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P14866 (HNRPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein L

Short name=hnRNP L
Gene names
Name:HNRNPL
Synonyms:HNRPL
ORF Names:P/OKcl.14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. Ref.8

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Nucleusnucleoplasm. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9

Domain

RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA (Ref.20). Ref.20

Post-translational modification

Several isoelectric forms of the L protein are probably the results of post-translational modifications.

Phosphorylation at Ser-544 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization.

Miscellaneous

Excess hnRNP L activates NMD of its own mRNA by promoting the inclusion of a 'poison exon' containing a premature stop codon and leading to nonsense-mediated decay. It also cross-regulates inclusion of an analogous 'poison exon' in the hnRNP L-like pre-mRNA (Ref.13).

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Sequence caution

The sequence CAA34261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14866-1)

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.
Isoform 2 (identifier: P14866-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 589589Heterogeneous nuclear ribonucleoprotein L
PRO_0000081862

Regions

Domain102 – 17675RRM 1
Domain193 – 27078RRM 2
Domain382 – 47897RRM 3
Domain495 – 58389RRM 4
Compositional bias39 – 8951Gly-rich
Compositional bias335 – 38248Pro-rich

Amino acid modifications

Modified residue521Phosphoserine Ref.10 Ref.15 Ref.17
Modified residue1011Phosphoserine Ref.17
Modified residue1851Phosphoserine Ref.15 Ref.17
Modified residue2691N6-acetyllysine Ref.14
Modified residue2911Phosphoserine Ref.17
Modified residue2981Phosphoserine Ref.10 Ref.15 Ref.17
Modified residue5441Phosphoserine; by CaMK4 Ref.18

Natural variations

Alternative sequence1 – 133133Missing in isoform 2.
VSP_044301

Experimental info

Mutagenesis1051H → A: 6-fold decrease in RNA-binding affinity. Ref.20
Mutagenesis1321V → A: 4-fold increase in RNA-binding affinity. Ref.20
Mutagenesis1411L → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. Ref.20
Mutagenesis1721N → A: 1-fold increase in RNA-binding affinity. Ref.20
Mutagenesis1741S → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. Ref.20
Mutagenesis5041H → A: Significant decrease in RNA-binding affinity. Ref.20
Mutagenesis5061F → A: Significant decrease in RNA-binding affinity. Ref.20
Sequence conflict3961C → G in BAB18649. Ref.1
Sequence conflict3961C → G in CAA34261. Ref.5

Secondary structure

............................................... 589
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 31EEB51AF1C65F83

FASTA58964,133
        10         20         30         40         50         60 
MSRRLLPRAE KRRRRLEQRQ QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG GSEGGRAPKR 

        70         80         90        100        110        120 
LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA SPVVHIRGLI DGVVEADLVE 

       130        140        150        160        170        180 
ALQEFGPISY VVVMPKKRQA LVEFEDVLGA CNAVNYAADN QIYIAGHPAF VNYSTSQKIS 

       190        200        210        220        230        240 
RPGDSDDSRS VNSVLLFTIL NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS 

       250        260        270        280        290        300 
VQSAQRAKAS LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP 

       310        320        330        340        350        360 
NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG GHRRGPSRYG 

       370        380        390        400        410        420 
PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF NVFCLYGNVE KVKFMKSKPG 

       430        440        450        460        470        480 
AAMVEMADGY AVDRAITHLN NNFMFGQKLN VCVSKQPAIM PGQSYGLEDG SCSYKDFSES 

       490        500        510        520        530        540 
RNNRFSTPEQ AAKNRIQHPS NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE 

       550        560        570        580 
RSSSGLLEWE SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS 

« Hide

Isoform 2 [UniParc].

Checksum: 59DD6B10F1F41E68
Show »

FASTA45650,561

References

« Hide 'large scale' references
[1]"Molecular basis of T cell-mediated recognition of pancreatic cancer cells."
Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
Cancer Res. 61:2038-2046(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Pancreatic cancer.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Synovium.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts."
Pinol-Roma S., Swanson M.S., Gall J.G., Dreyfuss G.
J. Cell Biol. 109:2575-2587(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-589 (ISOFORM 1).
[6]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 67-76; 199-215; 218-233; 386-403; 425-448 AND 549-558, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Keratinocyte.
[8]"Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter."
Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.
Nucleic Acids Res. 30:823-829(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APEX1.
[9]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL."
Oberdoerffer S., Moita L.F., Neems D., Freitas R.P., Hacohen N., Rao A.
Science 321:686-691(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HNRNPLL.
[12]"Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo."
Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y., Tempst P., Chen S., Zhu B., Reinberg D.
J. Biol. Chem. 284:15701-15707(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SETD2.
[13]"Auto- and cross-regulation of the hnRNP L proteins by alternative splicing."
Rossbach O., Hung L.H., Schreiner S., Grishina I., Heiner M., Hui J., Bindereif A.
Mol. Cell. Biol. 29:1442-1451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, MISCELLANEOUS.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-185 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-101; SER-185; SER-291 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"A conserved serine of heterogeneous nuclear ribonucleoprotein L (hnRNP L) mediates depolarization-regulated alternative splicing of potassium channels."
Liu G., Razanau A., Hai Y., Yu J., Sohail M., Lobo V.G., Chu J., Kung S.K., Xie J.
J. Biol. Chem. 287:22709-22716(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-544.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: insights into its roles in alternative splicing regulation."
Zhang W., Zeng F., Liu Y., Zhao Y., Lv H., Niu L., Teng M., Li X.
J. Biol. Chem. 288:22636-22649(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 90-180, X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 380-589, RRM DOMAINS, MUTAGENESIS OF HIS-105; VAL-132; LEU-141; ASN-172; SER-174; HIS-504 AND PHE-506.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB044547 mRNA. Translation: BAB18649.1.
AK292115 mRNA. Translation: BAF84804.1.
AC008982 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56828.1.
X16135 mRNA. Translation: CAA34261.1. Different initiation.
PIRA33616.
RefSeqNP_001005335.1. NM_001005335.1.
NP_001524.2. NM_001533.2.
UniGeneHs.644906.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R27X-ray2.04A/B90-180[»]
3TO8X-ray1.82A380-589[»]
ProteinModelPortalP14866.
SMRP14866. Positions 97-290, 379-582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109432. 73 interactions.
DIPDIP-36355N.
IntActP14866. 30 interactions.
MINTMINT-1422378.
STRING9606.ENSP00000221419.

PTM databases

PhosphoSiteP14866.

Polymorphism databases

DMDM215274006.

2D gel databases

REPRODUCTION-2DPAGEIPI00027834.
SWISS-2DPAGEP14866.

Proteomic databases

PaxDbP14866.
PRIDEP14866.

Protocols and materials databases

DNASU3191.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221419; ENSP00000221419; ENSG00000104824. [P14866-1]
ENST00000600873; ENSP00000470231; ENSG00000104824. [P14866-2]
GeneID3191.
KEGGhsa:3191.
UCSCuc002ojk.3. human. [P14866-2]
uc021uuh.1. human. [P14866-1]

Organism-specific databases

CTD3191.
GeneCardsGC19M039327.
H-InvDBHIX0174642.
HGNCHGNC:5045. HNRNPL.
HPACAB016326.
HPA051748.
MIM164021. gene.
603083. gene.
neXtProtNX_P14866.
PharmGKBPA162391389.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326285.
HOGENOMHOG000293298.
HOVERGENHBG105786.
InParanoidP14866.
KOK13159.
OMAPYEGRRM.
OrthoDBEOG7HMS2K.
PhylomeDBP14866.
TreeFamTF354318.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP14866.
BgeeP14866.
CleanExHS_HNRNPL.
GenevestigatorP14866.

Family and domain databases

Gene3D3.30.70.330. 4 hits.
InterProIPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPL. human.
GeneWikiHNRNPL.
GenomeRNAi3191.
NextBio12694.
PROP14866.
SOURCESearch...

Entry information

Entry nameHNRPL_HUMAN
AccessionPrimary (citable) accession number: P14866
Secondary accession number(s): A6ND69, A6NIT8, Q9H3P3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM