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Protein

Protein arginine N-methyltransferase 5

Gene

PRMT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21258366, PubMed:21917714, PubMed:22269951, PubMed:21081503). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:12411503, PubMed:11747828, PubMed:17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed:12718890). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21917714, PubMed:21258366). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed:25092918). Symmetrically methylates NCL (PubMed:21081503).By similarity17 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.2 Publications

Enzyme regulationi

Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei304Peptide substrate1 Publication1
Binding sitei307Peptide substrate1 Publication1
Binding sitei324S-adenosyl-L-methionine1 Publication1
Sitei327Critical for specifying symmetric addition of methyl groupsBy similarity1
Binding sitei392S-adenosyl-L-methionine1 Publication1
Active sitei435Proton donor/acceptor1 Publication1
Active sitei444Proton donor/acceptor1 Publication1

GO - Molecular functioni

  • core promoter sequence-specific DNA binding Source: UniProtKB
  • histone-arginine N-methyltransferase activity Source: Reactome
  • histone methyltransferase activity (H4-R3 specific) Source: UniProtKB
  • identical protein binding Source: IntAct
  • methyl-CpG binding Source: UniProtKB
  • methyltransferase activity Source: MGI
  • protein-arginine N-methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N symmetric methyltransferase activity Source: UniProtKB
  • protein heterodimerization activity Source: MGI
  • ribonucleoprotein complex binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • circadian regulation of gene expression Source: UniProtKB
  • DNA-templated transcription, termination Source: UniProtKB
  • endothelial cell activation Source: UniProtKB
  • Golgi ribbon formation Source: UniProtKB
  • histone H4-R3 methylation Source: UniProtKB
  • liver regeneration Source: Ensembl
  • negative regulation of cell differentiation Source: Ensembl
  • peptidyl-arginine methylation Source: UniProtKB
  • peptidyl-arginine N-methylation Source: WormBase
  • positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: WormBase
  • positive regulation of oligodendrocyte differentiation Source: Ensembl
  • regulation of DNA methylation Source: Ensembl
  • regulation of ERK1 and ERK2 cascade Source: Ensembl
  • regulation of mitotic nuclear division Source: ProtInc
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: GO_Central
  • spliceosomal snRNP assembly Source: UniProtKB

Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processBiological rhythms, Transcription, Transcription regulation
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:HS02092-MONOMER
BRENDAi2.1.1.125 2681
ReactomeiR-HSA-191859 snRNP Assembly
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-6804760 Regulation of TP53 Activity through Methylation
SIGNORiO14744

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 5 (EC:2.1.1.3202 Publications)
Alternative name(s):
72 kDa ICln-binding protein
Histone-arginine N-methyltransferase PRMT5
Jak-binding protein 1
Shk1 kinase-binding protein 1 homolog
Short name:
SKB1 homolog
Short name:
SKB1Hs
Cleaved into the following chain:
Gene namesi
Name:PRMT5
Synonyms:HRMT1L5, IBP72, JBP1, SKB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000100462.15
HGNCiHGNC:10894 PRMT5
MIMi604045 gene
neXtProtiNX_O14744

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365 – 369Missing : Increased MAPK1/MAPK3 phosphorylation in response to EGF. 1 Publication5
Mutagenesisi367 – 368GR → AA: Abolishes enzymatic activity. 1 Publication2

Organism-specific databases

DisGeNETi10419
OpenTargetsiENSG00000100462
PharmGKBiPA35794

Chemistry databases

ChEMBLiCHEMBL1795116
GuidetoPHARMACOLOGYi1256

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123421 – 637Protein arginine N-methyltransferase 5Add BLAST637
Initiator methionineiRemoved; alternateCombined sources2 Publications
ChainiPRO_00004176022 – 637Protein arginine N-methyltransferase 5, N-terminally processedAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine; in Protein arginine N-methyltransferase 5, N-terminally processedCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO14744
MaxQBiO14744
PaxDbiO14744
PeptideAtlasiO14744
PRIDEiO14744
ProteomicsDBi48200
48201 [O14744-2]

PTM databases

iPTMnetiO14744
PhosphoSitePlusiO14744
SwissPalmiO14744

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000100462
CleanExiHS_PRMT5
ExpressionAtlasiO14744 baseline and differential
GenevisibleiO14744 HS

Organism-specific databases

HPAiCAB012459
HPA005525
HPA064708

Interactioni

Subunit structurei

Forms, at least, homodimers and homotetramers. Component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A (PubMed:21081503). Found in a complex composed of PRMT5, WDR77 and RIOK1 (PubMed:21081503). RIOK1 and CLNS1A associate with PRMT5 in a mutually exclusive fashion, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (PubMed:21081503). Interacts with PRDM1 (By similarity). Identified in a complex composed of methylosome and PRMT1 and ERH (PubMed:25284789). Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation. Interacts with HOXA9. Interacts with SRGAP2. Found in a complex with COPRS, RUNX1 AND CBFB. Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1 (PubMed:25284789). Interacts with EPB41L3; this modulates methylation of target proteins. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with JAK2, SSTR1, SUPT5H, BRAF and with active RAF1. Interacts with LSM11, PRMT7 and SNRPD3 (PubMed:17709427, PubMed:16087681). Interacts with COPRS; promoting its recruitment on histone H4. Interacts with CLNS1A/pICln (PubMed:21081503, PubMed:9556550). Identified in a complex with CLNS1A/pICln and Sm proteins. Interacts with RPS10 (PubMed:20159986). Interacts with WDR77. Interacts with IWS1. Interacts with CRY1. Interacts with POLR2A (PubMed:26700805). Interacts with SMN1/SMN2 (PubMed:26700805). Interacts with LYAR; this interaction is direct (PubMed:25092918).By similarity23 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi115688, 190 interactors
ComplexPortaliCPX-696 Methylosome
CORUMiO14744
DIPiDIP-33172N
IntActiO14744, 102 interactors
MINTiO14744
STRINGi9606.ENSP00000319169

Chemistry databases

BindingDBiO14744

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Helixi26 – 35Combined sources10
Beta strandi39 – 46Combined sources8
Beta strandi54 – 56Combined sources3
Helixi59 – 61Combined sources3
Helixi70 – 72Combined sources3
Helixi75 – 81Combined sources7
Beta strandi82 – 85Combined sources4
Helixi97 – 117Combined sources21
Beta strandi120 – 125Combined sources6
Helixi132 – 142Combined sources11
Beta strandi144 – 146Combined sources3
Beta strandi150 – 158Combined sources9
Helixi160 – 163Combined sources4
Helixi181 – 183Combined sources3
Helixi184 – 195Combined sources12
Turni196 – 198Combined sources3
Beta strandi202 – 207Combined sources6
Helixi215 – 219Combined sources5
Turni220 – 223Combined sources4
Beta strandi226 – 232Combined sources7
Helixi233 – 235Combined sources3
Helixi248 – 259Combined sources12
Beta strandi263 – 268Combined sources6
Helixi273 – 275Combined sources3
Helixi279 – 289Combined sources11
Helixi296 – 300Combined sources5
Helixi302 – 304Combined sources3
Beta strandi309 – 311Combined sources3
Turni314 – 316Combined sources3
Helixi321 – 327Combined sources7
Helixi331 – 348Combined sources18
Helixi351 – 353Combined sources3
Turni354 – 356Combined sources3
Beta strandi358 – 365Combined sources8
Turni367 – 369Combined sources3
Helixi370 – 381Combined sources12
Beta strandi385 – 393Combined sources9
Helixi395 – 407Combined sources13
Helixi410 – 412Combined sources3
Beta strandi413 – 418Combined sources6
Turni420 – 422Combined sources3
Beta strandi429 – 433Combined sources5
Helixi442 – 444Combined sources3
Helixi446 – 453Combined sources8
Helixi454 – 456Combined sources3
Beta strandi457 – 465Combined sources9
Beta strandi467 – 476Combined sources10
Helixi478 – 485Combined sources8
Helixi496 – 499Combined sources4
Beta strandi502 – 505Combined sources4
Beta strandi516 – 524Combined sources9
Beta strandi527 – 529Combined sources3
Beta strandi534 – 541Combined sources8
Beta strandi546 – 560Combined sources15
Beta strandi563 – 566Combined sources4
Helixi569 – 571Combined sources3
Beta strandi582 – 592Combined sources11
Beta strandi597 – 606Combined sources10
Beta strandi608 – 621Combined sources14
Helixi628 – 630Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GQBX-ray2.06A1-637[»]
4X60X-ray2.35A2-637[»]
4X61X-ray2.85A2-637[»]
4X63X-ray3.05A2-637[»]
5C9ZX-ray2.36A2-637[»]
5EMJX-ray2.27A2-637[»]
5EMKX-ray2.52A2-637[»]
5EMLX-ray2.39A2-637[»]
5EMMX-ray2.37A2-637[»]
5FA5X-ray2.34A1-637[»]
ProteinModelPortaliO14744
SMRiO14744
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini308 – 615SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 292TIM barrel1 PublicationAdd BLAST280
Regioni333 – 334S-adenosyl-L-methionine binding1 Publication2
Regioni419 – 420S-adenosyl-L-methionine binding1 Publication2
Regioni465 – 637Beta barrel1 PublicationAdd BLAST173
Regioni488 – 494Dimerization1 Publication7

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0822 Eukaryota
ENOG410XNZM LUCA
GeneTreeiENSGT00390000001141
HOGENOMiHOG000175933
HOVERGENiHBG057083
InParanoidiO14744
KOiK02516
OMAiFPMFFPT
OrthoDBiEOG091G03PD
PhylomeDBiO14744
TreeFamiTF300626

Family and domain databases

InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR007857 Arg_MeTrfase_PRMT5
IPR035075 PRMT5
IPR035248 PRMT5_C
IPR035247 PRMT5_TIM
IPR029063 SAM-dependent_MTases
PANTHERiPTHR10738 PTHR10738, 1 hit
PfamiView protein in Pfam
PF05185 PRMT5, 1 hit
PF17286 PRMT5_C, 1 hit
PF17285 PRMT5_TIM, 1 hit
PIRSFiPIRSF015894 Skb1_MeTrfase, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seems to exist. According to EST sequences.
Isoform 1 (identifier: O14744-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF
60 70 80 90 100
KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI RPDSKVEKIR
110 120 130 140 150
RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM
160 170 180 190 200
FWMRVPLVAP EDLRDDIIEN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK
210 220 230 240 250
RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKMH
260 270 280 290 300
QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF
310 320 330 340 350
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP
360 370 380 390 400
EEEKDTNVQV LMVLGAGRGP LVNASLRAAK QADRRIKLYA VEKNPNAVVT
410 420 430 440 450
LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL
460 470 480 490 500
DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM
510 520 530 540 550
PYVVRLHNFH QLSAPQPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG
560 570 580 590 600
FAGYFETVLY QDITLSIRPE THSPGMFSWF PILFPIKQPI TVREGQTICV
610 620 630
RFWRCSNSKK VWYEWAVTAP VCSAIHNPTG RSYTIGL
Length:637
Mass (Da):72,684
Last modified:January 23, 2007 - v4
Checksum:i522E255B384F25E7
GO
Isoform 2 (identifier: O14744-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE

Note: No experimental confirmation available.
Show »
Length:620
Mass (Da):71,320
Checksum:i0E489272643DD83C
GO
Isoform 4 (identifier: O14744-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     106-259: Missing.

Note: No experimental confirmation available.
Show »
Length:466
Mass (Da):53,580
Checksum:i62386C5B867CF619
GO
Isoform 5 (identifier: O14744-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-120: Missing.

Note: No experimental confirmation available.
Show »
Length:593
Mass (Da):67,674
Checksum:iD609BFECAFB7D108
GO
Isoform 3 (identifier: O14744-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVA → MRGPNSGTEKGRLVIPE
     77-120: Missing.

Note: No experimental confirmation available.
Show »
Length:576
Mass (Da):66,311
Checksum:i988C2D288FC214A1
GO

Sequence cautioni

The sequence BC005820 differs from that shown. Reason: Frameshift at position 370.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti183E → K in BAG63592 (PubMed:14702039).Curated1
Sequence conflicti247S → F in AAB66581 (PubMed:9843966).Curated1
Sequence conflicti420M → T in BAG63592 (PubMed:14702039).Curated1
Sequence conflicti553G → V in AAB66581 (PubMed:9843966).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0433821 – 34MAAMA…LGAVA → MRGPNSGTEKGRLVIPE in isoform 2, isoform 3 and isoform 4. 2 PublicationsAdd BLAST34
Alternative sequenceiVSP_05468577 – 120Missing in isoform 3 and isoform 5. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_054768106 – 259Missing in isoform 4. 1 PublicationAdd BLAST154

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015913 mRNA Translation: AAB66581.1
AF167572 mRNA Translation: AAF04502.1
AK075251 mRNA Translation: BAG52095.1
AK301812 mRNA Translation: BAG63261.1
AK302240 mRNA Translation: BAG63592.1
CR456741 mRNA Translation: CAG33022.1
AB451246 mRNA Translation: BAG70060.1
AB451370 mRNA Translation: BAG70184.1
AL132780 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW66218.1
CH471078 Genomic DNA Translation: EAW66219.1
CH471078 Genomic DNA Translation: EAW66220.1
CH471078 Genomic DNA Translation: EAW66221.1
BC005820 mRNA No translation available.
BC025979 mRNA Translation: AAH25979.1
CCDSiCCDS41922.1 [O14744-2]
CCDS61394.1 [O14744-3]
CCDS61395.1 [O14744-4]
CCDS61396.1 [O14744-5]
CCDS9579.1 [O14744-1]
PIRiT03842
RefSeqiNP_001034708.1, NM_001039619.2 [O14744-2]
NP_001269882.1, NM_001282953.1 [O14744-3]
NP_001269884.1, NM_001282955.1 [O14744-5]
NP_001269885.1, NM_001282956.1 [O14744-4]
NP_006100.2, NM_006109.4 [O14744-1]
UniGeneiHs.367854

Genome annotation databases

EnsembliENST00000216350; ENSP00000216350; ENSG00000100462 [O14744-3]
ENST00000324366; ENSP00000319169; ENSG00000100462 [O14744-1]
ENST00000397440; ENSP00000380582; ENSG00000100462 [O14744-4]
ENST00000397441; ENSP00000380583; ENSG00000100462 [O14744-2]
ENST00000553897; ENSP00000452555; ENSG00000100462 [O14744-5]
GeneIDi10419
KEGGihsa:10419
UCSCiuc001whl.3 human [O14744-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiANM5_HUMAN
AccessioniPrimary (citable) accession number: O14744
Secondary accession number(s): A8MTP3
, A8MZ91, B4DX49, B4DY30, B5BU10, D3DS33, E2QRE7, Q6IBR1, Q9UKH1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 171 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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