wanglab/gogpt-training-data huggingface dataset:
Protein: Sorting nexin-27 (Q96L92)
Organism: Homo sapiens (Human)
Function: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:25851603}; Peripheral membrane protein. Cytoplasm, cytosol. Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products.
Interaction partners:
- Vacuolar protein sorting-associated protein 26A
- Ubiquitin thioesterase otulin
- Sorting nexin-1
- Diacylglycerol kinase zeta
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 29
- Beta-2 adrenergic receptor
- Cytohesin-interacting protein
Sequence:
MADEDGEGIHPSAPHRNGGGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNHVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPRYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVISHSFVRKLAPNEFPHKLYIQNYTSAVPGTCLTIRKWLFTTEEEILLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLYEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT
Protein: Claudin-5 (Brain endothelial cell clone 1 protein) (Lung-specific membrane protein) (O54942)
Organism: Mus musculus (Mouse)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}.
Interaction partners:
- Occludin
- Tight junction protein 1
- Cadherin-5
- Tight junction protein 2
- Endothelial cell-selective adhesion molecule
- Junctional adhesion molecule A
- Transcription factor SOX-18
- Tight junction protein ZO-3
- Claudin-3
- Angiopoietin-related protein 4
Sequence:
MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV
Protein: V-type proton ATPase subunit F (V-ATPase subunit F) (Vacuolar proton pump subunit F) (Q55AH5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Interaction partners:
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase subunit B
- V-ATPase proteolipid subunit C-like domain-containing protein
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d
- V-type proton ATPase subunit G
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E
- V-type proton ATPase proteolipid subunit
Sequence:
MATKSLSETALVAVIGDEDVVTGFLLAGVGQKDKKKNENFLVVDSKTSQAKIETAFKSFTTRNDIAIIMITQKVADEIRYLIDEYHQVIPTILEIPSKDHPYDPKKDSVMLKVKKMTGSD
Protein: Transmembrane emp24 domain-containing protein eca (Protein eclair) (Q9I7K5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected. Involved in Golgi organization.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane emp24 domain-containing protein bai
- CHOp24, isoform A
- P24-related-1, isoform A
- IP11573p
- Opossum, isoform A
- Secretory 22, isoform B
- LP01981p
- LD30746p
- Protein transport protein Sec61 subunit beta
Sequence:
MRDQFISLALILCVLHSACGLYFHISETERKCFIEEVPDETTVIVNYKVELYDPRSNGFMPSSPGIGMHVEVRDSDDKIVLSRVYSSQGRISFTSHTPGEHVICMFSNSTAWFSGAQLRVHLDIQVGEHAIDYAHVAQKEKLTELQLRIRQLLDQVEQITKEQNYQRYREERFRHTSESTNSRVLWWSLAQTVVLVCMGFWQMRHLKSFFEAKKLV
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (Q9VU38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368116}.
Interaction partners:
Sequence:
MCDRVREGILVGCGNPLLDISAVVPLNFLQKYSMNEDDAILAEDRHMPIYGELVEGYQAEFLAGGSVQNSLRIAQWILRQPRVAVFFGCVGEDRYANILKEKAQAAGLDVHYQVKKDVPTGTCAVLITGTHRSLCANLAAANNFTIDHLEEPSNKALVDNAQYYYISGFFLTVNPPSIMQVAATAHAKQRPFLMNLSAPFISQFYMAPLLAALPYVDIIFGNEAEAQAFAEAQQWPSGDLREIGKRLVAMEKKNPTRPRIAILTQGCDPVLLIQQDSVQEFPVTKLAVHEIVDTNGAGDAFVGGFLSQFVQGKSLDVCIRCGNYAAGHIIKNPGCTYSGEPEFVE
Protein: Reproductive homeobox on X chromosome 8 (Q4TU85)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MEPQEVTQSSLLRDDEIKESDDAAAWIVSQEMKEREENAGIQDCPLLGAMAAEGEGENEEEGEEGEEGEEGEEGEEGEEGEEGEEGEEEEEEEEEEEEEEEEEEEEEEEEEEGEEGEEGEEGDEGGEGGEGGEEGEEEGEEEEGGEGEGEEEEEEEEEEEEEEEEEEEEEEEEEAAAAAAARDETTAGSSAPVDDRSHDAGASSNGEDRGQGEELIPGGTKGLEALPSPSGQLPRNRYRFTKFQLQELERIFERNHYPSAAARRELARWIGVTESRVENWFKSRRAKYRKCLM
Protein: Dystrobrevin (A0A8I5ZQM2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR038204}.
Interaction partners:
Sequence:
MIEDSGKRGNTMAERRQLFAEMRAQDLDRIRLSTYRTACKLRFVQKKCNLHLVDIWNVIEALRENALNNLDPNIELNVARLEAVLSTMFYQLNKRMPSTHQIHVEQSISLLLNFLLAAFDPEGHGKISVFAVKMALATLCGGKIMDKLRYIFSMISDSSGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCFSQQKKVTLNGFLDTLMSDPPPQCLVWLPLLHRLANVENVFHPVECSYCHSESMMGFRYRCQQCHNYQLCQDCFWRGHAGGSHSNQHQMKEYTSWKSPAKKLTNALSKSLSCASSREPLHPMFPDQPEKPLNLAHIVPPRPVTSMNDTLFSHSVPSSGSPFITRSSPPKDSEVEQNKILARAAPAFLKGKGIHYSLNVADRLADEHVLIGLYVNMLRNNPSCMLESSNRLDEEHRLIARYAARLAAESSSSQPTQQRSAPDVSFTIDANKQQRQLIAELENKNREILQEIQRLRVEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKEEELKQGTQGAGSPRSSPSHTISRPIPMPIRSTSACSTPAYTPQDSLTGVGGDVQEAFAQSSRRNLRNDLLVAADSITNTMSSLVKELNSEVASETESTVDSEFSRTQFEDLVPSPTSEKSFLAQIHARKPGYIHGGATSTMHGDMVPEDGDPYPQPEDGNYENESVRQLENELQMEEYLKQKLQDEAYQVSLQG
Protein: GM06280p (Q5BHZ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYTLTRAAHVRPSVDASPSDMDILVNERSERENFGSNLVNSSLESNTDNESCYDSQDESLAMRLSSSSTTSTSSIVLRKRQPKITEFMKERKRLAQAPKKLSPAKRMRTSSPSSSATSSSSSSGGFGLGAHFGAMLKRPRHN
Protein: Uncharacterized protein (Q4GZ80)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TRUD domain-containing protein
- Ribosomal protein L22p/L17e
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Large ribosomal subunit protein bL21m
- GTP-binding protein, putative
- Uncharacterized protein
- Tetratricopeptide repeat
- Uncharacterized protein
Sequence:
MLVRTWMLLNRPKGPQGLRPGKEYRLTVPYRSEVTMLRLANHKAINSNIRELFKKPLVMNNIKAIPRDLGEIPRDYVLRLLFFHQPIRLVDLWTICKEHDDVPLDSAKHLRLVLKIAKLQRWVYAEKNQTNNLYYYYVHQSRIQEVQQMVRASEVRKKEQESLREIEAEKLRMEEQERRKVALDENIVALQNALVSNIAQIQEFDPGFARSKPYVTESGAVNVGWGLNDGGSAACSSDLDGQQVA
Protein: Trehalose monomycolate exporter MmpL3 (TMM exporter MmpL3) (MmpL3 transporter) (Mycobacterial membrane protein large 3) (P9WJV5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane. Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (By similarity). Could also be part of a heme-iron acquisition system.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000250|UniProtKB:A0QP27}. Cell tip {ECO:0000250|UniProtKB:A0QP27}. Note=Colocalizes with TtfA to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. {ECO:0000250|UniProtKB:A0QP27}.
Interaction partners:
- Polyketide synthase Pks13
- NYN domain-containing protein
- tRNA
- Cytochrome bc1 complex cytochrome b subunit
- Decaprenylphosphoryl-beta-D-ribose oxidase
- Long-chain-fatty-acid--AMP ligase FadD32
- Conserved protein
- Transmembrane protein
Sequence:
MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVMLSAILSITVLPACLGILGKHVDALGVRTLFRVPFLANWKISAAYLNWLADRLQRTKTREEVEAGFWGKLVNRVMKRPVLFAAPIVIIMILLIIPVGKLSLGGISEKYLPPTNSVRQAQEEFDKLFPGYRTNPLTLVIQTSNHQPVTDAQIADIRSKAMAIGGFIEPDNDPANMWQERAYAVGASKDPSVRVLQNGLINPADASKKLTELRAITPPKGITVLVGGTPALELDSIHGLFAKMPLMVVILLTTTIVLMFLAFGSVVLPIKATLMSALTLGSTMGILTWIFVDGHFSKWLNFTPTPLTAPVIGLIIALVFGLSTDYEVFLVSRMVEARERGMSTQEAIRIGTAATGRIITAAALIVAVVAGAFVFSDLVMMKYLAFGLMAALLLDATVVRMFLVPSVMKLLGDDCWWAPRWARRLQTRIGLGEIHLPDERKRPVSNGRPARPPVTAGLVAARAAGDPRPPHDPTHPLAESPRPARSSPASSPELTPALEATAAPAAPSGASTTRMQIGSSTEPPTTRLAAAGRSVQSPASTPPPTPTPPSAPSAGQTRAMPLAANRSTDAAGDPAEPTAALPIIRSDGDDSEAATEQLNARGTSDKTRQRRRGGGALSAQDLLRREGRL
Protein: G-protein coupled receptor str-217 (Q9XX85)
Organism: Caenorhabditis elegans
Function: Probable G-protein coupled receptor.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-galactose transporter
- F-box domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- F-box domain-containing protein
- FBA_2 domain-containing protein.
- F-box domain-containing protein
- F-box domain-containing protein
Sequence:
MLLFQKTLSRVAAPISVAANLILILLIIFKSPAQMGNYKYLLIGLSIFEMSYAVLDVVSETTVLSIKKSFVVVVPYKDRSFGQETAMDINLIYCGFFGFSMGMFVVIFAYRSFLTTGNTILRKFEGFKIISWFAYPLFYAIVWILVAWGPLASFPEMDIVVRPFLLDELNMTVDEVAYTGRLFYSTIDNSLRYSAILTGVLQWVLTASSLFLVIFFGLRCYFHYGKLVQLTDVQSIRLRQLQNQLFLALVCQATVPLILMHIPVTILYTCCVLNIVFNPFSVATTIALFPAIDPLPTIFIVKNYRVALFEFVCPSCLCWSETLKHMGSNRITSYRSNTVNALSM
Protein: Protein PER1 (Protein processing in the ER protein 1) (P25625)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for efficient transport of GPI-anchor proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17021251}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17021251}.
Interaction partners:
- Cell division control protein 1
- Membrane-bound O-acyltransferase GUP1
- Protein CWH43
Sequence:
MRLAVVVTLLVHCFLVTCSPGDNLDEFIDCTYACEYNRRCPNSQINYIDPETNMFHDIEFFDTPPLYSKLLFWDCISDCDYQCQHIITRWRIDEEEEIYQFHGKWPFLRVLGTQEFFSTIFSIGNFIPHYKGFVKFSRIIREEGDRRRKNSRSILIWNYLYVTVAGMLAWTASSVFHCRDLIITEKLDYFFAGLTVLTGFHAIFARMTSMFLYPKIAQAFTASVAAIFALHILRLYVDWSYTYNMRFNIFFGVLQYILLIMLSCQNYHALQKQKLMGEFKKTAYSSFKRQIFKLCVIPILLVIVTTMAMSLELFDFFSYEWQIDAHALWHLCTIWPSWVLYDFFLEDYAYWGNRQLY
Protein: Immunoglobulin heavy constant mu [Cleaved into: Mu' chain (55 kDa mu' chain)] (P01872)
Organism: Mus musculus (Mouse)
Function: IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions (By similarity).
Subcellular location: [Isoform 1]: Secreted {ECO:0000269|PubMed:10899913, ECO:0000269|PubMed:11062505}. Note=During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:10899913}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
SQSFPNVFPLVSCESPLSDKNLVAMGCLARDFLPSTISFTWNYQNNTEVIQGIRTFPTLRTGGKYLATSQVLLSPKSILEGSDEYLVCKIHYGGKNRDLHVPIPAVAEMNPNVNVFVPPRDGFSGPAPRKSKLICEATNFTPKPITVSWLKDGKLVESGFTTDPVTIENKGSTPQTYKVISTLTISEIDWLNLNVYTCRVDHRGLTFLKNVSSTCAASPSTDILTFTIPPSFADIFLSKSANLTCLVSNLATYETLNISWASQSGEPLETKIKIMESHPNGTFSAKGVASVCVEDWNNRKEFVCTVTHRDLPSPQKKFISKPNEVHKHPPAVYLLPPAREQLNLRESATVTCLVKGFSPADISVQWLQRGQLLPQEKYVTSAPMPEPGAPGFYFTHSILTVTEEEWNSGETYTCVVGHEALPHLVTERTVDKSTGKPTLYNVSLIMSDTGGTCY
Protein: Probable D-xylose utilization operon transcriptional repressor (HTH-type transcriptional regulator GntR) (Q8GAL4)
Organism: Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans)
Function: Transcriptional regulator involved in the regulation of the entire oxidative D-xylose degradation pathway via repression of the corresponding genes.
Interaction partners:
Sequence:
MDATSKRLTRTTVASQVRDFIVMEIAQGRLPLGAPVREMEIAAQLGTSQTPVREAFRELAALGLLESRIHVGTRVRQLAEKDLVEAVPIRSALEGIAGRLAANNYHKHAEEVRGSFEAMKEVAEGGDRRVFAAASTTFHRSVVRAAENASLLRAWNALGIEVMTILAMASSDIPLDDAAESHRPIVDALEAGDPELAEHALTHHVAAYLPATAHSNGGVDAAVQAS
Protein: FERM domain-containing protein 4B (GRP1-binding protein GRSP1) (Q9Y2L6)
Organism: Homo sapiens (Human)
Function: Member of GRP1 signaling complexes that are acutely recruited to plasma membrane ruffles in response to insulin receptor signaling. May function as a scaffolding protein that regulates epithelial cell polarity by connecting ARF6 activation with the PAR3 complex. Plays a redundant role with FRMD4A in epithelial polarization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q920B0}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q920B0}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q920B0}. Note=Colocalized with PARD3 at adherens junction and tight junction. {ECO:0000250|UniProtKB:Q920B0}.
Interaction partners:
- Cytohesin-1
- Cytohesin-3
Sequence:
MASVFMCGVEDLLFSGSRFVWNLTVSTLRRWYTERLRACHQVLRTWCGLQDVYQMTEGRHCQVHLLDDRRLELLVQPKLLARELLDLVASHFNLKEKEYFGITFIDDTGQQNWLQLDHRVLDHDLPKKPGPTILHFAVRFYIESISFLKDKTTVELFFLNAKACVHKGQIEVESETIFKLAAFILQEAKGDYTSDENARKDLKTLPAFPTKTLQEHPSLAYCEDRVIEHYLKIKGLTRGQAVVQYMKIVEALPTYGVHYYAVKDKQGLPWWLGISYKGIGQYDIQDKVKPRKLFQWKQLENLYFREKKFAVEVHDPRRISVSRRTFGQSGLFVQTWYANSSLIKSIWVMAISQHQFYLDRKQSKAKIPSARSLDEIAMDLTETGTQRASKLVTLETKSQFIMASNGSLISSGSQDSEVSEEQKREKILELKKKEKLLQEKLLKKVEELKKICLREAELTGKMPKEYPLNIGEKPPQVRRRVGTAFKLDDNLLPSEEDPALQELESNFLIQQKLVEAAKKLANEPDLCKTVKKKRKQDYTDAMKKLQEIENAINEYRIRCGKKPSQKATVLPEDIIPSESSSLSDTTTYDDPSDAFTFPGQRSSSVPHSPRILPPKSLGIERIHFRKSSINEQFVDTRQSREMLSTHSSPYKTLERRPQGGRSMPTTPVLTRNAYSSSHLEPESSSQHCRQRSGSLESQSHLLSEMDSDKPFFSLSKSQRSSSTEILDDGSSYTSQSSTEYYCVTPVTGPYYTTQTLDTRTRGRRRSKKQNVSTSNSGSMPNLAQKDSLRNGVYSKSQEPPSSSYYIAGYTPYAECDFYYSGGYVYENDTEGQYSVNPSYRSSAHYGYERQRDYSRSFHEDEVDRVPHNPYATLRLPRKAAAKSEHITKNIHKALVAEHLRGWYQRASGQKDQGHSPQTSFDSDRGSQRCLGFAGLQVPCSPSSRASSYSSVSSTNASGNWRTQLTIGLSDYETPAHSSYTSCYGNVYNPLPSPSRQYTEISQLDGTDGNQLEDNLESSEQRLFWHEDSKPGTLV
Protein: Heterogeneous nuclear ribonucleoprotein H (hnRNP H) [Cleaved into: Heterogeneous nuclear ribonucleoprotein H, N-terminally processed] (O35737)
Organism: Mus musculus (Mouse)
Function: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA alternative splicing regulation. Inhibits, together with CUGBP1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Binds to the IR RNA. Binds poly(RG) (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250}.
Interaction partners:
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein A1
- Serine/arginine-rich splicing factor 1
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein A3
- Probable ATP-dependent RNA helicase DDX5
- Heterogeneous nuclear ribonucleoprotein F
Sequence:
MMLGAEGGEGFVVKVRGLPWSCSADEVQRFFSDCKIQNGAQGIRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNNVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGITLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMAMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYNGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSTFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEDAVAAMSKDKANMQHRYVELFLNSTAGASGGAYEHRYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDFQSNIA
Protein: Calcium-binding protein 8 (CaBP8) (Calneuron I) (Calneuron-1) (Q9JJG7)
Organism: Mus musculus (Mouse)
Function: Negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. May play a role in the physiology of neurons and is potentially important in memory and learning.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9BXU9}. Cell membrane {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRLPEQPGDGKPENETKGDQETPERGEEPRRSPAPDFPTWEKMPFHHVTAGLLYKGNYLNRSLSAGSDSEQLANISVEELDEIREAFRVLDRDGNGFISKQELGMAMRSLGYMPSEVELAIIMQRLDMDGDGQVDFDEFMTILGPKLVSSEGRDGFLGNTIDSIFWQFDMQRVTLEELKHILYHAFRDHLTMKDIENIIINEEESLNETSGNCQTEFEGVHSQKQNRQTCVRKSLICAFAMAFIISVMLIAANQILRSGME
Protein: UDP-glycosyltransferase 72E2 (EC 2.4.1.111) (Hydroxycinnamate 4-beta-glucosyltransferase UGT72E2) (EC 2.4.1.126) (Q9LVR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the O-glucosylation of monolignols (alcohol monomers of lignin). Glucosylates coniferyl alcohol to form coniferyl alcohol 4-O-glucoside. Glucosylates sinapyl alcohol to form sinapyl alcohol 4-O-glucoside. Glucosylates coniferyl aldehyde to form coniferyl aldehyde 4-O-glucoside. Glucosylates sinapyl aldehyde to form sinapyl aldehyde 4-O-glucoside. Possesses low activity with sinapate and ferulate as substrates.
Interaction partners:
- Cytochrome P450 84A1
- Flavone 3'-O-methyltransferase 1
- F5F19.5 protein
- UDP-glycosyltransferase 72E3
- Cytochrome P450 84A4
- UDP-glycosyltransferase 72E1
- Peroxidase 13
- Peroxidase 71
- Peroxidase 73
- Aldehyde dehydrogenase family 2 member C4
Sequence:
MHITKPHAAMFSSPGMGHVIPVIELGKRLSANNGFHVTVFVLETDAASAQSKFLNSTGVDIVKLPSPDIYGLVDPDDHVVTKIGVIMRAAVPALRSKIAAMHQKPTALIVDLFGTDALCLAKEFNMLSYVFIPTNARFLGVSIYYPNLDKDIKEEHTVQRNPLAIPGCEPVRFEDTLDAYLVPDEPVYRDFVRHGLAYPKADGILVNTWEEMEPKSLKSLLNPKLLGRVARVPVYPIGPLCRPIQSSETDHPVLDWLNEQPNESVLYISFGSGGCLSAKQLTELAWGLEQSQQRFVWVVRPPVDGSCCSEYVSANGGGTEDNTPEYLPEGFVSRTSDRGFVVPSWAPQAEILSHRAVGGFLTHCGWSSTLESVVGGVPMIAWPLFAEQNMNAALLSDELGIAVRLDDPKEDISRWKIEALVRKVMTEKEGEAMRRKVKKLRDSAEMSLSIDGGGLAHESLCRVTKECQRFLERVVDLSRGA
Protein: Nitric oxide synthase-interacting protein (E3 ubiquitin-protein ligase NOSIP) (RING-type E3 ubiquitin transferase NOSIP) (M0R3B2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTRHGKNCTAGAVYTYHEKKKDTAASGYGTQNIRLSRDAVKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQKKEIARQMKAYEKQRGTRREEQKELQRAASQDHVRGFLEKESAIVSRPLNPFTAKALSGTSPDDVQPGPSVGPPSKDKDKVLPSFWIPSLTPEAKATKLEKPSRTVTCPMSGKPLRMSDLTPVHFTPLDSSVDRVGLITRSERYVCAVTRDSLSNATPCAVLRP
Protein: RNA helicase (EC 3.6.4.13) (Q382F6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Sas10 C-terminal domain-containing protein
- Nrap protein domain-containing protein
- rRNA biogenesis protein, putative
- KRR1 small subunit processome component
- Nop14-like protein
- Probable eukaryotic initiation factor 4A
- DDB1- and CUL4-associated factor 13
- BING4 C-terminal domain-containing protein
- Probable eukaryotic initiation factor 4A
- Uncharacterized protein
Sequence:
MDIFSALSTGAKFEPKKHGTAIKRFRQASGNREQTGALNLVSLSRGSVELPTPSHTLEIFGVPKRMRCQETSAEGDEESRGRCDTDTSSAATGHKPLKNMSVKRRRNIWRKNELDVTGMDVPQPIEHFSQLLRPPLSLDECLISNLFERNHRIPTPIQMQTIPCLVQGRDVLACAPTGSGKTVAFLIPMFARLGKPDRDAGVRALIITPTMELAEQIEREAFFLLKGKRWKLVQHGQTTRNKDIFITTPGRVSTLLERKLVDLSNIQYLVFDEGDRLWDSSTDNLRVMDIVLTACTYKEKVVALFTATLSEKIEAAARSVMGPDPVRIIVSGRAKANKNVKQELVFCGNELGKVVAIRNIVREGVTPPVLIFVQSIERTKELHEEIQCQGLRIAIMNAKMTHEERDETMMNFRLGKIWVLVTTELLSRGIDFKNVGTVINFDIPTTVESYIHRVGRCGRAGKTGKAITFFTEDDKHRIPPIARVMKESGSPIEDWMLEIKTHRSVRRRLQRTTPHRMIVSTRKRMLVADQRMKRQLRRLEYENAQKAEGQGVEEVQ
Protein: Cingulin (H0Y4A8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQDPTMLQFKSTPDLLRDQQEAAPPGSVDHMKATIYGILREGSSESETSVRRKVSLVLEKMQPLVAVAGQGELTRKVEELQRKLDEEVKKRQKLEPSQVGLERQLEEKTEECSRLQELLERRKGEAQQSNK
Protein: Palmitoyltransferase ZDHHC14 (EC 2.3.1.225) (DHHC domain-containing cysteine-rich protein 14) (DHHC-14) (NEW1 domain-containing protein) (NEW1CP) (Zinc finger DHHC domain-containing protein 14) (Q8IZN3)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and thereby regulate G protein-coupled receptor signaling. May play a role in cell differentiation and apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:27481942}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPPGGGGPMKDCEYSQISTHSSSPMESPHKKKKIAARRKWEVFPGRNKFFCNGRIMMARQTGVFYLTLVLILVTSGLFFAFDCPYLAVKITPAIPAVAGILFFFVMGTLLRTSFSDPGVLPRATPDEAADLERQIDIANGTSSGGYRPPPRTKEVIINGQTVKLKYCFTCKIFRPPRASHCSLCDNCVERFDHHCPWVGNCVGKRNYRFFYMFILSLSFLTVFIFAFVITHVILRSQQTGFLNALKDSPASVLEAVVCFFSVWSIVGLSGFHTYLISSNQTTNEDIKGSWSNKRGKENYNPYSYGNIFTNCCVALCGPISPSLIDRRGYIQPDTPQPAAPSNGITMYGATQSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLTSDELHLPGKPGLGTPCASLTLGPPTPPASMPNLAEATLADVMPRKDEHMGHQFLTPDEAPSPPRLLAAGSPLAHSRTMHVLGLASQDSLHEDSVRGLVKLSSV