wanglab/gogpt-training-data huggingface dataset:
Protein: Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)] (Q14005)
Organism: Homo sapiens (Human)
Function: Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.
Subcellular location: [Interleukin-16]: Secreted.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
Interaction partners:
- T-cell surface glycoprotein CD4
- Interleukin-1 alpha
- C-C chemokine receptor type 5
- C-C motif chemokine 27
- Interleukin-3
- Caspase-3
- Tumor necrosis factor
- Interleukin-17A
- Interleukin-1 beta
- C-C motif chemokine 4
Sequence:
MESHSRAGKSRKSAKFRSISRSLMLCNAKTSDDGSSPDEKYPDPFEISLAQGKEGIFHSSVQLADTSEAGPSSVPDLALASEAAQLQAAGNDRGKTCRRIFFMKESSTASSREKPGKLEAQSSNFLFPKACHQRARSNSTSVNPYCTREIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDCPAGKAAGTSRPTRSLSTAQLVQPSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKTIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTAPPSLCSHLSPPLCRSLSSSTCITKDSSSFALESPSAPISTAKPNYRIMVEVSLQKEAGVGLGIGLCSVPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEISDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVENTKFGKERHQWSLEGVKRLESSWHGRPTLEKEREKNSAPPHRRAQKVMIRSSSDSSYMSGSPGGSPGSGSAEKPSSDVDISTHSPSLPLAREPVVLSIASSRLPQESPPLPESRDSHPPLRLKKSFEILVRKPMSSKPKPPPRKYFKSDSDPQKSLEERENSSCSSGHTPPTCGQEARELLPLLLPQEDTAGRSPSASAGCPGPGIGPQTKSSTEGEPGWRRASPVTQTSPIKHPLLKRQARMDYSFDTTAEDPWVRISDCIKNLFSPIMSENHGHMPLQPNASLNEEEGTQGHPDGTPPKLDTANGTPKVYKSADSSTVKKGPPVAPKPAWFRQSLKGLRNRASDPRGLPDPALSTQPAPASREHLGSHIRASSSSSSIRQRISSFETFGSSQLPDKGAQRLSLQPSSGEAAKPLGKHEEGRFSGLLGRGAAPTLVPQQPEQVLSSGSPAASEARDPGVSESPPPGRQPNQKTLPPGPDPLLRLLSTQAEESQGPVLKMPSQRARSFPLTRSQSCETKLLDEKTSKLYSISSQVSSAVMKSLLCLPSSISCAQTPCIPKEGASPTSSSNEDSAANGSAETSALDTGFSLNLSELREYTEGLTEAKEDDDGDHSSLQSGQSVISLLSSEELKKLIEEVKVLDEATLKQLDGIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGTTHHDALAILRQAREPRQAVIVTRKLTPEAMPDLNSSTDSAASASAASDVSVESTAEATVCTVTLEKMSAGLGFSLEGGKGSLHGDKPLTINRIFKGAASEQSETVQPGDEILQLGGTAMQGLTRFEAWNIIKALPDGPVTIVIRRKSLQSKETTAAGDS
Protein: Calreticulin (P27798)
Organism: Caenorhabditis elegans
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis. Protects dopaminergic neurons against oxidative stress-induced neurodegeneration. May play a role in protection against ER stress. Plays a role in modulating lifespan, acting by influencing ER calcium homeostasis.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Endoplasmin homolog
- Protein disulfide-isomerase
- Calnexin
- Heat shock 70 kDa protein C
- Protein disulfide-isomerase 2
- BZIP domain-containing protein.
- Tr-type G domain-containing protein
- Heat shock protein 90
- Inositol 1,4,5-trisphosphate receptor itr-1
- Heat shock protein 70
Sequence:
MKSLCLLAIVAVVSAEVYFKEEFNDASWEKRWVQSKHKDDFGAFKLSAGKFFDVESRDQGIQTSQDAKFYSRAAKFDKDFSNKGKTLVIQYTVKHEQGIDCGGGYVKVMRADADLGDFHGETPYNVMFGPDICGPTRRVHVILNYKGENKLIKKEITCKSDELTHLYTLILNSDNTYEVKIDGESAQTGSLEEDWDLLPAKKIKDPDAKKPEDWDEREYIDDAEDAKPEDWEKPEHIPDPDAKKPEDWDDEMDGEWEPPMIDNPEYKGEWKPKQIKNPAYKGKWIHPEIENPEYTPDDELYSYESWGAIGFDLWQVKSGTIFDNIIITDSVEEAEAHAAETFDKLKTVEKEKKEKADEETRKAEEEARKKAEEEKEAKKDDDEEEKEEEEGHDEL
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (Q59000)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the isomerization of glucose-6-P to fructose-6-P.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
Interaction partners:
- Triosephosphate isomerase
- Bifunctional ADP-specific glucokinase/phosphofructokinase
- Enolase
- Probable transaldolase
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- 3-hexulose-6-phosphate isomerase
- Probable glycogen synthase
- Pyruvate kinase
- Glutamine--fructose-6-phosphate aminotransferase
Sequence:
MLSYDYENALKVGEISLEDINKVDFANAYSNLMEKLDNGVVGFRDVIYDENLDKYKSLNGYENVVVIGMGGSILGTMAIYYAISPFNNNAYFIDNSDPEKTLSILKKVDLNESIIYIISKSGNTLETLVNYYLIKKRIEKLNSFKGKLVFITNGGKLKREAEKNNYDIFSIPENVPGRFSVFTAVGLAPLYSLGVDISKILEGAREMDKICQNEDILKNPALLNGVIHYLYDKRGKDISVIMSYVESLKYFGDWYKQLIGESLGKNKHGITPLLSIGAKDQHSLLQLYMDGKKDKIITFMVAKKYRLDEEIEFEDINDEKISCRYSDIIRSQQKATEIALTNNGVPNVRITLDEINEMAMGALLYMYEMQVGFMGELYNINAYNQPAVEEEKKICWRLIKQ
Protein: B-cell receptor-associated protein 31 (BCR-associated protein 31) (Bap31) (6C6-AG tumor-associated antigen) (Protein CDM) (p28) (P51572)
Organism: Homo sapiens (Human)
Function: Functions as a chaperone protein. Is one of the most abundant endoplasmic reticulum (ER) proteins. Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD). Also serves as a cargo receptor for the export of transmembrane proteins (By similarity). Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by stimulating the translocation of NDUFS4 and NDUFB11 from the cytosol to the mitochondria via interaction with TOMM40. In response to ER stress, delocalizes from the ER-mitochondria contact sites and binds BCL2. May be involved in CASP8-mediated apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9334338, ECO:0000269|PubMed:9396746}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:11042173, ECO:0000269|PubMed:9396746}; Multi-pass membrane protein {ECO:0000255}. Note=May shuttle between the ER and the intermediate compartment/cis-Golgi complex (PubMed:9396746). Associates with the mitochondria-associated endoplasmic reticulum membrane via interaction with TOMM40 (PubMed:31206022). {ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:9396746}.; SUBCELLULAR LOCATION: Note=(Microbial infection) Upon SV40 infection, colocalizes with DNAJC18, DNAJB12 and DNAJB14 in punctate structures within the endoplasmic reticulum membrane. {ECO:0000269|PubMed:25631089}.
Interaction partners:
- Mitochondrial fission 1 protein
- Phosphofurin acidic cluster sorting protein 2
- Caspase-8
- Cell death-inducing p53-target protein 1
- Calnexin
- B-cell receptor-associated protein 29
- Vesicle-associated membrane protein-associated protein B/C
- Ubiquitin-conjugating enzyme E2 N
- Dynamin-1-like protein
- Bcl-2-like protein 1
Sequence:
MSLQWTAVATFLYAEVFVVLLLCIPFISPKRWQKIFKSRLVELLVSYGNTFFVVLIVILVLLVIDAVREIRKYDDVTEKVNLQNNPGAMEHFHMKLFRAQRNLYIAGFSLLLSFLLRRLVTLISQQATLLASNEAFKKQAESASEAAKKYMEENDQLKKGAAVDGGKLDVGNAEVKLEEENRSLKADLQKLKDELASTKQKLEKAENQVLAMRKQSEGLTKEYDRLLEEHAKLQAAVDGPMDKKEE
Protein: Pathogenesis-related protein 10 (E6YBW4)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Involved in resistance against the pathogen Phytophtora sojae. Inhibits hyphal growth of Phytophtora sojae. Possesses ribonuclease activity in vitro.
Interaction partners:
- Profilin
- Pathogenesis-related protein
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Pathosis-related protein 1
Sequence:
MGVVTQIYDTPAAVPPTRLFKAMTLDFHNLFPKLVDSIHSIVFTQGNGGPGTIKKITTIEGDKTKYVLHRVDAIDEANFVYNFSITEGTALADTLEKVSFESQLVEAPNGGSIRKVSVQFFTKGDATLSEEELTANKAKIQGLVKLVEGYLLANPDY
Protein: PilY2 protein (Pilus assembly protein PilY) (Q51537)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MKVLPMLLALAVPGLCWAEDPQTFEGAGVVFEVQVEKNLVDIDHRLYRLPNSTVRNGMPSLFQVKPGSVVSYSGTVSQPWSTITDIYIHKQMSEQELAEMIEKEQPRQDGEEQPR
Protein: Phosphatidylinositol transfer protein, membrane-associated 2 (F1LXD6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGQGSGVEILENRPYTDGPGGSGQYTHKVYHVGMHIPGWFRSILPKAALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDTGENNNVFNLSPVEKNQLITDIIDIVKDPVTPSEYKTEEDPKLFQSIKTRRGPLSENWIQEYKKRLLPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLTMEKIRELEKEVQLMLSRKMAQFSEEGPSELSKESTIKDQATGATPEPSSSNGESLGRGLKKQWSTSSKSSRSSKRGASPSRHSISEWRMQSIARDSDESSEEEFFDAQENLQHKEEMYTKDITKWSSNDLMDKMENPEPEESQDSLYHQSGSEFRVASSVEQLNTIEDEVSQPLATPPSKIHVLLLVLHGGTILDTGAGDPSSKQGDTNTITNVFDTVMRVHYPSALGHLAIRLVPCPPICADAFALVSNLSPYGHDEGCLSSSQDHIPLAALPLLATSSPQYQEAVATVIQRANLAYGDFIKSQEGVTFNGQVCLIGDCVGGILAFDALCYSGQPVSESQSSSRRGSVVSMQDADLLSPGILVNAAHCSGGSGGGSGGGSSLESSRHLSRSNIDIPRSNGTEDSRKQMPRKRSDSSTYELDTIQQHQAFLSSLHASVLRNEPSSRRSSSSTMLDGAGALGKFDFEIADLFLFGCPLGLVLALRKTVIPSLDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHTLPPFNIPRYQRYPLGDGCSTLLVETVQRNPELVLEGGPLAPLPHGDSFLETSIPVPALTWQDGPRQSLGCSESDALQTHNTVFQEHAAPSSPGTAPASRGFRRASEISIASQVSGMAESYTASGIAQIAAKWWGQKRIDYALYCPDALMAFPTVALPHLFHASYWESTDVVSFLLRQVMRHDSASILELDGKEVSVFTPSQPREKWQRKRTHVKLRNVAANHRINDAVANEDGPQVVTGRFMYGPLDMVTLTGEKVDVHIMTQPPSGEWLYLDTLVTNSSGRVSYTIPETHRLGVGVYPIKMVVRGDHTFADSYITVLPKGTEFVVFSIDGSFAASVSIMGSDPKVRAGAVDVVRHWQDLGYLIIYVTGRPDMQKQRVVAWLAQHNFPHGVVSFCDGLVHDPLRHKANFLKLLISELHLRAHAAYGSTKDVAVYNSISLSPMHIYIVGRPTKKLQQQCQFITDGYAAHLAQLKYNHRARPARNTATRMALRKGSFGLPGQGDFLRSRNHLLRTISAQPSGPSHRHDRTQTQMDLEQRGQRSMSMAASCWGRAMAGRLEPGAATGPK
Protein: Zwei Ig domain protein zig-4 (2 Ig domain protein zig-4) (G5ECB1)
Organism: Caenorhabditis elegans
Function: Required for maintaining axon position of PVQ and PVP neurons postembryonically in the ventral nerve cord (VNC) by preventing axons drifting into the opposite side of the VNC that could occur during body growth and movement.
Subcellular location: Secreted {ECO:0000255}.
Interaction partners:
- Mesocentin
- LIPaSe related
- Zwei Ig domain protein zig-8
- LIPaSe related
- Uncharacterized protein.
- Zwei Ig domain protein zig-7
- Putative pyridoxal-phosphate dependent protein F13B12.4
- Neuroglian
Sequence:
MFAIALLSFLVVLINAHPPMHAEMHSAVVTLANEIDTNYLTSPAKIKIVAPLESALIPGGETYQLRCDIMSTPAATIHWKFNGKLIQGSNELNVEEKLLNFGKAIVDTGIVASILTIQCPSAENSGTYSCVGYNGHQTIETVAEVEIEGEASGCRSNHKSAPEIVFWTDSRFEMTGNVATLVCRANQQVDWVWMSNDELVKNNDKFTVLSNGDLVIKNIVWDDMGTYTCIARNQFGEARQETFLYPTAKKSSF
Protein: Ribonuclease P protein component, mitochondrial (RNase P) (EC 3.1.26.5) (Q02773)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ribonuclease P generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular location: Mitochondrion.
Interaction partners:
- Ribonuclease P protein subunit RPR2
- Ribonucleases P/MRP protein subunit POP6
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease MRP protein subunit RMP1
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP7
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease P/MRP protein subunit RPP1
- tRNA-splicing endonuclease subunit SEN54
Sequence:
MAFKSFIYSKGYHRSAAQKKTATSFFDSSYQYLRQNQGLVNSDPVLHASHLHPHPVVVANVNYNNVDDILHPHDLDSSINNTNNPLTHEELLYNQNVSLRSLKQQQSTNYVNNNNNNQHRYYSTGPTLPTNQYDPLNFSNRNFQDLSLKTSQPSVQQPQNEYSLLKDENAPVWKEDTEPCLNKSTYLQTHIDEINRCYEQKNYNKINSLYQSLKRNDIVPPLEIFTKVLDSLCKRPLDNNDLDNKMYELLTCYQDMINNRLKPPDEIYNIVLLSLFKGSILAYQFENPNGSDFYKIAIELFNTTTNDPKQKSVVKFRNFSKDVLDYNLLAMNIYPGHITLSKAQQVIKSSPAFIKDSFYFIACFSYAKLTNDKFAIKELYEDFRLSLSSGSPDQGLFDDQFEIYSVILSSFIETGEVELATNLLDDLVSKIQSSNGLASNISLLLSSFLISMSKVDPSKAYEIWFKFHNLNWIPEFSYEFYLVFMANSFQDWNLTKKIYDYIFPMERNLSPLKKQKLSDYLLHPIGVDSITTSLLDYSLQLKDNEVIMKILEESIVKNFSFDIGIYPFVFNYLREIQCGEDYLMRFIESHAEFIKKSNSINKFQFLNMIVDNFQSQSLLNKISHAKFFKNFVEDFNLENCELVSYNGLISCINNFIKIPKTIKDFPYILEIHAILVTKLFDFDTYPILQNGNNEVLLKFRDQIEHQFKMLAQNFCRLNLDPNLLAGVVSQAMKMVNLDDTANGQDLLNFFNHPGDWDKSYPLSLGSFIRNSPRGGIREFTKLSKEGYCFDYDTYKELIIKRAINKQIIDKCLEVCPDSIELKNIVNLMISKIPGRNLTQLIINNPKFSKVFVPNLRNDSMLKLIENCESLSNFIRICDFPEKFKSIAIQAENKNAIELIYERLFDGGKYADILRYNNIVPVLNLELLLKSCIRSGEFKKYESLSKKFNDKISESSKIDIQLEYLINKNDLKGAFTLFEKTPRELRTPHKTMDLYTFALFLDSFNRNITYYESPENTLQFANILSSQTSFINLLSTYNLIAHSDHLMNFNVGGMAAKVKKEILNQMLNNLYDSIRLLSPSIENDKSMKEKLREKVKNYCRFKAYLKSPELDMDELKTLVSVESFLNPFTPSMLFNNLIETIYINEHASSLVLQNGLIYSLQQKGLNKILSYLEESFITSGNDANIEKVREFRSLLRKSKPLQA
Protein: Serpin family B member 7 (G3V6B5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Albumin
- Thyroglobulin
- Interleukin-5
- Interleukin-4
- Granulocyte-macrophage colony-stimulating factor
- Interferon gamma
- Interleukin-13
- Myoglobin
Sequence:
MASLAAANAEFGFDLFREMDSSQGNGNVFFSSLSIFTALSLIRLGARGDCARQIDKALHFISPSRQGNSSNSQLGLQYQLKRVLADINSSHKDYELSIANGVFAEKVFDFHKSYMECAENLYNAKVERVDFTNDIQETRFKINKWIENETHGKIKKVLGDSSLSSSAVMVLVNAVYFKGKWKSAFTKSDTLSCHFRSPTCPGKAVNMMHQERRFNLSTIQEPPMQILELQYHGGISMYIMLPEDDLSEIESKLSFQNLMDWTNSRKMKSQYVNVFLPQFKIEKDYEMRSHLKSVGLEDIFVESRADLSGIASGGRLYVSKLMHKSLIEVSEEGTEATAATESNIVEKLLPESTVFRADRPFLFVIRKNGIILFTGKVSCP
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FV26)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- RP41
- 40S ribosomal protein S7
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS3
- 40S ribosomal protein S4
- Small ribosomal subunit protein eS25
- 40S ribosomal protein S8
- Small ribosomal subunit protein uS10
Sequence:
MTAANNNTTVFVSGASGFIAQHIIRQLLDQNYKVIGSVRSTEKGDNLKNAIFKSANFNYEIVKDIADLNAFDPVFEKHGKDIKVVLHTASPLNFTTTEYEKDLLIPAVNGTKGILESIKKYAAQTVERVVVTSSFASHTSTVDMCNTKGKITEDSWNQDSWENCQTDAVRAYFGSKKFAEEAAWEFLNKNKDAVKFKLATVDPVYVFGPQNHIEPGKKVLNVSSEVINQLVHLKKDDPLPQVACGYIDVRDIAKAHILAFQKDELIGQRLLLHSGLFTVQTLLDAINEQFPELRGKIPAGEPGSNKPEDLLTPIDNTKTKKLLGFEFRDLKTIIQDTVSQILEAENASAKL
Protein: Protein Jumonji (Jumonji/ARID domain-containing protein 2) (Q92833)
Organism: Homo sapiens (Human)
Function: Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts as an accessory subunit for the core PRC2 (Polycomb repressive complex 2) complex, which mediates histone H3K27 (H3K27me3) trimethylation on chromatin. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells, thereby playing a key role in stem cell differentiation and normal embryonic development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases (By similarity). Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5 (By similarity). Participates in the negative regulation of cell proliferation signaling (By similarity). Does not have histone demethylase activity (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:20075857, ECO:0000269|PubMed:29499137}. Note=Colocalizes with the PRC2 complex on chromatin. {ECO:0000269|PubMed:29499137}.
Interaction partners:
- Zinc finger protein AEBP2
- Polycomb protein SUZ12
- Polycomb protein EED
- Histone-binding protein RBBP4
- Histone-lysine N-methyltransferase EZH2
- Metal-response element-binding transcription factor 2
- Histone-lysine N-methyltransferase EZH1
- Histone-binding protein RBBP7
- PHD finger protein 19
- PHD finger protein 1
Sequence:
MSKERPKRNIIQKKYDDSDGIPWSEERVVRKVLYLSLKEFKNSQKRQHAEGIAGSLKTVNGLLGNDQSKGLGPASEQSENEKDDASQVSSTSNDVSSSDFEEGPSRKRPRLQAQRKFAQSQPNSPSTTPVKIVEPLLPPPATQISDLSKRKPKTEDFLTFLCLRGSPALPNSMVYFGSSQDEEEVEEEDDETEDVKTATNNASSSCQSTPRKGKTHKHVHNGHVFNGSSRSTREKEPVQKHKSKEATPAKEKHSDHRADSRREQASANHPAAAPSTGSSAKGLAATHHHPPLHRSAQDLRKQVSKVNGVTRMSSLGAGVTSAKKMREVRPSPSKTVKYTATVTKGAVTYTKAKRELVKDTKPNHHKPSSAVNHTISGKTESSNAKTRKQVLSLGGASKSTGPAVNGLKVSGRLNPKSCTKEVGGRQLREGLQLREGLRNSKRRLEEAHQAEKPQSPPKKMKGAAGPAEGPGKKAPAERGLLNGHVKKEVPERSLERNRPKRATAGKSTPGRQAHGKADSASCENRSTSQPESVHKPQDSGKAEKGGGKAGWAAMDEIPVLRPSAKEFHDPLIYIESVRAQVEKFGMCRVIPPPDWRPECKLNDEMRFVTQIQHIHKLGRRWGPNVQRLACIKKHLKSQGITMDELPLIGGCELDLACFFRLINEMGGMQQVTDLKKWNKLADMLRIPRTAQDRLAKLQEAYCQYLLSYDSLSPEEHRRLEKEVLMEKEILEKRKGPLEGHTENDHHKFHPLPRFEPKNGLIHGVAPRNGFRSKLKEVGQAQLKTGRRRLFAQEKEVVKEEEEDKGVLNDFHKCIYKGRSVSLTTFYRTARNIMSMCFSKEPAPAEIEQEYWRLVEEKDCHVAVHCGKVDTNTHGSGFPVGKSEPFSRHGWNLTVLPNNTGSILRHLGAVPGVTIPWLNIGMVFSTSCWSRDQNHLPYIDYLHTGADCIWYCIPAEEENKLEDVVHTLLQANGTPGLQMLESNVMISPEVLCKEGIKVHRTVQQSGQFVVCFPGSFVSKVCCGYSVSETVHFATTQWTSMGFETAKEMKRRHIAKPFSMEKLLYQIAQAEAKKENGPTLSTISALLDELRDTELRQRRQLFEAGLHSSARYGSHDGSSTVADGKKKPRKWLQLETSERRCQICQHLCYLSMVVQENENVVFCLECALRHVEKQKSCRGLKLMYRYDEEQIISLVNQICGKVSGKNGSIENCLSKPTPKRGPRKRATVDVPPSRLSASSSSKSASSSS
Protein: Interleukin-21 receptor (IL-21 receptor) (IL-21R) (Lymphocyte receptor beta) (LR-beta) (Novel cytokine receptor 8) (NR8) (Novel interleukin receptor) (CD antigen CD360) (Q9JHX3)
Organism: Mus musculus (Mouse)
Function: This is a receptor for interleukin-21.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-21
- Cytokine receptor common subunit gamma
- Signal transducer and activator of transcription 3
- Tyrosine-protein kinase JAK1
- Interleukin-4
- Interleukin-7
- Interleukin-2
- Tyrosine-protein kinase JAK3
- Interleukin-15
- Interleukin-9
Sequence:
MPRGPVAALLLLILHGAWSCLDLTCYTDYLWTITCVLETRSPNPSILSLTWQDEYEELQDQETFCSLHRSGHNTTHIWYTCHMRLSQFLSDEVFIVNVTDQSGNNSQECGSFVLAESIKPAPPLNVTVAFSGRYDISWDSAYDEPSNYVLRGKLQYELQYRNLRDPYAVRPVTKLISVDSRNVSLLPEEFHKDSSYQLQVRAAPQPGTSFRGTWSEWSDPVIFQTQAGEPEAGWDPHMLLLLAVLIIVLVFMGLKIHLPWRLWKKIWAPVPTPESFFQPLYREHSGNFKKWVNTPFTASSIELVPQSSTTTSALHLSLYPAKEKKFPGLPGLEEQLECDGMSEPGHWCIIPLAAGQAVSAYSEERDRPYGLVSIDTVTVGDAEGLCVWPCSCEDDGYPAMNLDAGRESGPNSEDLLLVTDPAFLSCGCVSGSGLRLGGSPGSLLDRLRLSFAKEGDWTADPTWRTGSPGGGSESEAGSPPGLDMDTFDSGFAGSDCGSPVETDEGPPRSYLRQWVVRTPPPVDSGAQSS
Protein: Cu(2+)-transporting P-type ATPase (Q5AG51)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Copper metallochaperone
- Superoxide dismutase 1 copper chaperone
- High-affinity iron permease
- Copper transport protein
- Copper metallochaperone
- Ferroxidase
- RRN6 beta-propeller domain-containing protein
- Ferric/cupric reductase transmembrane component 1
- Siderophore transporter
- Fth1p
Sequence:
MKSSAILESNPNQNNNVTVVLEVLDLHTAKDITDVINILDELFPKLKSKDFDHQELTLIYDSNDYDDMSILNAISEIGFPVKILSSTAPQCKTTVNIQGMTCGACSASITEALEKTPGVYKASISLVTENGLIMHSPKLSPENIITIIEDCGFDAQIESSKTKQSSAPESSQDQSKRLNTTIGIIGMTCGACSASITNVLEKLPGVENVSVSLITEEASIVHDSTITTVQQLKEAIEDCGFTPTFNKSINLNQYQNTNDSNEEVTLKIVGVNHTTDLIGLRYNIEAYLRSISGVQKFELTLRGMNASSNIMPTQVGTLITEEDTIADVKSLVNELVFQYDSDSVGIRDIIDGLNTISDNIEFMVINSLDQSSATQLKLLSKVKDINYWKKIFIQSLLFGIPVLFLNHTKNWPIWKTTMIFPGLYLVSLLELILSTYIQFYLGSVFIKKFSSFLRKKFKGATMDVLVCISTMCSYIFSLTTIIVSVWNGQKNGPPPVLFDTLVMLISFVSFGKLLENKAKGATSTALSSLLSLTPSTCTIINDIPGYQKFIEDQQSLEKSEKSNSLSMQEFPTRVISIDLVQPNDIAIVLPGGKVPADGEIVFGETEIDESLITGEPLPVYKKLKDKVIGGSINGPHLIHIKVTHTGKKSQLQQIINLVKESQVNKAPVQKFSDYIAARFVPFVLLLAIFTFILWMIICFTIHQDKLPKIFQNETNGKFFVCLKLSISVIVVACPCALGLAAPTAVMVGTGVGAINGVLIKGAKVLEKITGVNIILFDKTGTLTTGEMSLVNFQPIMSKSSITISDWWKLVGSVECHSEHPIGRALTKSAKTNLNLNFDDDHFDTTVNDINVLIGLGIQANVTLANNPQTQFNVYVGNDKLIESKFPNLLNNIDEKLLHSANTVSHVIIDGEYSGYIELTDALKSGSWEVVNYLKTQGYIVGMVTGDNRGAALKIAQEVGIPFDNVFYEVSPIHKDNVITDLHNRLGGNQSSSVNVAFIGDGINDAPALAKADIGMAISSGTDIAIESADIVLIGGRSNQTDLHGVVNALQISTATFNRIKINFLWAIIYNIFMLPFAMGCFLPLNIVLPPVAAGAAMMFSSLSVVFSSLLLKRWTPPKIETKKTFIDDLEMGNNATGGDGDGFSLKNGTIEEFNNVKRKSAVNFSSLFAKMTTTRRNRRGGGGGGGRSNGNNNQSYELVSNRFS
Protein: Tectonic-like complex member MKS1 (Meckel syndrome type 1 protein homolog) (Q5SW45)
Organism: Mus musculus (Mouse)
Function: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:21725307}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme.
Interaction partners:
- Coiled-coil and C2 domain-containing protein 2A
- B9 domain-containing protein 1
- B9 domain-containing protein 2
- Tectonic-1
- Tectonic-2
- Centrosomal protein of 290 kDa
- Transmembrane protein 231
- Transmembrane protein 216
- Meckelin
- Jouberin
Sequence:
MAEAVWSTDTGEAVYRSRDPVRNLRLRVHLQRITSSNFLHYQPAAQMGKDLIDLATFRPPQAASGHRPDEEEEEEVVIGWQEKLFSQFEVDLYQNESACQSPLDHQYRQEILKLENSGGRKNRRIFTYTDSDRYTDLEEYCQKITTSASEVPSFLAERMANVRRRRQDRRGVEGSKLKSRIVTWEPSEDFIKNNHAINTPLQTMYIMADLGPYGKLGYKVHEHVLCILKVDSNGVITVKPDFTGIKGPYRIETEGEKQEHTSAWKYTIDNVSSLAQPEEEEREQRVFKDLYGRHKEYLSSLVGTDFEMIAPGALRLFVNGEVVSAQGYEYDNLYVHFFVELPAANWSSPPFQQLSGVTQACATKSLGMDKVAYFSFPFTFEAFFLHEDESAESLPEWPVLYCKVLSLDFWQRYRVEGYGAVVLPATPGSHTLTVSTWRPMELGLVAELRRFFIGGSLELEDPSYVRIPGTFKGERLSRFGFRTETTGTVTFRLHCLQQSRAFMESNSLQKQMRSVLDRLEGFSQQSSTHNVLEAFRRARRRMQEARESLPQDLVSPTGTLT
Protein: Chaperone protein DNAJ, putative (Q381B2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Heat shock protein, putative
- Chaperone protein DNAJ, putative
- Heat shock protein 70
Sequence:
MRGLAAAHTSNTKLVSFLFVSFACLGFAPVVHSHDDSGDGADEIDYYAVLGLTPEATDREVRQRFRELSRKYHPDVSSGGDAREMFSRITRANEVLSDKKKRRMYDMRGEEGLRQLKRLEAESGGEQFGSISQLFRHHAARRLRGKNTEATLHLPLDVVYTGGRRTVTINKQKVCTKCRGTGAKRPSGLKTCEHCGGHGILRQRLQLAPGMFQEIRQTCPYCGGRGSIMKERCGVCGGNGVHRADVELTVDIDAGMPEGHVLSFEMEADESPDTIPGDLLLSVQTKKHPRFSRRANDVDLDMTLVVTLKEALLGFQRRVEHLDGSEFFVNETGITQYGSVLKVPGKGMPRHNVPSEFGDLYVKVLFEMPDMLTKEQREELAEHL
Protein: Atlastin-1 (EC 3.6.5.-) (Spastic paraplegia 3A homolog) (Q8BH66)
Organism: Mus musculus (Mouse)
Function: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. May also regulate Golgi biogenesis. May regulate axonal development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8WXF7}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WXF7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8WXF7}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum tubular network. {ECO:0000269|PubMed:24668814}.
Interaction partners:
- Receptor expression-enhancing protein 1
- Spastin
- Reticulon-2
- Receptor expression-enhancing protein 2
- Magnesium transporter NIPA1
- Protrudin
- ADP-ribosylation factor-like protein 6-interacting protein 1
- Spartin
- Reticulon-3
- Endoplasmic reticulum junction formation protein lunapark
Sequence:
MAKSRRDRNSWGGFSEKSSDWSSEEEEPVRKAGPVQVLIVKDDHSFELDEAALNRILLSQAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEVFLINKLDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPERLDIKEINGNKITCRGLLEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEVCGGDKPFLAPNDLQSKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLCHQAFPAPKSEPTQQPEKKKI