wanglab/gogpt-training-data huggingface dataset:
Protein: Protein MCM10 homolog (Q0VBD2)
Organism: Mus musculus (Mouse)
Function: Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7L590}. Note=Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase (By similarity). {ECO:0000250|UniProtKB:Q7L590}.
Interaction partners:
- Cell division control protein 45 homolog
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- Cell division control protein 6 homolog
- DNA replication licensing factor MCM3
- DNA replication factor Cdt1
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM2
- DNA helicase MCM8
Sequence:
MDVEEDDLCLLTSLLEENEAVLPCSSEKDKSLSLGDGDPDEFDELFDADGDGESYTEEAGSGEEGKTGNQEERLATLFGDVEDLTDDEVATSKVGNSGPPPAPSQEKTSEELQDELKKLQEQMKSLQEQLKAASIKQPPGTAPLQEPPDSSLQPLLKEKRIRRIQESACFSAELDVPTLPKAKRVARKPKTPAESSSRMRTPAQPLQVSSSFLEPNHSSSSRSSTPSPQAVPGNKCSRTIRNQNTVSPGNSGDRPQQVSQVSVEAFSGLRLRRPRVSSTEMSRKMAGRKLIRLPQIKEKMATENLEETDWVTFGVILRKVTPQSATSGQTFSIWKLNDLHDLTQCVSLFLFGDVHKDLWKTEQGTVIGLLNANPMKPKDGLKEVCLSIDHPQKVLIMGEAMDLGACKAKKKNGEPCTQTVNLHDCEYCQYHIQAQYKKLSAKRTDLQSTFSGGRIPKKFRKGTSLKERLCQDGFYYGGVSSESFAASRAAAIAPKKKVQTTLTNLVVRGTNSIIQETKQKLGIPQKSLSCSEEFRELMALPTFGARNLQKHLARAKASGSSKPAIQSISASALLKQQKQQMLEMRKRRSEDIQKRFLQSSSEVQSPAVPSSSRQAAAQSPRTGAEFPRLEGTATPRMPKLGRGISEGDDVLFFDDSPPPRPKLSAAAEAKKLAAIAKLRAKGQILTKVDPNNTVRKQMDGRAMLGVKERVENSNTVSPEEELEPARKKRREQLAYLESEEFQKILKAKSKHTDILKEAEAELQKSYFEPLVKKEQMEEKMRATREVKCRVVTCRTCTYTHFKPLETCVSEQHNLHWHDGVKRFFKCPCGNRTISLDKLPNKHCRNCGLYKWERDGMLKEKTGPKIGGETLLPRGEEHAKFLNSLK
Protein: Protein NEGATIVE REGULATOR OF RESISTANCE (NPR1-interactor) (Q5ZEF1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Acts as negative regulator of disease resistance. Acts on basal resistance, age-related resistance and resistance mediated by the LRR receptor kinase XA21. Plants over-expressing NRR display enhanced susceptibility to the bacterial blight Xanthomonas oryzae pv. oryzae (Xoo). Binds to and represses NPR1/NH1-mediated transcriptional activation of LG2 in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:16115061}.
Interaction partners:
Sequence:
MDATTTAKRKRPAASDIADDAPTTVDEVSDAEVEEFYAILRRMRDATRRLGARPPPPRAPAWRPSFSWEDFADAPPKQAPPPPQQPADHERVAENATPPRRPAPGLDLNVEPPSDAPATPRSARAPA
Protein: Lysine-rich arabinogalactan protein 18 (Lys-rich AGP 18) (Q9FPR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Lysine-rich arabinogalactan protein 19
- Arabinogalactan protein 12
- Classical arabinogalactan protein 4
- Arabinogalactan protein 15
- Classical arabinogalactan protein 6
- GLABROUS1 enhancer-binding protein-like 1
- Hydroxyproline O-galactosyltransferase GALT3
- Classical arabinogalactan protein 11
- Classical arabinogalactan protein 1
- Arabinogalactan protein 16
Sequence:
MDRNFLLTVTLICIVVAGVGGQSPISSPTKSPTTPSAPTTSPTKSPAVTSPTTAPAKTPTASASSPVESPKSPAPVSESSPPPTPVPESSPPVPAPMVSSPVSSPPVPAPVADSPPAPVAAPVADVPAPAPSKHKKTTKKSKKHQAAPAPAPELLGPPAPPTESPGPNSDAFSPGPSADDQSGAASTRVLRNVAVGAVATAWAVLVMAF
Protein: Cytosolic iron-sulfur assembly component 2A (Zgc:73185) (Q6PBY9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MELVSGLLSKALFLTGLSNETNDKRRKKMEEKALEVYDVIRTIRDPEKPNTLEELDVVTEKCVEVQELGDDEYLIVIKFSPTVPHCSLATLIGLCLQVKLQRCLPFKHKLEIYITEGTHSIEEDINKQINDKERVAAAMENPNLREIVEQCVTEPDD
Protein: Tubulin beta-4B chain (Tubulin beta-2C chain) (Q6P9T8)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P68372}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:P68372}.
Interaction partners:
- Tubulin alpha-1A chain
- Tubulin alpha-4A chain
- Tubulin alpha-1B chain
- Tubulin alpha-8 chain
- Tubulin alpha-1C chain
- Tubulin alpha chain
- Microtubule-associated protein tau
- Gap junction alpha-1 protein
- Tubulin alpha-3 chain
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTACLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEAEEEVA
Protein: mRNA-binding ribosome synthesis protein (Q59M49)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pescadillo homolog
- RNA-binding GTPase
- Ribosome biogenesis protein ERB1
- RNA-binding ribosome biosynthesis protein
- rRNA-binding ribosome biosynthesis protein
- rRNA-processing protein EBP2
- Ribosome production factor 2 homolog
- Nucleolar protein 2
- Nucleolar complex-associated protein 3
- Csi2p
Sequence:
MAKASKQTKKFQNKHLKHTIEQRKKVQAQNKKIASRKKSGSSSSGESNAPKRADGKAKEVFEDMSVDDFFGGGFEVPKEKNKNKNKQDTIEENEEEDSSSEEEDEEAMKENLKKLEADDPEFYKYLKDNDNDLLDFEAVNPLDAISDDEGDEDDDEEIEKEVPSDDDSEEEPTLGKVKGSKIEITKSLVKKWNQQLDKPTPKITRNILIAFKAAVNIHNSDSEDYKFSITDPKAFSELMLLVLKKVPISVQKLVKYKTNTQGVRTIPQKNQYATQIAAILKSHAGSFITLLNDITNTETAALILASIYEVFPFYLSHRRLLKQILTAVVNVWSSSSDIDTQISTFAFLNNVSREYPKSVLETVLKLTYSSFLQNCRKTNVHTMAQINFCKNSAVELFGINETLGYQVGFEYVRQLAIHLRNSINATSNAKEGYKTIYNWQYCHSLDFWSRVLSQHCNPEKELQNHKSKESPLRQLIYPLVQVTLGAIRLIPTAQFFPLRFYLIRSLIRLSQSTGVFIPLFPLISEILSSTAMTKAPKASTLQAVDFEHNIKVNQAYLGTRVYQDGLCEQFIELSGEFFGLYAKSIAFPELVTPAVLALRRFVKKSKNVKFNKQLQQLIEKLNANAVFITGKRSNVEYGPSNKAEVQQFLSDFEWEKTPLGQYVSVQRQLKAERLRILKEAQEEEAKAQAEQKKKEEEEDEQEDEDIVMEEEDDE
Protein: Transcription factor E2-alpha (Transcription factor 3) (Q56R80)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Stem cell protein
- Myogenic factor
- Myogenic factor
- Rhombotin-2
- Myogenin
Sequence:
MNDQQGHRMAVETDKELSDLLDFSAMFAPPVANGKTRPTTLASSQFGGSGLDERSGSSPWAAGEQGSPSFNHGRSYSEGSHYSEHDGLSSPFLSSGIGGKNERGPYPSFGAQQGFLPSDIVMANADAMSPSGLKSGSQFYPTFSNNPRRRPPDGNIDTQPKKIRKPPGLPSSVYASTSGDEYPRDSAGYPGSKPGPVYPGSFYMQEGLQPSSDPWASSGPLGQSGYSAMLGNSPHISQPGSFTAINPQDRMKRQPLPLSPQNYPLHGADVNGFHSGSGTYNHTSSVNGADSIMVSRSSATGSSGDEIGKALASIYPSDHNSNNFPSAPSTPVGSPQGIAGASQWPRSASQTALSPSYEGGLHALQNKMEDHLEEAIHVLRSHAVGQGPGSSLGGAHSDVHSLLSAVSASIHNGALGSLGQGFPGAGLALGSRHPAMGGSHHDDPACLPPSSSSLLPTSHASGTPQPAGAPEGFTSLPGGVATHSSNSSDIKREDKEDDENSSIADKSEEEKKDPKVSRNRTRKEAFSLQIHSSVSDQGEDKDDDEDDEDLPAEVKLEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSTDKPQTKLLILHQAVNVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDSPMQLPGPHPALGGDGHSSVGHI
Protein: ATP-dependent lipid A-core flippase (EC 7.5.2.6) (Lipid A export ATP-binding/permease protein MsbA) (Q9HUG8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01703}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01703}.
Interaction partners:
- Lipopolysaccharide export system protein LptC
- LPS-assembly protein LptD
- LPS-assembly lipoprotein LptE
- Bifunctional protein HldE
- Probable ATP-binding component of ABC transporter
- Toluene tolerance protein
- O-antigen ligase
Sequence:
MSDSPQNPGPSSLKIYFRLLGYVKPYIGMFLLSIVGFLIFASTQPMLAGILKYFVDGLSNPDAALFPNVQWPWLRDLHLVYAVPLLIILIAAWQGLGSFLGNFFLAKVSLGLVHDLRVALFNKLLVLPNRYFDTHSSGHLISRITFNVTMVTGAATDAIKVVIREGLTVVFLFLYLLWMNWKLTLVMLAILPVIAVMVTTASRKFRKQSKKIQVAMGDVTHVASETIQGYRVVRSFGGEAYEEKRFLDASQSNTDKQLRMTKTGAVYTPMLQLVIYVAMAILMFLVLWLRGDASAGDLVAYITAAGLLPKPIRQLSEVSSTVQRGVAGAESIFEQLDEAAEEDQGTVEKERVSGRLEVRNLSFRYPGTDKQVLDDISFIAEPGQMIALVGRSGSGKSTLANLVPRFYQHNDGKILLDGVEVEDYRLRNLRRHIALVTQQVTLFNDSVANNIAYGDLAGAPREEIERAAKAANAKEFIDNLPQGFDTEVGENGVLLSGGQRQRLAIARALLKDAPLLILDEATSALDTESERHIQAALDEVMKGRTTLVIAHRLSTIEKADLILVMDQGQIVERGSHAELLAQNGHYARLHAMGLDEQAPAPVG
Protein: Glycosylphosphatidylinositol anchor attachment 1 (A0A8I6A119)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLLSDPVRRRALARIVLRLNTPLCVLSYVAGIAWFLALAFPPLTQRTYMSENAMGSTMVEEQFVGGDRARNFARDFAAHRKKPGALPVAWLERAMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGPDTTNSQAVGLLLALAAHFRGQIYWAKDIIFLVTEHDLLGTEAWLEAYHDINVTGIQSSPLQGRAGAIQAAVALELSSDVVTSLDVTVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPQDWTSLEGPLQGLQTLLLMVLRQASGRPHGPHGLFLRYGVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFFYLLPALSRFVSIGLYMPATGFLLLVLGLKSVSLASLMAPLLISQAMGLALYFLPVLGQHVAAQHFPVAEAEAVVLTLLAIYVAGLALPHNTHRVVSSQVPDRGWMALKLVALIYLALQLGCIALLNFSLGFLLAATMVPAAALTKPHGPRTLYAALLVVTSPAVTLFGSLFLWRELQEVPLSLAEGWQLFLTALAQGVLEHYTYGALLFPILALGLYPCWLLFWNVLFWK
Protein: Endosomal maturation defective, isoform C (A0A0B4KH88)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFRSRSWFGGPWGGRPKNRLSLEHLKYLYSILEKNTTVSESNRGLLVESLRCIAEILIWGDQHDSLVFDFFLEKNMLSYFLHIMRQKSGGSSFVCVQLLQTLNILFENIRNETSLYYLLSNNHVNSIMVHKFDFSDEDVMGYYILFLKTLSLKLNTHTIHFFYNEHTNDFPLYTEAIKFFNHPESMVRIAVRTISLNVYKVQNPSMLRFIRDKTAAPYFSNLVWFIGKHILELDTCVRTDIDHQSNQKLSNLVAEHLDHLHYLSDILLLEIKDLNAVLTEHLLHKLFVPLYIFSLTPAPPPPSLAVVTQNLAAVLNRNVDIDIQEMHNPRVSSIVALFLLSLVFLVVSHAPLVHALAWVILNGDHSVFKEGAAEILNSYVEHREVVVPGFGEPDESLEQALDTVTGQSSSSSYALSEDSGVESSSPATTELDSQADAVEAEQIKLRNITDEEKQLLQKSSSSTKADFAEMAKPFLDTVLHALDCTENDYLALLSLCLIYAMSHNRASRIRLITVEIALELLVTFTRPSSDDSRCITAAQQDLLFSARNQSMVVIRNFYKSEDIFLDLFEDEYNEMRKAQLNVEFLCMDSTILLPPTGTPLTGINFTRRLPCGEVEKARRAIRVYFLLRRTCQKFLNEKESLLPLTNVVNLVQVENVLDLNNSDLIACTVVAKDSSKQRRFLVIDALQLILVEPDAKLLGWGVAKFVGFLQDVEVQGDKDDSRCLHITVHRGGVTHNRTPLLSAKFLFDDHIRCMAAKQRLTKGRSKARQKKMYQIAQLIEIPGQMDSPVYAVGGTMVASSSGGSGNSSGSSSRSSHHRPMFSTANRVPGFAAVLRGSNSAGVSRTQMAPNRSIEGIRNESAGRSRRRSPSSTSGSNLRADHSDRERSPSVSMGSHSSSQSRENSQPRSTGNRSRESSPRMPRPRSEEIPLEDFQHSRNNSPHSRGNPSPASRSHTPIRVLHYDQLSGHSGSPREASLGGTNALLSQLNGLNREVLPTQSSEETSFIGSDGNEATGGSEGRRRGAIETV
Protein: Porcupine O-acyltransferase (Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.250)) (B0S7W7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein Wnt
- Porcupine O-acyltransferase-like
- Protein Wnt-1
- Protein Wnt-5b
- Protein Wnt
- O-acyltransferase.
- O-acyltransferase
- O-acyltransferase
- Protein Wnt
- Protein Wnt
Sequence:
MGSLSRQAFFQELGSGCLLPTVQQGLEQVWQLLLICLVCRLSWRLGLPNFLKHLSTVVGGFYTLYLFFELHMVWVVLLSLLCYLILFLCRHSSSRGPFLSITILIYLLLGELHMMDTTTWHKMRGSQMVVAMKAVSLAFDLDKGIVDKVPSPVEFMGYIYFVGTVIFGPWISFNSYMDAVESRKLSVSWFMKSVISCVKSQLCLLISNCVAPYLFPYFIPVFGNKLLRKWLQAYENSLSFHFSNYFVSFLGETTTTLAGAGFTEEKDNLKWDMTIAKPLYVEFPRSMVEVVTSWNLPMSRWLNTYVFRKALRYGSFTAIIMTYTASALLHGLSFHIGAVLLTLGFITYIEHVLRKRLSAILNACVLSKRCPSDCKHRHKKELWVYLINGTFSMLALLHLTYLGSDFRPQDGVASHTIQKWTQLSWTSHWLTFALWVFYRLIL
Protein: H/ACA ribonucleoprotein complex subunit 2 (Nucleolar protein family A member 2) (snoRNP protein NHP2) (Q9NX24)
Organism: Homo sapiens (Human)
Function: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.
Subcellular location: Nucleus, nucleolus. Nucleus, Cajal body. Note=Also localized to Cajal bodies (coiled bodies).
Interaction partners:
- H/ACA ribonucleoprotein complex subunit DKC1
- H/ACA ribonucleoprotein complex subunit 1
- Nucleolar protein 58
- Telomerase Cajal body protein 1
- H/ACA ribonucleoprotein complex subunit 3
- Telomerase reverse transcriptase
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 56
- NHP2-like protein 1
- Ubiquitin-like protein FUBI
Sequence:
MTKIKADPDGPEAQAEACSGERTYQELLVNQNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMVLAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVKPHEEYQEAYDECLEEVQSLPLPL
Protein: Uncharacterized protein (Q38DG6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQTNERVVTTVDELTSRVAQRSNLSGDAVPFTPSFLQVPAASTTVPTTVTQQSGVVTVAHVRENGGKGMSEEGKLKRRNHNSKSGNRKANRDKDRKDVSTISPQQHGGESGGDLEMCQEEIVKALTLVAPIYNALEGMTEDEKLLLEGYLCNSGTNNESETYDIDEDDRLFVNDDDGINSEEEVWILQQMMDADARVCEQHEE
Protein: Guanyl-specific ribonuclease pgl-1 (Q304E5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEVSDLRVSKRTTRRERGSCNFDLVPIFFSVFLLFWFHPFHMEANKREIVDFGGLRSYFFPNLAHYITKNDEELFNNTSQANKLAAFVLGASKDAPGDEDILEMILPNDANAAVIAAGMDVCLLLGDKFRPKFDAAAEKLSGLGHAHDLVSVIDDDKKLGMLARKAKLKKTEDAKILQALLKVIAIDDAAEKFVELTELVSQLDLDFDVYVLTKILGLISEETSDEVDIIRDNVVNAFDSCKPLLKQLMLDGPKSEPADPFISLLMDPLEESVGKVVNHIAQLFEEASKNEGDESLVLRSQLGYQLFFLIVRSLADGKREVSKKILSGIPTSVRAEVFPGLQRSVYKSAVFLGNHIIQVLLGSKKSFEDWDVVGVAKDLESAWKRRAIAELIKKFQVSILEQCFDKPVPLIPQSPLNNDAVIDNVNKALQFALWLTEFYGSENETEALGELRFLDSTSKNLLVDSFKKFVQGINSKTHVTRIVESLEKCCLSDTPSGRKSNVQPSTSQQQDSAYTKEEMTTVHNTYSVNTKAQVLNGLSDTNSSGLLVDSKDSLSLQEISCDEVDSSTLLSSSRNIGEGVTVKAVDPVPEKVNDAQQQQTVNEIEMASDANQDTSSSASPEVAPSFSTDGWDSPTKSVALPPGMQQIDEEETTVADKDSTPQPQARAETAWGSGDATPMPLPAPTNQYKVSGFGEAKVAKGFGQFAPTSSAYGGGGGRGGYGGGDRGGRGGYGGDRGGRGGYGGGDRGGRGGYGGDRGRGGYGGRGGRGGF
Protein: Glutathione-specific gamma-glutamylcyclotransferase 1 (Gamma-GCG 1) (EC 4.3.2.7) (Cation transport regulator-like protein 1) (Q5SPB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Glutathione depletion is an important factor for apoptosis initiation and execution. Acts as a pro-apoptotic component of the unfolded protein response pathway by mediating the pro-apoptotic effects of the ATF4-ATF3-DDIT3/CHOP cascade. Negative regulator of Notch signaling pathway involved in embryonic neurogenesis: acts by inhibiting Notch cleavage by furin, maintaining Notch in an immature inactive form, thereby promoting neurogenesis in embryos.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BUX1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8R3J5}.
Interaction partners:
- Gamma-glutamylcyclotransferase a
- Gamma-glutamylcyclotransferase b.
- 5-oxoprolinase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase.
- Aminopeptidase
- Glutathione synthetase
- Glutathione peroxidase
- Glutathione peroxidase
Sequence:
MKPQDIVAGKSSLWIFGYGSLVWKPDFKYKRSKVGYIKGYKRRFWHGDNFHRGDDEMPGRVVTLIEEDDVCTWGVAFEVTGSQMEESLKYLNVREAVRGGYLTRAVDFFPRGTNQPPVQALVYIATPDNPIYLGPASTEEIASQIAVCKGNSGHNIEYLLRLAEFMRVSCPDVDDPHLFSIEAALLATIRPILLAA
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Ribophorin-2) (Q7K110)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU366029}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU366029}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- GH11935p
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- DSec61alpha
- Inactive rhomboid protein 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Malectin domain-containing protein
Sequence:
MLKLGLVIFCVLVASGPTWSARTVDSHLGQKDLSRLQKVFVDGFGSSDLQSIFFSSLNIQLTDATQKEPLCKKIATLHSESKLNSFEKDYYYIGASRNLGCSAKIDEGLLSKVYSSLNSELGSSQEIFYRVVTHKVLGVEINEATQEKLVKRLQELLKKDDTLSGLGYAFNVAPLLGASASFIANRVEDAIVQADEVDGKLLQFEGGLSITSLIINGAFGVSKTFNKPVPITADQAVKFANYFLSRRSVQTAKGAHVLIEALKTISGADKIAPVCVQLIGNGQLDAQSPTLNVAVVDLLGKPLSPAPKVINAKVIRKKDSSVLADKITVASKSSDKTTYVADLASLKPARGVYQAELSADGVYTQTLQFKVLGRVKVQSLEVGIAESDASAATRKQSVTYPGKLQEVLSADSTQKLLLKAVLVDESTSKPLAVHQAFVRLYNKKTDKEIIFVAEQDSSKAYKFDMDVGNNGKNFNYQSGTYSIYLTVGDSSLSNSFEWLVAEVQLKFNEDKEVKPKNTSGPLPEIIHQFRVPDKRPPRIVSDIFTGLCITPLVLLFVFWGKLGINVSNLTLAPSTIGFHLGFGGILVLFFVFWLQLNMFQTLRLLIPIAVFTFLAGNRLLRRLYAQRNSKASAS
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q8IIK8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
- Ran-specific GTPase-activating protein 1, putative
- Nucleoporin NUP221, putative
- Cysteine proteinase falcipain 1
- Falcipain-3
- Serine repeat antigen 3
- ADP/ATP translocase
- Thioredoxin-like protein
Sequence:
MNKLVSIILVIFFLFHKYALCAEEHEITHKTYFDITIDDKPLGRIVFGLYGKVAPKTVENFVSICKGTVVDGKMLHYTNSIFHRIIPNFMAQGGDITNFNGTGGLSIYGKKFEDENFKVNHSKRGLLSMANAGKNTNGSQFFILFIPTPWLDGRHVVFGEVVEGLDKLVHIEAVGTDSGEPLKRVLVKESGELPL
Protein: Heat shock 70 kDa protein 3 (AtHsp70-3) (Heat shock protein 70-3) (Heat shock cognate 70 kDa protein 3) (AtHsc70-3) (Heat shock cognate protein 70-3) (O65719)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:14505352}. Nucleus matrix {ECO:0000269|PubMed:14505352}.
Interaction partners:
- Heat shock protein 90-2
- Heat shock protein 90-3
- Heat shock 70 kDa protein 17
- Heat shock protein 90-1
- Chaperone protein dnaJ 2
- Chaperone protein dnaJ 3
- Ankyrin repeat family protein
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Heat shock protein 90-4
- Hsp70-Hsp90 organizing protein 3
Sequence:
MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFTDSSVQSDIKLWPFTLKSGPAEKPMIVVNYKGEDKEFSAEEISSMILIKMREIAEAYLGTTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGIDFYAPITRARFEELNIDLFRKCMEPVEKCLRDAKMDKNSIDDVVLVGGSTRIPKVQQLLVDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVDAKNALENYAYNMRNTIRDEKIGEKLAGDDKKKIEDSIEAAIEWLEANQLAECDEFEDKMKELESICNPIIAKMYQGGEAGGPAAGGMDEDVPPSAGGAGPKIEEVD
Protein: Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (Biosynthesis of nicotinic acid protein 7) (N-formylkynurenine formamidase) (FKF) (Q04066)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Interaction partners:
- Indoleamine 2,3-dioxygenase
- Kynureninase
- Kynurenine 3-monooxygenase
- Probable kynurenine--oxoglutarate transaminase BNA3
- Formate dehydrogenase 1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- 3-hydroxyanthranilate 3,4-dioxygenase
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Phosphoenolpyruvate carboxykinase
Sequence:
MSNTVRAISPDITLFNKTLTFQEISQNTREAVIYIHGGAWNDPENTPNDFNQLANTIKSMDTESTVCQYSIEYRLSPEITNPRNLYDAVSNITRLVKEKGLTNINMVGHSVGATFIWQILAALKDPQEKMSEAQLQMLGLLQIVKRVFLLDGIYSLKELLVEYPEYDCFTRLAFPDGIQMYEEEPSRVMPYVKKALSRFSIDMHLVHSYSDELLTLRQTNCLISCLQDYQLSFKLYLDDLGLHNDVYKNGKVAKYIFDNIC
Protein: Cytochrome c oxidase subunit 6B2 (Cytochrome c oxidase subunit VIb isoform 2) (COX VIb-2) (Cytochrome c oxidase subunit VIb, testis-specific isoform) (Q80ZN9)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00429}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00429}; Intermembrane side {ECO:0000250|UniProtKB:P00429}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 4 isoform 2, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MLGVQAQKPPPGQWTTPPFDPRFPNQNQTRNCYQNFLDYHRCVKTMNRRGKSTQPCEYYFRVFHSLCPISWVQRWNEQIKQGTFPGKI
Protein: Pescadillo homolog (Lipid depleted protein 7) (Q95Y89)
Organism: Caenorhabditis elegans
Function: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}.
Interaction partners:
- Guanine nucleotide-binding protein-like 3 homolog
- Ribosome biogenesis protein BOP1 homolog
- Ribosome biogenesis protein NSA2 homolog
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein WDR12 homolog
- Nucleolar complex protein 2 homolog
- Probable rRNA-processing protein EBP2 homolog
- Brix domain-containing protein F44G4.1
- ATP-dependent RNA helicase
- WD repeat-containing protein 74
Sequence:
MKDRFKQKYTAGAAVAYMSRKQALKKLQLTLKDFRRLCIIKGIYPHEPAHKKQANKGSTANKVFYYRKDINFLAHEPIINKFRDYKVFLRKLNHLKAKKEEDKLKKLYENKPVYSLDTIVKERFPTFGSALRDMDDALSLCFTFAMLPHTRVLKEGMIDSCRKLTAEFMHYVIESQSLRNTFISIKGIYYQAEVHGEKITWVVPHERGLPHVTDVDFTVLVTFVEFYIAMLGFVNFKLYQDIGLFYPPQIGQVVKTDEMETEEYKEKVYSLAKPLAKRKDVEQAEDDEPLDLLGEDSDALAQKVREAKSIKTMFKGCVFYLNRECPKEALTFIIRNGGGIVGWEGGPTDLKADSKNISHHVVDRPMDKLEVNRLYVQPQWVFDCLNARRKLPTERYMPGVALPPHFSPFTSEKAGDYIPFERLEELRSMGKDVSDLEAAIPKTMDELPMRRKEVKPEKPKGIHIAVGQMHKKSKEKFHETVEKGQELKMRELMISKKHQRVYHSMKTTFKRNRNDALKLKKKAKLAKATEA