wanglab/gogpt-training-data huggingface dataset:
Protein: Gem-associated protein 7 (Gemin-7) (SIP3) (Q9H840)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:12065586}. Nucleus, gem {ECO:0000269|PubMed:12065586}. Cytoplasm {ECO:0000269|PubMed:12065586}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
Interaction partners:
- Serine-threonine kinase receptor-associated protein
- Gem-associated protein 8
- Gem-associated protein 6
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 2
- Gem-associated protein 4
- Gem-associated protein 5
- Survival motor neuron protein
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D1
Sequence:
MQTPVNIPVPVLRLPRGPDGFSRGFAPDGRRAPLRPEVPEIQECPIAQESLESQEQRARAALRERYLRSLLAMVGHQVSFTLHEGVRVAAHFGATDLDVANFYVSQLQTPIGVQAEALLRCSDIISYTFKP
Protein: Leucine-rich repeat-containing protein 17 (Q9CXD9)
Organism: Mus musculus (Mouse)
Function: Involved in bone homeostasis. Acts as a negative regulator of RANKL-induced osteoclast precursor differentiation from bone marrow precursors.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:19336404}.
Interaction partners:
Sequence:
MRIVAILLLFCLCRAAEPRKSSPGVLRSQGNPSRSHGRGGRRGSSPVKRYAPGLPCDVYTYLHEKYLDCQERKLVYVLPDWPQDLLHMLLARNKIRVLKNNMFAKFKRLKSLDLQQNEISKIESEAFFGLNKLTTLLLQHNQIKVLTEEAFIYTPLLSYLRLYDNPWHCTCELETLISMLQIPRNRNLGNYAKCGSPPALRNKKLLQLKPQELCDEEEKEQLDPKPQVSGIPAVIRPEADSTLCHNYVFPIQTLDCKRKELKKVPSNIPPDIVKLDLSSNKIRQLRPKEFEDVHELKKLNLSSNGIEFIDPAAFLGLIHLEELDLSNNSLQNFDYGVLEDLYFLKLLWLRDNPWRCDYSIHYLYYWLKHHYNVHYNGLECKTPEEYKGWSVGKYVRSYYEECPKDKLPAYPETFDQDTEDDEWQKIHRDHPAKKHRVRITIVG
Protein: Small ribosomal subunit protein uS7cz/uS7cy (30S ribosomal protein S7, chloroplastic) (P0C491)
Organism: Oryza sativa subsp. japonica (Rice)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Os01g0220300 protein
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS19
- Os10g0411700 protein
- Small ribosomal subunit protein uS14c
- 40S ribosomal protein S29, putative, expressed
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein uS2c
- Os07g0658200 protein
Sequence:
MSRRGTAEKRTAKSDPIFRNRLVNMVVNRIMKDGKKSLAYQILYRAVKKIQQKTETNPLLVLRQAIRRVTPNIGVKTRRNKKGSTRKVPIEIGSKQGRALAIRWLLEASQKRPGRNMAFKLSSELVDAAKGGGGAIRKKEATHRMAEANRALAHFR
Protein: Hsc70Cb, isoform G (Hsc70Cb, isoform H) (M9MSL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- DnaJ-like-2, isoform A
- Stress-induced-phosphoprotein 1
- LD01461p
- RE23625p
- LD28549p
- Heat shock protein 83
- E3 ubiquitin-protein ligase CHIP
- Cyclin-G-associated kinase
- DnaJ protein homolog 1
Sequence:
MSVIGIDFGNESCYVAAARSGGIETLANDYSLRATPSFVAFDGKKRIIGVAAKNQQVTNMKNTVGGFKRLLGRKFNDPHVQHELTSIPARVEARGDGSIGIKVNYLGEDQHFGPEQLTAMLFTKLKETSAAAMQTQVNDCVIACPVFFTNAERKALLDAAQIAGLNVLRLMNETTATALAYGFYKNDLFEDKPRNVIFVDFGHSSLQASACAFTKGKLKMLASTWDQIGGRDIDLALGDYFAKEFQERYKINAKTNARANLRLLTEIEKLKKQMSANSTKLPLNIECFLDDIDVSSSMQRSQMEELCAPVLQRVEQTFKRLLAESKLQLDDIHSVEIVGGSSRIPSVKQLIEQVFNKPASTTLNQDEAVSRGAALQCAIMSPAVRVREFGVTDIQNYAVKVLWDSEGSAAPGEIEIFPQYHASPFSRLLTINRKGPFNVSIVYGQQVPYPDQTIGVWKVKDVKPTERGEGQDVKLKVRINNNGIVLISSATLVEKKEAEEAAAAAEQAASEEKPGDQTNNTGEPADGQQEAYCENEDDNNTSTASSPGGQGWAQRVKGWFGSGADKKKKASKATELPLECTTHGFSPVDLSNYTQQESKMIGNDQKETERIDAKNALEEFVYDMRNKLQGGPFERYVVEAEREKIVSQLNDLENWLYEDGEDCERDIYTSRLQALHQKTDPIKLRASDYEQGPAAFDELKNSIAIARLAVAEFRKGVPKYDHLTETEFINISETADKAQSWLDANLPKFTQSPRTADSPVQISAVRQEVQTLNSCVSSVINRAKPKPTPAKTATPPKDEANAEQNGGEPAANSGDKMDVDNNGQSAAGNDPSMEVE
Protein: Guanine nucleotide-binding protein negative regulator 1 (G protein negative regulator 1) (WD repeat-containing protein gnr1) (O59762)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Negatively regulates the pheromone-response pathway. Acts as a structural mimic of the G protein beta subunit thereby interacting with gpa1 which then inhibits gpa1 signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-1 subunit
- H/ACA ribonucleoprotein complex subunit cbf5
- Guanine nucleotide-binding protein subunit beta
- H/ACA ribonucleoprotein complex subunit gar1
- H/ACA ribonucleoprotein complex subunit nhp2
- Guanine nucleotide-binding protein alpha-2 subunit
- Guanine nucleotide-binding protein subunit gamma
- H/ACA ribonucleoprotein complex subunit nop10
- tRNA pseudouridine synthase 4
Sequence:
MDNCVNSFEDQKDDLVHKKKSQNFGYVCGSINLGTNVIAQSPTKPLNFFHSSRWSPDGSTILSLTEDQCLNCWNVPFSDLSKKADGPLNFSKHLSYKYQSPETVYSYSWYSRMKLDDPSSNLFAVSSRDQPIKLINFTTGKNKASYHMIDHQERYQGSHCLQFTNDGEYLIAGDKNCLHHFNIRTGCKEPVMTTVTHGYKVPLWEFSLKGIQSCFSLNPMDSKTLAVGTYSNRVGIYNDCGRRPCQLEFSIERGNGVTHLQWCEDGEKLYVGSRCSDKIEVWDIRYVRDMVYALEGHRGDTNQRILFDTDKKDEILAGGTDGSIRRWRNKDLVEETHVTGNYDLTVNTVQANPINMQIKCVCYGNRIYKYEKDESEEEDESKEKDLWTGTVSALQVWMD
Protein: Elongator acetyltransferase complex subunit 1 (F5H2T0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWDPVTPYRLHVLCQGWHYLAYDWHWTTDRSVGDNSSDLSNVAVIDGNRVLVTVFRQTVVPPPMCTYQLLFPHPVNQVTFLAHPQKSNDLAVLDASNQISVYKCGDCPSADPTVKLGAVGGSGFKVCLRTPHLEKRYKIQFENNEDQDVNPLKLGLLTWIEEDVFLAVSHSEFSPRSVIHHLTAASSEMDEEHGQLNVSSSAAVDGVIISLCCNSKTKSVVLQLADGQIFKYLWESPSLAIKPWKNSGGFPVRFPYPCTQTELAMIGEEECVLGLTDRCRFFINDIEVASNITSFAVYDEFLLLTTHSHTCQCFCLRDASFKTLQAGLSSNHVSHGEVLRKVERGSRIVTVVPQDTKLVLQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIYDHNPKVFLGNVETFIKQIDSVNHINLFFTELKEEDVTKTMYPAPVTSSVYLSRDPDGNKIDLVCDAMRAVMESINPHKYCLSILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLHLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFPECLNLIKDKNLYNEALKLYSPSSQQYQDISIAYGEHLMQEHMYEPAGLMFARCGAHEKALSAFLTCGNWKQALCVAAQLNFTKDQLVGLGRTLAGKLVEQRKHIDAAMVLEECAQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNVKPSILEAQKNYMAFLDSQTATFSRHKKRLLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEMSGKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALSEVVQNTENLKDEVYHILKVLFLFEFDEQGRELQKAFEDTLQLMERSLPEIWTLTYQQNSATPVLGPNSTANSIMASYQQQKTSVPVLDAELFIPPKINRRTQWKLSLLD
Protein: MKIAA3011 protein (Q6ZPF1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GATATMAESTPTRHRRKRRATPLAPATPPSQTTEKSPYFQTTEISLWTVVAAIQAVEKKMESQAARLQSLEGRAGSAEKKLADFEKTAVEFSNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNKNFWVLRLPPGSKGETPKVSGSLENDGVCFSEQEWENLEDWQKELYRNVMESNYETLVSLKVLGQPEEEVELGAEMVGDLVEEGTHLDRAMVKQEMLYKQEGPAGLPNMFSSAVEQQAFFGAEQAMFWNSPGDSALLESGPGDSNPESVETSRDPAPGRNLDCPRKQKSHRQVQLGQECGQGLKVKRDSSPYKCPECQISFRYKQQLTAHLQSHAGRESYSATEPEESLRPRPRLKPQAKRSKLHQCDVCHRSFSCKVSLVTHQRCHQQEGPSTSPQIQERFSPNSLVALPGHIPWRKSRSSLICGYCGKSFSHPSDLVRHQRIHTGERPYSCPECEKSFVQKQHLLQHQKIHQRERGGLASESARPNGLL
Protein: Rab proteins geranylgeranyltransferase component A 1 (Choroideremia protein homolog) (Rab escort protein 1) (REP-1) (P37727)
Organism: Rattus norvegicus (Rat)
Function: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12356470, ECO:0000269|PubMed:1525821, ECO:0000269|PubMed:8513495}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Geranylgeranyl transferase type-2 subunit beta
- Ras-related protein Rab-7a
- Ras-related protein Rab-27A
- Ras-related protein Rab-3A
- Ras-related protein Rab-1B
- Ras-related protein Rab
- small monomeric GTPase
- GTP-binding protein Rab-3D
- Ras-related protein Rab-6A
Sequence:
MADNLPSDFDVIVIGTGLPESIIAAACSRSGQRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENNDVVTENSMWQEQILENEEAIPLSSKDKTIQHVEVFCYASQDLHKDVEEAGALQKNHASVTSAQSAEAAEAAETSCLPTAVEPLSMGSCEIPAEQSQCPGPESSPEVNDAEATGKKENSDAKSSTEEPSENVPKVQDNTETPKKNRITYSQIIKEGRRFNIDLVSQLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGTVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCVEYEEHPDEYRAYEGTTFSEYLKTQKLTPNLQYFVLHSIAMTSETTSCTVDGLKATKKFLQCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAVIDQFGQRIISKHFIIEDSYLSENTCSRVQYRQISRAVLITDGSVLKTDADQQVSILAVPAEEPGSFGVRVIELCSSTMTCMKGTYLVHLTCMSSKTAREDLERVVQKLFTPYTEIEAENEQVEKPRLLWALYFNMRDSSDISRDCYNDLPSNVYVCSGPDSGLGNDNAVKQAETLFQQICPNEDFCPAPPNPEDIVLDGDSSQQEVPESSVTPETNSETPKESTVLGNPEEPSE
Protein: Tropomyosin alpha-3 chain (Gamma-tropomyosin) (Tropomyosin-3) (Tropomyosin-5) (hTM5) (P06753)
Organism: Homo sapiens (Human)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Tropomyosin alpha-1 chain
- Tetraspanin-16
- Actin, alpha cardiac muscle 1
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
- Actin, alpha skeletal muscle
- High affinity nerve growth factor receptor
- Protein TFG
- Troponin C, slow skeletal and cardiac muscles
- Troponin T, slow skeletal muscle
Sequence:
MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44) (Q8C2S0)
Organism: Mus musculus (Mouse)
Function: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Promotes also the deubiquitination of histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin (By similarity). Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin. Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability. Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-linked polyubiquitin chains and stabilizing it (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H0E7}. Cytoplasm {ECO:0000250|UniProtKB:Q9H0E7}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Transcription and mRNA export factor ENY2
Sequence:
MDRCKHVEQLQLAQGHSILDPQKWYCMVCNTTESIWACLSCSHVACGKYIQEHALKHFQESSHPVAFEVNDMYAFCYLCNDYVLNDNAAGDLKSLRSTLSTIKSKKYPCVVPSDSVLHPVDAQDRVYSLLDGTQSLPGNEDPTCAALWHRRRVLMGKAFRTWFEQSAIGRKGQEPTQERMVAKREAKRRQQQELEQQMKAELESTPPRKSLRLQGSSEEAATIEIVPVRAPPPPPASPAKDKAALPTSEDRTFKKVSDSLIKRRPMVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVAASDKARSYKHSAVTEAAAQQMNEGQEKEKGFVCSRHSGLSSGLSGGASKGRNMELIQPREPSSPYSSLCHELHILFQVMWSGEWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTKLPALIPTSQRRLIEQVLNVVNNIFHGQFLSQVTCLACDNKSDTIESFWDLSLEFPERYQCSGKDAASQPCLVTDMLDKFTETEALEGKIYMCDHCNSKRRKFSSKSVVFTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVVFEETLNMEPYCCRETLNALRPECFLYNLSAVVIHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMEEVRKAQAYILFYTQRVTENGHSKLLPPELLSNSQHPSKETDASSNEVLS
Protein: ADP-ribosylation factor-like protein 3 (Q9WUL7)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). Required for normal cytokinesis and cilia signaling. Required for targeting proteins to the cilium, including myristoylated NPHP3 and prenylated INPP5E. Targets NPHP3 to the ciliary membrane by releasing myristoylated NPHP3 from UNC119B cargo adapter into the cilium (By similarity). Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for PKD1:PKD2 complex targeting from the trans-Golgi network to the cilium.
Subcellular location: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250|UniProtKB:P36405}. Note=Detected predominantly in the photoreceptor connecting cilium. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). Present on the mitotic spindle. {ECO:0000250}.
Interaction partners:
- Protein unc-119 homolog A
- Cilia- and flagella-associated protein 36
- Protein XRP2
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Protein unc-119 homolog B
- Nephrocystin-3
- ADP-ribosylation factor-like protein 13B
- Tubulin-specific chaperone C
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 27 homolog
Sequence:
MGLLSILRKLKSAPDQEVRILLLGLDNAGKTTLLKQLASEDISHITPTQGFNIKSVQSQGFKLNVWDIGGQRKIRPYWRSYFENTDILIYVIDSADRKRFEETGQELTELLEEEKLSCVPVLIFANKQDLLTAAPASEIAEGLNLHTIRDRVWQIQSCSALTGEGVQDGMNWVCKNVNAKKK
Protein: Probable ATP-dependent RNA helicase DHX37 (EC 3.6.4.13) (DEAH box protein 37) (Q8IY37)
Organism: Homo sapiens (Human)
Function: ATP-binding RNA helicase that plays a role in maturation of the small ribosomal subunit in ribosome biogenesis. Required for the release of the U3 snoRNP from pre-ribosomal particles. Plays a role in early testis development. Probably also plays a role in brain development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:30582406, ECO:0000269|PubMed:31337883, ECO:0000269|PubMed:34516797}. Cytoplasm {ECO:0000269|PubMed:31337883}. Nucleus membrane {ECO:0000269|PubMed:31337883}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 14 homolog A
- Something about silencing protein 10
- WD repeat-containing protein 46
- rRNA-processing protein FCF1 homolog
- Nucleolar complex protein 4 homolog
- Ribosomal RNA small subunit methyltransferase NEP1
- Nucleolar protein 6
- Nucleolar protein 14
- Small subunit processome component 20 homolog
- Probable U3 small nucleolar RNA-associated protein 11
Sequence:
MGKLRRRYNIKGRQQAGPGPSKGPPEPPPVQLELEDKDTLKGVDASNALVLPGKKKKKTKAPPLSKKEKKPLTKKEKKVLQKILEQKEKKSQRAEMLQKLSEVQASEAEMRLFYTTSKLGTGNRMYHTKEKADEVVAPGQEKISSLSGAHRKRRRWPSAEEEEEEEEESESELEEESELDEDPAAEPAEAGVGTTVAPLPPAPAPSSQPVPAGMTVPPPPAAAPPLPRALAKPAVFIPVNRSPEMQEERLKLPILSEEQVIMEAVAEHPIVIVCGETGSGKTTQVPQFLYEAGFSSEDSIIGVTEPRRVAAVAMSQRVAKEMNLSQRVVSYQIRYEGNVTEETRIKFMTDGVLLKEIQKDFLLLRYKVVIIDEAHERSVYTDILIGLLSRIVTLRAKRNLPLKLLIMSATLRVEDFTQNPRLFAKPPPVIKVESRQFPVTVHFNKRTPLEDYSGECFRKVCKIHRMLPAGGILVFLTGQAEVHALCRRLRKAFPPSRARPQEKDDDQKDSVEEMRKFKKSRARAKKARAEVLPQINLDHYSVLPAGEGDEDREAEVDEEEGALDSDLDLDLGDGGQDGGEQPDASLPLHVLPLYSLLAPEKQAQVFKPPPEGTRLCVVATNVAETSLTIPGIKYVVDCGKVKKRYYDRVTGVSSFRVTWVSQASADQRAGRAGRTEPGHCYRLYSSAVFGDFEQFPPPEITRRPVEDLILQMKALNVEKVINFPFPTPPSVEALLAAEELLIALGALQPPQKAERVKQLQENRLSCPITALGRTMATFPVAPRYAKMLALSRQHGCLPYAITIVASMTVRELFEELDRPAASDEELTRLKSKRARVAQMKRTWAGQGASLKLGDLMVLLGAVGACEYASCTPQFCEANGLRYKAMMEIRRLRGQLTTAVNAVCPEAELFVDPKMQPPTESQVTYLRQIVTAGLGDHLARRVQSEEMLEDKWRNAYKTPLLDDPVFIHPSSVLFKELPEFVVYQEIVETTKMYMKGVSSVEVQWIPALLPSYCQFDKPLEEPAPTYCPERGRVLCHRASVFYRVGWPLPAIEVDFPEGIDRYKHFARFLLEGQVFRKLASYRSCLLSSPGTMLKTWARLQPRTESLLRALVAEKADCHEALLAAWKKNPKYLLAEYCEWLPQAMHPDIEKAWPPTTVH
Protein: Parathyroid hormone-related protein (PTH-rP) (PTHrP) [Cleaved into: Osteostatin] (F5GZD9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368098}. Nucleus {ECO:0000256|RuleBase:RU368098}. Secreted {ECO:0000256|RuleBase:RU368098}.
Interaction partners:
Sequence:
MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLEL
Protein: Splicing factor 3A subunit 3 (Protein noisette) (O46106)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable subunit of a splicing factor complex required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA (By similarity). Involved in male fertility.
Subcellular location: Nucleus. Note=Excluded from the nucleoli.
Interaction partners:
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 5
- LD45152p
- Splicing factor 3B subunit 3
- U1 small nuclear ribonucleoprotein A
- Splicing factor 3B subunit 4
- Probable U2 small nuclear ribonucleoprotein A'
- LD21442p
Sequence:
METLLEQQRRLHEERERLVKLMVDEHATKKPGEKERIHSEHRLKYLMELHHNSTSQLRDLYEDKDNERKAEIAALSGPNEFNEFYARLKQIKQFYKSHPAEVSVPLSVEFDEMIRVYNNPDDMSALVEFTDEEGGGRYLDLNECYELYLNLRSVEKLDYITYLMSFDHVFDIPRERKNREYRIYIETLNDYLHHFILRIQPLLDLEGELLKVELDFQRQWLMGTFPGFSIKETESALANTGAHLDLSAFSSWEELASLGLDRLKSALVALGLKCGGTLEERAQRLFSTKGKSTLDPALMAKKPSAKTASAQSREHERHKEIAQLEALLYKYADLLSEQRAATKENVQRKQARTGGERDDSDVEASESDNEDDPDADDVPYNPKNLPLGWDGKPIPYWLYKLHGLNISYNCEICGNFTYKGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAITLWEKLKSQKQSERWVADQEEEFEDSLGNVVNRKTFEDLKRQGLL
Protein: Galactose/lactose metabolism regulatory protein GAL80 (P04387)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It binds to GAL4 and so blocks transcriptional activation by it, in the absence of an inducing sugar.
Interaction partners:
- Regulatory protein GAL4
- Protein GAL3
- Galactokinase
- Galactose transporter
- Bifunctional protein GAL10
- Galactose-1-phosphate uridylyltransferase
- Regulatory protein MIG1
- Orotidine 5'-phosphate decarboxylase
- Phosphoribosylaminoimidazole carboxylase
- Cysteine proteinase 1, mitochondrial
Sequence:
MDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKIETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLKYLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIEIAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNIPEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIHGTKGDLKLEGDAGFAEISNLVLYYSGTRANDFPLANGQQAPLDPGYDAGKEIMEVYHLRNYNAIVGNIHRLYQSISDFHFNTKKIPELPSQFVMQGFDFEGFPTLMDALILHRLIESVYKSNMMGSTLNVSNISHYSL
Protein: Signal recognition particle receptor subunit alpha (SR-alpha) (Docking protein alpha) (DP-alpha) (P06625)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the SRP (signal recognition particle) receptor (By similarity). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit SRP54 (By similarity). SRP receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32916}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32916}; Cytoplasmic side {ECO:0000250|UniProtKB:P32916}. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
Interaction partners:
- SRP receptor subunit beta.
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP68
- Signal recognition particle 19 kDa protein
- Ribosomal protein L8.
- Signal recognition particle 9 kDa protein
- Ribosomal protein L5.
- Ribosomal_L18_c domain-containing protein.
- Signal recognition particle 14 kDa protein
Sequence:
MLDFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRLLREREESSKIRAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKESSDGPLATGKAVPAEKSGLPAGPENGVELSKEELIRRKREEFIQKHGRGLEKSSKSTKSDAPKEKGKKAPRVWALGGCANKEVLDYSAPTTNGAPDAAPPEDINLIRGTGPGGQLQDLDCSSSDDEETAQNASKPSATKGTLGGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDMLRDIMDAQRHQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEHVRTHTRRLSALHPPEKHAGPTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQTPRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMKA