNPELIKRVHMEYLEAGADIVVTSSYQATIPGFLSRGLSIEESESLLQKSVELAVEARDRFWEKVSKVSGHSYNRALVAASIGSYGAYLADGSEYSGHYGENVSLDKLKDFHRRRLQVLVEAGPDLLAFETIPNKLEAQACVELLEEEKVQIPAWICFTSVDGEKAPSGESFEECLEPLNKSNNIYAVGINCAPPQFIENLIRKFAKLTKKAIVVYPNSGEVWDGKAKQWLPSQCFGDDEFEMFATKWRDLGAKLIGGCCRTTPSTINAISRDLKRR
Protein: Prolyl hydroxylase EGLN3 (EC 1.14.11.-) (Egl nine homolog 3) (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 3) (HIF-PH3) (HIF-prolyl hydroxylase 3) (HPH-3) (Prolyl hydroxylase domain-containing protein 3) (PHD3) (SM-20) (Q91UZ4)
Organism: Mus musculus (Mouse)
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A. Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (By similarity). Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A (By similarity). Also hydroxylates HIF2A (By similarity). Has a preference for the CODD site for both HIF1A and HIF2A (By similarity). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (By similarity). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (By similarity). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes (By similarity). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia (By similarity). Also hydroxylates PKM in hypoxia, limiting glycolysis (By similarity). Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis (By similarity). In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (By similarity). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (By similarity). Also essential for hypoxic regulation of neutrophilic inflammation. Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H6Z9}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6Z9}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250|UniProtKB:Q62630}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Hypoxia-inducible factor 3-alpha
- Egl nine homolog 1
- Protein kinase C beta type
- Protein kinase C alpha type
- Prolyl hydroxylase EGLN2
- Protein kinase C gamma type
- Aryl hydrocarbon receptor nuclear translocator
- von Hippel-Lindau disease tumor suppressor
Sequence:
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHYNGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAINFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGVLRIFPEGKSFVADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALAKD
Protein: ALX homeobox protein 1 (Cartilage homeoprotein 1) (V9HWA7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEFLSEKFALKSPPSKNSDFYMGAGGPLEHVMETLDNESFYSKASAGKCVQAFGPLPRAEHHVRLERTSPCQDSSVNYGITKVEGQPLHTELNRAMDNCNSLRMSPVKGMQEKGELDELGDKCDSNVSSSKKRRHRTTFTSLQLEELEKVFQKTHYPDVYVREQLALRTELTEARVQVWFQNRRAKWRKRERYGQIQQAKSHFAATYDISVLPRTDSYPQIQNNLWAGNASGGSVVTSCMLPRDTSSCMTPYSHSPRTDSSYTGFSNHQNQFSHVPLNNFFTDSLLTGATNGHAFETKPEFERRSSSIAVLRMKAKEHTANISWAM
Protein: SD06513p (Q95R28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGLNPSRPASSPPPPLSSASQMCRQVQPTGTSASHPHQESTLKASSPDRCTASTEAMSTEHYRCLIQKLRDTNGDAGDMSFELNSIFLKRLDEIDCLDEHEGDDMHTCQLRLITFQEWVDFLLHVNSVILGNVSDLEKEAYSKIVACCQSVQVRQQHTLEENRRLREDICAIIERVQHSPHCTDFDFNGISLETLTVNQLRGVGKDPAHAECESEKMSESMKSLVGEIAAKHDEIGELKSQINALDEVVHTARQKLLLKDQCIAQLNQQLHEITRCIESRDQAKMEESPNDTLTADAITSDMLENLSIHDTQESEMLRLLNAELNDLLDLHNKQEFQTIEIRRKRVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSCLISVDPESEPCDLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKIKISELEARIESESSVLQRNSVVLREIAELICSLGSKEFSYNEIYDESSKENPFCTTIADIFARKFEEEQNQVAIECDTKTPSQTRKPTKTTKIPGATAKTNKQQPTTKPSNKPTTTKTIPTKNTTTTFRTSK
Protein: Protein COP1 SUPPRESSOR 2 (F4HVZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibits E3 ubiquitin-protein ligase activity of COP1, a central repressor of seedling photomorphogenesis. Represses COP1-mediated turnover of HY5 in the dark. Required for primary root development under normal light growth conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:26714275}. Nucleus speckle {ECO:0000269|PubMed:26714275}. Note=Is recruited to nuclear speckles by COP1. {ECO:0000269|PubMed:26714275}.
Interaction partners:
- AT4g02720/T10P11_1
- Pre-mRNA-splicing factor SYF2
- E3 ubiquitin-protein ligase CSU1
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Expressed protein
- 7-dehydrocholesterol reductase-like protein
- At3g05070
- Protein XAP5 CIRCADIAN TIMEKEEPER
- Pre-mRNA-processing-splicing factor 8B
- Pre-mRNA-processing-splicing factor 8A
Sequence:
MPPKRNFRKRSFEEEEEDNDVNKAAISEEEEKRRLALEEVKFLQKLRERKLGIPALSSTAQSSIGKVKPVEKTETEGEKEELVLQDTFAQETAVLIEDPNMVKYIEQELAKKRGRNIDDAEEVENELKRVEDELYKIPDHLKVKKRSSEESSTQWTTGIAEVQLPIEYKLKNIEETEAAKKLLQERRLMGRPKSEFSIPSSYSADYFQRGKDYAEKLRREHPELYKDRGGPQADGEAAKPSTSSSTNNNADSGKSRQAATDQIMLERFRKRERNRVMRR
Protein: H(+)/Cl(-) exchange transporter 7 (Chloride channel 7 alpha subunit) (Chloride channel protein 7) (ClC-7) (O70496)
Organism: Mus musculus (Mouse)
Function: Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:16525474, ECO:0000269|PubMed:31155284}; Multi-pass membrane protein {ECO:0000269|PubMed:16525474}.
Interaction partners:
- Osteopetrosis-associated transmembrane protein 1
- V-type proton ATPase subunit a
- Pleckstrin homology domain-containing family M member 1
- Potassium-transporting ATPase alpha chain 1
- Potassium-transporting ATPase alpha chain 2
- V-type proton ATPase subunit d 2
- Cathepsin K
Sequence:
MANVSKKVSWSGRDRDDEEGAPLLRRTGQPDEETPLLNGAGPGARQSHSALFRIGQMNNVELDDELLDPEVDPPHTFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKDNIDKFTEKGGLSFSLLLWATLNSAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGILGAVFNALNYWLTMFRIRYIHRPCLQVIEAMLVAAVTATVAFVLIYSSRDCQPLQGSSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPMTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGIIVDVLSDTASNHNGFPVVEDVGDTQPARLQGLILRSQLIVLLKHKVFVERSNMGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNHNQVVGLVTRKDLARYRLGKGGLEELSLAQT
Protein: Beta-fructofuranosidase, insoluble isoenzyme CWINV1 (EC 3.2.1.26) (Cell wall beta-fructosidase 1) (AtbetaFRUCT1) (Cell wall invertase 1) (AtcwINV1) (Sucrose hydrolase 1) (Q43866)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}. Secreted, cell wall {ECO:0000305}. Note=Associated to the cell wall. {ECO:0000305}.
Interaction partners:
- alpha-D-xyloside xylohydrolase
- Probable fructokinase-7
- Probable fructokinase-4
- Probable fructokinase-3
- Probable galactinol--sucrose galactosyltransferase 4
- Probable fructokinase-5
- Probable fructokinase-1
- Probable fructokinase-2
- Probable fructokinase-6, chloroplastic
- Hexokinase-1
Sequence:
MTKEVCSNIGLWLLLTLLIGNYVVNLEASHHVYKRLTQSTNTKSPSVNQPYRTGFHFQPPKNWMNDPNGPMIYKGIYHLFYQWNPKGAVWGNIVWAHSTSTDLINWDPHPPAIFPSAPFDINGCWSGSATILPNGKPVILYTGIDPKNQQVQNIAEPKNLSDPYLREWKKSPLNPLMAPDAVNGINASSFRDPTTAWLGQDKKWRVIIGSKIHRRGLAITYTSKDFLKWEKSPEPLHYDDGSGMWECPDFFPVTRFGSNGVETSSFGEPNEILKHVLKISLDDTKHDYYTIGTYDRVKDKFVPDNGFKMDGTAPRYDYGKYYASKTFFDSAKNRRILWGWTNESSSVEDDVEKGWSGIQTIPRKIWLDRSGKQLIQWPVREVERLRTKQVKNLRNKVLKSGSRLEVYGVTAAQADVEVLFKVRDLEKADVIEPSWTDPQLICSKMNVSVKSGLGPFGLMVLASKNLEEYTSVYFRIFKARQNSNKYVVLMCSDQSRSSLKEDNDKTTYGAFVDINPHQPLSLRALIDHSVVESFGGKGRACITSRVYPKLAIGKSSHLFAFNYGYQSVDVLNLNAWSMNSAQIS
Protein: Rab GDP dissociation inhibitor (B5X1S6)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU363124}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MNEEYDVIVLGTGLTECILSGIMSVKGKKVLHMDRNSYYGAESASITPLEDLYKRFSLPGAPPESMGKGRDWNVDLIPKFLMANGQLVRMLLITQVTRYLDFKVIEGSFVYKKGSIYKVPSTETEALASSLMGLFEKRRFRKFLVFVANFDENDPKTMEGVDPNKTTMRDVFKKFDLGQDVIDFTGHSLALYRTDEYLDLPCMDSLNRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIVMEDGKVVGVKSEGEIARCKQLICDPSYLMDRTTKVGQVIRVICIMSHPIKNTSDANSCQIIIPQNQVNRKHDIYVCMISYTHNVAAQGKYVAIVSTTVETDNPEMEVKPAMDLLEPVEQKFVSISDQYAPTDMGAESQIFMSRTYDATTHFETTCDDIKDIYKRMTGTEFDFAEMERKKNDIFGDAADQ
Protein: trypsin (EC 3.4.21.4) (Q8T4B1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MSSQNLLVLLVISFFPIYNCLGDSPRNAFSSLNRVKRLSDGDFDEDSIALSNYCVSLRSRSAEKFFGDNHFCSGVILAPMFVMTSAHCLINKRRVLISSRVLLIVAGTLNRLKYIPNRTFVTPVTHIWLPDSFTMRNKQDFGLLKVKNPFPRNNEHISIARLPVHPPLPGLKCKVMGWGRMYKGGPLASYMLYIDVQVIDSEACAKWLRVPSVEHVCAVDSDDLTAQQPCGGDWGAPMLHNGTVYGIVTILAGCGVSHLPSLYTNVHSNANWIHEKIISSAGSILLVPPLFRYLSIALIYVVTLFNFVMKYNGVM
Protein: RNA-binding motif, single-stranded-interacting protein 1 (Single-stranded DNA-binding protein MSSP-1) (Suppressor of CDC2 with RNA-binding motif 2) (P29558)
Organism: Homo sapiens (Human)
Function: Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication.
Subcellular location: Nucleus.
Interaction partners:
- Complement receptor type 2
- Myc proto-oncogene protein
Sequence:
MGKVWKQQMYPQYATYYYPQYLQAKQSLVPAHPMAPPSPSTTSSNNNSSSSSNSGWDQLSKTNLYIRGLPPHTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPAAAQKAVSALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELENMLKPFGQVISTRILRDSSGTSRGVGFARMESTEKCEAVIGHFNGKFIKTPPGVSAPTEPLLCKFADGGQKKRQNPNKYIPNGRPWHREGEVRLAGMTLTYDPTTAAIQNGFYPSPYSIATNRMITQTSITPYIASPVSAYQVQSPSWMQPQPYILQHPGAVLTPSMEHTMSLQPASMISPLAQQMSHLSLGSTGTYMPATSAMQGAYLPQYAHMQTTAVPVEEASGQQQVAVETSNDHSPYTFQPNK
Protein: Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein) (O43043)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Escort protein required for sre1 processing at low sterol as well as oxygen levels. May regulate export of the scp1/sre1 complex from the ER at low sterol or oxygen levels. 4-methyl sterols bound to scp1 may mask an ER export signal in scp1 leading to retention of the complex in the ER. Release of 4-methyl sterols may trigger a conformational change in the SSD domain of scp1 unmasking the ER export signal leading to recruitment into COPII-coated vesicles, transport to the Golgi complex, proteolytic cleavage of sre1 in the Golgi, release of the transcription factor fragment of sre1 from the membrane, its import into the nucleus and up-regulation of genes required for ergosterol biosynthesis as well as anaerobic growth (By similarity). Binds 4-methyl sterols.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97260}.
Interaction partners:
- Sterol regulatory element-binding protein 1
- INSIG family protein
- Putative transcription factor sre2
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Negative regulator of ofd1
- Rhomboid-type serine protease 2
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- UBX domain-containing protein 10
- C-4 methylsterol oxidase erg25
- Chromatin assembly factor 1 subunit A
Sequence:
MRIFTLGKGRISRGYARQVNPSLFAKYSYCIANNPWYFILVFTLLSITGIYSSLVAYQQSLYDQSLARWSAWYAESINAEANVITKQLYLLGTNTSVFSEDYLSNAYRWETSFHQYLAEYGYPCIRDEKSCVTISPIPKYYGKVDPVAQYSYTKGLPENEREVNKLRNDTIAEGFDSLSAFVITYFLKPEQVDTFHVVLKKFISETPNLYASLLDTSPTTVVARIPDLTVIYRWYLWVGFGVGLFAYLYLSLVRLHDIRAKFGLTATIFIQSGTAYFSTCSLLYFFERTGPICPWPMAYYIIIFMDIENSFRLLRAVIASPQTKRVPSRIMEGFSSTIIASFSSLLKKLLTLFVLSFFVYPLVQEFCLFLACSFVVSFLLHGSFFLAVLSVDIRRLELQDFLDSNSSNRNSKWWVPYLEYVRFMWSPWIIDNLGTVSFHMYVIYLQLQSSTDINGSWRLASPNIRFLITLYHRLGRILRERKLFPLITTGWFGDPTFLEALKEKTMAENLVIALYRPVILDTVNRRDYTNVYNSFHDRRVWRWSTFFSILFAIDFAVGLLVKALLRGWSDHDELSTDTTLHEEKFRIEPVPVHHQLDILKIAVSENYKTFASVGLDRCLVVWDLRQWCTKLVLSKEQMPRTLKAIALDPQGNYVSLFSKDTLFILNVESPCLMLQHSYHCKPNSKLNVFWMPGTHKDDEWKNFELVVVESSGEIQVFSLTIEIEGADIALVEKFQLSSPIIKSISIVSPTANRIACLTESGEVTVYSKKGPVWSPKILSQNKNYLTETKKDIYGIAMADILFLARDSGVDMIDLKNDELLHSFTLPPIKVNTFSVGVSNSRFVNGQFRVSSISFCFTHAVTEKVLYYYYGNECNESYIILNKWDQQPNLVDVHDPDNSLACLTFDELQENIHEVEDASECVMSSDGLYIFGMRRKSSSGICPTADEKNEDNGFTLRNRKLRTGHYNWTSYVPLLDSYMQDMEHKKNTHSGGETQVWEVWMYSQSEKKHRCKSLKMYNSLIIADPGPSLAVSDRCVAIVLGNYVALVGYGSEIFRDFYQIRNSDEMDRILRRKRKNLQRKRSGTIGC
Protein: Cytochrome P450 (Q2UM74)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MPVLATFLESHYFFQGIAVALALIFVSNFYRELADGLPYRKIPLVGRSRWEISNTKAKKLFVTSAKDLMVQGFSQGRTVFQAMFTAGPTIVLHPRYVDELKNHPHLDFGEAVRKSFFGATIPGFEPFNNQTKEDIVIEVINKKLTHTLGQLTIPLSKETAAVLTDKLPGSDEWKPFTFAQEIPHMVARLSSLVFLGEKICRNETWLDVSVNYTIDAFNAARELRDLPAVARPFIHWFMPSMQKLRHHRKVAAEIVQQEIIKRDMIREGKLPEENPPRTHADALDWFREVAAGRPCDETVSQIGLSVAAIHTTSNMLTNVMYDLTAHPEYIQPLRDEIKAIVEQDGILKKTSLTKMKLMDSVMKESQRTNPVSIAFFNRIATEAVVLSDGTSIPKGANVVVSAHVMEDESIYPNAKVYDGFRFYNKRQVPGNEHRYQFVTTSPEHLGFGHGMHACPGRFFANNEIKILLAHLLLKYDWKFADRVDRPKSFLHGTEIICDPTVKLLYKSRQPEVDLSALGEGTTD
Protein: Calmodulin-binding transcription activator 4 (AtCAMTA4) (AtFIN21) (Ethylene-induced calmodulin-binding protein 4) (EICBP4) (Ethylene-induced calmodulin-binding protein d) (EICBP.d) (Signal-responsive protein 5) (AtSR5) (Q9FYG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00767, ECO:0000269|PubMed:19245862}.
Interaction partners:
- IQ domain-containing protein IQM6
- Zinc finger CCCH domain-containing protein 16
Sequence:
MSSVAEDNSFTCDIATIFVAICRNPPANPSDSLFQYEISTLYQEAHSRWLKPPEVLFILQNHESLTLTNTAPQRPTSGSLLLFNKRVLKFFRKDGHQWRRKRDGRAIAEAHERLKVGNAEALNCYYAHGEQDPTFRRRIYWMLDPEYEHIVLVHYRDVSEREEGQQTGGQVYQFAPILSTQNVSYNQYIGDSSDIYQQSSTSPGVAEVNSNLEGSASSSEFGQALKMLKEQLSIGDEHVNSVDPHYIQPESLDSLQFLEYSDIDHLAQPTTVYQRPENNKLERCYGGNFGAQYSAKNDSNKLERCYGGYVGGAEYHSSNLMLVKNGSGPSGGTGGSGDQGSESWKDVLEACEASIPLNSEGSTPSSAKGLLAGLQEDSNWSYSNQVDQSTFLLPQDLGSFQLPASYSALVAPENNGEYCGMMEDGMKIGLPFEQEMRVTGAHNQKFTIQDISPDWGYANETTKVIIIGSFLCDPTESTWSCMFGNAQVPFEIIKEGVIRCEAPQCGPGKVNLCITSGDGLLCSEIREFEYREKPDTCCPKCSEPQTSDMSTSPNELILLVRFVQTLLSDRSSERKSNLESGNDKLLTKLKADDDQWRHVIGTIIDGSASSTSTVDWLLQELLKDKLDTWLSSRSCDEDYITCSLSKQEQGIIHMVAGLGFEWAFYPILAHGVNVDFRDIKGWSALHWAAQFGSEKMVAALIASGASAGAVTDPSRQDPNGKTAASIAASNGHKGLAGYLSEVALTNHLSSLTLEETENSKDTAQVQTEKTLNSISEQSPSGNEDQVSLKDTLAAVRNAAQAAARIQAAFRAHSFRKRKQREAALVACLQEYGMYCEDIEGISAMSKLTFGKGRNYNSAALSIQKNFRGYKDRKCFLELRQKVVKIQAHVRGYQIRKNYKVICWAVRILDKVVLRWRRKGVGLRGFRQDVESTEDSEDEDILKVFRKQKVDVAVNEAFSRVLSMSNSPEARQQYHRVLKRYCQTKAELGKTETLVGEDDDGLFDIADMEYDTLFSLP