wanglab/gogpt-training-data huggingface dataset:
Protein: Smog, isoform D (M9ND25)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Rho guanine nucleotide exchange factor 2, isoform D
- LD16635p
- Guanine nucleotide-binding protein subunit beta-1
Sequence:
MELCIATKSKIETAQSSMPQSSQCSSSSNCRNYQKKCHQNQTNTQVQSTQRSNCSSHSDRDHLTNQQKQQNQRTNSATAASAAAATLSESTRCNIIISSSSSSSSSTKSSKNIREPSSSSSTQLNTLYSLLVLLIVGLATATASPSPSPSHAPFGRESRRDALLAYYKRAHLPQSSSSGISLGHKYHLLHDANGLDFDELTPTASSVSALSRAERFRLRKRSATPTTPATAAGVTSLDVATAAAAATDAAAKDAGSGKKPEEKCEPKVLETLPDEPFYDYTDIAEDAARQFIEFLSGKFPNANTPIAIDEPTRAEVSRRANGIASYALNEDDNLLAFAIAAPSIHTVVVKFRDNVTIPPDQVHNKAYLGSYWRELGAAWNSTDGTQEWGAPFRDCNLLTRRWLWPFRISFSEHRIKVVAAAFIAADEDVCNDGLEEVFGRRHGCDRNTTFCLLTENKPAATRDVYTCLCRESYYLPNSTLQGFRGDRVELSEGYDNYSCIPCPGGCTNCDSNGVCLTFQEEEVLNVDACLRLLVAIVLGACILCCIVLGVIVFRQRKCKAIASGMWTVLETILLGIVLLYASVAVHFFPASTERCLLEPWLRELGFITCYGAIILKLYRHLVDFRTRKAHRWVLRDVDLLKYLGTMVFAVICYMAAFTASSLDLLESAQLESLREADTNTCHPLKWELVTQTSEMLILCFGLHLSIASRNANTQFRERQFLVTALTLEFLVSSSFYFLRFVYLPEMSPSAILLALFIRSQLTNSFALGLIFVPKLWYQHKQVRSLAYDLSIRLPVDAFKGTSHDAGQRLGGGYAGLCLGDPDIGELTISEMSPEDIRAELKRLYTQLEIMKNKTLRQDNPHISKRRGGRKAGHRRFSLQKKGSKDKALSAKHRSNKHHQDIEITEAEPSRTPEDSVCSAEGPTDTYAEISGVSHSMLSHSMVSHSVVSHSK
Protein: MADS-box protein FLOWERING LOCUS C (MADS-box protein FLOWERING LOCUS F) (Q9S7Q7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor that seems to play a central role in the regulation of flowering time in the late-flowering phenotype by interacting with 'FRIGIDA', the autonomous and the vernalization flowering pathways. Inhibits flowering by repressing 'SUPPRESSOR OF OVEREXPRESSION OF CONSTANS 1'. At elevated temperatures (e.g. 29 degrees Celsius), maintained at high levels in a JMJ30/JMJ32-dependent manner to prevent extreme precocious flowering.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Inactive protein FRIGIDA
- Protein FLOWERING LOCUS T
- Zinc finger protein CONSTANS
- Ypt/Rab-GAP domain of gyp1p superfamily protein
- Pliceosome associated protein-like protein
- MADS-box protein SVP
- FRIGIDA-like protein 1
- FRIGIDA-like protein 5
Sequence:
MGRKKLEIKRIENKSSRQVTFSKRRNGLIEKARQLSVLCDASVALLVVSASGKLYSFSSGDNLVKILDRYGKQHADDLKALDHQSKALNYGSHYELLELVDSKLVGSNVKNVSIDALVQLEEHLETALSVTRAKKTELMLKLVENLKEKEKMLKEENQVLASQMENNHHVGAEAEMEMSPAGQISDNLPVTLPLLN
Protein: Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic (EC 6.3.2.6) (SAICAR synthetase) (P38025)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Adenylosuccinate lyase
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Adenylosuccinate lyase
- Phosphoribosylamine--glycine ligase, chloroplastic
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- phosphoribosylaminoimidazole carboxylase
- AICARFT/IMPCHase bienzyme family protein
- Amidophosphoribosyltransferase 1, chloroplastic
- Amidophosphoribosyltransferase 2, chloroplastic
- Amidophosphoribosyltransferase 3, chloroplastic
Sequence:
MAQCVRSTLNPVRTPQSFTRKAYVKSPAFASVSFLRAVPEFNKYPKPCSLVMSCQGKAQNQQEERPQLSLDDLVTSNRKGEVLGTIKDSLSNCLSETNLLATVPGLKSRIKGKVRDIYDAGDYLVLITTDRLSAFDRNLASIPFKGQVLNETSLWWFNNTQHITPNAIVSSPDRNVVIAKKCSVFPIEFVVRGYVTGSTDTSLWTVYNKGVRNYCGNELSDGLVKNQKLPANILTPTTKAADHDVPISPNEIVEGGFMTQAEFDEASMKALSLFEFGQGVAKKHGLILVDTKYEFGRSSDGSILLIDEIHTPDSSRYWLAGSYEERFQKGLEPENVDKEFLRLWFKENCNPYEDEVLPAAPAELVTELAWRYIFLYETITGSRIDIIPTQEPIHDRISRNTSQALSSLRQL
Protein: Immunoglobulin superfamily member 11 (IgSF11) (Brain and testis-specific immunoglobulin superfamily protein) (Bt-IGSF) (V-set and immunoglobulin domain-containing protein 3) (Q5DX21)
Organism: Homo sapiens (Human)
Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- V-type immunoglobulin domain-containing suppressor of T-cell activation
Sequence:
MTSQRSPLAPLLLLSLHGVAASLEVSESPGSIQVARGQPAVLPCTFTTSAALINLNVIWMVTPLSNANQPEQVILYQGGQMFDGAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDIGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRNIGLIAGAIGTGAVIIIFCIALILGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSAKAFHTEISSSDNNTLTSSNAYNSRYWSNNPKVHRNTESVSHFSDLGQSFSFHSGNANIPSIYANGTHLVPGQHKTLVVTANRGSSPQVMSRSNGSVSRKPRPPHTHSYTISHATLERIGAVPVMVPAQSRAGSLV
Protein: Transcriptional regulator (A0A1D8PED2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcription factor MBP1
- Transcription factor MBP1
- G1/S-specific cyclin CLN3
- Cyclin-dependent kinase 1
- Bub3p
- Cdh1p
- Origin recognition complex subunit 5
- Rme1p
- Mitogen-activated protein kinase MKC1
- Hypha-specific G1 cyclin-related protein 1
Sequence:
MDSPIHIGDLTTQSIQQKLFETHINNNNKNKTINNNCALLSTIYSSIYSGVKTIQLTMKLDSDKNNNNNNNNNDLKFDNKSHGEIIVLRRVQDSFVNVTQLFQILIKLEVLPTSQVDNYFDNEILSNLKYFGSSSNTPQYLDLRKHQNIYLQGIWIPYDKAVNLALKFDIYEITKKLFLVDVHDFDKLPKANKRLYEEDANSDSDILDSPSKKQKLDKKSKKDLLSNGKAITKKLIASSVSQNSNYPFTLPAVIIDNSNSEIANDIKVKLGDVFKRDDEKPDGISFEDVKSAFADALSRYTPETIIDIPLDSKGQTALHFASTLASLNLVSSFIELGLNSPIRGNNAGESPLISCIQVTNSMEKGNFTKILSNWLYPDIWLLDKRKRTVFHHLTLQIDKNDSFRFYTTKILEYIISDNNQNLLDFRANILNAQDEDGNTALHLAIEKDSKWFIKVLVDLGADTSISNKRGTKPSDFEIIRDLGSIENDDQIFDLISTGLEFLNKRLEIGGEKLPEVESPKVVTTPKLIDQEGSSSSGKIFNSIQQLLSNTNVEYENILNSKREQIKQLDRALHDATIVTANNRFNTKKITEKLINLDNLKLQVANVTDKLALSKQELNEEIDDTKEYDADAPFIIPQIYDKLKKGKDPIQDLKTDDYLLSQLQPAPILKARIQAYKDINSKLEKELKTLVDYSDLTSKFKKVVSICTNVGVNEVDEFLDGLLEAVEGQQ
Protein: Polyprotein pp62 (60 kDa polyprotein) (p60) (62 kDa polyprotein) (p62) [Cleaved into: p15; p35 (PIG1) (UB18); p8] (Q65179)
Organism: African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V) (ASFV)
Function: Essential for the correct assembly and maturation of the core of the virion.
Subcellular location: [Polyprotein pp62]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:9223468}. Note=Found in perinuclear cytoplasmic viral factories during assembly. {ECO:0000269|PubMed:9223468}.; SUBCELLULAR LOCATION: [p35]: Virion {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000269|PubMed:33629764}.; SUBCELLULAR LOCATION: [p15]: Virion {ECO:0000269|PubMed:30185597, ECO:0000269|PubMed:33629764}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000269|PubMed:33629764}.; SUBCELLULAR LOCATION: [p8]: Virion {ECO:0000269|PubMed:30185597}. Note=Located in the core shell, which functions like a matrix between the DNA and the inner envelope. {ECO:0000303|PubMed:30185597}.
Interaction partners:
Sequence:
MPSNMKQFCKISVWLQQHDPDLLEIINNLCMLGNLSAAKYKHGVTFIYPKQAKIRDEIKKHAYSNDPSQAIKTLESLILPFYIPTPAEFTGEIGSYTGVKLEVEKTEANKVILKNGEAVLVPAADFKPFPDRRLAVWIMESGSMPLEGPPYKRKKEGGGNDPPVPKHISPYTPRTRIAIEVEKAFDDCMRQNWCSVNNPYLAKSVSLLSFLSLNHPTEFIKVLPLIDFDPLVTFYLLLEPYKTHGDDFLIPETILFGPTGWNGTDLYQSAMLEFKKFFTQITRQTFMDIADSATKEVDVPICYSDPETVHSYTNHVRTEILHHNAVNKVTTPNLVVQAYNELEQTNTIRHYGPIFPESTINALRFWKKLWQDEQRFVIHGLHRTLMDQPTYETSEFAEIVRNLRFSRPGNNYINELNITSPAMYGDKHTTGDIAPNDRFAMLVAFINSTDFLYTAIPEEKVGGNETQTSSLTDLVPTRLHSFLNHNLSKLKILNRAQQTVRNILSNDCLNQLKHYVKHTGKNEILKLLQE
Protein: Brevinin-2ISc (F1T155)
Organism: Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae)
Function: Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=50 ug) and against Gram positive bacteria S.aureus ATCC 6538 (MIC=25 ug). Has no activity against methicillin-resistant S.aureus ATCC 43300, B.subtilis ATCC 6633 and against fungus C.albicans ATCC 90028.
Subcellular location: Secreted {ECO:0000305|PubMed:21193000}.
Interaction partners:
Sequence:
MFTLKKSLLLLFFLGTISLSLCEEERDADEDEGEMTEEEVKRSVLGTVKDLLIGAGKSAAQSVLTTLSCKLSNSC
Protein: Protein phosphatase 1 regulatory subunit INH3 (Protein INHIBITOR-3) (AtINH3) (Q8S8F7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibitor of protein-phosphatase 1 (PP1). Binds to and inhibits PP1 activity. Required for early embryogenesis progression.
Interaction partners:
- Serine/threonine-protein phosphatase PP1 isozyme 4
- Serine/threonine-protein phosphatase PP1 isozyme 1
- Serine/threonine-protein phosphatase PP1 isozyme 2
- Serine/threonine-protein phosphatase PP1 isozyme 3
- Serine/threonine-protein phosphatase PP1 isozyme 5
- Serine/threonine-protein phosphatase PP1 isozyme 8
- Serine/threonine-protein phosphatase PP1 isozyme 7
- Serine/threonine-protein phosphatase PP1 isozyme 6
- Serine/threonine-protein phosphatase PP1 isozyme 9
- AT5g22320/MWD9_11
Sequence:
MSTATRPSSSATTSVILENPVSQSQPTERLVLRLNRKKKKVSWKDGTVDNEFMQKKSSKKCCIFHKQKPFDEDDSEEEDDNNHHCDHNHEHSESGEASSSNDSKAVD
Protein: P-type ATPase (Q55FW3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Translationally-controlled tumor protein homolog 2
Sequence:
MSKSGGLSKSRSGSQHEIELGSSSSNLKKSKSMESVEFITEPQIPLYYSMVKEKERQREVKLRNRIKNKLKKNKSNTTTTTTTTDVGASPSTIEPIDGNDKEPMSAIDLAQDNIEKKTQHKPKDLATQTTEELTHDHTLPLEELIIKLKTNININDPRHSFGLSREFASERLEIDGKNALTPSKPVPKWVKYLKEFLGLFPIMLEVGGILSIIAFGIDTETGKDNLYLGIILWIVVFLTCTFSYIQNSKSTGVMEGFKKLAPSSTKVLRDDNLIEIDSEDLVVGDVVIVRAGDKVPADLRVIASHHFKVDNASLTGETEPQTRSPNCTDENPLETQNLTFYGTLACQGDCVGVVIATGDRTVIGKIAKLASNSKPNSTPMKEEIEKFIKIISIVAFSLGAIFLAIGFGRSVEWILVIIYTIGIVVSQVPEALLPTLTVTLNLTAKRMSRKNVLVKNLLTVETLGSTTTIASDKTGTLTQNIMTVVHLWYDGTIYSCNSLTASNFFNAQATTFKKLYQVAALCNRTVFDKSENQDDIPIQLRKCIGDASESALLKFCEQVENVEQYRDRFPKYFEIPFNSVNKWQMSVHTIGDDGEFFMVMKGAPERIIKMCNRILIEGEEQELDEKHLQNFQSSYEHLAGKGERVLGLAYLPLDPQQYPNNYIFDMEEKNFPTKDLVFVGLTALMDPPRPGVPEAIRTCKEAGIRVMMVTGDHPLTGTAIAKQVGIIETDETLNDIAEREGVDVLSLDFSRGTSIAITGSMLDDLTSEQWDKILSLRELCFCRTSPEQKLQIVAHLQKRGEIVAVTGDGVNDSPALKKADLGCAMGITGSDVAKEAASIVLLDDNFASIIAGVEEGRMIFDKLKKSICYTLSSNIPEAIPFFCFFVLQMPVALSGILILCIDLGTDLIPVISYAYEGSETDLMKRKPRNVKKDKLVSLRLAIFSYLWLGCWQCAAGFLNYFLLFKDYGYSASDLYNVSSTYFKKDAPLYGGHDDAKQIQILNEAQTAYFIAIVISRVGACFCAKTRIISIFQQGFGNMVFNFGVCSMLAIALFIVHVPGVRTFFGCTIVSYKYWLIPIPFAVFLVASNELRLWLIRRYPKSTFANLCAW
Protein: Protein held out wings (KH domain protein KH93F) (Protein muscle-specific) (Protein struthio) (Protein wings held out) (Putative RNA-binding protein) (Quaking-related 93F) (O01367)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for integrin-mediated cell-adhesion in wing blade. Vital role in steroid regulation of muscle development and to control heart rate. Required during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.
Subcellular location: Nucleus {ECO:0000269|PubMed:23788626, ECO:0000269|PubMed:9169854}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 10
Sequence:
MSVCESKAVVQQQLQQHLQQQAAAAVVAVAQQQQAQAQAQAQAQAQQQQQAPQVVVPMTPQHLTPQQQQQSTQSIADYLAQLLKDRKQLAAFPNVFTHVERLLDEEIARVRASLFQINGVKKEPLTLPEPEGSVVTMNEKVYVPVREHPDFNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDANRGKPNWEHLSDDLHVLITVEDTENRATVKLAQAVAEVQKLLVPQAEGEDELKKRQLMELAIINGTYRDTTAKSVAVCDEEWRRLVAASDSRLLTSTGLPGLAAQIRAPAAAPLGAPLILNPRMTVPTTAASILSAQAAPTAAFDQTGHGMIFAPYDYANYAALAGNPLLTEYADHSVGAIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ
Protein: Bifunctional AAC/APH (EC 2.7.1.190) (O05841)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible phosphotransferase
- Aminoglycoside 2'-N-acetyltransferase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycocerosic acid synthase-like polyketide synthase
- Phthioceranic/hydroxyphthioceranic acid synthase
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks1
Sequence:
MRFAKLSDGLSDGIVTLSPLCLDDVDAHLAGGDERLVRWLSGMPSTRASVEAYIRHCREQWVTGGPLRSFGIRTVAETIVGTIDLRFDGEGLASGQVNVAYGLYPSWRGRGLATRAVDLVCQYAAEHGATEAVIKVEPENSASARVALRAGFAFVRRICEQDGTVFDRYERVLRAKMHADEVDIDEDLVRRLLRAQFPQWADLPIAPVRSAGTDNAMYRLGEDLAVRIPRIGWAIESLRTEQQWLPRIAAHLGVASPVPVGLGSPAEGFGWPWSVCRWVAGENPSAAEFVEPNRAVEDLADFITALRATDPMGGPPAKRGAPLGEQDAEVRAALAALDGIIDVHAATAAWESALRVPPYAGPPMWFHGDLSRFNILTAQGRLTGVIDFGLMGVGDPSVDLIIAWNLLSAPARAQFRVAVGAADDDWMRGRGRALAIALIALPYYQDTNPPLAASARYAIGEVLADFRYGARPGC
Protein: Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1) (Q13469)
Organism: Homo sapiens (Human)
Function: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway.
Subcellular location: Cytoplasm. Nucleus. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription.
Interaction partners:
- Protein c-Fos
- Transcription factor Jun
- Forkhead box protein P3
- Nuclear factor of activated T-cells, cytoplasmic 1
- Calcineurin subunit B type 1
- Protein phosphatase 3 catalytic subunit alpha
- Cyclic AMP-responsive element-binding protein 1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Myocyte-specific enhancer factor 2D
- Glycogen synthase kinase-3 beta
Sequence:
MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNEEEPNAHKVASPPSGPAYPDDVLDYGLKPYSPLASLSGEPPGRFGEPDRVGPQKFLSAAKPAGASGLSPRIEITPSHELIQAVGPLRMRDAGLLVEQPPLAGVAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNGGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVALPPGASPQRSRSPSPQPSSHVAPQDHGSPAGYPPVAGSAVIMDALNSLATDSPCGIPPKMWKTSPDPSPVSAAPSKAGLPRHIYPAVEFLGPCEQGERRNSAPESILLVPPTWPKPLVPAIPICSIPVTASLPPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPTDEYDPTLICSPTHGGLGSQPYYPQHPMVAESPSCLVATMAPCQQFRTGLSSPDARYQQQNPAAVLYQRSKSLSPSLLGYQQPALMAAPLSLADAHRSVLVHAGSQGQSSALLHPSPTNQQASPVIHYSPTNQQLRCGSHQEFQHIMYCENFAPGTTRPGPPPVSQGQRLSPGSYPTVIQQQNATSQRAAKNGPPVSDQKEVLPAGVTIKQEQNLDQTYLDDVNEIIRKEFSGPPARNQT
Protein: Glycosyltransferase (Q9HTB5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Class I SAM-dependent methyltransferase
- Methyltransferase type 11 domain-containing protein
- Acyltransferase 3 domain-containing protein
- DUF1127 domain-containing protein
- Glycosyltransferase WbpX
- D-rhamnosyltransferase WbpZ
- GDP-6-deoxy-D-mannose reductase
- Glycosyltransferase
- ABC subunit of A-band LPS efflux transporter
- GDP-mannose 4,6-dehydratase
Sequence:
MNFILYSDINERSIGHNLGRPEYSYYFVLKAYRPILESLGQVHLVQSTDEVDPLYRQLHEQGEDCLFLSFTPPHKAARGLQCPMLCVVAWEFETIPDVAWDGDPAQDWSQVLAGHGAAITLSEQTARAVRRVLGEDFPVLALPTPIWEDFAAIRQQGERNPVKSGETLQLKGCVIDSRLLGLSADGLIAPIREETEDEILEVLPETPAEPEPEPVPEPEPEPEPVPLDWRRRLVISKHYLLLWYREAVSDLVPIPVRRWLFRHLRRPLPPPPTALETLPEPLPQAIEPMPPAEPEHPPALLPAVDQHQQVVVDGVVYVSVFNPLDGRKNWHQLITAFCWAFRDTSDATLVLKMTQSDLTTYHVELLTLLSQLSPFACRVIALHGYLDAAEYARLYGAASYYVNASRCEGLCLPLMEFMSCGTPAIAPDHSAMADYMDAQVGFVVRSSQEPAAWPQDSRRLYSTRRYRPSWESLKEAYLESYRVAREQPERYRQLSAAANQRMRGYCAGDVVRQRLEPFLSARKATPAPGVELAATATGNVPC
Protein: Caldesmon 1 (Q8VCQ8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLSGSGSQGRRCLATLSQIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEAHVQNSVPDEESKPASSNTQVEGDEEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSGPSRRMQNDSAENETAEGEEKRESRSGRYEVEETEVVIKSYQKNSYQDAEDKKKEEKEEEEQEKLKGGSLGENQIKDEKIKKDKEPKEEVKSFLDRKKGFTEVKAQNGEFMTHKLKQTENAFSPSRSGGRASGDKEAEGAPQVEAGKRLEELRRRRGETENEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKAREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSEDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSGVRSTHQAAVVSKIDSRLEQYTNAIEGTKASKPMKPAASDLPVPAEGVRNIKSMWEKGSVFSAPSASGTPNKETAGLKVGVSSRINEWLTKSPDGNKSPAPKPSDLRPGDVSGKRNLWEKQSVDKVTSPTKV
Protein: Glycerophosphodiester phosphodiesterase GDPD1, chloroplastic (EC 3.1.4.46) (Glycerophosphodiester phosphodiesterase 1) (AtGDPD1) (Protein SENESCENCE-RELATED GENE 3) (Q9SGA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine in vitro. May be involved in release of inorganic phosphate (Pi) from phospholipids during Pi starvation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21323773}.
Interaction partners:
- Glycerophosphodiester phosphodiesterase GDPD6
- Glycerophosphodiester phosphodiesterase GDPD5
- Probable choline kinase 2
- Probable choline kinase 3
- Probable choline kinase 1
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Glycerophosphodiester phosphodiesterase GDPD2
- Glycerophosphodiester phosphodiesterase GDPD3
- SPX domain-containing protein 1
Sequence:
MSLKAIHVSEVPSLDHFPENPSLICSSRKANNKFVVVGHRGHGMNMSQSPDLRFSALKENSILSFNAASKFPLDFIEFDVQVTRDGCPIIFHDDFIYSEEQGVVYEKRVTEVCLSEFMSYGPQRDTGKTGKPLLRKSKEGKIHKWSVATDDSFCTLQEAFEKVENPNLGFNIELKLDDNVFYSSDHLSRLLLPILQVVSDIGNDRTIIFSSFHPDAALLVRKLQTTYPVFFLTNGGTEMYHDTRRNSLEEAIKVCLEGGLQGIVSEVKGVFRNPALVNKIKESKLSLMTYGKLNNVAEAVYMQHLMGIEGVIVDHVEEITEAVREMMKPSNRDADGTKPKPNFSDRELSFLLKLIPELIQH
Protein: Tubulin-folding cofactor B (Cytoskeleton-associated protein 1) (Cytoskeleton-associated protein CKAPI) (Tubulin-specific chaperone B) (Q99426)
Organism: Homo sapiens (Human)
Function: Binds to alpha-tubulin folding intermediates after their interaction with cytosolic chaperonin in the pathway leading from newly synthesized tubulin to properly folded heterodimer. Involved in regulation of tubulin heterodimer dissociation. May function as a negative regulator of axonal growth (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15831477, ECO:0000269|PubMed:22777741}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15831477}. Note=Colocalizes with microtubules. In differentiated neurons, located in the cytoplasm. In differentiating neurons, accumulates at the growth cone. {ECO:0000269|PubMed:15831477}.
Interaction partners:
- Tubulin-specific chaperone D
- Tubulin-specific chaperone E
- Gigaxonin
- Tubulin alpha-1A chain
- Tubulin alpha-4A chain
- Tubulin-specific chaperone E
- Tubulin alpha-1B chain
- Tubulin beta-6 chain
- Tubulin beta-4B chain
- Tubulin-specific chaperone C
Sequence:
MEVTGVSAPTVTVFISSSLNTFRSEKRYSRSLTIAEFKCKLELLVGSPASCMELELYGVDDKFYSKLDQEDALLGSYPVDDGCRIHVIDHSGARLGEYEDVSRVEKYTISQEAYDQRQDTVRSFLKRSKLGRYNEEERAQQEAEAAQRLAEEKAQASSIPVGSRCEVRAAGQSPRRGTVMYVGLTDFKPGYWIGVRYDEPLGKNDGSVNGKRYFECQAKYGAFVKPAVVTVGDFPEEDYGLDEI
Protein: Repressor protein cI (P03034)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Acts as a transcriptional repressor that allows virus to establish and maintain latency. Prevents both the viral DNA replication and the exit programs. Clamps the two operator OL (operator left made of OL1, OL2 and OL3 sites) and OR (operator right made of OR1, OR2 and OR3 sites) together by binding to them and arranging the intervening DNA in a loop. This step allows repression of lytic pR and pL promoters by binding to OL1, OL2, OR1 and OR2 simultaneously. The binding of cI on OR2 additionally activates the transcription of the cI gene thereby mediating an autoregulatory function to maintain the latent state. Once cI is present in sufficient amount, it can repress its own transcription by binding to OL3 and OR3.
Interaction partners:
Sequence:
MSTKKKPLTQEQLEDARRLKAIYEKKKNELGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLAKILKVSVEEFSPSIAREIYEMYEAVSMQPSLRSEYEYPVFSHVQAGMFSPELRTFTKGDAERWVSTTKKASDSAFWLEVEGNSMTAPTGSKPSFPDGMLILVDPEQAVEPGDFCIARLGGDEFTFKKLIRDSGQVFLQPLNPQYPMIPCNESCSVVGKVIASQWPEETFG
Protein: Delta-like protein C (DeltaC) (delC) (Q9IAT6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a ligand for Notch receptors and is involved in somitogenesis. Can activate Notch receptors. Required in somite segmentation to keep the oscillations of neighboring presomitic mesoderm cells synchronized.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Hairy and enhancer of split-related-7.
- Hairy-related 1.
- Neurogenic locus notch homolog protein 1
- Notch receptor 1b.
- E3 ubiquitin-protein ligase mib1
- Notch receptor 3.
- Neurogenic locus notch homolog protein 2 precursor
Sequence:
MARVLLTCFFILISSHLGKSSGVFELKVLSFTSTSSVCKGSSDCQIFFRVCLKHSQALILPEPPCTYGTGMSEILSADSISSSAYISVPFNFKWPGIVSLIIETWNAETSDQSTENNNNMISRLATKRRLAISEDWSQDVHLGRQSQLRFSYRVVCDEFYHGEECSDFCRPRNDTFGHFNCDAAGNRICLPGWKGDYCTEPICLSGCSEENGYCEAPGECKCRIGWEGPLCDECTRHPGCLHGTCNQPFQCTCKEGWGGLFCNEDLNFCTNHKPCRNDATCTNTGQGSYTCICKPGFSGKNCEIETNECDSNPCKNGGSCNDQENDYTCTCPQGFYGKNCEVSAMTCADGPCFNGGTCMEKGSGSYSCRCPPGYMGSNCEKKIDRCSSDPCANGGQCLDLGNKATCRCRPGFTGSRCETNIDDCSSNPCQNAGTCVDGINGYTCTCTLGFSGKDCRVRSDACSFMPCQNGGTCYTHFSGPVCQCPAGFMGTQCEYKQKPTPVNSPALPAALIVSFTLGLITLTLVICAAIVVLRQMRQNHKASSTTVRNNLDSVNNRISLSPTSPLGREKEAFLIPGGPFKVSNKDMALRSTSVDTHSSDKSNYKQKMVDYNLSIDEKHTNNKLEKNSESTLLVPPLNYPKEGVYHPVYIIPEHIEQRVFATEV
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (Q2YGT9)
Organism: Sus scrofa (Pig)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02878}. Cytoplasm {ECO:0000269|PubMed:24930395}. Rough endoplasmic reticulum {ECO:0000269|PubMed:24930395}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (PubMed:24930395). {ECO:0000250|UniProtKB:Q02878, ECO:0000269|PubMed:24930395}.
Interaction partners:
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL30
- Ribosomal protein L24.
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL4
Sequence:
MAGEKAEKPGTKEKKPEAKKADAGGKVKKAKKVKKGKPHCSRNPVLVRGIGRYSRSAMYSRKALYKRKYSAAKSKVEKKKKVRVLATVTKPVGGDKNGGTRVVKLRKMPRYYPTEDVPRKLLSHGKKPFSKHVRKLRASITPGTILIILTGRHRGKRVIFLKQLSSGLLLVTGPLSLNRVPLRRTHQKFVIATSTKIDISGVKIPEHLTDAYFKKKKLRKPRHQEGEIFDTEKEKYEISEQRKVDQKAVDSQILRRIKAVPQLQGYLRSVFALTNGIYPHKLVF
Protein: Testicular acid phosphatase (EC 3.1.3.2) (Acid phosphatase 4) (Q9BZG2)
Organism: Homo sapiens (Human)
Function: May dephosphorylate receptor tyrosine-protein kinase ERBB4 and inhibits its ligand-induced proteolytic cleavage. May play a role in odontogenesis.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Enamelin
Sequence:
MAGLGFWGHPAGPLLLLLLLVLPPRALPEGPLVFVALVFRHGDRAPLASYPMDPHKEVASTLWPRGLGQLTTEGVRQQLELGRFLRSRYEAFLSPEYRREEVYIRSTDFDRTLESAQANLAGLFPEAAPGSPEARWRPIPVHTVPVAEDKLLRFPMRSCPRYHELLREATEAAEYQEALEGWTGFLSRLENFTGLSLVGEPLRRAWKVLDTLMCQQAHGLPLPAWASPDVLRTLAQISALDIGAHVGPPRAAEKAQLTGGILLNAILANFSRVQRLGLPLKMVMYSAHDSTLLALQGALGLYDGHTPPYAACLGFEFRKHLGNPAKDGGNVTVSLFYRNDSAHLPLPLSLPGCPAPCPLGRFYQLTAPARPPAHGVSCHGPYEAAIPPAPVVPLLAGAVAVLVALSLGLGLLAWRPGCLRALGGPV