wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial (EC 2.5.1.47) (EC 4.4.1.9) (Q76MX2)
Organism: Solanum tuberosum (Potato)
Function: The cyanoalanine synthesis reaction is more efficient than the cysteine synthase activity. Probably involved in detoxification of toxic cyanide produced in plant tissues.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Isopenicillin N epimerase
- Cysteine desulfurylase
- assimilatory sulfite reductase
- Cystathionine beta-lyase, chloroplastic
- cystathionine gamma-synthase
- Cystathionine gamma-synthase
- Cystathionine gamma-synthase
- Adenosylhomocysteinase
- Indole-3-glycerol phosphate lyase IGL1
- Glutathione hydrolase
Sequence:
MASLLRRRFYSSESSFAQRLRDLPKYLPGTNIKTQVSQLIGKTPLVYLNKVSEGCGAYIAVKQEMMQPTSSIKDRPAFAMINDAEKKGLITPGKTTLIEPTSGNMGISMAFMAAMKGYKMILTMPSYTSLERRVTMRAFGADLVTTDPTKGMGGTIKKAYDLLESTPNAYMLQQFSNPANTQAHFETTGPEIWEDTQGNVDIFVMGIGSGGTVSGVGQYLKSKNPNVKIYGIEPTESNVLNGGNPGPHEITGNGVGFKPDILDMDVMEEVLMVSSEESVNMARELALKEGLMVGISSGANTVAALRLANRPENKGKLIVTIHPSFGERYLSSVLYEDIRKEAQNMQPVSVD
Protein: Rugosin-LK1 (C3RT23)
Organism: Limnonectes kuhlii (Kuhl's Creek frog) (Rana kuhlii)
Function: Has antimicrobial activity against Gram-positive bacteria S.aureus ATCC 2592 (MIC=10.0 uM), S.aureus ATCC 43300 (MIC=15.0 uM) and B.subtilis (MIC=40.0 uM), against Gram-negative bacteria E.coli ML-35P (MIC=10.0 uM), P.aeruginosa PA01 (MIC=5.0 uM) and P.aeruginosa ATCC 27853 (MIC=5.0 uM) and against fungus C.albicans ATCC 2002 (MIC=10.0 uM).
Subcellular location: Secreted {ECO:0000255, ECO:0000269|PubMed:23054029}.
Interaction partners:
Sequence:
MFTMKKSLLFLFFLGTISLSFCEEERSADEDDEGEMTEEEKRSIRDKIKTMAIDLAKSAGTGVLKTLICKLDKSC
Protein: Cytochrome c oxidase assembly factor 6 homolog (Q8BGD8)
Organism: Mus musculus (Mouse)
Function: Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18614015}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5JTJ3}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Sequence:
MAAPSMKERQACWGARDLYWRCLDDNAEDAARCQKLRSSFEASCPQQWIKYFDKRRDYLKFKEKFEAGGFQSSQSTENS
Protein: Protein vav (G5EF62)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein unc-112
- Cell division control protein 42 homolog
- LIM domain-containing protein unc-95
- Muscle M-line assembly protein unc-89
- PDZ domain-containing protein
- Zyxin
- Protein espinas
- Dystrophin-like protein 1
- Disorganized muscle protein 1
- CTD small phosphatase-like protein 1
Sequence:
MSIGFSWFRRRFSYYEDKQQFSECANDDEPTVQLQGYRQRDREHEVDPRMTQSMISERIQRSQSPVDVSLALSEDSTITITELNNRNGSTFNANSINATPVMRRRRSQMSGVRQRNYRILDQNESKYILQQQSAAAIEEKKGTLLRRKSSKKLIEPLPMIITPPVLMARTQCCAVCYKEKSTGYSVSSRTQSYPLEAMSSVTTDRSTEEETARLSFVSSSTGYSSARSSLRSSDGGDESNNNSAGNRDSAISNTFSLSSQSSARRSALLTKGSLTHLDRIAIELLDTERTYVEDLNAVIKGYMDFLVEDREKLKVTLDAISSLFGCIERIFAFNKQLYNQLDAADLDCVKMSRCFVESSGKFEDYIEYCTNYHRMMSTLYHLQQQPLVARALQERQLALNHSLQLSAYLLKPVQRILKYHLFLENILKNMPSTTHPEELIQVKRAHEVMTSQAARINDEKKKAEHIERVGQLQSTLQKWKADEIQISNLSAYGDLLLEATFRQAGSKTTRLLFLFEEMLLIVKQRGANYVCKDYIMCSNLMLNEWICPEEPLSFQVLSFDNPRAQYVFMASSMEQKRTWMQELKRMMLDHYSVEIPEKTKQLMLSIDNTRIVPFGRPEFAEVSMKNHKKVPKYLEKRRKSVDAKEESNRRRSLSASRLLGGSKTSISEPIKEEQKCTCHMNGGIYNGANPTTSKSIISHPSLTYQQSHPTQSTDPNYCRPPVCRTQSAATIDLNQVHITEPNSAAVMSSRSRYQQARNRRLPPRHNQESRSTSSRRMGEEEIDRTFDQLYEELVSFGDSTKPTVTSNRSQRLRSEAPQSTVTTITVAATPATATLSIAECANTRLRSKSLTRLDEYEAEPISLKPSIERRYSKVDQLKKRSRKYQVNQEPEAADVLRPSVGRFSLTDHEIIIHGEEPYKRSSGRQRTPLTAQQTAELDDYFPSSNSMNSAPQTCSSSATPSLMSIIRQYENA
Protein: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic (AtMurE) (Protein ALBINO OR PALE-GREEN 13) (Protein PIGMENT DEFECTIVE EMBRYO 316) (F4I3P9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in chloroplast biogenesis. Required for thylakoid membrane development. Seems to be required for plastid-encoded plastid RNA polymerase (PEP)-dependent gene expression.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18036201}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Fructokinase-like 2, chloroplastic
- At3g57220
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Plastid transcriptionally active 3
- Thioredoxin-like protein CITRX, chloroplastic
- At1g63720/F24D7_9
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Phospho-N-acetylmuramoyl-pentapeptide-transferase homolog
Sequence:
MAFTFLSPHPVFLSLTGTTSSFSYKPVLLPFSRNSRTLTVAAGPARRNSYPNPADDDPPEAPEDSMHGVSKFQQIQRQAARARKLEEEDFEKNRNTYLSAIADVEDAAETGRDDEESGGDLFSDIDRAISMKRSEFVKQGLLKPNPPKTASLKKIGEEGNEEEGDVTDDVDELDEEEVVDLDEIDKLTGLTEISDEEDWVDEEGNTRINKKKEFGSDHQFEFDLDDFGESKARIVEPKFKMCLAELLDESKVVPISVYGDLDVEITGIQHDSRGVSAGDLFVCCLGSENFLSEADKRGAVAVVASKEIDIEDTLGCRALVIVEDTNAVLAALASSFYRHPSKNMSVIGVTGTDGKTTTTYLIKSLYEAMGVRTGMFSTVSCYIHGDNKLDTPNATMNPDAVLVQSLMAKMLHNGTESLVMEASPQELALGKCDEVDFDIAVFTNLTRENTDFRGTDEEYRDAEAKLFSRMVDPERHRKVVNIDDPNAAFFVQQGNPNVPVVTFAMENTKADVHPLKFELSLFETQVLVNTPQGILEISSGLLGRHNIYNILAAVAVGIAVGAPLEDIVRGVEEVDAVPGRCELIDEEQAFGVIVDHANTPDGLSRLLDSIRELKPRRIITVIGCEGENERGKRPLMTKIATEKSDVTMLTSDNPRNEDPLDILDDMLSGIGWTMQEYLKHGEHDYYPPLANGHRLFLHDIRRVAVRCAVAMGEEGDMVVVAGKGHEAYQLEGEKKEFYDDREECREALQYVDELHQAGIDTSEFPWRLPESH
Protein: Orofacial cleft 1 candidate gene 1 protein (Orofacial clefting chromosomal breakpoint region candidate 1 protein) (Q8IZS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEREKFQQKALKQTKQKKSKSAEFLMVKEDREATEGTGNPAFNMSSPDLSACQTAEKKVIRHDMPDRTLAAHQQKFRLPASAEPKGNEYGRNYFDPLMDEEINPRQCATEVSREDDDRIFYNRLTKLFDESRQGEPQDESGREETLNSEAPGSSNKSHEIHKEASEATTAHLEEFQRSQKTIILLGSSPLEQEIRSTSLHCMEDEMSHPWILLLKVTAVIRSRRYYREQRF
Protein: Nucleoprotein (EC 3.1.13.-) (Nucleocapsid protein) (Protein N) (P09992)
Organism: Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Function: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of host IRF3, a protein involved in interferon activation pathway, leading to the inhibition of interferon-beta and IRF3-dependent promoters activation. Encodes also a functional 3'-5' exoribonuclease that degrades preferentially dsRNA substrates and thereby participates in the suppression of interferon induction.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:3962189}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:3962189}.
Interaction partners:
Sequence:
MSLSKEVKSFQWTQALRRELQSFTSDVKAAVIKDATNLLNGLDFSEVSNVQRIMRKEKRDDKDLQRLRSLNQTVHSLVDLKSTSKKNVLKVGRLSAEELMSLAADLEKLKAKIMRSERPQASGVYMGNLTTQQLDQRSQILQIVGMRKPQQGASGVVRVWDVKDSSLLNNQFGTMPSLTMACMAKQSQTPLNDVVQALTDLGLLYTVKYPNLNDLERLKDKHPVLGVITEQQSSINISGYNFSLGAAVKAGAALLDGGNMLESILIKPSNSEDLLKAVLGAKRKLNMFVSDQVGDRNPYENILYKVCLSGEGWPYIACRTSIVGRAWENTTIDLTSEKPAVNSPRPAPGAAGPPQVGLSYSQTMLLKDLMGGIDPNAPTWIDIEGRFNDPVEIAIFQPQNGQFIHFYREPVDQKQFKQDSKYSHGMDLADLFNAQPGLTSSVIGALPQGMVLSCQGSDDIRKLLDSQNRKDIKLIDVEMTREASREYEDKVWDKYGWLCKMHTGIVRDKKKKEITPHCALMDCIIFESASKARLPDLKTVHNILPHDLIFRGPNVVTL
Protein: Glutathione S-transferase F7 (EC 2.5.1.18) (AtGSTF8) (GST class-phi member 7) (Glutathione S-transferase 11) (Q9SRY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase U19
- Methionine--tRNA ligase, cytoplasmic
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione S-transferase DHAR2
- Glutathione synthetase, chloroplastic
- Probable glutathione peroxidase 5
- Probable glutathione peroxidase 8
- Probable glutathione peroxidase 2
- Probable glutathione peroxidase 3, mitochondrial
- Probable glutathione peroxidase 4
Sequence:
MAGIKVFGHPASTATRRVLIALHEKNLDFEFVHIELKDGEHKKEPFIFRNPFGKVPAFEDGDFKLFESRAITQYIAHFYSDKGNQLVSLGSKDIAGIAMGIEIESHEFDPVGSKLVWEQVLKPLYGMTTDKTVVEEEEAKLAKVLDVYEHRLGESKYLASDKFTLVDLHTIPVIQYLLGTPTKKLFDERPHVSAWVADITSRPSAKKVL
Protein: Small ribosomal subunit protein eS1A (40S ribosomal protein S1-A) (S3aE-A) (Q09781)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein eS7
- Elongation factor 3
- mRNA export factor elf1
Sequence:
MAVGKNKRLSKGKKGIKKRVVDPFSRKDWYDIKAPAFFEVKNVGKTLVNRTAGLKNANDSLKGRILEVSLADLQKDEEHSFRKVKLRVEDIQGKSCLTSFNGFDMTSDKLRSLVRKWQSTIEANQTIKTTDGYLCRIFVIGFTSRRVNQVKKTTYAQSSQIRAIHQKMFQVIQNQANGCSMKELVQKLIPEVIGRAIEKATNNIYPLQNVFVRKVKILKAPKHDAQKLLELHGESQDVGSKVISDVAPLESV
Protein: Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A) (P21274)
Organism: Mus musculus (Mouse)
Function: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein receptor type-1A
- Noggin
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein receptor type-1B
- Activin receptor type-2A
- Activin receptor type-2B
- Chordin
- Activin receptor type-1
- Repulsive guidance molecule B
- Hemojuvelin
Sequence:
MVAGTRCLLVLLLPQVLLGGAAGLIPELGRKKFAAASSRPLSRPSEDVLSEFELRLLSMFGLKQRPTPSKDVVVPPYMLDLYRRHSGQPGAPAPDHRLERAASRANTVRSFHHEEAVEELPEMSGKTARRFFFNLSSVPSDEFLTSAELQIFREQIQEALGNSSFQHRINIYEIIKPAAANLKFPVTRLLDTRLVNQNTSQWESFDVTPAVMRWTTQGHTNHGFVVEVAHLEENPGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Protein: Kinesin-like protein 5 (O14343)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in establishing metaphase during mitosis. Required for chromosome segregation where it generates tension during kinetochore capturing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11967147}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11967147}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11967147}. Note=Cytoplasmic microtubules in interphase, mitotic kinetochores in metaphase and spindle midzone in anaphase and telophase.
Interaction partners:
- Kinesin-like protein 6
- Anaphase spindle elongation protein 1
- Phosphoprotein p93
- Spindle pole body component alp14
- Mitotic spindle checkpoint component mad2
- Microtubule integrity protein mal3
- Kinesin-like protein 2
- Tubulin alpha-2 chain
- Microtubule protein alp7
- Tip elongation protein 1
Sequence:
MSRQSSITVTVRVRPFSTAESANLIASSDRLSFGTSSSLRNPGSGRQIRRVVKVLDGRVLVFDPPDETTATLSATNRRLSTSQQSLARLSRKSNNSAGFGRDLRYAFDRVFDETATQQQVYERTARPLLDNILDGFNATIFAYGATGCGKTHTISGTMQDPGLIYLTLKELFERMDHLRDEKIFDLRLSYLEIYNETIRDLLVSPTPNQAKPLNLREDADRRITVPGLTSLSPESLEEIIDIIMKGNANRTMSPTEANAASSRSHAVLQVTLIQKPRTAGINEDHTLATLSIIDLAGSERATATKLRGSRLFEGANINKSLLALGNCINALCDPHRRAHVPYRDSKLTRLLKFSLGGNCRTVMIVCVSPSSVHYEETHNTLKYANRAKNIKTEVLRNMISVDRHVSQYVKAIVELREQISELENRLAQIDLSSQSNGSDQDAVTQSFAHESKLAEARNLLRMTFEETLPLQNDTINKVEKVKHFDDSIRVLKYWLSCYERILPNSADERVFLVRSKLESLLTRRAEIIADIDPELVYQKFQRSVSHIINTYKQEGATMYADVLQDEVDLLKSIIENQVLDAQNKVDEFTPVLESLLRSSFKASSLLKEGGMQELFSILEKWLLGIGLGEKPNISVLSESYKLNSTSDDSRTINRDRVHSFPTQPLLNNNLPRMFFVKSPKKPVVFSKRSPKKRVRFDDSMSTSDSGASAYNSPIQTSKLKNMNFFNTMHMPSTPAHKRPENKNQIDVEINLTSPVSPMLEDKPEPGLLIKSPLEKKQEVNSESTQLDQLLAEDSSTDDVSLPHLDTIDLDGSPVPKVPDLNFSRANMDSPTFILNNEAIHNFDFSKPKTRQSLSSLTTLHLSNPANIIRKSLSMAENEEEKAT
Protein: Flavin mononucleotide hydrolase 1, chloroplatic (AtcpFHy1) (EC 3.1.3.102) (5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase) (AtcpFHy1/PyrP1) (EC 3.1.3.104) (5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase) (ARPP phosphatase) (Q84VZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: FMN hydrolase that catalyzes the dephosphorylation of flavin mononucleotide (FMN) to riboflavin. Can also dephosphorylate 5-amino-6-(5-phospho-D-ribitylamino)uracil, also known as ARPP. Not required for riboflavin biosynthesis in planta, but may help maintaining flavin homeostasis within chloroplasts.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:22002057}.
Interaction partners:
- 5-amino-6-
- 6,7-dimethyl-8-ribityllumazine synthase, chloroplastic
- Nudix hydrolase 23, chloroplastic
- Bifunctional riboflavin kinase/FMN phosphatase
- FAD synthetase 1, chloroplastic
- Riboflavin synthase
- Riboflavin biosynthesis protein PYRD
- Riboflavin biosynthesis protein PYRR
- FAD synthetase 2, chloroplastic
- Purple acid phosphatase 3
Sequence:
MAAAAMHTSAEFINLKPNMWKKNPVRASGSCCLGSSSGDEISRKRKLPILLFDVMDTIVRDPFYQDVPAFFGMPMKQLLECKHPMVWIEFEKGLIDEEELARNFFIDGRDFDLEGLKECMRSGYSYLDGMQELLQTLAADDFEIHAFTNYPIWYNIIEDKLKLSAYLSWTFCSCIAGKRKPDPEFYLEVVGHLGVEPCDCIFIDDRPTNVKCAIEIGMGGLCFENADSLAKDLSDLGINVSVPKL
Protein: Keratin, type I cytoskeletal 9 (Cytokeratin-9) (CK-9) (Keratin-9) (K9) (P35527)
Organism: Homo sapiens (Human)
Function: May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly.
Interaction partners:
- Keratin, type I cytoskeletal 20
- Alpha- and gamma-adaptin-binding protein p34
Sequence:
MSCRQFSSSYLSRSGGGGGGGLGSGGSIRSSYSRFSSSGGGGGGGRFSSSSGYGGGSSRVCGRGGGGSFGYSYGGGSGGGFSASSLGGGFGGGSRGFGGASGGGYSSSGGFGGGFGGGSGGGFGGGYGSGFGGFGGFGGGAGGGDGGILTANEKSTMQELNSRLASYLDKVQALEEANNDLENKIQDWYDKKGPAAIQKNYSPYYNTIDDLKDQIVDLTVGNNKTLLDIDNTRMTLDDFRIKFEMEQNLRQGVDADINGLRQVLDNLTMEKSDLEMQYETLQEELMALKKNHKEEMSQLTGQNSGDVNVEINVAPGKDLTKTLNDMRQEYEQLIAKNRKDIENQYETQITQIEHEVSSSGQEVQSSAKEVTQLRHGVQELEIELQSQLSKKAALEKSLEDTKNRYCGQLQMIQEQISNLEAQITDVRQEIECQNQEYSLLLSIKMRLEKEIETYHNLLEGGQEDFESSGAGKIGLGGRGGSGGSYGRGSRGGSGGSYGGGGSGGGYGGGSGSRGGSGGSYGGGSGSGGGSGGGYGGGSGGGHSGGSGGGHSGGSGGNYGGGSGSGGGSGGGYGGGSGSRGGSGGSHGGGSGFGGESGGSYGGGEEASGSGGGYGGGSGKSSHS
Protein: Protein NRT1/ PTR FAMILY 1.2 (AtNPF1.2) (Nitrate transporter 1.11) (Q9M817)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity nitrate transporter involved in xylem-to-phloem transfer for redistributing nitrate into developing leaves. Not involved in dipeptides transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24006285}; Multi-pass membrane protein {ECO:0000269|PubMed:24006285}.
Interaction partners:
- High affinity nitrate transporter 2.5
- High-affinity nitrate transporter 2.1
- High affinity nitrate transporter 2.4
- Major facilitator superfamily protein
- High affinity nitrate transporter 2.7
- High-affinity nitrate transporter 2.2
- High-affinity nitrate transporter 3.1
Sequence:
MENPPNETEAKQIQTNEGKKTKGGIITMPFIIANEAFEKVASYGLLPNMIMYLIRDYRFGVAKGTNVLFMWSAASNFTPLLGAFLSDSYLGRFLTISIASLSSFLGMVLLWLTAMLPQVKPSPCDPTAAGSHCGSSTASQLALLYSAFALISIGSGGIRPCSLAFGADQLDNKENPKNERVLESFFGWYYASSAVAVLIAFTGIVYIQEHLGWKIGFGVPAVLMLIAALLFILASPLYVTRGVTKSLFTGLAQAIVAAYKKRKLSLPDHHDSFDCYYHMKDSEIKAPSQKLRFLNKACLISNREEEIGSDGFALNPWRLCTTDKVEELKALIKVIPIWSTGIMMSINTSQSSFQLLQATSMDRRLSRHGSSFQVPAGSFGMFTIIALALWVILYDRAVIPLASKIRGRPFRLSVKLRMGLGLFMSFLAMAISAMVESFRRKKAISQGYANNSNAVVDISAMWLVPQYVLHGLAEALTAIGQTEFFYTEFPKSMSSIAASLFGLGMAVASLLASVVLNAVNELTSRNGKESWVSDNINKGHYNYYYWVLAIMSFINVIYYVICSWSYGPLVDQVRNGRVNGVREEEELIDIVGKGFEKEDLSPVVKTN
Protein: Mitogen-activated protein kinase kinase kinase mom-4 (EC 2.7.11.25) (Q9XTC6)
Organism: Caenorhabditis elegans
Function: Part of the Wnt signaling pathway essential for the specification of the mesodermal cell fate in early embryos. Stimulates the wrm-1/lit-1-dependent phosphorylation of pop-1 and plays a role in the initial nuclear accumulation of wrm-1.
Interaction partners:
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Serine/threonine kinase NLK
- Dual specificity mitogen-activated protein kinase kinase sek-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Protein phosphatase ppm-1.A
- Mitogen-activated protein kinase kinase kinase
- Armadillo repeat-containing protein wrm-1
- Protein mom-5
- Ubiquitin-conjugating enzyme E2 13
Sequence:
MDNSSQSKPSSSSSSHSPSPAAITPTQRTTRDSGLCSTIDIPEIQAQCIDNLNSHYLGKGTYGLVEKTRYRKTRQDDFRPAAIKYSSQLHMATLIREAKVMWDLRNHPNIIKIYGLYKSPRNGQGVVMEYMDCGSMADLLYDRTHINYTIDHVASWMFQLSSAVDFFHSNSQVHRDLKLQNMLLSDRYRTMKLCDFGTFTSMHQSMTSNRGTPITMAPEVFRCEQYNMKSDIYSIGIIMWQIIARNHPYRRDLSVPGLLYNVATANLRPQELECNPILSEFYKKCWNDNADIRPTSSECVEYFTLLKDEYPNGSVPLSDSSTNGPAETPPPHAHRPTMLGTSSGSGIGSNNRTPTASKLLNPQQPGQGHRRNRSETFVVQPDLPYPTVPGEAGASRIPKSQSEAKNFRDRAKSEQRQPHRDARPPPPFEHRRDSNDEEKHAVFMNICSNEETRPIDPDTRDEKSLEIFHQHCDNNKQYADAWVIKKEVMRAKHELIAQWPQHDHTVELLERKYYLEQEIARYRDIQDDNYFSTERM
Protein: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MECDP-synthase) (MECPP-synthase) (MECPS) (EC 4.6.1.12) (P9WKG5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Interaction partners:
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 1
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- RNA polymerase-binding transcription factor CarD
- 1-deoxy-D-xylulose-5-phosphate synthase
- Uncharacterized tRNA/rRNA methyltransferase Rv3579c
Sequence:
MNQLPRVGLGTDVHPIEPGRPCWLVGLLFPSADGCAGHSDGDVAVHALCDAVLSAAGLGDIGEVFGVDDPRWQGVSGADMLRHVVVLITQHGYRVGNAVVQVIGNRPKIGWRRLEAQAVLSRLLNAPVSVSATTTDGLGLTGRGEGLAAIATALVVSLR
Protein: MSL complex subunit 1 (J3QQY0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDEPGAAEAHFLPRHRKLKEPGPPLASSQGGSPAPSPAGCGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPAAAGAGCSPRPKYQAVLPIQTGSLVAAAKEPTPWAGDKGGAASPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSMRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKKDNEKERHKLFQGYETEEREETELSEKIKLECQPELSETSQTLPPKPFSCGRSGKGHKRKSPFGSTERKTPVKKLAPEFSKVKTKTPKHSPIKEEPCGSLSETVCKRELRSQETPEKPRSSVDTPPRLSTPQKGPSTHPKEKAFSSEIEDLPYLSTTEMYLCRWHQPPPSPLPLRESSPKKEETVASKA
Protein: LD31235p (Torsin interacting protein, isoform A) (Torsin interacting protein, isoform B) (Q9VW40)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Torsin-like protein
- Muscle-specific protein 300 kDa, isoform G
Sequence:
MSNLARRPLHGNEPGALSQSKDDVDQDHSYNRQPVQSYEEGTSSADELEESESHDEPSIPKPTDQSRRRSISTSRPSSRQEQHNSINEHHNGIGIKLALAGVLFGLLVVYGYGSSIIEEKQCDFKDLRTKYPQQQEKVWRALQKGIEGLINKKDKHPSVFLFLHQDPKLEKLIDEIAIEASMCFGGPRKLIHMKKEHMKEYGLAIEQFKSKINDGKVFLIVNLNEIAPNGARALHTICDTYSPLVEDAVIFLSLRTFNTTAVNNSVNLATDTLYDLWDQELGDHELDPLITRVTDQVLHLS
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit) (Ribophorin II) (RPN-II) (Ribophorin-2) (Q9DBG6)
Organism: Mus musculus (Mouse)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:F1PCT7}. Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Protein transport protein Sec61 subunit gamma
- Malectin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
Sequence:
MAPPGSSAVFLLALTITASVQALTPTHYLTKQDVERLKASLDRPFTDLESAFYSIVGLSSLGVQVPDVKKACTFIKSNLDPSNVDSLFYAAQSSQVLSGCEISVSNETKELLLAAVSEDSPIAQIYHAVAALSGFGLPLASNEALGALTARLGKEETVLATVQALQTASHLSQQADLRNIVEEIEDLVARLDELGGVYLQFEEGLELTALFVAATYKLMDHVGTEPSMKEDQVIQLMNTIFSKKNFESLSEAFSVASAAAALSQNRYHVPVVVVPEGSTSDTQEQAILRLQVSNVLSQPLAQAAVKLEHAKSAATRATVLQKTPFSLVGNVFELNFKNVKLSSGYYDFSVRVEGDSRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQSLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTVIFHLGHAAMLGLMYIYWTQLNMFQTLKYLAVLGTVTFLAGNRMLAQHAVKRTAH