Reviewed, UniProtKB/Swiss-Prot P31942 (HNRH3_HUMAN)

Names and origin

Protein names

Recommended name:
    Heterogeneous nuclear ribonucleoprotein H3
      Short name=hnRNP H3
      Short name=hnRNP 2H9

Gene names

Name:	HNRNPH3
Synonyms:	HNRPH3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction.
Subcellular location	Nucleus.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Ref.2 Non-traceable author statement. Source: UniProtKB
Cellular component	heterogeneous nuclear ribonucleoprotein complex Ref.1 Ref.2 Non-traceable author statement. Source: UniProtKB
Molecular function	RNA binding Ref.1 Ref.2 Non-traceable author statement. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STK24	Q5T5B3	1	EBI-711437,EBI-1054809
TOB1	P50616	1	EBI-711437,EBI-723281

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P31942-1)

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: P31942-2)

Also known as: 2H9A;

The sequence of this isoform differs from the canonical sequence as follows:
     132-146: Missing.

Isoform 3 (identifier: P31942-3)

Also known as: 2H9B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Isoform 4 (identifier: P31942-4)

Also known as: 2H9C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.

Isoform 5 (identifier: P31942-5)

Also known as: 2H9D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.

Isoform 6 (identifier: P31942-6)

Also known as: 2H9E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-145: RGGDGYDG → MCFSLNYT
     259-276: QHRYIELFLNSTPGGGSG → RKWCLWHTILFPKREFIK
     277-346: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Heterogeneous nuclear ribonucleoprotein H3		PRO_0000081861
Regions
	Domain	16 – 93	78	RRM 1
	Domain	195 – 270	76	RRM 2
	Compositional bias	108 – 344	237	Gly-rich
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.7
	Modified residue	121	1	Asymmetric dimethylarginine Ref.10
	Modified residue	216	1	Phosphoserine Ref.12 Ref.14 Ref.15
	Modified residue	287	1	Omega-N-methylarginine Ref.7
	Modified residue	296	1	Phosphotyrosine Ref.11 Ref.13
	Modified residue	298	1	Phosphoserine
	Modified residue	314	1	Phosphothreonine
Natural variations
	Alternative sequence	1 – 137	137	Missing in isoform 6.		VSP_005841
	Alternative sequence	1 – 131	131	Missing in isoform 4 and isoform 5.		VSP_005839
	Alternative sequence	1 – 49	49	Missing in isoform 3.		VSP_005838
	Alternative sequence	132 – 146	15	Missing in isoform 2.		VSP_005840
	Alternative sequence	138 – 145	8	RGGDGYDG → MCFSLNYT in isoform 6.		VSP_005842
	Alternative sequence	259 – 276	18	QHRYI…GGGSG → RKWCLWHTILFPKREFIK in isoform 5 and isoform 6.		VSP_005843
	Alternative sequence	277 – 346	70	Missing in isoform 5 and isoform 6.		VSP_005844
	Natural variant	163	1	N → S: dbSNP rs2273903.		VAR_020333
	Natural variant	284	1	G → A: dbSNP rs16925347.		VAR_052226

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: F7D14C2947930E9E	FASTA	346	36,926
	10 20 30 40 50 60 MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM DYQGRSTGEA 70 80 90 100 110 120 FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY DPPRRLLGQR PGPYDRPIGG 130 140 150 160 170 180 RGGYYGAGRG SMYDRMRRGG DGYDGGYGGF DDYGGYNNYG YGNDGFDDRM RDGRGMGGHG 190 200 210 220 230 240 YGGAGDASSG FHGGHFVHMR GLPFRATEND IANFFSPLNP IRVHIDIGAD GRATGEADVE 250 260 270 280 290 300 FVTHEDAVAA MSKDKNNMQH RYIELFLNST PGGGSGMGGS GMGGYGRDGM DNQGGYGSVG 310 320 330 340 RMGMGNNYSG GYGTPDGLGG YGRGGGGSGG YYGQGGMSGG GWRGMY
	Isoform 2 (2H9A). Checksum: A3BA8D0F5FC07369	FASTA	331	35,239
	10 20 30 40 50 60 MDWVMKHNGP NDASDGTVRL RGLPFGCSKE EIVQFFQGLE IVPNGITLTM DYQGRSTGEA 70 80 90 100 110 120 FVQFASKEIA ENALGKHKER IGHRYIEIFR SSRSEIKGFY DPPRRLLGQR PGPYDRPIGG 130 140 150 160 170 180 RGGYYGAGRG SYGGFDDYGG YNNYGYGNDG FDDRMRDGRG MGGHGYGGAG DASSGFHGGH 190 200 210 220 230 240 FVHMRGLPFR ATENDIANFF SPLNPIRVHI DIGADGRATG EADVEFVTHE DAVAAMSKDK 250 260 270 280 290 300 NNMQHRYIEL FLNSTPGGGS GMGGSGMGGY GRDGMDNQGG YGSVGRMGMG NNYSGGYGTP 310 320 330 DGLGGYGRGG GGSGGYYGQG GMSGGGWRGM Y
	Isoform 3 (2H9B). Checksum: AAE63A29063E5153	FASTA	297	31,525
	10 20 30 40 50 60 MDYQGRSTGE AFVQFASKEI AENALGKHKE RIGHRYIEIF RSSRSEIKGF YDPPRRLLGQ 70 80 90 100 110 120 RPGPYDRPIG GRGGYYGAGR GSMYDRMRRG GDGYDGGYGG FDDYGGYNNY GYGNDGFDDR 130 140 150 160 170 180 MRDGRGMGGH GYGGAGDASS GFHGGHFVHM RGLPFRATEN DIANFFSPLN PIRVHIDIGA 190 200 210 220 230 240 DGRATGEADV EFVTHEDAVA AMSKDKNNMQ HRYIELFLNS TPGGGSGMGG SGMGGYGRDG 250 260 270 280 290 MDNQGGYGSV GRMGMGNNYS GGYGTPDGLG GYGRGGGGSG GYYGQGGMSG GGWRGMY
	Isoform 4 (2H9C). Checksum: 969F8FE2710D2646	FASTA	215	22,322
	10 20 30 40 50 60 MYDRMRRGGD GYDGGYGGFD DYGGYNNYGY GNDGFDDRMR DGRGMGGHGY GGAGDASSGF 70 80 90 100 110 120 HGGHFVHMRG LPFRATENDI ANFFSPLNPI RVHIDIGADG RATGEADVEF VTHEDAVAAM 130 140 150 160 170 180 SKDKNNMQHR YIELFLNSTP GGGSGMGGSG MGGYGRDGMD NQGGYGSVGR MGMGNNYSGG 190 200 210 YGTPDGLGGY GRGGGGSGGY YGQGGMSGGG WRGMY
	Isoform 5 (2H9D). Checksum: 286234CBE7C9C996	FASTA	145	16,084
	10 20 30 40 50 60 MYDRMRRGGD GYDGGYGGFD DYGGYNNYGY GNDGFDDRMR DGRGMGGHGY GGAGDASSGF 70 80 90 100 110 120 HGGHFVHMRG LPFRATENDI ANFFSPLNPI RVHIDIGADG RATGEADVEF VTHEDAVAAM 130 140 SKDKNNMRKW CLWHTILFPK REFIK
	Isoform 6 (2H9E). Checksum: F1E137E637675D93	FASTA	139	15,413
	10 20 30 40 50 60 MCFSLNYTGY GGFDDYGGYN NYGYGNDGFD DRMRDGRGMG GHGYGGAGDA SSGFHGGHFV 70 80 90 100 110 120 HMRGLPFRAT ENDIANFFSP LNPIRVHIDI GADGRATGEA DVEFVTHEDA VAAMSKDKNN 130 MRKWCLWHTI LFPKREFIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human 2H9 heterogeneous nuclear ribonucleoproteins. Relation with splicing and early heat shock-induced splicing arrest." Mahe D., Mahl P., Gattoni R., Fischer N., Mattei M.-G., Stevenin J., Fuchs J.-P. J. Biol. Chem. 272:1827-1836(1997) [PubMed: 8999868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]	"The hnRNP 2H9 gene, which is involved in the splicing reaction, is a multiply spliced gene." Honore B. Biochim. Biophys. Acta 1492:108-119(2000) [PubMed: 10858537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[3]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). Tissue: Brain and Placenta.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterus.
[5]	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. , 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].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Ovary and Skin.
[7]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-6; 56-76; 85-90; 98-104; 175-200; 223-253 AND 262-323, ACETYLATION AT MET-1, METHYLATION AT ARG-287, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[8]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 56-67; 206-222; 233-253 AND 262-287, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]	"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: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 94-104 AND 288-298. Tissue: Keratinocyte.
[10]	"A post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-Arg, found in a natural HLA class I peptide ligand." Yague J., Vazquez J., Lopez de Castro J.A. Protein Sci. 9:2210-2217(2000) [PubMed: 11152131] [Abstract] Cited for: PROTEIN SEQUENCE OF 116-127, METHYLATION AT ARG-121.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-296, MASS SPECTROMETRY.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-296, MASS SPECTROMETRY.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-298 AND THR-314, MASS SPECTROMETRY. Tissue: T-cell.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L32610 mRNA. Translation: AAD45179.1. AF132360 Genomic DNA. Translation: AAF68843.1. AF132360 Genomic DNA. Translation: AAF68844.1. AF132360 Genomic DNA. Translation: AAF68845.1. AF132360 Genomic DNA. Translation: AAF68846.1. AF132360 Genomic DNA. Translation: AAF68847.1. AF132360 Genomic DNA. Translation: AAF68848.1. AF132361 mRNA. Translation: AAF68849.1. AF132362 mRNA. Translation: AAF68850.1. AF132363 mRNA. Translation: AAF68851.1. AF132364 mRNA. Translation: AAF68852.1. AK091411 mRNA. Translation: BAG52353.1. AK291547 mRNA. Translation: BAF84236.1. AL117395 mRNA. Translation: CAB55897.1. CH471083 Genomic DNA. Translation: EAW54281.1. CH471083 Genomic DNA. Translation: EAW54282.1. BC004511 mRNA. Translation: AAH04511.2. BC039824 mRNA. Translation: AAH39824.1.
IPI	IPI00013877. IPI00216492. IPI00216493. IPI00216494. IPI00216495. IPI00216496.
PIR	T17207.
RefSeq	NP_036339.1. NP_067676.2.
UniGene	Hs.643472
3D structure databases
SMR	P31942. Positions 10-97, 194-270.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31942. 13 interactions.
STRING	P31942.
PTM databases
PhosphoSite	P31942.
2-D gel databases
Aarhus/Ghent-2DPAGE	2222. IEF.
Proteomic databases
PRIDE	P31942.
Genome annotation databases
Ensembl	ENST00000265866; ENSP00000265866; ENSG00000096746; Homo sapiens. [Genome view]
GeneID	3189.
KEGG	hsa:3189.
UCSC	uc001jnw.2. human. uc001jnx.2. human. uc001jny.2. human.
Organism-specific databases
CTD	3189.
GeneCards	GC10P069762.
H-InvDB	HIX0008872. HIX0008873.
HGNC	HGNC:5043. HNRNPH3.
MIM	602324. gene.
PharmGKB	PA29367.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P31942.
OMA	PYDRPLG
OrthoDB	EOG9KH5F9
Gene expression databases
ArrayExpress	P31942.
Bgee	P31942.
CleanEx	HS_HNRNPH3.
Genevestigator	P31942.
GermOnline	ENSG00000096746. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	12680.
SOURCE	Search...

Entry information

Entry name

HNRH3_HUMAN

Accession

Primary (citable) accession number: P31942
Secondary accession number(s): A8K682 , B3KRE1, Q9BSX1, Q9NP53, Q9NP96, Q9NPA7, Q9NPI4, Q9UFU4, Q9Y4J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	September 19, 2002
Last modified:	November 24, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.