wanglab/gogpt-training-data huggingface dataset:
Protein: Iron transport multicopper oxidase FET3 (EC 1.-.-.-) (Q96WT3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Iron transport multicopper ferroxidase required for Fe(2+) high affinity uptake. Required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- P-type Cu
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
Sequence:
MMVPLLLSTYFITAVYGATHTFHWTTGWGNRNVDGIKERPVITCNGEYPWPDVRVAKGDRIEVYLTNGFNNTNTSLHFHGMFQRGTNQMDGVPYLTQCPIGPGDTMLYNFTVDENVGTYWYHSHTDGQYEDGMRGLFVIEDGENNKNFPYEYDEDVMLSIGEWYDTTVDVLTRKFLNLNNPTGAEPIPQNLILNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMEVVEVDGVYVEKNTTNMLYITVAQRYAVLVHTKNDTSKNFAIMQKFDDTMLDVIPKDLQLNATSYLVYDKSKPMPEQNYVDSIDDYLDDFYLVPMDKEELYPEADHVITIDVIMDNLINGVNYAFFNNITYTTPKVPTLLTVLSAGQDALNPFIYGTNTNTFVLKKGEVVDLIVNNQDTGKHPFHLHGHVFQTILRDREFDDAKGEKPHSFNDSDHAAYPSIPMKRDTVYLNPQSNMVLRFKADNPGVWFFHCHIEWHLLQGLAVVMVEDPISIQNTASQHLTANGLQVCGNVKVPTQGNAAANDSDFFNLEGQNVQHKSIPTGFTKKGIIAMTFSCLAGVLGITMIAIYGFSEIPEPEIKVMRNLHLNPEDVLEKTSSSSVISASNSSSLEDSRNQKKKFIFF
Protein: Receptor-type guanylate cyclase gcy-27 (EC 4.6.1.2) (Q9XU42)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). May be involved in sensitivity to quinine by regulating egl-4 activity through the production of cGMP. Promotes the calcium flux to the cytoplasm in ASJ sensory neurons upon removal of a nitric oxide (NO) stimulus and is thereby involved in the behavioral avoidance response to NO-producing organisms like P.aeruginosa.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-4 subunit
Sequence:
MIDGEAYFEKNSTGKLGSWGWRDVNLQFIICTLPVPIYFVVVAIWTINGASNSYRFPFLQTYMILTDRFWLFFRCFTIVAWCGWCSNYIFFPCLMNAILYIISLSLSRDTTFILFIFYQMNKLITVIRDFSYSVYNWCYETVIGENTRKYKMTWKVPKESLKIIVNKNADARMQRELENRTAKDEANALTSRRRVFGSYALIGTQRAEFIQFRQIKHIDITNASLDFLYNLKQLKHDNLANFYGIQLNDDLNTMTILHALVERGTLEEFCLDRDFGMDETFKSAFMRDILKGLQYLHLSPVAYHGHLHAATCLIDINWVLKIALYGVTNFVCDNFDAENITMPDRSDYTISYAQYVCFPPEHIREYDATGKLPTRFVRGSKQGDIYCVGMIFYMMIEREDPYRLIHSVERPGSGLMMEILDHNLMPFISNNETQEDTLLDKCKECWNRDPEKRPTIENLRNAIAICYADSKGNLIDQMIRMNEKYADELETLVAARSADLALAQMQTMRLLNEMLPASIAKDLKNGVIAPARSYASATVMFVQICDFIVILKRRPPKEVIGFLNDIFDQFDTVIKRHDAYKVETTGETYMVASGVPNENEGRHVFEVAEMSLEIRAISLSYTLENDKNYKLRVRIGFHAGPIAAGVIGIKNPRYCLFGDTVNFASRMQSNCPPLQIQTSEITARMLLATHEYKLVKRGIVHVKGKGEVNCYWLNEHIHKDEEIEESGTISHPLES
Protein: HTH-type transcriptional regulator MurR (MurPQ operon repressor) (P77245)
Organism: Escherichia coli (strain K12)
Function: Represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). Binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate, the substrate of MurQ, is the specific inducer that weakens binding of MurR to the operator. Also represses its own transcription.
Interaction partners:
- N-acetylmuramic acid 6-phosphate etherase
- PTS system N-acetylmuramic acid-specific EIIBC component
- Putative D-alanyl-D-alanine carboxypeptidase
- Uncharacterized protein YbbC
Sequence:
MLYLTKISNAGSEFTENEQKIADFLQANVSELQSVSSRQMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASREKTNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALLDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKIGYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLTDSPLRRLAHFTLDTVSGETEWRSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRLK
Protein: Man1/Src1-like C-terminal domain-containing protein (Q54C61)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
- Charged multivesicular body protein 4
- IST1-like protein
Sequence:
MSEDGIPRVSVSNLKKKFQASNNNNNNGESTQRISGVVAKSKDPSSFSLSSSLKKRPTENTASFLSSSLSSSSSILSADDLIKKNRRKSFGESKEKEEKEKEKEKEKEKEKEKEKEKSSSSTTTTTTTTTSKLKPKSTLTSSSSSSSHIATYSEPLKDHSSEPKEKEKEKEKEKEKENKDKSNSTLTPTNVVKKLKRKSIESGNIFQFDQAKESLSTSSSSSSGTTATSTTTTTTSSSSSISKDKEPKESNKKKLKVSVQSSQTEENENENENQLEEQPEEKSSKKKVSKTSSLESTGEKKKKRSSTSGTSKKSSTFDSIKSILDDDDENDFDYEKDDNGNGEKVKEKEKKKKKKKSSSKKVSTFEEGEGMVVEQQQQQQQQQQQQPIFDGSSSVIGTTSNVINKQSKAYPKTPLPNKSKRSTTTQYDNDFEDETINNFMSSVNSSKMYFTPKATFGQPPTPSSSGTNYQNRTNVSIHNYPNSPISFESEQQQHHHQQQHGFEYSDSPVSIPNISYITPSERDISFDTDHQAADFLEDEFVDQEEDFFDDDDEELQYVQQQTQQRRKELKQQQHKQLKEQQKRHKQQIISQSKAGAVISSDNGESKAKFVLLIITFAIWIGLLIVLAQFFYHYNDIKYCDTGAVPKKINDTTFSCVPCPDKGVCMNGIFENCMDGYVIRNGECILNPSKVESLVQIINQISQILRDRKGLFECGSKDTFLMTNEELKKEIAKRNWFSKDQAIESFDTIIQFIDNRKDSEEIGLDHKLLSSIGYTFEDNQFKYYSNDSGIRPLWCQTIFFFKNLIKNNLHFIGIFVIGFLGFKLVQIRKKNKQEELLAIEHNCKKSLKILQQRTQFEDPWISELILKDEVMGSNNDKKSNLIWEKTLEKISSNVRVLCTVKLIHGESQKTLEWTDSNQTPRRASISSPINYDDDELNNNSFEN
Protein: Aminodeoxychorismate synthase component 1 (ADC synthase) (ADCS) (EC 2.6.1.85) (4-amino-4-deoxychorismate synthase component 1) (P05041)
Organism: Escherichia coli (strain K12)
Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia.
Interaction partners:
- Bifunctional protein TrpGD
- Aminodeoxychorismate synthase component 2
- Aminodeoxychorismate lyase
- Tryptophan synthase beta chain
- Tryptophan synthase alpha chain
- Tryptophan biosynthesis protein TrpCF
- Chorismate synthase
- Bifunctional chorismate mutase/prephenate dehydratase
- Sodium/proline symporter
- T-protein
Sequence:
MKTLSPAVITLLWRQDAAEFYFSRLSHLPWAMLLHSGYADHPYSRFDIVVAEPICTLTTFGKETVVSESEKRTTTTDDPLQVLQQVLDRADIRPTHNEDLPFQGGALGLFGYDLGRRFESLPEIAEQDIVLPDMAVGIYDWALIVDHQRHTVSLLSHNDVNARRAWLESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLNQANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAVKLANSAKDRAENLMIVDLMRNDIGRVAVAGSVKVPELFVVEPFPAVHHLVSTITAQLPEQLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSIGYLSFCGNMDTSITIRTLTAINGQIFCSAGGGIVADSQEEAEYQETFDKVNRILKQLEK
Protein: Prestalk protein (Extracellular matrix protein ST310) (P11976)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the stalk tube, the matrix that encases stalk cells.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Prespore-specific protein A
- Spore coat protein SP70
- Spore coat protein SP60
- Basic-leucine zipper transcription factor B
- Myb domain-containing protein
- Transmembrane protein
- Prespore protein Dp87
- Extracellular matrix protein
- Signal transducer and activator of transcription A
- Extracellular matrix protein
Sequence:
MNKIYLILILFTFVGIILANVEKAEVSCTCDENCNDGNKCTLDKCNNGCCSNTPININDNDECTVDTCNPKTGISHTPVNCDDGNSCTADSCLCGKGCQHVPIACDDNNACTVDSCSNSTGCCHTPLSCDDNNPCTVDSCSNSTGCCHTPINVDDHNACTEDKCTQSGGVTHTPIACDDKNACTVDSCSNSTGCCHTPLSCDDNNACTVDSCSNSTGCVHTPINVDDHNACTEDKCTQSGGVTHTPIACDDKNACTADSCSNSTGCCHTPITCDDNNACTVDSCSNSTGCCHTPINVDDNNACTEDKCTQSGGVTHTPIACDDKNACTVDSCSNSTGCVHTPLACDDKNPCTVDSCSNSTGCCHTPINVDDNNACTEDKCTQSGGVTHTPINCDDNNKCTVDSCSNSTGCCHTPMSCDDNNPCTVDSCSNSTGCVHTPINVDDNNACTEDKCTQNGGVTHTPIACDDKNACTVDSCSNSTGCCHTPLKCDDNNACTVDSCSNSTGCVHTPINVDDNNACTEDKCTQSGGVTHTPISCDDKNPCTIDSCSNSTGCVHTPMSCDDRNPCTSDFCSWEKGCQHVALSCNDFNACTMDSCSNSTGCTHTPIACDDKNACTVDSCSNSTGCVHTPLTCDDNNPCTVDSCSNSTGCCHTPINVDDHNACTEDKCTQSGGVTHTPIACDDKNACTVDSCSNSTGCCHTPLSCDDNNACTVDSCSNSTGCVHTPINVDDNNACTEDKCTQNGGVTHTPIACDDKNACTVDSCSNSTGCCHTPLKCDDNNPCTVDSCSNSTGCVHTPMNVDDNNACTEDKCTQNGGVTHTPIRCDDLNSCTADSCSNSTGCVHTPINCDDNNKCTADSCSNSTGCCHTPISCDDNNPCTVDSCSNSTGCCHTPINVDDNNPCTEDKCTQSGGVTHTPIGCNDNNACTVDSCSNSTGCTHTPMKCDDNNPCTIDSCSNSTGCVHTPMNCDDGNFCTLDSCCSTGCTHTPIIIDDNNPCTVDSCCNSTGVVHTPVDCNDNNVLTCDYCSIKQGGKCIHVPMTQCKTFGKCGDDL
Protein: Cilia- and flagella-associated protein 45 (A0A2I6SFG9)
Organism: Schmidtea mediterranea (Freshwater planarian flatworm)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
Sequence:
VSRISRVEENLFGEPNYLKLRKTASNVELNVHESEPTVNYCSDRKVCSNNNEYKEKEETIRIITKDMVRNLRVPREDPSFKSMVLDSDSFLKLRNRARIVSHDEKLKREEAIKTQKDEEMMASHGRRQEMKRHDILRQKNDKMTDLEEEAYQKAQTLLKKAMEQRQEQEDEIKKLNELISNAKIQAIRDAQILEKEIIKKENLEEDHRLDQMMEIERINAIRMQEGIELRRKEDELLAASSIIQQIEQNEQERLIELERKDQENKLERERVAVLMEEELVKRSKIRQNQEKLRNDLNKSNEEMLERKIREKELEQLLDLRVLEIQREKALREAEFEAEAMRVKAEKEREVARLRALQERAKDEQAERDELRARRAMEEAEREWRRKEIEHEIKKKQVEEDLLQARAEQAEMKEHFLAIQAARDRAEFERTIRAQRELIERDKQMEEIEKSKRSEYSKEIRNQIRKNEETKIAERNAFFKEGEKIEEEKRLRRMRMEEAKNRKLEELRNAGISEKFLKQI
Protein: CMRF35-like molecule 7 (CLM-7) (CD300 antigen-like family member B) (Immune receptor expressed on myeloid cells 3) (IREM-3) (Leukocyte mono-Ig-like receptor 5) (CD antigen CD300b) (Q3U497)
Organism: Mus musculus (Mouse)
Function: Acts as an activating immune receptor in mast cells through its interaction with ITAM-bearing adapter TYROBP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17928527}; Single-pass type I membrane protein {ECO:0000269|PubMed:17928527}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Hematopoietic cell signal transducer
Sequence:
MWLSPALLLLSFPGCLSIQGPALVRGPEQGSVTVQCRYSSRWQTNKKWWCRGASWSTCRVLIRSTGSEKETKSGRLSIRDNQKNHSFQVTMEMLRQNDTDTYWCGIEKFGTDRGTRVKVNVYSVGKDTMSTSNQLPWPTVDGSTDMVSSDLQKRTYYMLLVFVKVPALLILVGAVLWLKRSTQKVPEEQWRHTLCSDLDSELLAKDISP
Protein: CRAL-TRIO domain-containing protein (Guanine nucleotide exchange factor UNC-73A) (O61528)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-related protein ced-10
- Rac-like GTPase
- Netrin receptor unc-40
- Guanine nucleotide-binding protein subunit alpha
- Ras-related protein rac-2
- DH domain-containing protein
- CED-5
- Ras-like GTP-binding protein rhoA
- Protein sax-3
- Kinesin-like protein vab-8
Sequence:
MGDYDGKMTMKAEDILHVLRDGIAVLPGGRCRAGQAVIVCPSREQPVNQDNLRNVFLYLFEVTSKMAREKGFLVVIDMRGKQTWTNVRHILKALSSIESSSTVQVFIIKPEKFWEKQKAQMSLGTWDFEVEMISFESLIKIIDSSHLPKTVGGSYPYDHDEWLELRLDLEKWIWNITEIMEKLESVRREICEGEQPVDVTTANAALKKSQHAKNSIFNVPVEGIETEGNKIATRILKPSKGVKNPDLEATTPYISNLTDSLRLLKGEVAKNWEVRQMELSKVYQQKQFERDAEHMIETLRPYKKACERSMGDVGGCANDVVRLSAEFEQFQIAVRGMEVSVKQVFDKENHLRTIGARNQITDHVAARLAEEWHLVKELMERRSAVLHNAKEFFTSAQRYFAEVPRWTAQPGVNPNDVLFNQESLEEAIRKHDAFWAQVEEVYAQAYDDASKVTRALKEADAEDNVAREHSSRLQRAHKQLMEKWKERQVLLHHMLAMIAFETDVRLVVDWLEQHGEPYLRRNIHIGENVNQARSFQRNHTNFQRVAANTYGNVQKLHQVYQDVTKSGSKICDVDTMHGLMTDLSAKIEKFTKIENSRELLLRQSVLFHTHYKELTDWYGKMGEKYKDRRIDLTVPTCDKNKERFVLETDETAQAYAMTIDEGKTLIEMMQRATRVFDVDYSASVAHIQLLISDIEDKNTQISSEWSPRRTLLHIASKFAMFEQNQFEVLEQIKSWEVDMREMAESDSFYDKADSVLPFHKDNQQQVRNAIADIQKSAKELSQALYSQKLTDLRDKRDRVVLEAIREHVRELEIAESRVMTYANETSMRMQAASEVGDLRRISNSVCKLIDNQLSALTQLGVIPNDYNDTVQKQEELRAFRDAVQHKLKEPYDAFVIRFRELMENRLANRDEVVYHNEAIQAKYCRLMNLCEDRNKLLKSAHGCYKTYETAVLPILNQLESEYHSPTVTDWCAGCTSSIDADRAAYVADLLSKHMDYKERFGKGCTYALRNGDFLLRYIRRSTVNQSERKRHETKIADMKNNIRERQSNILELWMQKKLLLEGCQSFIFIEASAKELLEFMKGEGNRKLKHFEKKGRRESTDDDDEFAKFKSEVKQKKTDIQTFLMLSTNETMSRGVHGDEIDRCIEQVKDEFSRFSRRVGDCEVVLRGENGSTQSSKDEFSLDRHSDTAIFNEKKINERREENRKMLEPMRELIQSERDYIKDLERCVNIYVKEFDQAAKNGTIPTLNPLKYEIFGNIEKIFKFHNDKLLHELIKYENQPEAVGASFIVWIDLLNELYTEYCVNKEQKNHVIATPDAVSFFTGIRERHGLEINNEIASLLIKPVQRITRYRLLIEQLMRSCTDKTNDLKEAYEVVCSVPRKVNDLIHYNCLDLKDFKVDELGPFVTQDTLTFWEPRAYFKGRGKERQVFLFDISIVFAKRIEVSPKNIKYVIKGKPLPLSEVSIVEHVEGDTCRFGLRVGTVSSNDNRIDLKANNHHTKVKWVQKIRDLTAGMLPLGLGVSEAYSVGTLSTARSVSVRSGASTSSGGENRQSQDVESLLRHRYSVHSCDSEQSSEVWIVTADFDGQVEGHLTVHKGDRVEIVEDQATDCAEYVQVVLCDQPTKHGLVPASIIAPPESGSVPDRPDDSNASGSTVSKRKSLRRIFANSSKERAAAANSSSSNNNSPATRQSTSTSSPVTANGHTTESSTSAPIGVLSSGEPTSSNSIPSSSTPTHTVPSSVPATVIPIVVAEDEKAEDCLPPPMENITINNSIDEKDMNEDSVAASDAVEPEVALPAKVEKTPEETARFKRSYVLMELVETEQDYVKDLTSVVEGYIGNLNKMDLPADLVGKDKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVKYERRLHTLYVTYCQNKPKSDYLLAQDDFEAFFADTKAKLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAKDKTDTLKKALQVMHVVPKACDDMMQVGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEPNVPDDPLRFVIKSSDPTQPTSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRYNDMSSGMGDLSLGAPGGDRRGAPSSANRSAASSSKKPAESPKKEGKSKSSLFSFGKKPAKSPTSPPPLDAAAAGKFQKVADDQVNLETDEKVKVLDVKNGYASVKKADGTVGKCPSYFLTMSDIPGTNFAEQIQYRREWQRRVDETDVEYGPSAFDTATSSTDNFDVLLELTTCERPVVVEDMKDIEVVEGNDVEMCPIISSHTDFTVIWHGPAVDSKRARIQTNQLNSRLLIKHVKKCDAGAYSVIAKNSFGVTSTVAFLSVISIPDPPTDFTVKISGDHEVRLKWKAESGLKYCIEYRILDDSSPENWLIASTNIEKTHVSLRNFARNSYSFRVFAYNQRVRSAPSQCICICFDGTEM
Protein: UvrABC system protein B (Protein UvrB) (Excinuclease ABC subunit B) (P0A8F8)
Organism: Escherichia coli (strain K12)
Function: The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
Subcellular location: Cytoplasm.
Interaction partners:
- UvrABC system protein A
- UvrABC system protein C
- DNA helicase II
- Holliday junction branch migration complex subunit RuvB
- Excinuclease cho
- Holliday junction branch migration complex subunit RuvA
- Protein RecA
- Crossover junction endodeoxyribonuclease RuvC
- DNA mismatch repair protein MutL
- LexA repressor
Sequence:
MSKPFKLNSAFKPSGDQPEAIRRLEEGLEDGLAHQTLLGVTGSGKTFTIANVIADLQRPTMVLAPNKTLAAQLYGEMKEFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASVNEHIEQMRLSATKAMLERRDVVVVASVSAIYGLGDPDLYLKMMLHLTVGMIIDQRAILRRLAELQYARNDQAFQRGTFRVRGEVIDIFPAESDDIALRVELFDEEVERLSLFDPLTGQIVSTIPRFTIYPKTHYVTPRERIVQAMEEIKEELAARRKVLLENNKLLEEQRLTQRTQFDLEMMNELGYCSGIENYSRFLSGRGPGEPPPTLFDYLPADGLLVVDESHVTIPQIGGMYRGDRARKETLVEYGFRLPSALDNRPLKFEEFEALAPQTIYVSATPGNYELEKSGGDVVDQVVRPTGLLDPIIEVRPVATQVDDLLSEIRQRAAINERVLVTTLTKRMAEDLTEYLEEHGERVRYLHSDIDTVERMEIIRDLRLGEFDVLVGINLLREGLDMPEVSLVAILDADKEGFLRSERSLIQTIGRAARNVNGKAILYGDKITPSMAKAIGETERRREKQQKYNEEHGITPQGLNKKVVDILALGQNIAKTKAKGRGKSRPIVEPDNVPMDMSPKALQQKIHELEGLMMQHAQNLEFEEAAQIRDQLHQLRELFIAAS
Protein: Uncharacterized protein YNR014W (P53719)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MSSTDIKPCAVNIPVSAHITFHYKSIADRSSSRSSSSSSCSSATSKACSPRGSSVGLPPALSTDNEIVETVLNVSAPVVADPTRPSLFKSNYTAASCLTSDPTSPSLLPSSRRNSVLPASDFHQCAHHKNFQRRASEPQLPSFDNRSSSEMKRSVSYAQHSMMFPISDQQEPQTSASPNDHSDPSCPCNRHHHRRNSVAVKFDKPLYERLET
Protein: Keratin-associated protein 10-1 (High sulfur keratin-associated protein 10.1) (Keratin-associated protein 10.1) (Keratin-associated protein 18-1) (Keratin-associated protein 18.1) (P60331)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 10-5
- Keratin-associated protein 10-3
- Keratin-associated protein 10-7
- Keratin-associated protein 10-9
- Keratin-associated protein 10-10
Sequence:
MAASTMSVCSSACSDSWQVDACPESCCEPHCCALSCCAPAPCLTLVCTPVSRVSSPCCQAACEPSPCQSGCTSSCTPSCCQQSSCQPACCTSSPCQQACCVPVCCKPVCCLPTCSKDSSSCCQQSSCQPTCCASSSSQQSCCVPVCCKPVCYVPTCSEDSSSCCQQSSCHPACCTSSPCQQACCVPVRCKPVCCKPICCVPVCSGASTSCCQQSSCQPACCTTSCCRPSSSVSLLCRPVCRPACCMPVSSCCAPASSCQASCCRPASCVSLLCRPACSRPAC
Protein: Glutathione S-transferase U20 (AtGSTU20) (EC 2.5.1.18) (FIN219-interacting protein 1) (GST class-tau member 20) (Q8L7C9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits glutathione-dependent thiol transferase activities. Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as substrates. Involved in the regulation of far-red light influence on development. Regulator of the interplay between light and JA signaling by increasing JAR1/FIN219 efficiency. Maybe involved in gravitropic signal transduction (Probable).
Subcellular location: Nucleus {ECO:0000269|PubMed:17220357}. Cytoplasm, cytosol {ECO:0000269|PubMed:17220357}.
Interaction partners:
- Jasmonoyl--L-amino acid synthetase JAR1
- Glutathione S-transferase F11
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase F10
- Glutathione S-transferase F9
- Glutathione S-transferase Z1
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase DHAR2
- Cytochrome P450 83A1
- carnosine N-methyltransferase
Sequence:
MANLPILLDYWPSMFGMRARVALREKGVEFEYREEDFSNKSPLLLQSNPIHKKIPVLVHNGKPVCESLNVVQYVDEAWPEKNPFFPSDPYGRAQARFWADFVDKKFTDAQFKVWGKKGEEQEAGKKEFIEAVKILESELGDKPYFGGDSFGYVDISLITFSSWFQAYEKFGNFSIESESPKLIAWAKRCMEKESVSKSLPDSEKIVAYAAEYRKNNL
Protein: 26S proteasome regulatory subunit 8 homolog A (26S proteasome AAA-ATPase subunit RPT6a) (26S proteasome subunit 8 homolog A) (Regulatory particle triple-A ATPase subunit 6a) (Q9C5U3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 12 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 1 homolog B
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
Sequence:
MAAVGVDSRRPETAMEETCNVKGAAAKQGEGLKQYYLQHIHELQRQLRQKTNNLNRLEAQRNELNSRVRMLREELQLLQEPGSYVGEVVKVMGKNKVLVKVHPEGKYVVDIDKSIDITKITPSTRVALRNDSYVLHLVLPSKVDPLVNLMKVEKVPDSTYDMIGGLDQQIKEIKEVIELPIKHPELFESLGIAQPKGVLLYGPPGTGKTLLARAVAHHTDCTFIRVSGSELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSARMESGSGNGDSEVQRTMLELLNQLDGFEASNKIKVLMATNRIDILDQALLRPGRIDRKIEFPNPNEESRFDILKIHSRKMNLMRGIDLKKIAEKMNGASGAELKAVCTEAGMFALRERRVHVTQEDFEMAVAKVMKKDTEKNMSLRKLWK
Protein: Large ribosomal subunit protein eL8 (60S ribosomal protein L7a) (PLA-X polypeptide) (Surfeit locus protein 3) (P62424)
Organism: Homo sapiens (Human)
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 {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Elongation factor 2
Sequence:
MPKGKKAKGKKVAPAPAVVKKQEAKKVVNPLFEKRPKNFGIGQDIQPKRDLTRFVKWPRYIRLQRQRAILYKRLKVPPAINQFTQALDRQTATQLLKLAHKYRPETKQEKKQRLLARAEKKAAGKGDVPTKRPPVLRAGVNTVTTLVENKKAQLVVIAHDVDPIELVVFLPALCRKMGVPYCIIKGKARLGRLVHRKTCTTVAFTQVNSEDKGALAKLVEAIRTNYNDRYDEIRRHWGGNVLGPKSVARIAKLEKAKAKELATKLG
Protein: Neurogenin-3 (NGN-3) (Helix-loop-helix protein mATH-4B) (mATH4B) (Protein atonal homolog 5) (P70661)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator. Together with NKX2-2, initiates transcriptional activation of NEUROD1. Involved in neurogenesis. Also required for the specification of a common precursor of the 4 pancreatic endocrine cell types.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor HES-1
- Homeobox protein Nkx-6.1
- Paired box protein Pax-4
- Homeobox protein Nkx-2.2
- Insulinoma-associated protein 1
- Pro-glucagon
- Pancreas/duodenum homeobox protein 1
- Somatostatin
- DNA-binding protein RFX6
- POU domain, class 5, transcription factor 1
Sequence:
MAPHPLDALTIQVSPETQQPFPGASDHEVLSSNSTPPSPTLIPRDCSEAEVGDCRGTSRKLRARRGGRNRPKSELALSKQRRSRRKKANDRERNRMHNLNSALDALRGVLPTFPDDAKLTKIETLRFAHNYIWALTQTLRIADHSFYGPEPPVPCGELGSPGGGSNGDWGSIYSPVSQAGNLSPTASLEEFPGLQVPSSPSYLLPGALVFSDFL
Protein: Kinesin-like protein (Q583A3)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTTLSLDSTAVRVVARCRPLLPSERNHTTSRIQINAEAGTITLAEKGLGVGRCFTFDRVFLPNAQQHDVAEEVSPLISHVLEGFCATIFAYGQTGSGKTHTVEGFEYIRNGRGGPKVNIDTDPEKHGIIPRVIQLIFDRVREKQFADANTSYHLKCSYYQIYNERVTDLLNPSSEASKGTGLKVRWCRDDTFTVENLYICECDQPGEMRRMFLSGAKAKEMGSHMMNQQSSRSHCVFTIHVERSDSDIPGNSVKSQLTIVDLAGSEKLTALDANPSSKLTKESIDINTSLFALGKVITSLAQRSKHNQKNGAGANQLHIPYRDSKLTKLLKHALGGNSLTTMLACISPSDNYAEETMSTLMFATTARTIKNVPYVAEDPVTQVVNQLRSELGNVKEELNYYQNLVGSNLINSGPTRPQPMYHVQASNDEAVNAQVNELSDKLLQACDALQKIMSINTQLRSAFDVVKEAKAELERREMELNAENLALRERIEMLESVVLKEDLTECFGNGAKSQEGYLKNNGYYYSSARASLLTNASDPKSCHAPTRPHSASVHESPAPTTAGQTNPRAYAADGAWAAERPPIAEDNPRPMTGPSVRPSAEGFVPSAQLAEERLRGEQSINKRREKLTKGLAEYANRYCQPDRFVNYAEYYGKARRLVTTNRSVSSTVDDMSKTLRQIPESIASTVPNSLKTTSQFGMLHFGGSREELGELEERRRQREEKRQALIAQQDALRGDVARAFVGITEKKEPIRAGKEPYEQGSLASTDTTGKQMPKLPSAQPAPADSVSRLKAYLEQEIGMRGEL