wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear egress protein 2 (P10218)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04024, ECO:0000269|PubMed:12163613, ECO:0000269|PubMed:16415024}. Note=Also localizes at the transient membrane of perinuclear virions. {ECO:0000255|HAMAP-Rule:MF_04024}.
Interaction partners:
Sequence:
MAGLGKPYTGHPGDAFEGLVQRIRLIVPSTLRGGDGEAGPYSPSSLPSRCAFQFHGHDGSDESFPIEYVLRLMNDWAEVPCNPYLRIQNTGVSVLFQGFFHRPHNAPGGAITPERTNVILGSTETTGLSLGDLDTIKGRLGLDARPMMASMWISCFVRMPRVQLAFRFMGPEDAGRTRRILCRAAEQAITRRRRTRRSREAYGAEAGLGVAGTGFRARGDGFGPLPLLTQGPSRPWHQALRGLKHLRIGPPALVLAAGLVLGAAIWWVVGAGARL
Protein: MAGE family member A10 (C9J958)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPRAPKRQRCMPEEDLQSQSETQGLEGAQAPLAVEEDASSSTSTSSSFPSSFPSSSSSSSSSCYPLIPSTPEEVSADDETPNPPQSAQIACSSPSVVASLPLDQSDEGSSSQKEESPSTLQVLPDSESLPRSEIDEKVTDLVQFLLFKYQMKEPITKAEILESVIRNYEDHFPLLFSEASECML
Protein: GDNF family receptor alpha-1 (GDNF receptor alpha-1) (GDNFR-alpha-1) (GFR-alpha-1) (RET ligand 1) (TGF-beta-related neurotrophic factor receptor 1) (P56159)
Organism: Homo sapiens (Human)
Function: Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q62997}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q62997}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q62997}. Endosome {ECO:0000250|UniProtKB:Q62997}. Endosome, multivesicular body {ECO:0000250|UniProtKB:Q62997}. Note=Localizes mainly to the plasma membrane. In the presence of SORL1, shifts to vesicular structures, including trans-Golgi network, endosomes and multivesicular bodies. {ECO:0000250|UniProtKB:Q62997}.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Glial cell line-derived neurotrophic factor
- Neurturin
- Artemin
- Persephin
- Neural cell adhesion molecule 1
- Beta-nerve growth factor
- Neurotrophic factor BDNF precursor form
- High affinity nerve growth factor receptor
- Endothelin receptor type B
Sequence:
MFLATLYFALPLLDLLLSAEVSGGDRLDCVKASDQCLKEQSCSTKYRTLRQCVAGKETNFSLASGLEAKDECRSAMEALKQKSLYNCRCKRGMKKEKNCLRIYWSMYQSLQGNDLLEDSPYEPVNSRLSDIFRVVPFISDVFQQVEHIPKGNNCLDAAKACNLDDICKKYRSAYITPCTTSVSNDVCNRRKCHKALRQFFDKVPAKHSYGMLFCSCRDIACTERRRQTIVPVCSYEEREKPNCLNLQDSCKTNYICRSRLADFFTNCQPESRSVSSCLKENYADCLLAYSGLIGTVMTPNYIDSSSLSVAPWCDCSNSGNDLEECLKFLNFFKDNTCLKNAIQAFGNGSDVTVWQPAFPVQTTTATTTTALRVKNKPLGPAGSENEIPTHVLPPCANLQAQKLKSNVSGNTHLCISNGNYEKEGLGASSHITTKSMAAPPSCGLSPLLVLVVTALSTLLSLTETS
Protein: Sucrose 6(F)-phosphate phosphorylase (EC 2.4.1.329) (Sucrose 6'-phosphate phosphorylase) (SPP) (D9TT09)
Organism: Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum)
Function: Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro. Is also able to catalyze transglycosylation reactions in vitro.
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- PTS system, beta-glucoside-specific IIABC subunit
- Sucrose-6-phosphate hydrolase
Sequence:
MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDICVQRGANLSLIYGDKYKSEDGFDVHQINCTYYSALNCDDDAYLAARAIQFFTPGIPQVYYVGLLAGVNDFEAVKKTKEGREINRHNYGLKEIEESVQKNVVQRLLKLIRFRNEYEAFNGEFFIEDCRKDEIRLTWKKDDKRCSLFIDLKTYKTTIDYINENGEEVKYLV
Protein: Microsomal triacylglycerol transfer protein (MTP) (Q9VIH3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the transport of phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine) and phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) between membranes. Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16478722}. Golgi apparatus {ECO:0000269|PubMed:16478722}.
Interaction partners:
- Protein disulfide-isomerase
- Apolipoprotein lipid transfer particle
- Apolipophorins
- Crossveinless d
Sequence:
MENKNKKCLRTLLLLALFLGLLEDGKTALIAPNSQQIFKLQNQVILQELGRDSSSAETSYTFETDLKINSVWSGDEDQLLEVFISGSKVDASGKARSITRIPDRPFYISLVRGQPDKVIAHTSKDQSLLNLERGIASLLQLRLDASQEEELDVSGLCRVSYNVKSSTKVEKTKRDCSLWDLRVNYNPEEALGVTQQAQETVFYELSSEGTLLHAESQENHRLNLAAKPDVGSFVKSSLILQHVSQGSEEVKQLQLGSLDKAIQSLLEWYRVFELESDVDGMISAIKEQTLEDQLKASLTELQSADVGKSSLALAYVKLIPLARITRQEQFEDLLTEHAEVLPQLVDLLGAVQTFDAHNATFGFLYKESETTSEQLDLLEKYLQSLAVATHPDRKIVEHLFGLLEQESIKKHLKLRESVIQTVATLTRQSGLDVEDPLLKEVRSYLLQGLTSKEPTLYIRALQNLQDPATIEALLEHAQTGEAPNLSVAALQALKAFPLGSFNSSHRLQFESIFYQRKRRFDSSARTLALDIILSLRPTQEQLGNFLDYLASNDRQFEIKTYVLQKLRMLAEKCPRFRALFKSELVKRRHVNNYNVLGQKGLTTVLTRQLSQAPAFNETLLSTQEVYQGILKRGSVEFLLHAGRSQASSFKLGIYTAGLGSLVGDGDSGDGNDAIPADDEFSEDEAVTAGMEISVQGAQLRPLVFFSGQTELMGHVWGGSASDSTPAYQATTLSQDNEHYIILTSGATLHWRVLGARSVDLNGKVGFSLWNRNAQTEIQQNTGSAVLGHLAVGFTYAKLVQDFSITHEPKLSLNADLDFYSGIKLCMQLQRPEQLLKQTNVRSVFLQSVDRPYAKHVRSTLSHKTAGCTFALNQKNNEMCNLIFRDL
Protein: Golgi reassembly-stacking protein 1 (Golgi peripheral membrane protein p65) (Golgi reassembly-stacking protein of 65 kDa) (GRASP65) (O35254)
Organism: Rattus norvegicus (Rat)
Function: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis. Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis. Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity).
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11706049, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:12015985, ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:9346242}; Peripheral membrane protein {ECO:0000269|PubMed:9346242}; Cytoplasmic side {ECO:0000269|PubMed:9346242}.
Interaction partners:
- Golgin subfamily A member 2
- Golgin-45
- Serine/threonine-protein kinase PLK1
- General vesicular transport factor p115
- Syntaxin-5
- GRIP and coiled-coil domain-containing protein 2
- Protein ERGIC-53
- Golgin subfamily A member 5
- small monomeric GTPase
- BET1 homolog
Sequence:
MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSNNTSVCPSLSSSSLLTPTAVSALGPEDIGSSSSSHERGGEATWSGSEFEISFPDSPGSQAQVDHLPRLTLPDGLTSAASPEEGLSAELLEAQTEEPAHTASLDCMAQTEGPAGQVQAAPDPEPGLCEGPW
Protein: Acid labile subunit (Convoluted, isoform A) (Convoluted, isoform B) (A1Z9N6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neural/ectodermal development factor IMP-L2
- Insulin-like peptide 2
- Insulin-like peptide 5
- Teneurin-m
- Death-associated inhibitor of apoptosis 2
Sequence:
MIQLRLRTLVLLHFIALASSEYVYGEPEFKCPKKSKALYPCECVKGSDNGLYIRCENTNLATLSVALQNLASFGMPIEELTIYRGHFVRLYGPLFAHIKARMLIIEETPLATIEDYVFYGVNNTLEQLHLLRTNLSHVGLLGFGILGKAKELVIDGHAFQQLPKDLFAGQEIANSLGIIRVTNGNLSDLPIETFQPLRKLKTLDLHGNQLENLKRNQFKNLRELEVLDISHNQIKKLEAQHIADLTKLGWCNVSHNALSELSRGTFARNSVLKVLHLSHNQIARLDANSFRGMRFLRRLFLSDNVLTDIGRGTFGSIARIGTIDLARNRLKKIEFQMFTQMNYVELLDLAENNITKIEKNSFKDIYQAIINVSHNALELIETAAFENCVNITVLDLSHNRLANFSRRSFDETTFATYFQLSYNNLTNLAQIPIQNMTGLKVLNASYNSITEIPKNCFPKLYELHTIDVSHNNISSIFNGVFQTLFSLRSIDLSHNSMREIKSSTFGTLPTLLEMDLSHNELVSVVRGSLAKLTSLRQLYLNNNQLEKLFQLPISLNELYFSHNRLTNIPSGTWPVMNSLIYLDLSHNQLGDTLNGESFTGLLVVQRLKLQNNGISQPPKDAVAVMSTLQYLHLENNNITTLERSAFGKLPVLFELNLYGNQVKDISKRAFEGLLQLLTLNLSSNGIQTLQNDIFVGLPSLRNLDLSFNSLTKLDNKTNGVLDDLLSLETLDLSHNRISFVTKKTFPSHQYIPYNLRNLNLSYNLMPILTYDITFGTKKLVRLDVSHNQINDLRRGVISNFTSLQSLDMSYNELSNLKSEEHIFDLPQNLSWLDLSHNKIYHLPFANLVKVKSLKYVDLTNNSLEDVPASIVGSMRNGSQVLLAGNPLHCGCNARPLKYFMLQQTIAGEDLKSIYCGTPALIKDKQLISLDDEYLHCAEDEQEMYKGIDYEQLTDVRFREVKTNKAGMLTLCWYVSGFSDVSDFHVYIRSSSNDVLHQSDYAYNNRTAQIPVEELSTLGEEKLRGAEICIVSRDSDGNTRKWFSGQCQQLPSLKRPRTFFFGNFQVRGGVSRTSSSLPRCLLYIILVLFVARL
Protein: Keratin-associated protein 5-5 (Keratin-associated protein 5-11) (Keratin-associated protein 5.11) (Keratin-associated protein 5.5) (Ultrahigh sulfur keratin-associated protein 5.5) (Q701N2)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (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 5-7
- Keratin-associated protein 5-1
Sequence:
MGCCGCSGGCGSGCGGRGSGCGGCGSGCGGCGSGCGGCGSGCGGCGGCGSGCAGCGGCGSGCCVPVCCCKPMCCCVPACSCSSCGKGGCGSCGGSKRGCVSCGVSKGACGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSYGCSQSSCCKPCCCSSGCGSSCCQSSCCKPYCCQSSCCKPYCCQSSCCKPCSCFSGCGSSCCQSSCYKPCCCQSSCCVPVCCQCKI
Protein: Propanoyl-CoA:succinate CoA transferase (EC 2.8.3.27) (Propionyl CoA:succinate CoA transferase) (P52043)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of coenzyme A from propionyl-CoA to succinate. Could be part of a pathway that converts succinate to propionate.
Interaction partners:
- Methylmalonyl-CoA mutase
- Methylmalonyl-CoA decarboxylase
- Propionate--CoA ligase
- GTPase ArgK
- 2-methylcitrate synthase
- Succinate--CoA ligase subunit beta
- Phosphate acetyltransferase
- Acetyl-coenzyme A synthetase
- Succinate--CoA ligase subunit alpha
- Formate acetyltransferase 1
Sequence:
METQWTRMTANEAAEIIQHNDMVAFSGFTPAGSPKALPTAIARRANEQHEAKKPYQIRLLTGASISAAADDVLSDADAVSWRAPYQTSSGLRKKINQGAVSFVDLHLSEVAQMVNYGFFGDIDVAVIEASALAPDGRVWLTSGIGNAPTWLLRAKKVIIELNHYHDPRVAELADIVIPGAPPRRNSVSIFHAMDRVGTRYVQIDPKKIVAVVETNLPDAGNMLDKQNPMCQQIADNVVTFLLQEMAHGRIPPEFLPLQSGVGNINNAVMARLGENPVIPPFMMYSEVLQESVVHLLETGKISGASASSLTISADSLRKIYDNMDYFASRIVLRPQEISNNPEIIRRLGVIALNVGLEFDIYGHANSTHVAGVDLMNGIGGSGDFERNAYLSIFMAPSIAKEGKISTVVPMCSHVDHSEHSVKVIITEQGIADLRGLSPLQRARTIIDNCAHPMYRDYLHRYLENAPGGHIHHDLSHVFDLHRNLIATGSMLG
Protein: Marginal zone B- and B1-cell-specific protein (Mesenteric estrogen-dependent adipose 7) (MEDA-7) (Plasma cell-induced resident endoplasmic reticulum protein) (Plasma cell-induced resident ER protein) (pERp1) (Proapoptotic caspase adapter protein) (Q8WU39)
Organism: Homo sapiens (Human)
Function: Associates with immunoglobulin M (IgM) heavy and light chains and promotes IgM assembly and secretion. May exert its effect by acting as a molecular chaperone or as an oxidoreductase as it displays a low level of oxidoreductase activity (By similarity). Isoform 2 may be involved in regulation of apoptosis. Helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.
Subcellular location: [Isoform 1]: Endoplasmic reticulum lumen {ECO:0000269|PubMed:19805157}. Secreted {ECO:0000269|PubMed:21688198}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11350957}. Note=Diffuse granular localization in the cytoplasm surrounding the nucleus (PubMed:11350957).
Interaction partners:
- Tumor necrosis factor receptor superfamily member 17
- Immunoglobulin J chain
- POU domain class 2-associating factor 1
- Derlin-3
- B-cell antigen receptor complex-associated protein alpha chain
- B-lymphocyte antigen CD20
- Protein disulfide-isomerase A6
- Endoplasmic reticulum chaperone BiP
- Immunoglobulin lambda-like polypeptide 1
- DnaJ homolog subfamily C member 10
Sequence:
MRLSLPLLLLLLGAWAIPGGLGDRAPLTATAPQLDDEEMYSAHMPAHLRCDACRAVAYQMWQNLAKAETKLHTSNSGGRRELSELVYTDVLDRSCSRNWQDYGVREVDQVKRLTGPGLSEGPEPSISVMVTGGPWPTRLSRTCLHYLGEFGEDQIYEAHQQGRGALEALLCGGPQGACSEKVSATREEL
Protein: Beta-glucuronosyltransferase GlcAT14A (EC 2.4.1.-) (GT14 family glucuronic acid transferase 1) (AtGlcAT14A) (Q9FLD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-glucuronosyltransferase involved in the biosynthesis of type II arabinogalactan (AG). Modifies both the beta-1,6-linked galactan and beta-1,3-linked galactan present in type II AG. Transfers glucuronate to beta-1,6-galactooligosaccharides with degrees of polymerization ranging from 3 to 11. Transfers glucuronate to beta-1,3-galactooligosaccharides with degrees of polymerization ranging from 5 to 7. The addition of glucuronate at the O6 position may terminate galactose chain extension. Required for cell elongation during seedling growth.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:24128328}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
- Beta-1,6-galactosyltransferase GALT29A
- Beta-1,6-galactosyltransferase GALT31A
- Hydroxyproline O-galactosyltransferase GALT2
- Beta-arabinofuranosyltransferase RAY1
- Fucosyltransferase 6
- Probable fucosyltransferase 4
- Hydroxyproline O-galactosyltransferase GALT5
- Hydroxyproline O-galactosyltransferase GALT6
- Beta-1,3-galactosyltransferase 7
Sequence:
MKKLRSYYSNVRHHQNHHHHHHHHSNIVSSERKWIFFPLLIGSIFALFLLFLTTTLTSPTGGVRFLPFTRPVLLTGSGSSAFVESKIKPQQISSLPSPPRFAYLISGSAGDGKSLRRTLLALYHPNNRYVVHLDRESSREEREELHGYIKNSSLFRRFMNVHMIEKANLVTYRGPTMVANTLHAAAILLREGADWDWFINLSSSDYPLVTQDDLLHIFSHLPRDLNFIDHTSNIGWKASQRAKPVIIDPGLYLNKKSDVFWVTQRRSIPTAFKLFTGSAWMALSRPFVDYCIWGWDNLPRTVLMYYSNFLSSPEGYFHTVLCNAEEFRNTTVNSDLHFISWDNPPKQHPHHLTLTDMTKMVNSNAPFARKFRREDPVLDKIDDELLNRGPGMITPGGWCIGSHENGSDPCAVIGDTDVIRPGPGARRLENLVTSLLSTENFRSKQCK
Protein: Esterase/beta-lactamase LipL (EC 3.1.1.-) (EC 3.5.2.6) (P71778)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Shows both esterase and beta-lactamase activities, with a much higher activity against phenyl esters than against beta-lactams. Shows esterase activity against both long-chain and short-chain p-nitrophenol (pNP) esters, with a preference for shorter chain esters. Hydrolyzes substrates containing beta-lactam ring such as nitrocefin and ampicillin. Functions as an immunogen that activates both humoral and cell-mediated responses.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:26398213}. Cell membrane {ECO:0000269|PubMed:26398213}.
Interaction partners:
- Triacylglycerol lipase
- Esterase LipC
- Peptidoglycan endopeptidase RipA
- Peptidoglycan endopeptidase RipB
- Esterase LipU
Sequence:
MMVDTGVDHRAVSSHDGPDAGRRVFGAADPRFACVVRAFASMFPGRRFGGGALAVYLDGQPVVDVWKGWADRAGWVPWSADSAPMVFSATKGMTATVIHRLADRGLIDYEAPVAEYWPAFGANGKATLTVRDVMRHQAGLSGLRGATQQDLLDHVVMEERLAAAVPGRLLGKSAYHALTFGWLMSGLARAVTGKDMRLLFREELAEPLDTDGLHLGRPPADAPTRVAEIIMPQDIAANAVLTCAMRRLAHRFSGGFRSMYFPGAIAAVQGEAPLLDAEIPAANGVATARALARMYGAIANGGEIDGIRFLSRELVTGLTRNRRQVLPDRNLLVPLNFHLGYHGMPIGNVMPGFGHVGLGGSIGWTDPETGVAFALVHNRLLSPLVMTDHAGFVGIYHLIRQAAAQARKRGYQPVTPFGAPYSEPGAAAG
Protein: DNA-binding protein StpA (H-NS homolog StpA) (P0ACG1)
Organism: Escherichia coli (strain K12)
Function: A DNA-binding protein that acts in a fashion similar to H-NS protein upon overexpression, represses a number of genes including the cryptic blg operon, hns, papB and the proU locus. A subset of H-NS/StpA-regulated genes also require Hha for repression; Hha and Cnu (YdgT) increases the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. Repression can be inhibited by dominant-negative mutants of StpA or H-NS.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}.
Interaction partners:
- OriC-binding nucleoid-associated protein
- Hemolysin expression-modulating protein Hha
- DNA-binding protein H-NS
- DNA-binding protein Fis
- RNA-binding protein Hfq
Sequence:
MSVMLQSLNNIRTLRAMAREFSIDVLEEMLEKFRVVTKERREEEEQQQRELAERQEKISTWLELMKADGINPEELLGNSSAAAPRAGKKRQPRPAKYKFTDVNGETKTWTGQGRTPKPIAQALAEGKSLDDFLI
Protein: Albumin (P07724)
Organism: Mus musculus (Mouse)
Function: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).
Subcellular location: Secreted.
Interaction partners:
- IgG receptor FcRn large subunit p51
- Alpha-2-HS-glycoprotein
- Fibronectin
- Prothrombin
- Alpha-1-antitrypsin 1-3
- Low-density lipoprotein receptor-related protein 2
- Cubilin
- SPARC
- Apolipoprotein A-I
- Alpha-1-antitrypsin 1-1
Sequence:
MKWVTFLLLLFVSGSAFSRGVFRREAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFAKTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNECFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFYAPELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKCSSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDLLECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPADLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGEYGFQNAILVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVEDYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDDFAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALA
Protein: NAD kinase 2, mitochondrial (H0Y9H7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSYYEISVDDGPWEKQKSSGLNLCTGTGSKAWSFNINRVATQAVEDVLNIVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVLLEQ
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (EC 7.1.1.2) (NADH dehydrogenase subunit 9) (Q35322)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase iron-sulfur protein 6
- Os07g0640100 protein
- CHCH domain containing protein, expressed
- NADH-ubiquinone oxidoreductase chain 3
- Os10g0576000 protein
- Os05g0509200 protein
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
Sequence:
MDNQFIFQYSWEILPKKWVHKMKRSEHGNRFYTNTDYLFPLLCFLKWHTYTRVQVLIDICGVDYPSRKRRFEVVYNLLSTRYNSRIRVQTSADEVTRISSVVSLFPSAGWWEREVWDMFGVSFINHPDLRRILTDYGFEGHPLRKDFPLSGYVEVRYDDPEKRVVSEPIEMTQEFRYFDFASPWEQRSDG
Protein: Tenascin C (Q80YX0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGAVTWLLPGIFLALFALTPEGGVLKKIIRHKRESGLNMTLPEENQPVVFNHIYNIKLPMGSQCSVDLESASGEKDLTPTPESSGSFQEHTVDGENQIVFTHRINIPRRACGCAAAPDVKELLSRLEELELLVSSLREQCTMGTGCCLQPAEGRLDTRPFCSGRGNFSAEGCGCVCEPGWKGPNCSEPDCPGNCNLRGQCLDGQCICDEGFTGEDCSQLACPNDCNDQGRCVNGVCVCFEGYAGPDCGLEVCPVPCSEEHGMCVDGRCVCKDGFAGEDCNEPLCLNNCYNRGRCVENECVCDEGFTGEDCSELICPNDCFDRGRCINGTCYCEEGFTGEDCGELTCPNDCQGRGQCEEGQCVCNEGFAGADCSEKRCPADCHHRGRCLNGQCECDDGFTGADCGDLQCPNGCSGHGRCVNGQCVCDEGYTGEDCSQRRCPNDCHNRGLCVQGKCICEQGFKGFDCSEMSCPNDCHQHGRCVNGMCICDDDYTGEDCRDRRCPRDCSQRGRCVDGQCICEDGFTGPDCAELSCPSDCHGHGRCVNGQCICHEGFTGKDCKEQRCPSDCHGQGRCEDGQCICHEGFTGLDCGQRSCPNDCSNQGQCVSGRCICNEGYTGIDCSEVSPPKDLIVTEVTEETVNLAWDNEMRVTEYLIMYTPTHADGLEMQFRVPGDQTSTTIRELEPGVEYFIRVFAILENKRSIPVSARVATYLPAPEGLKFKSIKETSVEVEWDPLDIAFETWEIIFRNMNKEDEGEITKSLRRPETSYRQTGLAPGQEYEISLHIVKNNTRGPGLKKVTTTREYQPRPVIELIVSLCNFWLIAYPLTQHLHQ
Protein: Endo-1,4-beta-xylanase 5 (Xylanase 5) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase 5) (Q12549)
Organism: Aspergillus niger
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKVTAAFASLLLTAFAAPAPEPVLVSRSAGINYVQNYNGNLGDFTYDESTGTFSMYWEDGVSSDFVVGLGWTTGSSKSITYSAQYSASSSSSYLAVYGWVNSPQAEYYIVEDYGDYNPCSSATSLGTVYSDGSTYQVCTDTRRTRPSITGTSTFTQYFSVRESTRTSGTVTIANHFNFWAQHGFGNSNFNYQVMAVEAWNGVGSASVTISS
Protein: Pesticidal crystal protein N-terminal domain-containing protein (Q55BT7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKKVIFLSLIVFLCLLLLPSNDAHLVNDPTLPDYIGLVRGGICSIPVYGAAIDSCLYFVFNLFYPKQPEEPKVTMKEFNERMEFMAKDMKIYTNRAINASVLQTCRYQFKTLKKSSDNYMDMLNIWKKEFGATGLTTEETKNNLPPVFYVFLSKLEDCLIQFSDPTRISLLAKLYIDTAVLYSALLRDANYNGISMGLHPGIVNGTNKDIIFSAKIRLHSLEVFSNYMIILPQILIQNDNRCATNSNGNWRCNDKFPVPDWSGTISLFLYSDVTRYDRDVVYKPTSTSSTGERISWERGDNTQKGDSGTIIIRDFADVGRNIKKGVVWTLPYERPQQSFDFLTGCYGIYVQSYPYRKYVSDDAVDITFVATENQPNYDIAFIQSFLLSKPNNQVKIRIYYSYHLNKTYEYIPNNFQLKVIKTNSNGYELNKIRRILASGSDDLYYLNKTYSFHTQGSSKNLVTRLTFHQNRSYQLYDRFVFETPKFDVGKDFSVILLPISRFSIHLFSIEVISDK