wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SFI1 (Suppressor of fermentation induced loss of stress resistance protein 1) (Q12369)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:14562095}. Note=Spindle pole, half bridge. {ECO:0000269|PubMed:14504268}.
Interaction partners:
- Cell division control protein 31
- Cell division control protein KAR1
- Spindle pole component BBP1
- Spindle pole body component SPC42
- NAP1-binding protein
- Spindle pole body assembly component MPS3
- Spindle pole component 29
- Spindle pole body component 110
- Monopolar spindle protein 2
- Cyclin-dependent kinase 1
Sequence:
MGKFGTTNKSTENLLRDKFVPETSPTNIPTDVLIKQGQITDSTESLIHGGAERYIVNALKPIELNKTEGFFEDPPFHLPSPPVDSTNLEYEDVTDLPKNGLRYDLNDISVEVIEDLYRQIEAFLVHFKLSRSFLQIFKNYVNILIQEGINPLRDEYFTILEDELKGFFTFNSVIEEILEIFLIHPRNKFIALSLAEYTYAKNKIRRHFNHWKTVCELNEEANRFANQAKLRVQEAVFYIWSDKTLKYSQMANDEAESFRNTWLLFRSFQQWITLTQTLKEQSRLADQAFLNKMFRKILKAQEHWKHLETVNTDNIKKIFLRTTFHIWKLRHKEINYHGLERRIFERIKQKVINYEYNKSIAEKVRSFSLQRKYLNKWEKKNIENEDKLGALYELENKFIKQKFFRKLNRSFQHSQQEAIAKSKLNQTLLRCVFEKMWLKRFEDHLHLYSIVSLKEANLVKRIFHSWKKLLYIDLKASDYSRTNLLKSSLRSWKLEVKLKIFEQKCKKSIQASAYRTWRKRIQYGKISSEHVKTAFCAKYLGVWKRRMLQMNSMNDEASKFYEEGLVNECLAIWKERLIKTKELEDRYNFLCKTHAILTVKRTLMHIDNVHLLYTKLAPSMDRVKLSKAFLKWRKATRFKVRHKLNDILHVYEKSKERELQSQLFNAWRNRFCFYTEECNIQAISKRNYQLEKMVLKKFRERLLEIVKSEELADEVREEFVLVKTFYIWKTHLDEIFYMSTLLEQSEANKQFIITSKFLKMWSLRFLKIKRNDETVEVFRHRWDRATVRGLLLLWKNRSDSSPKRRKDFNLKHELKTPIRSDSQNASTIPGSERIKQHRMEAMKSHYSRARRAIPSPVKSSSVLDSTAKKQINLESTTGLNGSPTRGKPLRYSPRRTTRNMPSKVDHIDFGRIPAVPFSLSANSPKIDQDMDYIREHDKSPLSRKRQ
Protein: Integrin beta-2-like protein (Protein pactolus) (Q3UV74)
Organism: Mus musculus (Mouse)
Function: During inflammatory stimulation, plays a role in retaining Cxcl13-expressing cells at the site of the inflammatory response.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}; Single-pass type I membrane protein {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}. Note=In unactivated neutrophils, the majority of the protein is contained in intracellular granules and is released to the cell surface following inflammatory activation or induction of necrotic or apoptotic cell death. {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}.
Interaction partners:
- Intercellular adhesion molecule 1
- Integrin alpha-L
- Integrin alpha-M
- Integrin alpha-X
- Junctional adhesion molecule C
- Protein-tyrosine kinase 2-beta
- Integrin beta-1
- Intercellular adhesion molecule 2
- Proto-oncogene vav
- Ras-related protein Rap-1A
Sequence:
MLGQCTLLPVLAGLLSLESALSQLCTKDNVSTCQDCIRSGPSCAWCQKLNFTGRGEPDSVRCDTPEQLLLKGCTSEYLVDPKSLAESQEDKERDQRQLSPRNVTVFLRPGQAATFKVDFQRTQDNSVDLYFLMGLSGSAQGHLSNVQTLGSDLLKALNEISRSGRIGFGSIVNMTFQHILKLTADSSQFQRELRKQLVSGKLATPKGQLDAVVQVAICLGEIGWRNGTRFLVLVTDNDFHLAKDKTLGTRQNTSDGRCHLDDGMYRSRGEPDYQSVVQLASKLAENNIQPIFVVPSRMVKTYEKLTTFIPKLTIGELSDDSSNVAQLIRNAYSKLSSIVVLNHSTIPSILKVTYDSYCSNGTSNPGKPSGDCSGVQINDQVTFQVNITASECFREQFFFIQALGFMDSVTVRVLPLCECQCQEQSQHHSLCGGKGAMECGICRCNSGYAGKNCECQTQGPSSQDLEGSCRKDNSSIMCSGLGDCICGQCECHTSDIPNKEIYGQYCECNNVNCERYDGQVCGGPERGHCSCGRCFCRYGFVGSACQCRMSTSGCLNNRMVECSGHGRCYCNRCLCDPGYQPPLCEKRPGYFHRCSEYYSCARCLKDNSAIKCRECWNLLFSNTPFSNKTCMTERDSEGCWTTYTLYQPDQSDINSIYIKESLVCAEISNTTILLGVIVGVLLAVIFLLVYCMVYLKGTQKAAKLPRKGGAQSTLAQQPHFQEPHHVEPVWNQERQGTQ
Protein: C-Maf inducing protein (A0A087WU05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALTSPLQDDSINQAPLEIVSKLLSENTNLTTQEHENIIVAIAPLLENNHPPPDLCEFFCKHCRERPRSMVVIEVFTPVVQRILKHNMDFGKCPRLRLFTQEYILALNELNAGMEVVKKFIQSMHGPTGHCPHPRVLPNLVAVCLAAIYSCYEEFINSRDNSPSLKEIRNGCQQPCDRKPTLPLRLLHPSPDLVSQEATLSEARLKSVVVASSEIHVEVERTSTAKPALTASAGNDSEPNLIDCLMVSPACSTMSIELGPQADRTLGCYVEILKLLSDYDDWRPSLASLLQPIPFPKEALAHEKFTKELKYVIQRFAEDPRQEVHSCLLSVRAGKDGWFQLYSPGGVACDDDGELFASMVHILMGSCYKTKKFLLSLAENKLGPCMLLALRGNQTMVEILCLMLEYNIIDNNDTQLQIISTLESTDVGKRMYEQLCDRQRELKELQRKGGPTRLTLPSKSTDADLARLLSSGSFGNLENLSLAFTNVTSACAEHLIKLPSLKQLNLWSTQFGDAGLRLLSEHLTMLQVLNLCETPVTDAGLLALSSMKSLCSLNMNSTKLSADTYEDLKAKLPNLKEVDVRYTEAW
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVG8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- RP28
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein uL30
- L17A
- Candida glabrata strain CBS138 chromosome M complete sequence
- L33
- 40S ribosomal protein S7
- Small ribosomal subunit protein uS14
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
Sequence:
MPGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSAGNEMPPQDSEGWFYKRAASVARHIYLRKEVGVGKLNKLYGNAKSRGARPSHHADASGSINRRVLQALEKIGVVELSPKGGRRISENGQRDLDRIAAQTLEEEE
Protein: Protocadherin gamma-B1 (PCDH-gamma-B1) (Q9Y5G3)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin gamma-B2
- Protocadherin gamma-B3
- Protocadherin gamma-A4
Sequence:
MQRAREAEMMKSQVLFPFLLSLFCGAISQQIRYTIPEELANGSRVGKLAKDLGLSVRELPTRKLRVSAEDYFNVSLESGDLLVNGRIDREKICGRKLECALEFETVAENPMNVFHVVVVIQDINDNAPRFVAKGIDLEICESALPGVKFSLDSAQDADVEGNSLKLYTINPNQYFSLSTKESPDGSKYPVLLLEKPLDREHQSSHRLILTAMDGGDPPLSGTTHIWIRVTDANDNAPVFSQEVYRVSLQENVPWGTSVLRVMATDQDEGINAEITYAFLNSPISTSLFNLNPNTGDITTNGTLDFEETSRYVLSVEAKDGGVHTAHCNVQIEIVDENDNAPEVTFMSFSNQIPEDSDLGTVIALIKVRDKDSGQNGMVTCYTQEEVPFKLESTSKNYYKLVIAGALNREQTADYNVTIIATDKGKPALSSRTSITLHISDINDNAPVFHQASYVVHVSENNPPGASIAQVSASDPDLGPNGRVSYSILASDLEPRELLSYVSVSPQSGVVFAQRAFDHEQLRAFELTLQARDQGSPALSANVSLRVLVGDLNDNAPRVLYPALGPDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASEPGLFSLGLRTGEVRTARALGDRDAARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDRPEPSDPQTELQFYLVVALALISVLFLLAVILAIALRLRRSSSLDTEGCFQTGLCSKSGPGVPPNHSEGTLPYSYNLCIASHSAKTEFNSLNLTPEMAPPQDLLCDDPSMVVCASNEDHKIAYDPSLSSHQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Beaten path Vb, isoform A (Beaten path Vb, isoform B) (GH08468p) (Q9VG19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Sidestep VI, isoform B
- Hexosyltransferase
Sequence:
MDLGRWLLQLGVHMLLVVRRIQCLRVTDINVPQIVDFRDNVTLSCSYDISGHTLNSVKWYKNGKEFFRYSPLTPPTYIPFAVEGVQLIDDGNECNESSCRVELNLLGVKSSGVYRCEVSGDAPHFQLTARDANMTVEALPQNNPLISSFHSTYRFNDFVEVNCSTDFSSLFTRITWYVNGIKVSLVDLLPSFETTIVAHGYSMRRIVSQLNFYANEPRFHQLQLQKLIQQKRTISPARLGLELRCVAEIDRYPHLQREGTMFAQLFRDDIDQKNQKLINSRSGATPNSQVQHLLLVAISMTMTAVRLFTPLTFQYGARKSARYKMAAT
Protein: Period circadian clock 1a (Period circadian protein homolog 1a isoform X1) (A0A0R4ICG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNNNNFQAPASCGGFADKAAIEMDEEEGQNNISPAMTDNQSLCPGLNITNESQQTHSGDTDAQSSGIDSTERENDGRLGHGTSTCSSLHGKGSATETTESKSSNGNSPSPPSSSVSFSLLSGSSEQDHSTSQASNSDQPARLQTQRELLKVLRELKIHMPAERRRKGRSSTLASLQYALSCVKQVRANQEYYHQWSVEESHGCCLDLSSFTIEELDNVTSEYTLQNTDTFSVAVSFLSGKVVYISSQAASLLRCKAERLQGALFSELLAPQDVSTFYSSTAPSRLPPWSSCAGTSSQVDCAEEKSMFCRISRGRDSNGEVKYHPFRLTPYQLTLRDSDTSQPEPCCLLIAERVHSGYEAPRIPADKRIFTTSHTPNCLFQEIDERAVPLLGYLPQDLVGKPVLVYLHPEDRLLMVAIHKKILQFAGQPFDHSPLRMRARSGEYLTIDTSWSSFINPWSRKVAFIVGRHKVRTSPLNEDVFTAPEGEEMKTMSPDVPQLNELIHRFLVQPVYGGSSQGYGSLGSSGSHEHQQGATSSSESNGHTSEDQIKPRKPMTFEQICQDMHMVKTSGQQVFIESRNRPPALKQGSLEALAKAADTAEASARDGLASLALSSPPRKELPMIYSYQQINCLDSIVRYLESFNVPGTVKRKCGSSSCTTSSTSDDDKQREGAGATQAETLVVTEGSKVVPAAPAHPLTPLALHCKAESVVSATSQCSFSSTIVHVGDKKPPESDIVMMEEPPTTPTASTSAPATSVASPIPVNPQPMPSPTAAVHEKEKEKERRSGGSAGKGLTKAVLSAHTQQEEQAFLNRFRDLSQLRMVQPSGLPPPRRCTSIPGTKGVNSSQNYPSVGNTSSRRHGRGGKRQKHQVDGNIPNNTPISASGPYRGPNPAQIRPNFPSVQQSSNSWAPSAASQTNGAPVGTSFPPSYMTMFPTSSPFSVTQMGTDPSLQTGVPRFPAQGFPSVMPPVMTFMMPNYMFPQLSNPGSQLNPANSQLNAQMNSFGQFPPPVVQMSVPMFNPAMGQFYPLGSQMNPAMPAMIPQQFYNPNYQLNFSNSPSMPAANVSTTPHGQSRSSTPQSTGPQAGERDGAGSPLFQSRCSSPLNLLQLEELPSNRTDATQQTPPPGGGATQGGVVVVQNSSNRSNTQDAKLNDHPEVSESNQDALSTSSDMLDLLLQEDSRSGTGSSGSGSGSGSFASGSNGCSTSGSGTRSSNTSKYFGSIDSSENDQNHKPASGDLGGEQFIKFVLQDPIWLLMANTDDKIMMTYQIPIKDKDSVLKEDRDALKAAQKHQPHFTEEQKKELTQVHPWIQTGCLPKAINVTSCTGCESPPDSSTLPPFDLEFHEMDLNVVLREEAKQEDKLAETAFPLSPPSSDNEQRDNQANLST
Protein: SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1) (Q5M824)
Organism: Rattus norvegicus (Rat)
Function: Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P29353}.
Interaction partners:
- Receptor protein-tyrosine kinase
- Growth factor receptor-bound protein 2
- SOS Ras/Rac guanine nucleotide exchange factor 1
- High affinity nerve growth factor receptor
- Insulin-like growth factor 1 receptor
- Proto-oncogene tyrosine-protein kinase Src
- Receptor tyrosine-protein kinase erbB-3
- SOS Ras/Rho guanine nucleotide exchange factor 2
- BDNF/NT-3 growth factors receptor
- Receptor tyrosine-protein kinase erbB-4
Sequence:
MNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGAMRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEELPDHQYYNDFPGKEPPLGGVVDMRLREGAARPTLPSTQMPSHLGATLPIGQHVTGDHEVRKQMLPPPPCPGRELFDDPSYVNIQNLDKARQAGGGAGPPNPSVNGSAPRDLFDMKPFEDALRVPPAPQSMSMAEQLQGESWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVDRKV
Protein: Defective proboscis extension response 16, isoform B (Q0KIC0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPSFLTYFAALAATATPMENASLIASPATGTSTMGSAGSPVLMLGDDQQQQEYDTTVVDSWSDRPDTATLTKGFSIPSYLPPFPEFIPADLPHMLRNASSGAAPPADIGPSGSPMPSKPNEQSRLHAYDSEQKAQQLRREKELAKERELLPRRQLSLPPLNATVQAGQHAYLPCKLNQHSGKPLSWVRLRDEHIIAVDHTTFINDARFASLLQSTTLTTLVSGGALSTTATPVAALGNSFAHAVPGGQERGNSSSLSWTLQIKYVNLEDAGWYECQLATEPKMSAKVQLFVITPRTELIGDRQRFVKAGSRVELHCIVRGTLEAPKYIFWYRGDQQVTAENEASGAQSGWYTQIDRNIFGSTEHNRNTIGSLVIPLVRKIHSGNYTCEPENSAAASMQLHVLSGEYSASAIKSTAARPHRLGHGYTSLHQWLIFLLVALNKT
Protein: DnaJ homolog subfamily C member 2 (M-phase phosphoprotein 11) (Zuotin-related factor 1) [Cleaved into: DnaJ homolog subfamily C member 2, N-terminally processed] (Q99543)
Organism: Homo sapiens (Human)
Function: Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21179169}. Cytoplasm, cytosol {ECO:0000269|PubMed:16002468, ECO:0000269|PubMed:21179169}.
Interaction partners:
- Heat shock 70 kDa protein 14
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- DnaJ homolog subfamily B member 4
- Zinc finger CCCH domain-containing protein 15
- Large ribosomal subunit protein eL31
- Heat shock 70 kDa protein 1-like
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 6
- DnaJ homolog subfamily B member 1
Sequence:
MLLLPSAADGRGTAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASASFQELEDKKELSEESEDEELQLEEFPMLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEGDNDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSVPSKSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCDRLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQASKNTEKSTGGGGNGSKNWSEDDLQLLIKAVNLFPAGTNSRWEVIANYMNIHSSSGVKRTAKDVIGKAKSLQKLDPHQKDDINKKAFDKFKKEHGVVPQADNATPSERFEGPYTDFTPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMKRYKELVEMVKAKKAAQEQVLNASRAKK
Protein: Chloride intracellular channel protein 5 (Chlorine channel protein p64) (Glutaredoxin-like oxidoreductase CLIC5) (EC 1.8.-.-) (P35526)
Organism: Bos taurus (Bovine)
Function: Required for normal hearing. It is necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti. Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. May play a role in the regulation of transepithelial ion absorption and secretion. Is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture. Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens.
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9NZA1}. Membrane {ECO:0000305|PubMed:7686908}; Single-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9NZA1}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Mitochondrion {ECO:0000250|UniProtKB:Q9EPT8}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q9EPT8}. Note=Colocalizes with AKAP9 at the Golgi apparatus as well as, to a lesser extent, the centrosome (By similarity). Associates with the cortical actin cytoskeleton (By similarity). Localizes to the apical region of cochlear hair cells, at the base of the actin-rich hair bundle (By similarity). Colocalizes with podocalyxin at the apical cell membrane in renal glomeruli (By similarity). May localize to the centrosome in lens epithelial cells (By similarity). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q8BXK9, ECO:0000250|UniProtKB:Q9EPT8, ECO:0000250|UniProtKB:Q9NZA1}.
Interaction partners:
Sequence:
MNDENYSTTIYNRVQTERVYEDSDPAENGGPLYDEVHEDVRREDNLYVNELENQEYDSVAVYPVGRQGRTSASLQPETGEYVLPDEPYSKAQDPHPGEPTADEDISLEELLSPTKDHQSDSEEPQASDPEEPQASDPEEPQGPDPEEPQENGNEMEADLPSPSSFTIQNSRAFSTREISPTSYSADDVSEGNESASASPEINLFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTPEKYPRLAAKHRESNTAGIDIFVKFSAYIKNTKQQSNAALERGLTKALKKLDDYLNTPLPEEIDADTRGDDEKGSRRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDFPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVAKRLSRS
Protein: Probable ethanolamine permease EutH (Ethanolamine utilization protein EutH) (P76552)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the diffusion of protonated ethanolamine (EA) into the cell at low pH. At low pH most EA is protonated, and this permease becomes necessary.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ethanolamine ammonia-lyase reactivase EutA
- Ethanolamine ammonia-lyase small subunit
- Ethanolamine utilization protein EutJ
- Ethanolamine ammonia-lyase large subunit
- Acetate kinase EutQ
- Bacterial microcompartment shell vertex protein EutN
- Corrinoid adenosyltransferase EutT
- Probable acetate kinase EutP
- Bacterial microcompartment shell protein EutL
- Bacterial microcompartment shell protein EutS
Sequence:
MGINEIIMYIMMFFMLIAAVDRILSQFGGSARFLGKFGKSIEGSGGQFEEGFMAMGALGLAMVGMTALAPVLAHVLGPVIIPVYEMLGANPSMFAGTLLACDMGGFFLAKELAGGDVAAWLYSGLILGSMMGPTIVFSIPVALGIIEPSDRRYLALGVLAGIVTIPIGCIAGGLVAMYSGVQINGQPVEFTFALILMNMIPVIIVAILVALGLKFIPEKMINGFQIFAKFLVALITLGLAAAVVKFLLGWELIPGLDPIFMAPGDKPGEVMRAIEVIGSISCVLLGAYPMVLLLTRWFEKPLMSVGKVLNMNNIAAAGMVATLANNIPMFGMMKQMDTRGKVINCAFAVSAAFALGDHLGFAAANMNAMIFPMIVGKLIGGVTAIGVAMMLVPKEDATATKTEAEAQS
Protein: ER membrane protein complex subunit 2 (Q9VEQ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367091}; Peripheral membrane protein {ECO:0000256|RuleBase:RU367091}; Cytoplasmic side {ECO:0000256|RuleBase:RU367091}.
Interaction partners:
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 8/9 homolog
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 7
- ER membrane protein complex subunit 6
- Membrane magnesium transporter
- Dynactin subunit 4
Sequence:
MSLDYEKMSWSDVRDQFRTWREETGRHSEEVVQLWVAVLEDKVHKTGNERHLILEQVIIAALDTARFDIATKCTKQLALEFPGSLRVMKFKAMRYEALEQYDEADEVLDAIIAKDETNAAPRKRKIAILKARGRRLEAIKELNEYLKKFMSDQEAWHELCNMYLAEGEFGKAAFCMEEVLLHNPHSHLIHQRLAEIRYTMGGVENMESARTYYSQALKLNPHNLRALYGIYLCCNHLDNSRAVSSKRKELQKLSQWALEQLLTKQTIVPLEAAFGNLEIKSN
Protein: Probable dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (DppIV) (Q5AZ42)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable dipeptidyl-peptidase 5
- Leucine aminopeptidase 1
- tripeptidyl-peptidase II
- Neutral protease 2 homolog AN3393
Sequence:
MKLSVLSVLLVSVAQAAAAPWRPREPRAAGSKRLTFNETVISAALSPSSISVQWIATENDGDYVYQEEDGSIKIESIVTNRSQTIVPAEKIPADAYSYWISPDLSAVLWATNYTKQYRHSFFADYYIQDVETLETVPLVEDMVGDIQYAEWSPSGDSIAFVRGNNLWTWSDGTVTAITKDGGPDMFHGVPDWIYEEEILGDRFALWFSPDSELLAFLTFNETGVPTFTVQYFMDNQEIAPPYPRELDIRYPKVSETNPTVKLNILQLSDNTVSTIPIDVFDPSELIVGEVAWVTDTHTELAVKAFNRVQDESKVVIVETASGETKIAHERDGTDGWLDNLLSISYVGPLALGSGDASSAYYVDLSDHSGWTHLYLFSTSGGDPIPLTEGEWEVTSIVSIDQERELVYYLSTQHHSTERHLYSVSYRTFEITPLVDDTVEAYWSVSFSAKAGYYILTYAGPSVPYQELYSVNQTAPLRTLTSNAALIEKLEEYALPNISYFELEIPSGEKLNVMQRLPVGFSPDKKYPVLFTPYGGPGAQEVSKRWQSLDFNAYIASDPELEYVTWTVDNRGTGYRGREFRSLVAKQLGKLEAEDQVYAAKQAAKLDWVDSEHIAIWGWSYGGYLTGKVLETDSGAFSLGLLTAPVSDWRLYDSMYTERYMKTLSTNAEGYNTTAIRHTDGFKNVEGGFLIQHGTGDDNVHFQNAAALGDTLIGNGVTPEKMQVQWFTDSDHSIRYNGGNVFLYRQLAQRLYKEKNRAKKEQHQWSKRSQDWVV
Protein: tRNA (guanine(37)-N(1))/4-demethylwyosine(37)-methyltransferase Taw22 (EC 2.1.1.-) (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA(Phe):m1G/imG2 methyltransferase) (Q9V2G1)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Catalyzes both the N1-methylation of guanosine and the C7-methylation of 4-demethylwyosine (imG-14) at position 37 in tRNA(Phe).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
Sequence:
MSGVKVRREDAKKVLELLKSVGILDGKRKAIRDEKYVIFPVTDTNIAKSLGLEVVDVELPMRPERQIYKNLEDLLPREIFKKLGRLDIVGDIAIVSIPDEILSEREVIVSAIRKLYPKVKVIARRGFHSGLYRIRELEVIWGENRLHTIHKENGVLIKVDLSKVFFNPRMKGERYRIAQLVNDGERILVPFAGVIPYPLVIARFKNVEVYAVEINEFAVKLAEENLELNRDRLKGKIKIIHGDVFEVLPNLPNFDRVVSPTPKGVDALSLTLSKAEKFLHYYDFVHESEIERFRERVLEECRRQGKECRVSVRKVSDYKPHVYKVCADVEILS
Protein: CLAVATA3/ESR (CLE)-related protein 25 [Cleaved into: CLE25p] (Q8LFL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular location: [CLE25p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- Protein CLAVATA 3
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MGGNGIRALVGVIASLGLIVFLLVGILANSAPSVPSSENVKTLRFSGKDVNLFHVSKRKVPNGPDPIHNRKAETSRRPPRV
Protein: Aldo-keto reductase a (Aldo-keto reductase family 1, member C12) (Q9JLI0)
Organism: Mus musculus (Mouse)
Interaction partners:
- Aldo-keto reductase family 1 member C13
Sequence:
MSSKQHYVKLNDGHLIPALGFGTYKPKEVPKSKSLEAACLALDVGYRHVDTAYAYQVEEEIGQAIQSKIKAGVVKREDLFITTKLWCGCFRPELVKPALEKSLKSLQLDYVDLYLIHYPVPMKPGDNESPLDENGKFLLDTVDFCDTWERLEECKDAGLVKSIGVSNFNHRQLERILNKPGLKYKPVCNQVECHLYLNQSKLLDYCKSKDIVLVAYGALGTQRYKEWVDQNSPVLLNDPVLCDVAKRNKRSPALIALRYLFQRGIVPLAQSFKENEMRENLQVFEFQLSPEDMKTLDGLNKNFRYLPAEFLADHPEYPFSEEY
Protein: Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 pre-mRNA-processing factor 4 homolog) (X2JAG8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pre-mRNA-processing factor 6
- U4/U6 small nuclear ribonucleoprotein Prp31
- Splicing factor 3B subunit 1
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-processing-splicing factor 8
- RE11167p
- SD09427p
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Ubiquitin carboxyl-terminal hydrolase 39
- Pinin, isoform B
Sequence:
MADDKSYDSSNNSETEERRAKHKKAKKHKKHKKSSTGKTEKDRHVHKKQKKAKKRPHRTSESTNESDAPENAKLKLSQNCGLSSKFTEIMQKASRNGADFRVGKPLLPTDPSSLVEEITKTIQNKMLPVLEVASSSSESDVPADAASPIILSIIEDELNLEELMRQKALLQARLGAYMSDPEAEDKGDLLPHTHSQQLVVHTKSVLKAVTSVPQPQPSKSAAPLATATSKHANIKKSTTHNSNESDVILLDDSSGGQRTPSPTPEKRRRHASPLPAAPRSRCRRDRRSRDRDRSPPRRRASDQQTQVRPRSRNRNMEDLRQEINRDKQRERRDHSRDRDRRGLDRPPPPTDMRPGRARERDVRPSRMQRSHSRSKFESDRRRERERQKDRDRGGGRVGARSGTDNGDRDRYKGSLSEGQNKLDKESSDEEVNVNIDILEEDDEERIIELRRKKREELLKKLGTGQESPAPHNSVSYESRSTSQGSSQRERPLRTPSPTMPCPNPLISEIPKDREDMDNSTSQKTCSAKEKRNEWDMFADQDVDSNFDVSRKISPNTIVQNKHQHENPALTDNWDDAEGYYRVRIGEVLDNRYLVNGYTGQGVFSNVVRGRDQARGQANVAIKIIRNNEIMHKTGLRELEILKKLNDADPEDRFHCLRLYRHFFHKQHLCMVFEPLAMNLREVLKKYGKNVGLHIKAVRSYTQQLFLALKLLKKTGILHADIKPDNILVNENNLILKLCDFGSASAISDNEITPYLVSRFYRSPEIILGIPYDYGIDTWSAGCTIYELYTGKILFSGKSNNQMLKFFMDVKGKIPNRIIRKGQFREQHFDQSCNFLYHEIDKLTEREKIVVMPVVKPSRSLQQELIADQNLPDDQHRKVTQLKDLLENMFALDPAKRISLNQALVHPFIQEKM
Protein: Probable pectate lyase 13 (EC 4.2.2.2) (Powdery mildew susceptibility protein) (Powdery mildew-resistant mutant 6) (Q93Z04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Susceptibility factor required for infection by most powdery mildews, but not by unrelated pathogens. Exact function not known, but clearly affects cell wall composition.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Protein PMR5
- Pectinesterase/pectinesterase inhibitor 3
- Probable polygalacturonase At3g15720
- LRR receptor-like serine/threonine-protein kinase FEI 2
- Callose synthase 12
- Protein REDUCED WALL ACETYLATION 2
- Probable WRKY transcription factor 7
- Cellulose synthase A catalytic subunit 3
- Plant UBX domain-containing protein 2
- Pectinesterase 31
Sequence:
MLLQNFSNTIFLLCLFFTLLSATKPLNLTLPHQHPSPDSVALHVIRSVNESLARRQLSSPSSSSSSSSSSSSSSCRTGNPIDDCWRCSDADWSTNRQRLADCSIGFGHGTLGGKNGKIYVVTDSSDNNPTNPTPGTLRYGVIQEEPLWIVFSSNMLIRLKQELIINSYKTLDGRGSAVHITGNGCLTLQYVQHIIIHNLHIYDCKPSAGFEKRGRSDGDGISIFGSQKIWVDHCSMSHCTDGLIDAVMGSTAITISNNYFTHHDEVMLLGHDDNYAPDTGMQVTIAFNHFGQGLVQRMPRCRRGYIHVVNNDFTEWKMYAIGGSGNPTINSQGNRYSAPSDPSAKEVTKRVDSKDDGEWSNWNWRTEGDLMENGAFFVASGEGMSSMYSKASSVDPKAASLVDQLTRNAGVFGGPRDDQGQSGNSYSPYGGDGGGGGSSGGSSGGGMDVMGGTTRGSSSSSGDDSNVFQMIFGSDAPSRPRLTLLFSLLMISVLSLSTLLL
Protein: Prothymosin alpha (Q9UMZ1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDAAVDTSSEITTEDLKEKKEVVEEAENGRDAPADEENGEQEADNEVDEEQEEGGEEEGDGEEEDGDEDEGAESATDKRAAEDDEDNDVDTKKQKTDEDD