wanglab/gogpt-training-data huggingface dataset:
Protein: U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) (D3ZCL3)
Organism: Rattus norvegicus (Rat)
Function: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03153}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D3
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein-associated protein N
- Small nuclear ribonucleoprotein Sm D1
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein polypeptide A'
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLIDKTTAAFQQGKIPPAPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGPPMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPTRPGMTRPDR
Protein: Cytochrome P450 17A2 precursor (Cytochrome P450 family 17 polypeptide 2) (A7U483)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MCSVSVCVCFSALLLLLLLLVRRLLEGVGSSSVSFPCLPRLPLLGSLLHLRSNLPPHLLFTQLSSQYGPLFGLYAGPHLTLVVSEIGLVREVLLQRGREFAGRPKMVTTDLLTQGGKDIAFADYSPLWKNHRRLVHSSFTLFGEGSNKLQTIVQEAADSLCEELQACRGQSSDLSVVLMRAVTNVICRLVFSSSYQPSDPELQTVIQYNDGIVQTIARGGLVDIFPWLRIFPNKDLKRLKECVSIRDQLLYKKLLEHKKSLTPGEPRDLLDALLIGQQRGSGGADDITEDHVLMTAAEAFGAGVETTSTTLLWTIAFLLHHPQLQERVQAELDECVGVDRPPCLSDRPHLPLLDAVLCEVMRIRPVSPILIPHVAMQDTSLGGHSVPKGTRVLVNMWAIHHDPKHWDQPEQFNPERFLEPSGKKKTQSSFLPFGAGPRVCVGESLARIELFLFVSRPLQRFSFSCPSEASLPDLQGRFGVVLQPERYTVTVTPRH
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (Somatomedin) (Q9N1C1)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
QVKMPITSSSHLFYLALCLLAFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKAQKEVHLKNTSRGSAGNKNYRM
Protein: Endo-1,4-beta-xylanase Xyn11E (EC 3.2.1.8) (V9TXH2)
Organism: Paenibacillus barcinonensis
Function: Involved in depolymerization of xylan, a major component of the lignocellulosic substrates. Acts as an endo-xylanase that efficiently hydrolyzes the beta-1,4 glycosidic linkages between the xylopyranosyl residues in the main chain of the polymer, leading to the degradation of xylan into short oligosaccharides. Shows high activity toward branched xylans from both softwoods (arabinoxylans) and hardwoods (glucuronoxylans), showing the highest activity on beechwood xylan. Also hydrolyzes long xylooligosaccharides (with a degree of polymerization of greater than or equal to 5), while oligomers shorter than xylotetraose are not degraded. Is not active on carboxymethyl cellulose (CMC), Avicel, starch, polygalacturonic acid, laminarin, pectin, beta-D-barley glucan, or lichenan.
Subcellular location: Secreted {ECO:0000305|PubMed:24549767}.
Interaction partners:
Sequence:
MFKFGKKLMTVVLAASMSFGVFAATTGATDYWQNWTDGGGTVNAVNGSGGNYSVNWQNTGNFVVGKGWTYGTPNRVVNYNAGVFSPSGNGYLTFYGWTRNALIEYYVVDNWGTYRPTGTYKGTVNSDGGTYDIYTTMRYNQPSIDGYSTFPQYWSVRQSKRPIGVNSQITFQNHVNAWASKGMNLGSSWSYQVLATEGYQSSGSSNVTVW
Protein: Transcription factor CPH1 (P43079)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor involved in the formation of pseudohyphae and hyphae. It is likely to play a role in the developmental switch between yeast and mycelial forms. May be involved in a signal transduction system, strengthening the possibility of a sexual phase up to now undetected, and similar to that of the yeast mating pathway.
Subcellular location: Nucleus.
Interaction partners:
- Extracellular signal-regulated kinase 1
- Mitogen-activated protein kinase
- Transcription activator TEC1
- Transcription factor of morphogenesis MCM1
- Serine/threonine-protein kinase STE7 homolog
- Enhanced filamentous growth protein 1
- Hyphal wall protein 1
- Transcriptional repressor TUP1
- Ras-like protein 1
- mitogen-activated protein kinase kinase kinase
Sequence:
MSITKTYNGDPTSLVPTQSVKESLRLIEDLKFFLATAPANWQENQVIRRYYLNHDEGFVSCVYWNNLYFITGTDIVRCIVYKFEHFGRKIIDRKKFEEGIFSDLRNLKCGADAILEPPRSEFLEFLFKNSCLRTQKKQKVFFWFNVPHDKLMADALERDLKKEKMGQRPTTMAHREPALSFHYDESSSLYTQLGKHMETQKRINDAATSSTSNTATTLTDTGVSSGLNNTTSGGGSDSATSTHNNNEASTKPSNGSEKSSPEYTTTARGRDEFGFLNEATPSQYKANSDYEDDFPLDYINQTTQNSEDYITLDANYQAGSYANMIEDNYDSFLDATLFIPPSLGVPTGTAATATTSNQVAFNDEYLIEQAQPIRTPLPPISSSTISGLLQPKSAAKFFSLQSANGGEEFFPAYQNDPSTANAGFVPPISAKYATQFATRQVATPTYIKAIPQTGAAAATGNGGQPQQYYDQATGNAFYPAEIPVSYNVVHPESEYWTNNSGAVATTAAATAPMYDASGFPIPINQSYMVMNEHEMVPYQYMNSNGAMIGMIPPHQQQQQQQQQIAMGYQSMLRQQQQQQQQQQQQQPSSTMTKKKKQIHSFNNNKSLSSNGGGITKKSHDNNNHSKVKTSYGSLNDVVNSKVTKVINKEEVKQSQT
Protein: Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK) (P09605)
Organism: Rattus norvegicus (Rat)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Interaction partners:
Sequence:
MASAFSKLLTGRNASLLFTTLGTSALTTGYLLNRQKVSADAREQHKLFPPSADYPDLRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDPRLMKHPADLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALGGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGRK
Protein: Iron-sulfur cluster assembly 1 homolog, mitochondrial (HESB-like domain-containing protein 2) (Iron-sulfur assembly protein IscA) (hIscA) (Q9BUE6)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15262227, ECO:0000269|PubMed:22323289}.
Interaction partners:
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- Glutaredoxin-related protein 5, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Cysteine desulfurase
- Ferredoxin-2, mitochondrial
- Iron-sulfur cluster co-chaperone protein HscB
- BolA-like protein 3
- Lipoyl synthase, mitochondrial
Sequence:
MSASLVRATVRAVSKRKLQPTRAALTLTPSAVNKIKQLLKDKPEHVGVKVGVRTRGCNGLSYTLEYTKTKGDSDEEVIQDGVRVFIEKKAQLTLLGTEMDYVEDKLSSEFVFNNPNIKGTCGCGESFNI
Protein: Leucine-rich tendon-specific protein, isoform C (MIP13715p) (D0IQL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Roundabout 1, isoform A
- Teneurin-m
- Latrophilin Cirl
- LP06937p
Sequence:
MNAASNVALFKFRTLIKRTSPIMRPKLSAILMLLLLCTLAAANDLKDLLEDSTTSSSTSTTSSTIPSSVTSPTTPTAYVVSAAAVPALVAGRGKSKSTSGKYVNKSSPRKRKAEQVSSLPLPVDDALMEWKCPNITGTRNAELECGCDLPHTLRCNIDLHGMMLLADRLRTSPYSISLLDCSLRNVTFLSDAKIFDNVSLHGLVISSGEIKRVHKSAFLGIRGPLQALGLPGNALMSVPWNALSTLSALERLDLANNKIKALGTADFVGLTSLVYLELSNNQISSISQRTFVNLRKLEVLKLGGNRLGDYAQSLRSLSQCLSLRQLDLQANNLNGPLSEQTLPGMRNLESLNLNRNLIKSIQNKALANFSRLVSLSLRHNQIDVLQDHAFFGLGALDSLDLSYNGIVAISSASLQHLSRLTVLDLTHNFLRALTSDLIAPLPSLRELRLAGNDISIVARNAMDGARELESLQMQENPLSCDCSIRPFAEWLQESQLHSSLSASCVTPPRLEGAPLLQVPVETLSCDMDNVEKDNANIMQHLETLAKPNQTSPIKDLSEEIILHELHFSTDYGLILTWLLNLSKKDYMCDAIFVYKEEHINEILIDNSPIHCESKVVNGQNTVSVIVPDSSSLEIGESYRFCLVMIQEQKPDSELNIGCSNITRLERSSPGAVPVSRQYQRRPYYNANELKPEVVHDAGEDYQVNQRRFNSVVGSQPQQTQQSTLLHSYTVIDSLNKSFLPGLGLGVLVTSVLVLIWGATRIRQTGGSSGGGGRNGDSIDSNSSSMHNNNNNSRPGTPTATTCYAASDHIARLADAENGTRYLKLQATTSL
Protein: Growth factor receptor-bound protein 14 (GRB14 adapter protein) (Q14449)
Organism: Homo sapiens (Human)
Function: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15210700, ECO:0000269|PubMed:19648926}. Endosome membrane {ECO:0000269|PubMed:15210700, ECO:0000269|PubMed:19648926}; Peripheral membrane protein {ECO:0000269|PubMed:15210700, ECO:0000269|PubMed:19648926}. Note=Upon insulin stimulation, translocates to the plasma membrane. {ECO:0000269|PubMed:15210700, ECO:0000269|PubMed:19648926}.
Interaction partners:
- Insulin receptor
- Fibroblast growth factor receptor 1
- GTPase HRas
- Poly [ADP-ribose] polymerase tankyrase-2
- Epidermal growth factor receptor
- Poly [ADP-ribose] polymerase tankyrase-1
- Cordon-bleu protein-like 1
Sequence:
MTTSLQDGQSAASRAAARDSPLAAQVCGAAQGRGDAHDLAPAPWLHARALLPLPDGTRGCAADRRKKKDLDVPEMPSIPNPFPELCCSPFTSVLSADLFPKANSRKKQVIKVYSEDETSRALDVPSDITARDVCQLLILKNHYIDDHSWTLFEHLPHIGVERTIEDHELVIEVLSNWGIEEENKLYFRKNYAKYEFFKNPMYFFPEHMVSFATETNGEISPTQILQMFLSSSTYPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKYGMQLYQNYMHPYQGRSGCSSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPKTFVLSMSHGQKIKHFQIIPVEDDGEMFHTLDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL
Protein: Tetratricopeptide repeat protein 30 homolog (TPR repeat protein 30 homolog) (Q9VK41)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for polyglutamylation of axonemal tubulin in sensory cilia. Plays a role in anterograde intraflagellar transport (IFT), the process by which cilia precursors are transported from the base of the cilium to the site of their incorporation at the tip.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 172 homolog
- No mechanoreceptor potential B, isoform D
- GH11140p
- Outer segment 5
- Clusterin associated protein 1
- Intraflagellar transport 52
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 46 homolog
- WD repeat-containing protein 35
Sequence:
MLHQGIILREGHVTRTIYNLIKDKRYEDVIECITSFGEAANTRAGLSTLGHCYYHAQKYEEAATCYEQLCQLAPKEAKYRFYYAQSLYQAGIFADALRVLKQMGDQEDELREQCLQLQSAILYSSEDFAGAQSLLNQRAGGTADTLNDEGCLLFQADQHEAAVQRFQAALQVGGFNPLVAYNVALAHFQKKQRAQALDYTSEIVERGMRNHPELGIGAQMDIPDGGARSVGNPITMAISGITQALNLKAAIEFQDGNEEAARDALLDLPPRAESELDPVTLHNMALTDVEGPVAGLRKLAFLLELGAPSCPKETFANILLICCKNELYETAADILAEHTDLTYKYLSQYLYELLDSLITAQTSAELAEKKLGTLASSLAGKLRSLAAKVQEVRATNEQQALRDALKDYEQALELYLPVVMARAWISWRDDDFVGAEREFHASAEFCSENSIWRLNAGHVLFMQGDKYNEAAAFYEPIVRQHSDDIMSVSAAVLANLCVSYIMTFQNEEAEELMRKVEKAEEMKGNLGKQYHHLCIVNLVVGTLYCAKSNYEFGLSRIAHALESGSGNRLYADTWLHVKHCILGLLTGMAKQNIILPYATVQEVLNFLRFCESYGLFTPANIFSATEQVPEEPLTIGLEARKLRLLLIKLSEYDNF
Protein: Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (G3V266)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPHSSDSSDSSFSRSPPPGKQDSSDDVRRVQRREKNRIAAQKSRQRQTQKSIKKDAQVPWHRARRAGNGYFSK
Protein: MARVEL domain-containing protein (Q18582)
Organism: Caenorhabditis elegans
Interaction partners:
- CUPID domain-containing protein
- F59G1.4
Sequence:
MSMYGKDKAYIENETKFRADRDYLSQPVYQQTVYREGPILKPDVEVSVVDVEPVECTPHMWGHPMGLLRWFQLLMFFVLQWLVQITCGGDACTMIMNVFGYTAMGQLFVLVIFLGLSMFCGVIILLFALNAHRCIPSIIIALEKVYAILGIVFMFIAGILGTWMAVLANDREVNYQGRGRGHIQGQWIAAAVLEFLMVIVYIFDFILQRRENYPFTGKEYKTVPSQQTGPGSMRSTTTNTKRSTDFIFQETF
Protein: cAMP-dependent protein kinase inhibitor gamma (F7F4X2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFGECDGPGMQLQPSGSLSKGNGSLLCTERWKLSKWVEWLTSSGRELDYNKWGLTWPETGKHPLKPRSAFHLGETGREKGQERAVCPTCPALLSSGFLFYLPILLTWDLCAWRPGSCLRSDATGMMEVESSYSDFISCDRTGRRNAVPDIQGDSEAVSVRKLAGDMGELALEGAEGQAEGSTPDKEASSQPESSDANTSS
Protein: Chitinase domain-containing protein 1 (Q9M159)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g12300/F28J15_117
Sequence:
MARRRRSSAAESLKRRNDGYESLCQVVQQDSDRRLITIFVIFFIVIPAVSIAVYKVKFADRVIQTESSIRQKGIVKTDINFQEILTEHSKASENSTRHYDYPVLAYITPWNSKGYDMAKIFNSKFTHLSPVWYDLKSQGSGLVLEGRHNADKGWIQELRSRGNALILPRVVLEAIPGEMLNKKKLREKAISLIVTECKEMEYNGIVLESWSRWAAYGVLHDPDLRKMALKFVKQLGDALHSTSSPRNNQQHMQFMYVVGPPRSEKLQMYDFGPEDLQFLKDSVDGFSLMTYDFSNPQNPGPNAPVKWIDLTLKLLLGSSNNIDSNIARKVLLGINFYGNDFVISGDSGGGGAITGRDYLALLQKHKPTFRWDKESGEHLFMYRDDKNIKHAVFYPTLMSILLRLENARLWGIGISIWEIGQGLDYFFDLL
Protein: Murein tetrapeptide carboxypeptidase (EC 3.4.17.13) (LD-carboxypeptidase A) (Muramoyltetrapeptide carboxypeptidase) (P76008)
Organism: Escherichia coli (strain K12)
Function: Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10428950}.
Interaction partners:
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
- N-acetylmuramoyl-L-alanine amidase AmiD
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- Anhydromuropeptide permease
- Murein peptide amidase A
- Beta-hexosaminidase
- D-alanyl-D-alanine carboxypeptidase DacB
- Endolytic peptidoglycan transglycosylase RlpA
- Endo-type membrane-bound lytic murein transglycosylase A
Sequence:
MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM
Protein: GRAM domain-containing protein (Q38EN1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGSTAHRGDSLELQPLIFNGPVPKPHPPCTDPTPDEQYRMASEEQLKKMEKKDQKAPPPEEQPAPEGGTKGSKMSSLFSGATRNICSIAHQVSSTVERAAVKASNATGNKMREINERMNHSWFKENFPHLRAQGETLVADYPCSAIHGPGYVHGRVYITANNLCFSTGTSSTFQRTKDVLKAAAFSGDGNEPIIRQIIPLADIASIQLSVHLETANKGPPYFMLLPAEVVIPTCLQVFTRRQQVFQFFSFGNRDKTDSLSDTLKGKPVEQAYNYIDHVWRAATTVPLPGVQYTQ
Protein: Pre-mRNA splicing factor ATP-dependent RNA helicase, putative (Q38A61)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- U3 small nucleolar RNA-associated protein 14
- Sas10 C-terminal domain-containing protein
- Probable eukaryotic initiation factor 4A
- Pre-mRNA-splicing factor SLU7
- U3 small nucleolar RNA-associated protein 25
- MI domain-containing protein
- Nop14-like protein
- RNA helicase
- Pre-mRNA-splicing factor 18
- Nrap protein domain-containing protein
Sequence:
MLNERRPQVHLPVTEARAAIVRMIRRHNAVVIVGETGSGKTTQIPQYVWDDIVSKGDGGIVGCTQPRRVAAVSIARHVAQQRGGKVGGEVAYAVRFDDTCTKNTKIKFMTDGILLREIQTDPDLTHYRCLILDEAHERTLHGDVLFGLLKDIARRRKNTLSIVIMSATLNEEHFSKFWWDAPVGVIHGRTFPVTIYHTVEPQADYVEAAVSALLQIHQREEPGDVLCFLTGREEIEDAKRMLEQRMKLLPNDIGDFVVLPLYSAMPYEQQLVVFDPAPPGKRKIIIATNIAETSITVEGIKYVVDSGVVKAKHYNSKTGMEVLAEVDVSRAQATQRAGRAGRVAAGKCFRLYTAQAFESLHENTVPEIQRCSLISVVLQMKSLNIDRIADFEFMDAPNPHALTKAEETLMLLNALDSEGCVTPLGKRLTDFPIEPAAAMVLLAGKALGVEREAVIAIAMTSTENLFVTSRDMKERADRCKGAFAKSAGDHATLVSIYQAFKHSPKDQRKLWCETNAISYRQMLKVQDVITQLMAILAEGDDEELLATLVPKSVRQALSHKATDESCAVVSGSNDDNTVTNGYDHQWEPGANGRSSGLKFRDFELLRRALCCGYFLNVAFYNAKIGNFQTVVGQQVVHIHPSSVLFTLRRKPALVLFNSVVRTTRRYMQNVSVVQEAWLRETSSFSRMML
Protein: Endoplasmic reticulum transmembrane helix translocase (EC 7.4.2.-) (Endoplasmic reticulum P5A-ATPase) (Q9HD20)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24392018}; Multi-pass membrane protein {ECO:0000269|PubMed:24392018}.
Interaction partners:
- Pecanex-like protein 3
Sequence:
MAAAAAVGNAVPCGARPCGVRPDGQPKPGPQPRALLAAGPALIANGDELVAAVWPYRRLALLRRLTVLPFAGLLYPAWLGAAAAGCWGWGSSWVQIPEAALLVLATICLAHALTVLSGHWSVHAHCALTCTPEYDPSKATFVKVVPTPNNGSTELVALHRNEGEDGLEVLSFEFQKIKYSYDALEKKQFLPVAFPVGNAFSYYQSNRGFQEDSEIRAAEKKFGSNKAEMVVPDFSELFKERATAPFFVFQVFCVGLWCLDEYWYYSVFTLSMLVAFEASLVQQQMRNMSEIRKMGNKPHMIQVYRSRKWRPIASDEIVPGDIVSIGRSPQENLVPCDVLLLRGRCIVDEAMLTGESVPQMKEPIEDLSPDRVLDLQADSRLHVIFGGTKVVQHIPPQKATTGLKPVDSGCVAYVLRTGFNTSQGKLLRTILFGVKRVTANNLETFIFILFLLVFAIAAAAYVWIEGTKDPSRNRYKLFLECTLILTSVVPPELPIELSLAVNTSLIALAKLYMYCTEPFRIPFAGKVEVCCFDKTGTLTSDSLVVRGVAGLRDGKEVTPVSSIPVETHRALASCHSLMQLDDGTLVGDPLEKAMLTAVDWTLTKDEKVFPRSIKTQGLKIHQRFHFASALKRMSVLASYEKLGSTDLCYIAAVKGAPETLHSMFSQCPPDYHHIHTEISREGARVLALGYKELGHLTHQQAREVKREALECSLKFVGFIVVSCPLKADSKAVIREIQNASHRVVMITGDNPLTACHVAQELHFIEKAHTLILQPPSEKGRQCEWRSIDGSIVLPLARGSPKALALEYALCLTGDGLAHLQATDPQQLLRLIPHVQVFARVAPKQKEFVITSLKELGYVTLMCGDGTNDVGALKHADVGVALLANAPERVVERRRRPRDSPTLSNSGIRATSRTAKQRSGLPPSEEQPTSQRDRLSQVLRDLEDESTPIVKLGDASIAAPFTSKLSSIQCICHVIKQGRCTLVTTLQMFKILALNALILAYSQSVLYLEGVKFSDFQATLQGLLLAGCFLFISRSKPLKTLSRERPLPNIFNLYTILTVMLQFFVHFLSLVYLYREAQARSPEKQEQFVDLYKEFEPSLVNSTVYIMAMAMQMATFAINYKGPPFMESLPENKPLVWSLAVSLLAIIGLLLGSSPDFNSQFGLVDIPVEFKLVIAQVLLLDFCLALLADRVLQFFLGTPKLKVPS
Protein: NUAK family SNF1-like kinase 2 (EC 2.7.11.1) (Omphalocele kinase 2) (SNF1/AMP kinase-related kinase) (SNARK) (Q9H093)
Organism: Homo sapiens (Human)
Function: Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube closure during embryonic development through LATS2 phosphorylation and regulation of the nuclear localization of YAP1 a critical downstream regulatory target in the Hippo signaling pathway.
Interaction partners:
Sequence:
MESLVFARRSGPTPSAAELARPLAEGLIKSPKPLMKKQAVKRHHHKHNLRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLMHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERQQLSEREARHFFRQIVSAVHYCHQNRVVHRDLKLENILLDANGNIKIADFGLSNLYHQGKFLQTFCGSPLYASPEIVNGKPYTGPEVDSWSLGVLLYILVHGTMPFDGHDHKILVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWWVNWGYATRVGEQEAPHEGGHPGSDSARASMADWLRRSSRPLLENGAKVCSFFKQHAPGGGSTTPGLERQHSLKKSRKENDMAQSLHSDTADDTAHRPGKSNLKLPKGILKKKVSASAEGVQEDPPELSPIPASPGQAAPLLPKKGILKKPRQRESGYYSSPEPSESGELLDAGDVFVSGDPKEQKPPQASGLLLHRKGILKLNGKFSQTALELAAPTTFGSLDELAPPRPLARASRPSGAVSEDSILSSESFDQLDLPERLPEPPLRGCVSVDNLTGLEEPPSEGPGSCLRRWRQDPLGDSCFSLTDCQEVTATYRQALRVCSKLT
Protein: Large ribosomal subunit protein eL38 (60S ribosomal protein L38) (P49167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL6B
- Large ribosomal subunit protein eL19A
- Small ribosomal subunit protein eS10A
- Large ribosomal subunit protein eL24B
- Small ribosomal subunit protein eS27A
Sequence:
MAREITDIKQFLELTRRADVKTATVKINKKLNKAGKPFRQTKFKVRGSSSLYTLVINDAGKAKKLIQSLPPTLKVNRL
Protein: DNA-Binding protein G5P (G5P) (GPV) (Single-stranded DNA-binding protein) (P69542)
Organism: Enterobacteria phage fd (Bacteriophage fd)
Function: Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single-stranded (progeny) viral DNA, prevents the conversion into the double-stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity).
Interaction partners:
Sequence:
MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEYPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK
Protein: DegQ (F8W672)
Organism: Legionella fallonii
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
Sequence:
MPSMAPVLKNIMPAIVNVAVQGYLPNDVTPPGSAGNDEENQPNNRPPQSRMPEKGRKFESIGSGVIIDPNNGVIITNDHVIRNASLITVTLQDGRRLKARLIGGDSETDLAVLKIDAKNLKSLVIGDSDKLEVGDFVVAIGNPFGLNSFGNSQSATFGIVSALKRSDLNIEGVENFIQTDAAINPGNSGGALVNAKGELIGINTAILSPYGGNVGIGFAIPINMVKDVAQQIIKFGSIHRGLMGIFVQHLTPELAQAMGYPEDFQGALVSQVNPNSPAELAGLKAGDIITQINDTKITQATQVKTTISLLRVGSTVKIIVERDNKPLTLSAVVTDIKSHEQKLQSNNPFLYGLALRAFEQESPPHGNVIGVQVVGASENSAGWRAGIRPGDIIISANKKPVTDVKSLQTIAQEKKKELLVQVLRGPGSMYLLVI
Protein: Sperm protamine R3 isoform 1 (P83266)
Organism: Hydrolagus colliei (Spotted ratfish) (Chimaera colliei)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:8875866}. Chromosome {ECO:0000269|PubMed:8875866}.
Interaction partners:
Sequence:
ARRRHSMKKKRKSVRRRKTRKNQRKRKNSLGRSFKQHGFLKQPPRFRP
Protein: Acid phosphatase-like protein (HAD superfamily, subfamily IIIB acid phosphatase) (Putative acid phosphatase) (Q9M0F5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLRSLSIWFFFFFVFVFLINPSISIRTSFIKLPGSDGSRYCDSWRLAAETNNVGTWDLIPSICVDSVAEYLNGDQFLSDYSVIVDYALAFAKSVEISGDGKDVWIFDIDETLLTNIDYYKAHGYGSEPYDDNKFSEWVEQGTAPAFDASLRLYNALKKLGFTIILLTGRDEHQRTSTETNLRDAGYSGWERLLLRGPNDQGKSATNYKSEQRSKLIEEGFKIRGNSGDQWSDLQGFAVADRSFKVPNPMYYIP