wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein subunit alpha (Q00743)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- G-protein beta subunit
- Developmental regulator flbA
- Adenylate cyclase
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein alpha-3 subunit
- cAMP-dependent protein kinase
- DUF7582 domain-containing protein
- Protein fluG
- Regulator of G protein signaling domain protein
Sequence:
MGCGMSTEDKEGKARNEEIENQLKRDKMMQRNEIKMLLLGAGESGKSTILKQMKLIHEGGYSRDERESFKEIIYSNTVQSMRVILEAMESLELPLEDARNEYHVQTVFMQPAQIEGDSLPSEVGNAIAALWQDAGVQECFKRSREYQLNDSAKYYFDSIERIAQSDYLPTDQDVLRSRVKTTGITETTFIIGDLTYRMFDVGGQRSERKKWIHCFENVTTILFLVAISEYDQLLFEDETVNRMQEALTLFDSICNSRWFVKTSIILFLNKIDRFKEKLPVSPMKNYFPDYEGGADYAAACDYILNRFVSLNQAEQKQIYTHFTCATDTTQIRFVMAAVNDIIIQENLRLCGLI
Protein: AT-hook motif nuclear-localized protein 29 (Protein SUPPRESSOR OF PHYB-4#3) (Q9C9K7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL18, AHL22 and AHL27 in the regulation of flowering and regulation of the hypocotyl elongation. Acts redundantly with AHL27/ESC to modulate hypocotyl growth inhibition in response to light.
Subcellular location: Nucleus {ECO:0000269|PubMed:18088311, ECO:0000269|PubMed:24218605}.
Interaction partners:
- Vascular-related unknown protein 1
- Auxin-responsive protein SAUR19
- Phytochrome B
- Probable indole-3-pyruvate monooxygenase YUCCA9
Sequence:
MDGGYDQSGGASRYFHNLFRPELHHQLQPQPQLHPLPQPQPQPQPQQQNSDDESDSNKDPGSDPVTSGSTGKRPRGRPPGSKNKPKPPVIVTRDSPNVLRSHVLEVSSGADIVESVTTYARRRGRGVSILSGNGTVANVSLRQPATTAAHGANGGTGGVVALHGRFEILSLTGTVLPPPAPPGSGGLSIFLSGVQGQVIGGNVVAPLVASGPVILMAASFSNATFERLPLEDEGGEGGEGGEVGEGGGGEGGPPPATSSSPPSGAGQGQLRGNMSGYDQFAGDPHLLGWGAAAAAAPPRPAF
Protein: Hypoxia-inducible factor 3-alpha (HIF-3-alpha) (HIF3-alpha) (HIF3-alpha-1) (Q9JHS2)
Organism: Rattus norvegicus (Rat)
Function: Acts as a transcriptional regulator in adaptive response to low oxygen tension. Attenuates the ability of transcription factor HIF1A, EPAS1 and the HIF1A-ARNT complex to bind to hypoxia-responsive elements (HRE) located within the enhancer/promoter of hypoxia-inducible target genes and hence inhibits HRE-driven transcriptional activation. Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis. May act as a tumor suppressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11237857}. Cytoplasm {ECO:0000269|PubMed:11237857}. Nucleus speckle {ECO:0000250|UniProtKB:Q0VBL6}. Mitochondrion {ECO:0000250|UniProtKB:Q0VBL6}. Note=In the nuclei of all periportal and perivenous hepatocytes. In the distal perivenous zone, detected in the cytoplasm of the hepatocytes (PubMed:11237857). Localized in the cytoplasm and nuclei under normoxia, but increased in the nucleus under hypoxic conditions. Colocalized with HIF1A in kidney tumors. Colocalizes with BAD in the cytoplasm. Colocalizes with EPAS1 and HIF1A in the nucleus and speckles. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. {ECO:0000250|UniProtKB:Q0VBL6, ECO:0000250|UniProtKB:Q9Y2N7}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Aryl hydrocarbon receptor nuclear translocator 2
- Prolyl hydroxylase EGLN3
- Prolyl hydroxylase EGLN2
- von Hippel-Lindau disease tumor suppressor
- Egl nine homolog 1
- Elongin-C
- Cullin 2
Sequence:
MDWDQDRSSTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVRKEGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPRPSLSKKKSEAATGRHFSLRMKSTLTSRGRALNLKAATWKVLHCSGHMRAYKPPAQTSPAGSPRSEPPLQCLVLICEAIPHPASLEPPLGRGAFLSRHSLDMKFTYCDERIAEVAGYSPDDLIGCSAYEYIHALDSDAVSRSIHTLLSKGQAVTGQYRFLARTGGYLWTQTQATVVSGGRGPQSESIICVHFLISRVEENGVVLSLEQTEQHTRRPPQLGTSSKKGIPGNSLDPPAPRILAFLHPPALSEASLAADPRRFCSPDLRRLMAPILDGPPTAATPSTPQAARRPQSPLPADLPDQLAVGLENAHRLSTARKNKTMETDLDIAQDPDTPDLEMLAPYISMDDDFQLNSSEQLPKVHRRPPRTARRPRARSFHGLSPPIPEATLLPRWGSDPRLNCSSPSKGDPPTAPLTPRTRKRALAQSSEDKGLELLETKPPKRSPRLEPGSVLLPPLSLSFLLQGRQLPGNQPDPRAPLVDSHEPLGLAPSLLSLYQHEETIQSRNHFLPAAGLAQTH
Protein: ATP-dependent RNA helicase SUV3, mitochondrial (EC 3.6.4.13) (P32580)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for intron-independent turnover and processing of mitochondrial RNA. It is a key control element in nuclear-mitochondrial interactions.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14576278}.
Interaction partners:
- Exoribonuclease II, mitochondrial
- Exosome complex exonuclease DIS3
- ATP-dependent RNA helicase MSS116, mitochondrial
- Exosome complex exonuclease RRP6
- Exosome complex component RRP46
- Exosome complex component RRP42
- Putative mitochondrial translation system component PET127
- Exosome complex component RRP43
- Exosome complex component CSL4
- Exosome complex component RRP4
Sequence:
MALVKYSTVFFPLRSLRLFVSIKKAYYHSEPHSIDLFHDKDWIVKRPKFLNLPKNEHSKLDIFQFNFNKSESNNVYLQDSSFKDNLDKAMQFIYNDKLSSLDAKQVPIKNLAWLKLRDYIYQQLKDPKLQAKTYVPSVSEIIHPSSPGNLISLLINCNKISNLVWKSVLKYSLSNNITTLDKFIHVLQQTFDHVYEQEILPMMTNTDDTDGAHNVDITNPAEWFPEARKIRRHIIMHIGPTNSGKTYRALQKLKSVDRGYYAGPLRLLAREVYDRFHAEKIRCNLLTGEEVIRDLDDRGNSAGLTSGTVEMVPINQKFDVVVLDEIQMMSDGDRGWAWTNALLGVVSKEVHLCGEKSVLPLVKSIVKMTGDKLTINEYERLGKLSVEEKPIKDGIKGLRKGDCVVAFSKKKILDLKLKIEKDTNLKVAVIYGSLPPETRVQQAALFNNGEYDIMVASDAIGMGLNLSIDRVVFTTNMKYNGEELMEMTSSQIKQIGGRAGRFKSRSASGGVPQGFITSFESKVLKSVRKAIEAPVEYLKTAVTWPTDEICAQLMTQFPPGTPTSVLLQTISDELEKSSDNLFTLSDLKSKLKVIGLFEHMEDIPFFDKLKLSNAPVKDMPMVTKAFTKFCETIAKRHTRGLLSYRLPFNLLDYNCIPNESYSLEVYESLYNIITLYFWLSNRYPNYFIDMESAKDLKYFCEMIIFEKLDRLKKNPYAHKPFGSTRGHLSSSRRRLRT
Protein: V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (P54647)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Interaction partners:
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
Sequence:
MSKNSGLPSFASTEADNSQGFVLSVSGPVVIANQLAGAAMYELVRVGHNQLVGEIIRLEEDTATIQVYEETSGLTVGDPVLRTHKPLTVELGPGIMNNIFDGIQRPLNAIAEITKGIYIPRGINTPSLNRTIKWPYQPDTKLKVGDNVSGGDIFGQVVENNLIIHKIMVPPKEMGTIVEIAPAGEYTLDHALLTIEFDGKRKQLTMVHNWPVRSARPVIEKLPCNYPLLTGQRVLDSLFPCVQGGTCAIPGAFGCGKTVISQSLSKFSNSDAIVYVGCGERGNEMAEVLMEFPELHTKVGDKEEPIMQRTCLVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVSCIGHPTRIGSVTIVGAVSPPGGDFADPVTAATLGIVQVFWGLDKKLAQRKHFPSINWLISFSKYMQALDTHYDQMDPEFVPLRTRAKEILQMEEDLSEIVQLVGQDSLGESEKITIEVARIIRDDFLQQNGFSPYDKCCPFFKTVWMLKNMMTFYNLAQKAVESSTADNKVTWNQIKNELKEIIHRITSMKFQDPTDGEQTLTAHFSTLNEDIITAFRNFSDLV
Protein: Imidazoleglycerol-phosphate dehydratase (IGPD) (EC 4.2.1.19) (Q12578)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Imidazole glycerol phosphate synthase hisHF
- Histidine biosynthesis trifunctional protein
- histidinol-phosphate transaminase
- ATP phosphoribosyltransferase
- 1-
- Candida glabrata strain CBS138 chromosome K complete sequence
- N-
- 3-isopropylmalate dehydrogenase
- Orotidine 5'-phosphate decarboxylase
- phosphoserine phosphatase
Sequence:
MAFVKRVTQETNIQLALDLDGGSVSVRESILGKEYASGDGQTIHVHTGVGFLDHMLTALAKHGGWSLILECIGDLHIDDHHTVEDCGIALGQAFKEALGSVRGIKRFGHGFAPLDEALSRAVVDFSNRPFAVVELGLKRERIGQLSTEMIPHFLESFATEARITMHVDCLRGTNDHHRSESAFKALAIAIREARTPTGRDDVPSTKGVLA
Protein: Uncharacterized protein At3g61260 (Q9M2D8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}.
Interaction partners:
- B3 domain-containing protein REM13
- B3 domain-containing protein REM1
- Remorin family protein
- Syntaxin-31
- Syntaxin-32
- At3g24315
- Centromere/kinetochore protein zw10 homolog
- Membrin-11
- Membrin-12
- VAMP-like protein YKT61
Sequence:
MAEEQKIALESESPAKVTTPAPADTPAPAPAEIPAPAPAPTPADVTKDVAEEKIQNPPPEQIFDDSKALTVVEKPVEEPAPAKPASASLDRDVKLADLSKEKRLSFVRAWEESEKSKAENKAEKKIADVHAWENSKKAAVEAQLKKIEEQLEKKKAEYAERMKNKVAAIHKEAEERRAMIEAKRGEDVLKAEETAAKYRATGIVPKATCGCF
Protein: Thioredoxin, mitochondrial (MTRX) (Mt-Trx) (Thioredoxin-2) (P97493)
Organism: Mus musculus (Mouse)
Function: Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity.
Subcellular location: Mitochondrion.
Interaction partners:
- Thioredoxin-interacting protein
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Peroxiredoxin-5, mitochondrial
- Mitogen-activated protein kinase kinase kinase 5
- 3-mercaptopyruvate sulfurtransferase
- Thioredoxin reductase 1, cytoplasmic
- Peroxiredoxin-1
- Mitochondrial peptide methionine sulfoxide reductase
Sequence:
MAQRLLLGRFLTSVISRKPPQGVWASLTSKTLQTPQYNAGGLTVMPSPARTVHTTRVCLTTFNVQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAIKNGDVVDKFVGIKDEDQLEAFLKKLIG
Protein: Angiomotin (Q8VHG2)
Organism: Mus musculus (Mouse)
Function: Plays a central role in tight junction maintenance via the complex formed with ARHGAP17, which acts by regulating the uptake of polarity proteins at tight junctions. Appears to regulate endothelial cell migration and tube formation. May also play a role in the assembly of endothelial cell-cell junctions (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250}. Note=Localized on the cell surface. May act as a transmembrane protein (By similarity). {ECO:0000250}.
Interaction partners:
- InaD-like protein
- Rho GTPase-activating protein 17
- Protein PALS1
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
- Merlin
- Plasminogen
- Serine/threonine-protein kinase LATS1
- Protein KIBRA
- Multiple PDZ domain protein
Sequence:
MRSSDDQPSGGTTVLQRLLQEQLRYGNPSENRSLLAIHQQATGNSSPFSTGSGNQGPQNDVLSSQDHHQQQLVAHPARQEPQGQEIQSENGVMEKQLSPRMQNNEELPTYEEAKVQSQYFRGQQHASVGAAFYVTGVTNQKMRTEGRPSVQRLTPGKMHQDEGLRDLKQGHVRSLSERLMQMSLATSGVKAHPPVTSAPLSPPQPNDLYKNATSSSEFYKAQGPPPSQHSLKGMEHRGPPPEYPFKGVPSQSVVCKSQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARATQDISSLSLSARNSQPHSPTSSLTAGASSLPLLQSPPSTRLPPGQHLVSNQGDHSAHLSRHQQHLLSSQSHQGDHYRHAQASLTSAQQQPGEAYSAMPRAQQSASYQPMPADPFAMVSRAQQMVEILSDENRNLRQELDGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRDRLETANKQLAEKEYEGSEDTRKTISQLFAKHKENQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNSQPTNASEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSSMRPAKSLMSISNAGSGLLAHSSTLTGAPIMEEKRDDKSWKGSLGVLLGGDYRVEPVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGPESTKTAAVTPISAPMAGPVAAAAPAAAINATAATNTATAATNTTIMVAAAPVAVAAVAAPAAAAATPSPANAAALAAAAAPATSVSAATSVSAANSISPAAPVAPAAVVPPAAPVSPAAAVQIPAAASLTPATVSPTAATATAAVAAATTAAITAAAAAATTAIQVAPATSAPVPSPASIPAPATAQASAPTPTQASTPAPTEPPSPVPTPTPALVQTEGPANPGASSGPRRLSTPNLMCNPDKPDAPAFHSSTLERKTPIQILGQEPDAEMVEYLI
Protein: GTPase-activating protein gyp10 (O94661)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in vesicular trafficking and septation during cytokinesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16291723, ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16291723, ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding protein ypt1
- Phosphatidylinositol 4-phosphate 5-kinase its3
- GTP-binding protein ryh1
- Guanine nucleotide exchange factor subunit ric1
Sequence:
MKKKEIKQLKNEIKIALLNSDVETLSHIGKEGHGFLMKSLRKSVWVSLCGLSCRHRMECLSRSTSQSSYADQNQVHLDSERSFFQYKLNPFLLRKHRSQLTKLLSVVFKHYPELCYYQGLHDIAQILLLTLPFSHALPLMEHLVFYRLRDFMLPTLDGTVKQLQLILAVIKARDPTLYEYLIKADIQCYFALSWLITWFAHDVSDISVVCRLFDFFISSHPLTVVYTCAQVVLDNRTSIIELLWDNSGADLLHSYLCKLPASINVNQLIKNTCATISAVPFSSLPLDRYQISPYSCLRNTGDPWEYMSRSNGLLLFRLQLAELQEEKHKPGTKVPAVFLQENIFNGCNMLAAITVIGIGIVASQLIPKSTSNS
Protein: Ribosome biogenesis protein BOP1 homolog (Q384Z1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03027}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03027}.
Interaction partners:
- Ribosome biogenesis protein NSA1
- rRNA processing protein, putative
- NLE domain-containing protein
- Pescadillo homolog
- Ribosome assembly factor mrt4
- Nucleolar complex protein 2
- Ribosome biogenesis protein NSA2 homolog
- Ribosome biogenesis protein, putative
- Nucleolar protein, putative
- Nucleolar GTP-binding protein 1
Sequence:
MVKKREPTSRVTSRVHKTPSPSPRAVDDSGKQKPDLSTTPPPSPGEGGNGDEVLTSSQTNATDLRDELIWSDRESDDEVFLFPDAQELVEPQGGPDCDVIRIGATQKLDESDSSEDEATLNRVGDIPLEWYKDEAHYGYDVEGRKLMKSERSALERLLEATDDPNAMRTIYDALHDEKKVLSNADLQMIFNLQRNRTPNPNYNMYEDVAVDTVEFDPLNHPLARSAGPSKRKFLPSDRDMKTIAKMVRRMMKEDKEKENKPKDETESETTILWDDGKVVMDTHTHFKYHNRVPKPKAAPPGTYESYRPPPEYLPSERAKERFARLRAIDKKEHFLPRAFDALRHVPFYNHTIQDRYQRCLDLAFFPRAQRTRLVVDPSKLLPELPDPRDLRPYPERLSFQYKGHTATVRSVAVNPNGQYLATACDDHLVRVYEVMTGRLMKRYDMGAPVQQVEFCPVKTLNILAVAVEYSLVFIVPRFAAHELVNENTLRHLRAPGTAVNNTEVEQVVGGEVSLGGGGITQAALDKDETAHSILQDLHDVEERDKRAEFFDASAKERRAGIVLKIALHAKVKRFTFHARGDYLCALCPKDHVKYRQTVMLQLSKRKVFCPFRKFSEVVTDCKFHPREPLFFLSTTNSVRMYNLLAHKLQRRYKAPGGITTCLSIHTEGDNFLVGDTTSHTQWYDCDFSDKPYKRMRSHKGVVNAVAFHTNTNAYPLFASGAADGQVHVFHGMVYDDYNKNALLVPVKILKHRRAVYSVAWHPTLPWIFTSTEDGVVSAWTE
Protein: Pantothenate transporter (O96156)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAKNQYMEDRNIREPNTLLGEETEQLVDSFHYENNSSSIYKKVNSNRSKNGKHSMAFHKSLAVVNVAAGLDGCDDQLLPASFRALEADLNLHPSLLGYITLAQTLMLSLFSPIWGFLSDKYSRKWMLVFGTALWGVATILLANINDFAHILFFRAINGLALGSIGPISQSILADAAKNESLGLSFGLVQLSSSLGRLIGGVVTTTVALKYFGGIRGWRLCFIVVGILSVLLSIIVALFVEDAPRQVRKNKKMDYLDGESNTNASNNNNNSNNNNINNNINMNNSLDNNNSFTGLSHQSTRTYILYQNIVELLKDSLSKKSIIIILLEGFTGTIPWLALSFNTMFFQYCGLSDLQAAIITGFLLIGSAIGGVVGGHFGDIMHDISNKHGRPLLGQLAMFGRVPLVLLIYLVIPKRKESFELFALSCFCIGLSSIAGVAVNRPIVSDIIRPDYRGTVFSLTIAIEGVGSSLIGAPLFGYLAEKIFKYQNNNLLISDMPEDIRINNAQALSKTLFYLTIIPWILSFIFYSLLHFTYGKEYLKMNEIIQNEYKYDDEDEETIPEKKMLT
Protein: 26S proteasome regulatory subunit rpn501 (P0CU17)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Required for proper proteasome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:12783882}.
Interaction partners:
- Probable 26S proteasome subunit rpt4
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome regulatory subunit rpn11
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit rpn8
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit 4 homolog
- Probable 26S proteasome regulatory subunit rpn3
- Probable 26S proteasome regulatory subunit rpn9
- Probable 26S proteasome regulatory subunit rpn6
Sequence:
MEQKPEVDYSEKFAELQKSLNNLNTIDIDANLEKLLIFEKQVRQASDTSTNTKVLIYIADLLFRAGDFQGLNEQLVSLFKKHGQLKQSMTSLVQHVMTYLPGIDDLKTKINLIETLRTITDGKIYVEVERARLTQLLSQIKEEQGDIKSAQEILCNEPVETYGSFDLKEKVAFILDQVRLFLLRSDYYMASTYTKKINVKFFEKEDVQSLKLKYYEQKIRIGLHDDAYLDVCKYYRAVYDTAVVQEDPEKWKEILENVVCFALLTPYDNEQADLLHRINADHKLNSLPLLQQLVKCFIVNELMRWPKIAEIYGSALRSNPVFAENDEKGEKRWSELRKRVIEHNIRVVANYYSRIHCSRLGVLLDMSPSETEQFLCDLIAKHHFYAKIDRPAQVISFKKSQNVQEQLNEWGSNITELLGKLEKVRQLIIKEEMMNSIQQAVAK
Protein: WASH complex subunit homolog 5 (WASH complex subunit strumpellin homolog) (Q9VUY8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts at least in part as component of the WASH complex which may regulate wash nucleation-promoting factor (NPF) activity and is required for its membrane targeting during endosomal sorting (By similarity). During embryogenesis, not involved in the wash-dependent developmental migration of hemocytes anteriorly from the tail.
Subcellular location: Early endosome {ECO:0000305}.
Interaction partners:
- WASH complex subunit 4
- WASH complex subunit 3
- WASH complex subunit 2
- WASH complex subunit 1
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
Sequence:
MSFLDDNNACGQNLLNIVSVGNSIIAEILRLKDYVPSIYRLDNKADKAKYGELILDFSYFKIAEDHERRIEQSPELTELDDEARAQLPLITRFYLAFQSIHHYASDLQQYIEELNTGYYIQQTLETVLQEEEGRQLLCESLYLFGVILLMVDFHIPGDVRERLLIAYYRYSGGDATPSGDESNIHDVCLLLRSTGYVHPSIAAKVLGLGGKQAGARAASLVVPRYPEAYFSRFRFDENFVDLVVARLRCDDIYNQLNLYPHPAHRSTALSTQAAMLYVCLYFCPQVLHSQGSQMREIVDKFFCDNWTISVYMGMTVNLVDAWLDFKAARSAIENVISPPAIKALCQQQKEQLGKITQKTQEIVREGVLNDNFVLEHANKIIHLMRQSNVLLRWFCLHTSREVFIFAHTATLTGQVQKCVLHELQFNRNTLYNLLLNCSQMELSVREFLAEIQQTKEERWTKSREEAMQRLNELSEAFAGSRPLSKIEQNPQLQQWFGEVAGRLQKLELSRPQKSGRLIIQVMQALDDVQEYHNLHSNMLVKQQLQETRDMLNQMAQLINLKEDIEIHIQMITDFSYAWHLLQFDFTPPMQEHIKRQPQAVIGIRAVFLKLASTLEVPLMRINQARSEDLVSVSNYYSTELANFLRRVLQIVPETMFSILAKIIYLLTNVIKEFPTKVEKERLKDYAQFEERAKVAQLTNSIAVFTKGILMMKTTLVGVIELDPKQLLEDGIRKELVNHLANAYNLGLIFTPEKGKTPVQLLQQKLQALAKTIEGYRRSFEYIEDYLRVQGLRILLEESQRIINYNVEKECNAFLRNKVQEFQSEHQSQIIPIPNFPPLLGDPSNNFIGRLAHEILRCTDPKQTIFLDLKSTWYEKKAPHQEVLAGSGFFEILREALAPAGMVGLERLYAHMLADELKRNLERLQRNLTSDRMWVDTLAALTRELEARDFPTPEVSKQPLKYYQAYTQRWLKVWPTLLDWVLCIGQKQLLRREIAGELSFSSKCDAKLLENTADTLNKALLLELSLSKDLCDEKGVVMLTELQETLLYTGNFEPLEQVFLITKNTHNMALFMFLFTIAHLGRMQHSTITDCLLPKSAKDNIDNVPFIVGLVTILQQFHKNVKMLYISYMSQYVVTVSEAQLLDKEILGPEVVTALHFLLAFIRIARLPLGVLEQRIPNIILSEYEYLSTLLK
Protein: Beta-galactosidase A (EC 3.2.1.23) (Acidic beta-galactosidase) (Ao-beta-gal) (Lactase A) (Q2UCU3)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Subcellular location: Secreted {ECO:0000269|PubMed:23688418}.
Interaction partners:
- Alpha-L-arabinofuranosidase B
- Probable alpha-galactosidase B
- Xylanolytic transcriptional activator xlnR
- Probable alpha-galactosidase C
- Probable beta-glucosidase A
- DNA-binding protein creA
- Exo-1,4-beta-xylosidase xlnD
- Probable endo-1,4-beta-xylanase B
Sequence:
MKLLSVAAVALLAAQAAGASIKHRLNGFTILEHPDPAKRDLLQDIVTWDDKSLFINGERIMLFSGEVHPFRLPVPSLWLDIFHKIRALGFNCVSFYIDWALLEGKPGDYRAEGIFALEPFFDAAKEAGIYLIARPGSYINAEVSGGGFPGWLQRVNGTLRSSDEPFLKATDNYIANAAAAVAKAQITNGGPVILYQPENEYSGGCCGVKYPDADYMQYVMDQARKADIVVPFISNDASPSGHNAPGSGTGAVDIYGHDSYPLGFDCANPSVWPEGKLPDNFRTLHLEQSPSTPYSLLEFQAGAFDPWGGPGFEKCYALVNHEFSRVFYRNDLSFGVSTFNLYMTFGGTNWGNLGHPGGYTSYDYGSPITETRNVTREKYSDIKLLANFVKASPSYLTATPRNLTTGVYTDTSDLAVTPLIGDSPGSFFVVRHTDYSSQESTSYKLKLPTSAGNLTIPQLEGTLSLNGRDSKIHVVDYNVSGTNIIYSTAEVFTWKKFDGNKVLVLYGGPKEHHELAIASKSNVTIIEGSDSGIVSTRKGSSVIIGWDVSSTRRIVQVGDLRVFLLDRNSAYNYWVPELPTEGTSPGFSTSKTTASSIIVKAGYLLRGAHLDGADLHLTADFNATTPIEVIGAPTGAKNLFVNGEKASHTVDKNGIWSSEVKYAAPEIKLPGLKDLDWKYLDTLPEIKSSYDDSAWVSADLPKTKNTHRPLDTPTSLYSSDYGFHTGYLIYRGHFVANGKESEFFIRTQGGSAFGSSVWLNETYLGSWTGADYAMDGNSTYKLSQLESGKNYVITVVIDNLGLDENWTVGEETMKNPRGILSYKLSGQDASAITWKLTGNLGGEDYQDKVRGPLNEGGLYAERQGFHQPQPPSESWESGSPLEGLSKPGIGFYTAQFDLDLPKGWDVPLYFNFGNNTQAARAQLYVNGYQYGKFTGNVGPQTSFPVPEGILNYRGTNYVALSLWALESDGAKLGSFELSYTTPVLTGYGNVESPEQPKYEQRKGAY
Protein: Capsid vertex component 1 (P16799)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04017}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04017}.
Interaction partners:
Sequence:
METHLYSDLAFEARFADDEQLPLHLVLDQEVLSNEEAETLRYVYYRNVDSAGRSTGRAPGGDEDDAPASDDAEDAVGGDRAFDRERRTWQRACFRVLPRPLELLDYLRQSGLTVTLEKEQRVRMFYAVFTTLGLRCPDNRLSGAQTLHLRLVWPDGSYRDWEFLARDLLREEMEANKRDRQHQLATTTNHRRRGGLRNNLDNGSDRRLPEAAVASLETAVSTPFFEIPNGAGTSSANGDGRFSNLEQRVARLLRGDEEFIYHAGPLEPPSKIRGHELVQLRLDVNPDLMYATDPHDRDEVARTDEWKGAGVSRLREVWDVQHRVRLRVLWYVNSFWRSRELSYDDHEVELYRALDAYRARIAVEYVLIRAVRDEIYAVLRRDGGALPQRFACHVSRNMSWRVVWELCRHALALWMDWADVRSCIIKALTPRLSRGAAAAAQRARRQRERSAPKPQELLFGPRNESGPPAEQTWYADVVRCVRAQVDLGVEVRAARCPRTGLWIVRDRRGRLRRWLSQPEVCVLYVTPDLDFYWVLPGGFAVSSRVTLHGLAQRALRDRFQNFEAVLARGMHVEAGRQEPETPRVSGRRLPFDDL
Protein: C-type lectin domain family 3, member B (D3ZUU6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Plasminogen
Sequence:
MGFWGTYLLFCLFSFLSQATTESPTPKTKKAATAKKDLVSPKMFEELKNRLDVLAQEVALLKEKQALQTVCLKGTKVNLKCLLAFTQPKTFHEASEDCISQGGTLGTPQSELENEALFEYARQSVGSEAELWLGLNDMASEGAWVDMTGGRLAYKNWETEITTQPDGGKAENCAALSGAANGKWFDKRCRDQLPYICQFAIV
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (H3BUD0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLSRLIAAERERELEECQRNHEGDEDDSHVRAQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQVRPAAGGAGPVAWSWAP
Protein: Metalloproteinase inhibitor 1 (Erythroid-potentiating activity) (EPA) (Fibroblast collagenase inhibitor) (Collagenase inhibitor) (Tissue inhibitor of metalloproteinases 1) (TIMP-1) (P01033)
Organism: Homo sapiens (Human)
Function: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.
Subcellular location: Secreted {ECO:0000269|PubMed:1730286, ECO:0000269|PubMed:24635319, ECO:0000269|PubMed:3010309, ECO:0000269|PubMed:3839290, ECO:0000269|PubMed:3903517, ECO:0000269|PubMed:8541540}.
Interaction partners:
- Matrix metalloproteinase-9
- Stromelysin-1
- Matrix metalloproteinase-14
- Interstitial collagenase
- CD63 antigen
- 72 kDa type IV collagenase
- Stromelysin-2
- Interleukin-10
- Fibronectin
- Interleukin-6
Sequence:
MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA