wanglab/gogpt-training-data huggingface dataset:
Protein: Cysteine and histidine-rich domain-containing protein morgana (Q9VCC0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates centrosome duplication and mitotic spindle dynamics. Also involved in controlling the size of dendritic arbors. May act as co-chaperone for Hsp83. During mitotic spindle assembly, regulates microtubule (MT) dynamics by binding to MTs and promoting MT polymerisation. Promotes the elongation and retraction of terminal branches in response to changes in body size, possibly acting downstream of the TORC2 pathway to enable proportional scaling of dendritic arbors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31907206}. Nucleus {ECO:0000269|PubMed:31907206}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:31907206}. Note=In syncytial embryos, mostly cytoplasmic during interphase, with enrichment in the perinuclear area and a weak nuclear localization. Upon nuclear envelope breakdown, localizes to the spindles and remains associated with the spindle microtubules throughout mitosis. {ECO:0000269|PubMed:31907206}.
Interaction partners:
- CG9617 protein
- Heat shock protein 83
- Heat shock protein 83
- protein-serine/threonine phosphatase
- LD23779p
- Heat shock protein 75 kDa, mitochondrial
Sequence:
MEQCYNRGCGQLFDPQTNNDESCRHHPGEPFFHDAYKGWSCCNKKSVDFTEFLNIKGCTLAKHSNVKPPEPEKPVKDESDKDEVIEVRAPIREALPRPPIDSPLTVIQPTVAPALKDMVFAVKTPAAQKSSDAIEVGTTCKNNGCTYSFTGNSSDFGECTYHPGVPIFHEGMKFWSCCQKRTSDFSQFMAQKGCTYGEHKWVKENDDKKVVQCRYDWHQTATNVVMAIYAKKYDYSQSVIELNPIRLHVNLVFPEQDNARFDLDLELRGIVNVSNASAHMYGTKVEIKLPKLEPGSWSNLNFPNKKLPVVKKSQVEEKKKQEESDEEFFDLDDIKAETSFRLSEMSMQSPNNLD
Protein: Truncated cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase (V9H0I4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MWLYLVALVGLWTLLCFFRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEQLRNKTSDRLETVILDVTKTESIVAATQWVKERVGNRGLWGLVNNTGISVPSGPSQWMDKQNFASILDVNLLGMIEVTLSMLPLVRKARGRVVNVSSIVG
Protein: Large ribosomal subunit protein mL53 (39S ribosomal protein L53, mitochondrial) (L53mt) (MRP-L53) (Q9D1H8)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96EL3}.
Interaction partners:
- Large ribosomal subunit protein mL50
- 39S ribosomal protein L40
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL29m
- Small ribosomal subunit protein mS33
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL51
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein uL10m
- Small ribosomal subunit protein mS31
Sequence:
MAAALARLGLRPVKLVRVQFCPFEKNVESTRTFLQTVSSEKVRATNLNCSVIADVRHDGSEPCVDVLFGDGYRLIMRGAHLTTQEMLSALASHIRDRNAAAASAPGADKVAPGTSTRR
Protein: Gag polyprotein (Pr71Gag) [Cleaved into: Gag protein (p68Gag); p3 (p3Gag)] (Q87039)
Organism: Simian foamy virus (isolate chimpanzee) (SFVcpz)
Function: Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity).
Subcellular location: [Gag protein]: Virion. Host nucleus. Host cytoplasm. Note=Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal. In the late phases of infection, Gag proteins assemble in the cytoplasm to form the virion's capsids (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [p3]: Virion {ECO:0000250}.
Interaction partners:
Sequence:
MASGSNVEEYELDVEALVVILRDRNIGRNPLHGEIIGLRLTEGWWGQLERFQMVRLILQDEDNEPLQRPRHEIIPRAVNPHTMFVLSGPLAELQLAFQDLDLPEGPLRFGPLANGHYVEGDPYSRSYRPVTMAETAQMTRDELEDTLNTQSEIEIQMINLLELYEVETRALRRQLAERSSIGQGGISPGASHSRPPVSSFSGLPSLPAIPGIHTRAPSPPRATSTPGNIPRSLGDDNMPSSSFAGPSQPRVSFHPGNPFAEAEGHRPRSQSRERRRDIPSAPVISAPVPSAPPMIQYIPVPPPPPVGAVIPIQHIRSVTGEPPRNPREIPIWLGRNAPAIDGVFPTTTPDLRCRIINALLGGNLGLSLTPGDCITWDSAVATLFIRTYGQYPLHQLGNVLKGIADQEGVATAYTLGMMLSGQNYQLVSGIIRGYLPGQAVVTAMQQRLDQEIDDQTRAETFIQHLNAVYEILGLNARGQSIRASVTPQPRPSRGRGRGQSAPEPSQGPVNSGRGRQCPAPGQNDRGSNIQNQGQENSSQGGYNLRSRTYQPQRYGGGRGRRWNENTNNSETRPTEQSPQTPRPIQAGSGVRGNQSQTYKPAAGRGGRGNQNRNQRSSGAGDSRAVNTVTQSATSSTDESSSTTTAAPSGGQGN
Protein: UDP-glucuronosyltransferase 3A1 (UDPGT 3A1) (EC 2.4.1.17) (Q6NUS8)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- UDP-galactose translocator
- Exostosin-2
Sequence:
MVGQRVLLLVAFLLSGVLLSEAAKILTISTLGGSHYLLLDRVSQILQEHGHNVTMLHQSGKFLIPDIKEEEKSYQVIRWFSPEDHQKRIKKHFDSYIETALDGRKESEALVKLMEIFGTQCSYLLSRKDIMDSLKNENYDLVFVEAFDFCSFLIAEKLVKPFVAILPTTFGSLDFGLPSPLSYVPVFPSLLTDHMDFWGRVKNFLMFFSFSRSQWDMQSTFDNTIKEHFPEGSRPVLSHLLLKAELWFVNSDFAFDFARPLLPNTVYIGGLMEKPIKPVPQDLDNFIANFGDAGFVLVAFGSMLNTHQSQEVLKKMHNAFAHLPQGVIWTCQSSHWPRDVHLATNVKIVDWLPQSDLLAHPSIRLFVTHGGQNSVMEAIRHGVPMVGLPVNGDQHGNMVRVVAKNYGVSIRLNQVTADTLTLTMKQVIEDKRYKSAVVAASVILHSQPLSPAQRLVGWIDHILQTGGATHLKPYAFQQPWHEQYLIDVFVFLLGLTLGTMWLCGKLLGVVARWLRGARKVKKT
Protein: Protein CbbY (RuCbby) (EC 3.1.3.-) (P95649)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Function: Highly selective xylulose-1,5-bisphosphate (XuBP) phosphatase. Shows also activity towards ribulose-1,5-bisphosphate (RuBP) and fructose-1,6-bisphosphate (FBP), but not towards fructose-6-phosphate (F6P) or ribulose-5-phosphate (Ru5P). Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself.
Interaction partners:
Sequence:
MIEAILFDVDGTLAETEELHRRAFNETFAALGVDWFWDREEYRELLTTTGGKERIARFLRHQKGDPAPLPIADIHRAKTERFVALMAEGEIALRPGIADLIAEAKRAGIRLAVATTTSLPNVEALCRACFGHPAREIFDVIAAGDMVAEKKPSPDIYRLALRELDVPPERAVALEDSLNGLRAAKGAGLRCIVSPGFYTRHEEFAGADRLLDSFAELGGLAGLDLTAPVA
Protein: Rolling pebbles, isoform G (M9PF75)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MPSLQQIALAMEGDQSELQTPPLPINPPPKVMANGIVYGFRTRHLSCIEENDSDSLHGSSIPHAYDMMQQADETFQKLNANEEQDESGSEDGGLENLDDTIAMIDESRLLEADYLDELVAEEQLQEQDEDEEESSDLVDSGNVEEDFWQPSFNRNDIMMTSVYGALNGSLTSEVSSTAAPGYSECATPRKEAEPVYATPEKRRASNRSFDSTCASLTSSLYGGSMNSSLDLKYSSLGGGDSVSGGISGTSTLRGTSVPPMDLSMISSDGVSALDWGSASVSCVLDSGDGNPAEELNEEMAAKCLSAAESDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSSSMSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: Periodic tryptophan protein 2 homolog (Q15269)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 6 homolog
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 4 homolog
- U3 small nucleolar RNA-interacting protein 2
- Transducin beta-like protein 3
- WD repeat-containing protein 36
- Nucleolar protein 6
- WD repeat-containing protein 43
- U3 small nucleolar ribonucleoprotein protein MPP10
- WD repeat-containing protein 3
Sequence:
MKFAYRFSNLLGTVYRRGNLNFTCDGNSVISPVGNRVTVFDLKNNKSDTLPLATRYNVKCVGLSPDGRLAIIVDEGGDALLVSLVCRSVLHHFHFKGSVHSVSFSPDGRKFVVTKGNIAQMYHAPGKKREFNAFVLDKTYFGPYDETTCIDWTDDSRCFVVGSKDMSTWVFGAERWDNLIYYALGGHKDAIVACFFESNSLDLYSLSQDGVLCMWQCDTPPEGLRLKPPAGWKADLLQREEEEEEEEDQEGDRETTIRGKATPAEEEKTGKVKYSRLAKYFFNKEGDFNNLTAAAFHKKSHLLVTGFASGIFHLHELPEFNLIHSLSISDQSIASVAINSSGDWIAFGCSGLGQLLVWEWQSESYVLKQQGHFNSMVALAYSPDGQYIVTGGDDGKVKVWNTLSGFCFVTFTEHSSGVTGVTFTATGYVVVTSSMDGTVRAFDLHRYRNFRTFTSPRPTQFSCVAVDASGEIVSAGAQDSFEIFVWSMQTGRLLDVLSGHEGPISGLCFNPMKSVLASASWDKTVRLWDMFDSWRTKETLALTSDALAVTFRPDGAELAVATLNSQITFWDPENAVQTGSIEGRHDLKTGRKELDKITAKHAAKGKAFTALCYSADGHSILAGGMSKFVCIYHVREQILMKRFEISCNLSLDAMEEFLNRRKMTEFGNLALIDQDAGQEDGVAIPLPGVRKGDMSSRHFKPEIRVTSLRFSPTGRCWAATTTEGLLIYSLDTRVLFDPFELDTSVTPGRVREALRQQDFTRAILMALRLNESKLVQEALEAVPRGEIEVVTSSLPELYVEKVLEFLASSFEVSRHLEFYLLWTHKLLMLHGQKLKSRAGTLLPVIQFLQKSIQRHLDDLSKLCSWNHYNMQYALAVSKQRGTKRSLDPLGSEEEAEASEDDSLHLLGGGGRDSEEEMLA
Protein: Fgr17p (A0A1D8PQ80)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- mRNA-decapping enzyme subunit 1
Sequence:
MSSKSRSYVSIACDNCRKRRRKCNGELPCHYCSGKNKPCVYDKTKDKRRRRVDLVYVDYLEHKYNNLLNFVKRIRSTTKDERLRAQCNEMLANNDPKFIDNKDLGLSNDESTHNNQSDKQQKEIIQLDNPMDELVSMKWELKFDESGNTKFLGPPVRQVDRCLVKDSMVAMEDPERVSYFNETVLADTEFMKELINTFFQNLLPFNLVLEEINVDEITREITSMTGKRSCYEAVSCLHLLALAILAYGFSILPKDHPYFQNLNGWNPFLSIVERSLFKLLRKSSHTTTGNLIDHSHIVYTILIITILHLGNYDESQAWVYSSILCSQIQHVGWNVSTDYPSESNDLSKFRSKLFWNCLVVEKISASMFGRSSPINFRQLLTDFYTSETKDINELVFQFNSKLWFIYDKFMGQVYSFHFNTQNKMLYKKVLMTATQSFQDFQGFMNQYLPLNETNLDNQNIILLHLTFHVFLLLIIRPYMKMPEIAGSIFQKSISITEQCYILINQYNSKFGNGVTTGWYNCHYGFLLYQVSVFLLCAIPVHDSVGPPGQHNVLIQRLHLFLQCLKNGSKYLPVYNVYYQTLLNIFNNMTLDEEISILVRQAYENESIEVKTSSVEKEDLVLDFDQDWQSYVNSLNLELNQDVYSYLEEGILDML
Protein: Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2 (PFP 2) (6-phosphofructokinase, pyrophosphate dependent 2) (PPi-PFK 2) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 2) (Q9C9K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- transaldolase
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
- Fructose-bisphosphate aldolase 6, cytosolic
Sequence:
MDSDFGIPRELSPLQQLRSQYHPELPPCLQGTTVRVELGDGTTVAKAGDAHIIARAFPHTLGQPLAHFLRATAKVADAQIITEHPVKRVGIVFCGRQAPGGHNVVWGLYEALKVHNAKNTLLGFLGGSEGLFAQKTLEITDEVLQTYKNQGGYDMLGRTKDQIRTTEQVNAALKACTDLKLDSLVIIGGVTSNTDAAHLAEFFAEAKCSTKVVGVPVTINGDLKNQFVEANVGFDTTCKVNSQLISNICTDALSAEKYYYFVRLMGRKHSHVALECTLQSHPNMVILGEEVTASKLTIFDIIKQICDAVQARAEQDKNHGVILIPEGLVESIPELYALLKEIHGLLKEGVQVDNISTQLSSWSSALFEFLPPFIKKQLLLHPESDDSAQLSQIETEKLLAYLVETEMNKRLKEGTYKGKKFNAICHFFGYQARGSLPSKFDCDYAYVLGHVCYHILAAGLNGYMATVTNLKSPVNKWKCGAAPISAMMTVKRWSQNSGSTTIGRPVIHPASVDLKGKAYDLLRQNAQKFLMEDMYRNPGPVQYDGPGADAKAVSLCVEDQDYMGKIKKLQEYLDQVRTIVKPGCSQDVLKAALSVMASVTDVLTTISSSSTSGQQFA
Protein: Chemotaxis protein CheA (EC 2.7.13.3) (Q8KLS7)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Interaction partners:
Sequence:
MSAPVEAGPDGGLLRVSSEKIGRLMDLVGELSLSVAETVHSPDLEGLELPAFDGAVHRLRMIVREVQDAATELRLVPVEEVFKRLRRMVRELERQTGKKIEMVFEGAETAIDKLVADQLYDPLLHVVRNSADHGLEPPEERRAAGKPETGRIVLAAAQAGSEVRISVADDGRGLSRPKILKRARERGLFGPDEEPEPATLWKVIFEPGFSTAEAVTNLSGRGVGMDVLNATMTALRGRIGVDSRDGQGSEVSLHIPVSLAFLDCIILRLGARLYALPIDAVSEIVQPKPCDLMGVGAAGGSEMLRLRGHWIPVCRLERFYGEAPSAVPPPAGQVLAVVSTATGLIALPVDEVLDRQQVVMKPLTGRLAQVRASWGCALLGTGEVALVLDGNRLAAGGAA
Protein: Probable transcriptional regulator WhiB7 (Q6MX01)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The apo- but not holo-form probably binds DNA (By similarity). Acts as a transcriptional regulator. Probably redox-responsive. Upon overproduction at least 10 other genes are up-regulated, among them are Rv1258c, Rv1988, Rv2301, Rv2416c, Rv2725c and whiB7 itself. Probably redox-responsive. The apo-form has been shown to act as a protein disulfide reductase.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- RNA polymerase sigma factor SigA
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- N-acetyltransferase Eis
- DNA-directed RNA polymerase subunit alpha
- RNA polymerase-binding protein RbpA
- 16S/23S rRNA
- RNA polymerase-binding transcription factor CarD
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor SigB
Sequence:
MSVLTVPRQTPRQRLPVLPCHVGDPDLWFADTPAGLEVAKTLCVSCPIRRQCLAAALQRAEPWGVWGGEIFDQGSIVSHKRPRGRPRKDAVA
Protein: Ubl carboxyl-terminal hydrolase 18 (EC 3.4.19.12) (43 kDa ISG15-specific protease) (ISG15-specific-processing protease) (Ubl thioesterase 18) (Q9WTV6)
Organism: Mus musculus (Mouse)
Function: Interferon-induced ISG15-specific protease that plays a crucial role for maintaining a proper balance of ISG15-conjugated proteins in cells. Regulates protein ISGylation by efficiently cleaving ISG15 conjugates linked via isopeptide bonds. Regulates T-cell activation and T-helper 17 (Th17) cell differentiation by deubiquitinating TAK1, likely to keep TAK1-TAB complexes in steady conditions. In turn, restricts activation of NF-kappa-B, NFAT, and JNK as well as expression of IL2 in T-cells after TCR activation. Acts as a molecular adapter with USP20 to promote innate antiviral response through deubiquitinating STING1. Involved also in the negative regulation of the inflammatory response triggered by type I interferon. Upon recruitment by STAT2 to the type I interferon receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I interferon signaling pathway.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon alpha/beta receptor 2
- 2'-5'-oligoadenylate synthase-like protein 2
- Interferon-induced protein 44
- Interferon regulatory factor 7
- Antiviral innate immune response effector IFIT1
- Receptor-transporting protein 4
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Antiviral innate immune response receptor RIG-I
Sequence:
MGKGFGLLRKPCQSVVAEPQQYSALEEERTMKRKRVLSRDLCSAWDSPHGLVGLHNIGQTCCLNSLLQVFMMNMDFRMILKRITVPRSAEERKRSVPFQLLLLLEKMQDSRQKAVLPTELVQCLQKYNVPLFVQHDAAQLYLTIWNLTKDQITDTDLTERLQGLFTIWTQESLICVGCTAESSRRSKLLTLSLPLFDKDAKPLKTLEDALRCFVQPKELASSDMCCESCGEKTPWKQVLKLTHLPQTLTIHLMRFSARNSRTEKICHSVNFPQSLDFSQVLPTEEDLGDTKEQSEIHYELFAVIAHVGMADFGHYCAYIRNPVDGKWFCFNDSHVCWVTWKDVQCTYGNHRYRWRETAYLLVYTKTGS
Protein: Phosphatidylinositol-glycan biosynthesis class F protein (PIG-F) (O09101)
Organism: Mus musculus (Mouse)
Function: Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10781593}; Multi-pass membrane protein {ECO:0000269|PubMed:10781593}.
Interaction partners:
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI ethanolamine phosphate transferase 2
- GPI alpha-1,2-mannosyltransferase 3
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGU
Sequence:
MKDTDIKRLLYTNLLCVFSIFLSIFIPSFFVDNFSVLEAHLTWLCICSASVTTVNLLSYLVVKPNVSSKRSSLSHKVTRALKCCVCFLMSCFLLHIIFVLYGAPLIELVLETFLFAVVLSTFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFTGAWLGAFPIPLDWERPWQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
Protein: MYG1 protein YER156C (P40093)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Deoxyhypusine hydroxylase
Sequence:
MNSVKRVKLNSKMSKQICTHSGSFHADESLAVYMLRLLPEFKDAKLVRSRNPKDWEASDILVDVGAQYDGVKFFDHHQRGFFETFNEKYKTKLSSAGLIFKHYGRDIIKTILNNKVSSSDLDLLYDKVYKQFVEALDANDNGISKYTIPKDSNLEPNFRDNAISIPGIISGMNPNWNEDTSDESFDRCFARASEFIGGVFVTLVRGYGQSWLPAKALVAQAIDERMDVDKSGKIIVLPQFCPWKEHLYELEREKNIEKQIEFVLFTDSSGAWRVSTVPINSTSFQFRRGLPEPLRGLRDEELSTKSGVPGCIFIHAAGFIGGAKSKEAVYELAKMSLA
Protein: ADAM metallopeptidase with thrombospondin type 1 motif 8 (F1S6D3)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MIWTNSASRSLGWDSATAPTHLRRISAPSSGATWMAQSPSAIRRTAACPGPMGRPVGPGASAGMAAVCLRRKWRSPSPWWMEAGPRGDPGESVRGPVEEEYSFHTASARTRSLRTEGDTAWVGEPSTSRATQRSVPLMGKASGSSSVRSTTPTTTQTWKGTSCSGSPSTRGCLPETAASCSAEPGGGVSSKCSRPSYGYNDIVTIPAGATNIDVKQRSHPGVQNDGNYLALKTADGQYLLNGNLAISAIEQDILVKGTILKYSGSIATLERLQSFRPLPEPLTVQLLTVPGEVFPPKVKYTFFVPNDVNFSIQSSKERATTNVIQPLLNAQWVLGDWSECSSSCGAGWQRRAVECLDPSGQASTTCDEALKPEDAKPCGSQPCPL
Protein: Biphenyl 2,3-dioxygenase subunit alpha (EC 1.14.12.18) (Biphenyl dioxygenase system, oxygenase component subunit alpha) (BDO, oxygenase component subunit alpha) (Rieske dioxygenase) (Terminal oxygenase component of biphenyl dioxygenase, large subunit) (Q53122)
Organism: Rhodococcus jostii (strain RHA1)
Function: Part of the oxygenase component of the biphenyl dioxygenase system that catalyzes the stereospecific dihydroxylation of the aromatic ring of biphenyl, yielding a dihydrodiol compound. Is essential for biphenyl degradation and growth of Rhodococcus sp. strain RHA1 on biphenyl as the sole source of carbon and energy. Can also use naphtalene and 4-chlorobiphenyl (4-CB) as substrates, as well as some polychlorinated biphenyls (PCB) such as 2,2'-dichlorobiphenyl, 2,3-dichlorobiphenyl and 2,5,2'-trichlorobiphenyl. Exhibits weak activity toward dibenzofuran and dibenzo-p-dioxin. Electrons are transferred from NADH to the [2Fe-2S] cluster in BphA1 via FAD of BphA4 and [2Fe-2S] cluster of BphA3.
Interaction partners:
Sequence:
MTDVQCEPALAGRKPKWADADIAELVDERTGRLDPRIYTDEALYEQELERIFGRSWLLMGHETQIPKAGDFMTNYMGEDPVMVVRQKNGEIRVFLNQCRHRGMRICRADGGNAKSFTCSYHGWAYDTGGNLVSVPFEEQAFPGLRKEDWGPLQARVETYKGLIFANWDADAPDLDTYLGEAKFYMDHMLDRTEAGTEAIPGIQKWVIPCNWKFAAEQFCSDMYHAGTTSHLSGILAGLPDGVDLSELAPPTEGIQYRATWGGHGSGFYIGDPNLLLAIMGPKVTEYWTQGPAAEKASERLGSTERGQQLMAQHMTIFPTCSFLPGINTIRAWHPRGPNEIEVWAFTVVDADAPEEMKEEYRQQTLRTFSAGGVFEQDDGENWVEIQQVLRGHKARSRPFNAEMGLGQTDSDNPDYPGTISYVYSEEAARGLYTQWVRMMTSPDWAALDATRPAVSESTHT
Protein: Capsid protein VP1 (P24029)
Organism: Aleutian mink disease parvovirus (strain G) (ADV)
Function: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 25 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 (10% abundance) and VP2 (90% abundance), which differ by the presence of an N-terminal extension in the minor protein VP1. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. VP1 binds DNA and may therefore play a role in viral DNA encapsidation.
Subcellular location: Virion {ECO:0000269|PubMed:12692232}. Host nucleus {ECO:0000269|PubMed:12692232}.
Interaction partners:
Sequence:
MSKIPQHYPGKKRSAPRHVFIQQAKKKKQTNPAVYHGEDTIEEMDSTEAEQMDTEQATNQTAEAGGGGGGGGGGGGGGGGVGNSTGGFNNTTEFKVINNEVYITCHATRMVHINQADTDEYLIFNAGRTTDTKTHQQKLNLEFFVYDDFHQQVMTPWYIVDSNAWGVWMSPKDFQQMKTLCSEISLVTLEQEIDNVTIKTVTETNQGNASTKQFNNDLTASLQVALDTNNILPYTPAAPLGETLGFVPWRATKPTQYRYYHPCYIYNRYPNIQKVATETLTWDAVQDDYLSVDEQYFNFITIENNIPINILRTGDNFHTGLYEFNSKPCKLTLSYQSTRCLGLPPLCKPKTDTTHKVTSKENGADLIYIQGQDNTRLGHFWGEERGKKNAEMNRIRPYNIGYQYPEWIIPAGLQGSYFAGGPRQWSDTTKGAGTHSQHLQQNFSTRYIYDRNHGGDNEVDLLDGIPIHERSNYYSDNEIEQHTAKQPKLRTPPIHHSKIDSWEEEGWPAASGTHFEDEVIYLDYFNFSGEQELNFPHEVLDDAAQMKKLLNSYQPTVAQDNVGPVYPWGQIWDKKPHMDHKPSMNNNAPFVCKNNPPGQLFVKLTENLTDTFNYDENPDRIKTYGYFTWRGKLVLKGKLSQVTCWNPVKRELIGEPGVFTKDKYHKQIPNNKGNFEIGLQYGRSTIKYIY
Protein: Cohesin subunit SA-1 (SCC3 homolog 1) (Stromal antigen 1) (Q9D3E6)
Organism: Mus musculus (Mouse)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750}. Chromosome {ECO:0000250}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation (By similarity). {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein 1A
- Structural maintenance of chromosomes protein 3
- Double-strand-break repair protein rad21 homolog
- Structural maintenance of chromosomes protein 1B
- Cohesin subunit SA-2
- Wings apart-like protein homolog
- Meiotic recombination protein REC8 homolog
- Nipped-B-like protein
- Separin
- Double-strand-break repair protein rad21-like protein 1
Sequence:
MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGDGDPVTLFEVVKLGKSAMQSVVDDWIELYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRSKKGRPPLHRKRVEDESLDNTWLNRTDTMIQTPGPLPTPQLTSTVLRENSRPMGEQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRAGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF