wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription initiation factor TFIID subunit 6 (RNA polymerase II TBP-associated factor subunit E) (Transcription initiation factor TFIID 70 kDa subunit) (TAF(II)70) (TAFII-70) (TAFII70) (Transcription initiation factor TFIID 80 kDa subunit) (TAF(II)80) (TAFII-80) (TAFII80) (P49848)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF6 homodimer connects TFIID modules, forming a rigid core.
Subcellular location: Nucleus.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000269|PubMed:18628956}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9B
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 4
Sequence:
MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGATTADGKGKEKKAPPLLEGAPLRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRAEFGSLGPLLCSQVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSAPSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPSGPGSVQKYIVVSLPPTGEGKGGPTSHPSPVPPPASSPSPLSGSALCGGKQEAGDSPPPAPGTPKANGSQPNSGSPQPAP
Protein: Telethonin (E9QCX4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cysteine and glycine-rich protein 1
- Actinin alpha 3b
- Titin, tandem duplicate 1.
- Myotilin
- Myosin heavy chain 7
- Desmin
- Uncharacterized protein.
- Ankyrin repeat domain 2
- Myozenin 2
- Vimentin-like
Sequence:
MQVCSVLEKKGGCVVGAELSCSVREENPNKRESYTADWRSINMKTQPEDRQSMLMSDDSRRESLSRYWQVRPLHQACPSGVRRVGTVDTGVREHQLLPYRNSLPLPIFKPAELGVRLGRGAPHTLEDLPPVRIPDGVCPDKRAVEQITRDLPPVKPMRMEFAKAPRALGRSMSQEAQRG
Protein: NADPH--cytochrome P450 reductase 3 (CPR) (P450R) (EC 1.6.2.4) (Q653S9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity). It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Os05g0503300 protein.
- Nitrate reductase 1
- Nitrate reductase
- Nitrate reductase
- Ferredoxin--nitrite reductase, chloroplastic
- Os01g0357500 protein
- Os02g0765900 protein
- Anamorsin homolog 2
- Anamorsin homolog 1
Sequence:
MDSGGGGGGGALRPSALDLVAALLTGRGRPEEEGWPPSLAENRHLIVLLTTSLAVLVGCGVALLVRRSSISAPAVRAQEPQPRAPAPAKRKQEAEPDPDDGRQRVAVFFGTQTGTAEGFAKALAEEAKSRYDKAVFKVLDLDEYAADDEEYEQKLKKEIIALFFVATYGDGEPTDNAARFYKWFGEGNERGEWLSNLRFGVFGLGNRQYEHFNKVGKVVDQLLAEQGGKRIVPLGLGDDDQCIEDDFNAWKELLWPELDKLLRVEDDKSAAPTPYTAAIPEYRVVLVKPEEAMHINKSFSLSNGHAVYDIQHPCRANVAVRRELHTPASYRSCIHLEFDISGTGLTYETGDHVGVYAENCTETVEEVENLLGYSPDTLFSIHADQEDGTPLFGGSLPPPFPSPCTVGTALARYADLLSFPKKSALIALASHASDPKDAERLRHLASPAGKKEYSQWIVSSQRSLLEVMTEFPSAKPPLGVFFAAIAPRLQPRYYSISSSPRMTPTRIHVTCALVYGQTPTGRIHKGVCSTWMKNSIPLEESQECSWAPIFVRQSNFKLPTDPTVPIIMIGPGTGLAPFRGFLQERLALKETGVELGHAVLFFGCRNRKMDFIYEDELNNFVETGALSELIVAFSREGPSKEYVQHKMAEKAPEIWSIISQGGYIYVCGDAKGMARDVHRTLHTIVQEQGSLDNSNTESYVKSLQMEGRYLRDVW
Protein: NAD-capped RNA hydrolase DXO1 (DeNADding enzyme DXO1) (EC 3.6.1.-) (Q8RY73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and promotes mRNA decay (By similarity). Its precise role is unclear: may be involved in the connection between RNA turnover and retrograde chloroplast-to-nucleus signaling independently of its deNADding activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30949699}. Nucleus {ECO:0000269|PubMed:30949699}.
Interaction partners:
- Ribosomal RNA-processing protein 42
- 5'-3' exoribonuclease 2
- 5'-3' exoribonuclease 3
- 5'-3' exoribonuclease 4
- ENTH/VHS family protein
- At5g10060
- At3g26990
- Pentatricopeptide repeat-containing protein At1g09820
- RING-type E3 ubiquitin transferase
- Probable CCR4-associated factor 1 homolog 2
Sequence:
MDSPPKKNPMDDLFGEDSDNDSRSSRSKSSSSGNASSSSSSSSSSSSSSSAAGGDGEGDGGGADSGSASDSGSGSSGGKEEHGDDKVESYRSNDNGESGVYPYEEEEEEEEDEKDLFGSDNEEYTKTPAISTYSIPVLPAGWSNDNHGGRGGMGRGRWSNGRGGPGLLPRPGPYPGRGGNRGGFGGRYQNYQRDERFVSELKLSKSKETLARKQTNFQEPCELTCYSRVEGGEVIYDDQGLRLFKRHIGEEIGADLNQGYDTFIEKKDLGSEGFGDLLGSIRAKNISLDNIHFVTFRNNLNKILGAAYNRHEPWEMGVHKRNGTIYLDVHKLPERPQSDLDRRRCYWGYCFESLATEDPGRAYGEEIHHVDANVEFCSVVRTKLGAHRVMMGAEMDCCDVSDKGKRFYVELKTTRELDDRTVDRFEREKLLKFWIQSFVAGVPYIVVGFRDDGGRLVRTERLTTRDIAHRARLKNYWQGGVCLAFADEVLCWLYGTVKENEDYILQFVHPFMRLELLQAQSCPDAITNHVHLLQNPASPPPPPQ
Protein: Ribosome assembly protein SQT1 (P35184)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in the late step of 60S ribosomal subunit assembly or modification in the cytoplasm.
Interaction partners:
- Large ribosomal subunit protein uL16
- Ribosome assembly protein RRB1
- Synchronized import protein 1
- Ankyrin repeat-containing protein YAR1
- Large ribosomal subunit protein uL3
- 60S ribosomal export protein NMD3
- Assembly chaperone of RPL4
- Probable metalloprotease ARX1
- Large subunit GTPase 1
- Ribosome biogenesis protein RPF2
Sequence:
MEPQEEFITTEEVEQEIVPTVEVEQDVPVDIEGENDDDDEMMNDDEEALEVDMSNNSLTYFDKHTDSVFAIGHHPNLPLVCTGGGDNLAHLWTSHSQPPKFAGTLTGYGESVISCSFTSEGGFLVTADMSGKVLVHMGQKGGAQWKLASQMQEVEEIVWLKTHPTIARTFAFGATDGSVWCYQINEQDGSLEQLMSGFVHQQDCSMGEFINTDKGENTLELVTCSLDSTIVAWNCFTGQQLFKITQAEIKGLEAPWISLSLAPETLTKGNSGVVACGSNNGLLAVINCNNGGAILHLSTVIELKPEQDELDASIESISWSSKFSLMAIGLVCGEILLYDTSAWRVRHKFVLEDSVTKLMFDNDDLFASCINGKVYQFNARTGQEKFVCVGHNMGVLDFILLHPVANTGTEQKRKVITAGDEGVSLVFEVPN
Protein: Conserved hypothetical alanine rich protein (O05445)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Tat
Sequence:
MVAADLPPGRWSAVLVGPWWPAPSAALRAAAQHWATWAMQKQELARNLISQHDLLLRNQGRTAEDLIGRYLRGAKSEVTKAEKYEIKKGAFNTAADAIDYLRSRLTGIAGEGNKEIDDVLASKKPLPEQLAEIQAIQTRCNADAANASRDAVDKVMTAMQEILEAEDIGDDPRTWARANGFNVDDAPPPRLIRENDLAALTGPGARGGSFGSVEGAGDLASPQSVGAGGFSGSGVQAACSQPAPRAIGASSRHASAGPVPPAPVVTTPAAATPPVIATGPRWRCPAGRCRRRPSDRAYRLRRLGNRLRPGW
Protein: Alcohol dehydrogenase 1A (EC 1.1.1.1) (Alcohol dehydrogenase subunit alpha) (P07327)
Organism: Homo sapiens (Human)
Function: Alcohol dehydrogenase. Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate.
Subcellular location: Cytoplasm.
Interaction partners:
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 1C
- Aldehyde dehydrogenase, mitochondrial
- Cytochrome P450 2E1
- Vasopressin-neurophysin 2-copeptin
- Aldehyde dehydrogenase 1A1
- Aldehyde oxidase
- Cytochrome P450 26A1
- Amine oxidase [flavin-containing] A
- Lecithin retinol acyltransferase
Sequence:
MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF
Protein: G-box-binding factor 4 (bZIP transcription factor 40) (AtbZIP40) (P42777)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the G-box motif (5'-CCACGTGG-3') of the rbcS-1A gene promoter. G-box and G-box-like motifs are cis-acting elements defined in promoters of certain plant genes which are regulated by such diverse stimuli as light-induction or hormone control.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:8146148}.
Interaction partners:
- bZIP transcription factor 68
- Basic leucine zipper 8
- Basic leucine zipper 43
Sequence:
MASFKLMSSSNSDLSRRNSSSASSSPSIRSSHHLRPNPHADHSRISFAYGGGVNDYTFASDSKPFEMAIDVDRSIGDRNSVNNGKSVDDVWKEIVSGEQKTIMMKEEEPEDIMTLEDFLAKAEMDEGASDEIDVKIPTERLNNDGSYTFDFPMQRHSSFQMVEGSMGGGVTRGKRGRVMMEAMDKAAAQRQKRMIKNRESAARSRERKQAYQVELETLAAKLEEENEQLLKEIEESTKERYKKLMEVLIPVDEKPRPPSRPLSRSHSLEW
Protein: ER membrane protein complex subunit 4 (P53073)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- Vacuolar protein sorting-associated protein 28
- Ubiquitin-conjugating enzyme E2 7
- Endoplasmic reticulum membrane protein complex subunit 10
- Protein SOP4
- Uncharacterized protein YGL230C
Sequence:
MSEQEPYEWAKHLLDTKYIEKYNIQNSNTLPSPPGFEGNSSKGNVTRKQQDATSQTTSLAQKNQITVLQVQKAWQIALQPAKSIPMNIFMSYMSGTSLQIIPIMTALMLLSGPIKAIFSTRSAFKPVLGNKATQSQVQTAMFMYIVFQGVLMYIGYRKLNSMGLIPNAKGDWLPWERIAHYNNGLQWFSD
Protein: Beta-lactamase (Penicillinase) (B1MCI3)
Organism: Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium abscessus)
Interaction partners:
Sequence:
MISRRALLVGGVSAVGVVAAGCSRNGNRRPAPDELASLEKDFGGRIGVYALDTGSGDTVGHRADERFLMCSTVKTFIVSAILRRRLSEPGLLDQRIQYTQSDVLEWAPITSQHVSTGMTVSELCDATLRYSDNTGANLLITQLGGPKETEKFVRSLGDNVTRMDRTEVQLNIPDGDLDTSTPQQLVANLRRLVLDEGLDSRGRDLLTDWLKRNTTGDQSIRAAVPAGWTVADKTGGGFKGETNDIAVIWPPGRAPIVMAVLTVPEDPTSTKGKPTIAAATRIVLRAFGA
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Q9W3K5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.
Interaction partners:
- GCS light chain
- FI11917p
- Gamma-glutamyl transpeptidase, isoform A
- RE13973p
- Uncharacterized protein, isoform C
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
Sequence:
MGLLSEGSPLSWEETKALADHVREHGVNQFINLYHRLKDRQGDILKWGDEVEYIIVKFDDEQKVARVALRAQDLLAQLNEKELADPNGVKSLWRPEYGAYMIEGTPGKPFGGLMAHFNLVEANMRYRREEVTELLAKDECVMSITNFPRLGAPNFTYPLAQPRPEDPLSSARSLYFPDEAIFPGHPRFKTLTRNIRKRRGEKVSIKLKVFKDTKTKLPVEGAPPGEPDVVLLDAMGFGMGCCCLQLTFQACNITEARRLYDQLAPLCPIMLALTAASPIYRGYLTESDCRWNVISSSVDCRTEEERGLAPLDQQKFRIAKSRYDSIDSYLSPEGAKYNDVPLTYDEKVYQRLVEGGIDHLLAQHVAHLFIRDTVSLFSEKVHQNDNEDTDHFENIQSTNWQTMRFKPPPPNSSIGWRVEFRPCEAQISDFENAAIVCFVVLLTRVILSYQLNFLTPISKVDENMQTAQKRDACRKEKFWFRKSSKTTEQRAAKAQAQAQAQAKAQAQTNGKATLNGNGLANGNGNGSENSDQEEQQPLTNGSAKMNGHGSGTTNGTNGSSNGSSNGTDSDHTDTDDEENELFQLLSINEIFNGKPNVFPGLVPLIRSYLQSMEVDTDTHCTIEQYLRFIQKRAAGELITTATWMREQVLSHPDYKQDSVVSERINYDLLKRIQGIQEGKQVEPALLGQDYHSKTKTKDFIPPALQKQLAKNGCCEEK
Protein: C-type mannose receptor 2 (C-type lectin domain family 13 member E) (Endocytic receptor 180) (Macrophage mannose receptor 2) (Urokinase-type plasminogen activator receptor-associated protein) (UPAR-associated protein) (Urokinase receptor-associated protein) (CD antigen CD280) (Q9UBG0)
Organism: Homo sapiens (Human)
Function: May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Macrophage mannose receptor 1
- Secretory phospholipase A2 receptor
- Urokinase plasminogen activator surface receptor
- Urokinase-type plasminogen activator
Sequence:
MGPGRPAPAPWPRHLLRCVLLLGCLHLGRPGAPGDAALPEPNVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGARTSNISKPGTLERGDQTRSGQWRIYGSEEDLCALPYHEVYTIQGNSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKKKPNATAEPTPPDRWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLWEVKNCTSFRARYICRQSLGTPVTPELPGPDPTPSLTGSCPQGWASDTKLRYCYKVFSSERLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGESEPEIHEQHWFWIGLNRRDPRGGQSWRWSDGVGFSYHNFDRSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICKIPRGTDVREPDDSPQGRREWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQEQHWWIGLHTSESDGRFRWTDGSIINFISWAPGKPRPVGKDKKCVYMTASREDWGDQRCLTALPYICKRSNVTKETQPPDLPTTALGGCPSDWIQFLNKCFQVQGQEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQEPLMYANWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTGRWDDRSCTEETHGFICQKGTDPSLSPSPAALPPAPGTELSYLNGTFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQPGGCTYVDVDGAWRTTSCDTKLQGAVCGVSSGPPPPRRISYHGSCPQGLADSAWIPFREHCYSFHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRGAWLGMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSMLSHNSCYWIQSNSGLWRPGACTNITMGVVCKLPRAEQSSFSPSALPENPAALVVVLMAVLLLLALLTAALILYRRRQSIERGAFEGARYSRSSSSPTEATEKNILVSDMEMNEQQE
Protein: Acid stress chaperone HdeB (10K-L protein) (P0AET2)
Organism: Escherichia coli (strain K12)
Function: Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_00947, ECO:0000269|PubMed:17085547}.
Interaction partners:
- Acid stress chaperone HdeA
- Protein HdeD
- Glutamate/gamma-aminobutyrate antiporter
- Glutamate decarboxylase beta
- Glutamate decarboxylase alpha
- Transcriptional regulator GadE
- Outer membrane protein Slp
- Putative magnesium transporter YhiD
- HTH-type transcriptional regulator GadX
- HTH-type transcriptional regulator GadW
Sequence:
MNISSLRKAFIFMGAVAALSLVNAQSALAANESAKDMTCQEFIDLNPKAMTPVAWWMLHEETVYKGGDTVTLNETDLTQIPKVIEYCKKNPQKNLYTFKNQASNDLPN
Protein: Replication factor C subunit 5 (Activator 1 36 kDa subunit) (A1 36 kDa subunit) (Activator 1 subunit 5) (Replication factor C 36 kDa subunit) (RF-C 36 kDa subunit) (RFC36) (P40937)
Organism: Homo sapiens (Human)
Function: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Replication factor C subunit 2
- Chromosome transmission fidelity protein 8 homolog
- Replication factor C subunit 4
- Replication factor C subunit 1
- Proliferating cell nuclear antigen
- Sister chromatid cohesion protein DCC1
- Chromosome transmission fidelity protein 18 homolog
- Cell cycle checkpoint protein RAD17
- Replication factor C subunit 3
- ATPase family AAA domain-containing protein 5
Sequence:
METSALKQQEQPAATKIRNLPWVEKYRPQTLNDLISHQDILSTIQKFINEDRLPHLLLYGPPGTGKTSTILACAKQLYKDKEFGSMVLELNASDDRGIDIIRGPILSFASTRTIFKKGFKLVILDEADAMTQDAQNALRRVIEKFTENTRFCLICNYLSKIIPALQSRCTRFRFGPLTPELMVPRLEHVVEEEKVDISEDGMKALVTLSSGDMRRALNILQSTNMAFGKVTEETVYTCTGHPLKSDIANILDWMLNQDFTTAYRNITELKTLKGLALHDILTEIHLFVHRVDFPSSVRIHLLTKMADIEYRLSVGTNEKIQLSSLIAAFQVTRDLIVAEA
Protein: Puromycin-sensitive aminopeptidase (PSA) (EC 3.4.11.14) (Cytosol alanyl aminopeptidase) (AAP-S) (Q4TT88)
Organism: Caenorhabditis elegans
Function: Aminopeptidase. Required for the exit from meiosis, probably upstream of cyclin cyb-3. Involved in the establishment of the anterior-posterior polarity at the embryonic 1-cell stage by regulating the dynamics of sperm-donated centrosomes. Plays a role in oocyte maturation. Required for embryonic development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20599902}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20599902}. Chromosome {ECO:0000269|PubMed:20599902}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20599902}. Note=During meiosis I, localizes to the cell cortex. During meiosis II, localizes to the cytoplasm. During embryonic mitosis, localizes around mitotic chromosomes at metaphase and anaphase and near the spindle poles. In spermatids, excluded from the chromosomes. {ECO:0000269|PubMed:20599902}.
Interaction partners:
Sequence:
MLGRLAVRQAVRCSKASIKPVNTHQLCLRNFSAIRRLSFVAGAQCRPYHTTANMLHRTARGEHGMAACGNPSAAVKFERLPTFAEPTHYNVRLSPCLNQFSFDGHATIDVTIKEATDVLKVHAQSLLIQSVSLITQPGDASKSLETSYDDKLNILTIKLPTTMQPQKVQLDFKFVGELNDKMRGFYRSQYKDKNGTEKFLASTQFESTYARYAFPCFDEPIYKATFDVTLEVENHLTALSNMNVISETPTADGKRKAVTFATSPKMSSYLVAFAVGELEYISAQTKSGVEMRVYTVPGKKEQGQYSLDLSVKCIDWYNEWFDIKYPLPKCDLIAIPDFSMGAMENWGLVTYREIALLVDPGVTSTRQKSRVALVVAHELAHLWFGNLVTMKWWTDLWLKEGFASFMEYMFVGANCPEFKIWLHFLNDELASGMGLDALRNSHPIEVEIDNPNELDEIYDSITYAKSNSVNRMLCYYLSEPVFQKGLRLYLKRFQYSNAVTQDLWTALSEASGQNVNELMSGWTQQMGFPVLKVSQRQDGNNRILTVEQRRFISDGGEDPKNSQWQVPITVAVGSSPSDVKARFLLKEKQQEFTIEGVAPGEWVKLNSGTTGFYRVEYSDEMLTAMLPDIASRRMPVLDRFGLINDLSALLNTGRVSIAQFVQVAASSAKEDEYVVWGAIDEGMSKLLACAREMSEDTLKSAKQLVVKMFEQTGAELGFAEQAGEDSQKMMLRSLVQARLARAGHQPTIDKFTQMFNDFLEKGTPIHPDIRLATFGVVARYGGKEGFDKLMNLRETTTFQEIERQTMVAMSQTPEESLLAQLFEYGFEKNKVRPQDQLYLFLGTGATHMGQQYAWKYFCEHIKEFLDKYGGANSSLFQRCLKFAGESFGNEKRAVEFQDFFCNCNVLSDTDRQTLARPIGQTVEAIRLNARLLESNRQIIENLLKQSNV
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (P38625)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9P772}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase 3
- Inosine-5'-monophosphate dehydrogenase 4
- Inosine-5'-monophosphate dehydrogenase 2
- Guanylate kinase
- Adenine phosphoribosyltransferase 1
- Adenine phosphoribosyltransferase 2
- Hypoxanthine-guanine phosphoribosyltransferase
- Ubiquitin carboxyl-terminal hydrolase 15
- Inosine triphosphate pyrophosphatase
- CTP synthase 1
Sequence:
MAAGEQVSNMFDTILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELGWTPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSNSLFKGMNDSTVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGPTAEVIGAVSGGVDSTVASKLMTEAIGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIKPKDGKEIQFLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGPGIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE
Protein: HEAT repeat-containing protein 1 (Protein BAP28) (U3 small nucleolar RNA-associated protein 10 homolog) [Cleaved into: HEAT repeat-containing protein 1, N-terminally processed] (Q9H583)
Organism: Homo sapiens (Human)
Function: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:38225354}.
Interaction partners:
- WD repeat-containing protein 36
- Transducin beta-like protein 3
- Ribosome biogenesis protein BMS1 homolog
- Protein RRP5 homolog
- Small subunit processome component 20 homolog
- Periodic tryptophan protein 2 homolog
- U3 small nucleolar RNA-interacting protein 2
- WD repeat-containing protein 3
- U3 small nucleolar RNA-associated protein 18 homolog
- RNA cytidine acetyltransferase
Sequence:
MTSLAQQLQRLALPQSDASLLSRDEVASLLFDPKEAATIDRDTAFAIGCTGLEELLGIDPSFEQFEAPLFSQLAKTLERSVQTKAVNKQLDENISLFLIHLSPYFLLKPAQKCLEWLIHRFHIHLYNQDSLIACVLPYHETRIFVRVIQLLKINNSKHRWFWLLPVKQSGVPLAKGTLITHCYKDLGFMDFICSLVTKSVKVFAEYPGSSAQLRVLLAFYASTIVSALVAAEDVSDNIIAKLFPYIQKGLKSSLPDYRAATYMIICQISVKVTMENTFVNSLASQIIKTLTKIPSLIKDGLSCLIVLLQRQKPESLGKKPFPHLCNVPDLITILHGISETYDVSPLLHYMLPHLVVSIIHHVTGEETEGMDGQIYKRHLEAILTKISLKNNLDHLLASLLFEEYISYSSQEEMDSNKVSLLNEQFLPLIRLLESKYPRTLDVVLEEHLKEIADLKKQELFHQFVSLSTSGGKYQFLADSDTSLMLSLNHPLAPVRILAMNHLKKIMKTSKEGVDESFIKEAVLARLGDDNIDVVLSAISAFEIFKEHFSSEVTISNLLNLFQRAELSKNGEWYEVLKIAADILIKEEILSENDQLSNQVVVCLLPFMVINNDDTESAEMKIAIYLSKSGICSLHPLLRGWEEALENVIKSTKPGKLIGVANQKMIELLADNINLGDPSSMLKMVEDLISVGEEESFNLKQKVTFHVILSVLVSCCSSLKETHFPFAIRVFSLLQKKIKKLESVITAVEIPSEWHIELMLDRGIPVELWAHYVEELNSTQRVAVEDSVFLVFSLKKFIYALKAPKSFPKGDIWWNPEQLKEDSRDYLHLLIGLFEMMLNGADAVHFRVLMKLFIKVHLEDVFQLFKFCSVLWTYGSSLSNPLNCSVKTVLQTQALYVGCAMLSSQKTQCKHQLASISSPVVTSLLINLGSPVKEVRRAAIQCLQALSGVASPFYLIIDHLISKAEEITSDAAYVIQDLATLFEELQREKKLKSHQKLSETLKNLLSCVYSCPSYIAKDLMKVLQGVNGEMVLSQLLPMAEQLLEKIQKEPTAVLKDEAMVLHLTLGKYNEFSVSLLNEDPKSLDIFIKAVHTTKELYAGMPTIQITALEKITKPFFAAISDEKVQQKLLRMLFDLLVNCKNSHCAQTVSSVFKGISVNAEQVRIELEPPDKAKPLGTVQQKRRQKMQQKKSQDLESVQEVGGSYWQRVTLILELLQHKKKLRSPQILVPTLFNLLSRCLEPLPQEQGNMEYTKQLILSCLLNICQKLSPDGGKIPKDILDEEKFNVELIVQCIRLSEMPQTHHHALLLLGTVAGIFPDKVLHNIMSIFTFMGANVMRLDDTYSFQVINKTVKMVIPALIQSDSGDSIEVSRNVEEIVVKIISVFVDALPHVPEHRRLPILVQLVDTLGAEKFLWILLILLFEQYVTKTVLAAAYGEKDAILEADTEFWFSVCCEFSVQHQIQSLMNILQYLLKLPEEKEETIPKAVSFNKSESQEEMLQVFNVETHTSKQLRHFKFLSVSFMSQLLSSNNFLKKVVESGGPEILKGLEERLLETVLGYISAVAQSMERNADKLTVKFWRALLSKAYDLLDKVNALLPTETFIPVIRGLVGNPLPSVRRKALDLLNNKLQQNISWKKTIVTRFLKLVPDLLAIVQRKKKEGEEEQAINRQTALYTLKLLCKNFGAENPDPFVPVLNTAVKLIAPERKEEKNVLGSALLCIAEVTSTLEALAIPQLPSLMPSLLTTMKNTSELVSSEVYLLSALAALQKVVETLPHFISPYLEGILSQVIHLEKITSEMGSASQANIRLTSLKKTLATTLAPRVLLPAIKKTYKQIEKNWKNHMGPFMSILQEHIGVMKKEELTSHQSQLTAFFLEALDFRAQHSENDLEEVGKTENCIIDCLVAMVVKLSEVTFRPLFFKLFDWAKTEDAPKDRLLTFYNLADCIAEKLKGLFTLFAGHLVKPFADTLNQVNISKTDEAFFDSENDPEKCCLLLQFILNCLYKIFLFDTQHFISKERAEALMMPLVDQLENRLGGEEKFQERVTKHLIPCIAQFSVAMADDSLWKPLNYQILLKTRDSSPKVRFAALITVLALAEKLKENYIVLLPESIPFLAELMEDECEEVEHQCQKTIQQLETVLGEPLQSYF