CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006029
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein H 
Protein Synonyms/Alias
 hnRNP H; Heterogeneous nuclear ribonucleoprotein H, N-terminally processed 
Gene Name
 HNRNPH1 
Gene Synonyms/Alias
 HNRPH; HNRPH1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35QRFFSDCKIQNGAQGubiquitination[1, 2, 3, 4]
87HRYVEVFKSNNVEMDubiquitination[1, 4]
98VEMDWVLKHTGPNSPubiquitination[1, 3, 4, 5]
167ASQEIAEKALKKHKEacetylation[6]
167ASQEIAEKALKKHKEubiquitination[1, 3, 4, 5, 7]
185HRYIEIFKSSRAEVRubiquitination[1, 2, 3, 4, 5]
200THYDPPRKLMAMQRPubiquitination[5]
349VAAMSKDKANMQHRYubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865
Functional Description
 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). 
Sequence Annotation
 DOMAIN 11 90 RRM 1.
 DOMAIN 111 188 RRM 2.
 REPEAT 234 249 1-1.
 DOMAIN 289 364 RRM 3.
 REPEAT 354 372 2-1.
 REPEAT 374 392 2-2.
 REPEAT 418 433 1-2.
 REGION 234 433 2 X 16 AA Gly-rich approximate repeats.
 REGION 354 392 2 X 19 AA perfect repeats.
 MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
 MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 63 63 Phosphoserine.
 MOD_RES 104 104 Phosphoserine (By similarity).
 MOD_RES 107 107 Phosphothreonine (By similarity).
 MOD_RES 233 233 Dimethylated arginine; alternate.
 MOD_RES 233 233 Omega-N-methylarginine; alternate.
 MOD_RES 246 246 Phosphotyrosine.
 MOD_RES 310 310 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 449 AA 
Protein Sequence
MMLGTEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE GRPSGEAFVE 60
LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT GPNSPDTAND GFVRLRGLPF 120
GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY 180
IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY 240
GGYDDYNGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA 300
TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA NMQHRYVELF 360
LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY 420
GGGYGGQSSM SGYDQVLQEN SSDFQSNIA 449 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008266; F:poly(U) RNA binding; TAS:ProtInc.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR012996; Znf_CHHC. 
Pfam
 PF08080; zf-RNPHF 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS