Reviewed, UniProtKB/Swiss-Prot Q14974 (IMB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Importin subunit beta-1
Alternative name(s):
    Karyopherin subunit beta-1
    Nuclear factor P97
    Importin-90

Gene names

Name:	KPNB1
Synonyms:	NTF97

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

General annotation (Comments)

Function	Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Imports PRKCI into the nucleus. Ref.9 Ref.10 Ref.15
Subunit structure	Forms a complex with an importin alpha subunit. Forms a heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone. Interacts with H2A, H2B, H3 and H4 histones By similarity. Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and ZNF259. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Binds to HIV-1 Rev and Tat. Interacts with HTLV-1 Rex. Interacts with SRY. Interacts with PRKCI/atypical protein kinase C iota. Interacts with human respiratory syncytial virus (HRSV) protein M.
Subcellular location	Cytoplasm. Nucleus envelope. Ref.15
Sequence similarities	Belongs to the importin beta family. Contains 8 HEAT repeats. Contains 1 importin N-terminal domain.

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	NLS-bearing substrate import into nucleus Ref.2 Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW protein import into nucleus, docking Inferred from electronic annotation. Source: InterPro protein import into nucleus, translocation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Ref.7 Inferred from Experiment. Source: Reactome nuclear pore Ref.2 Traceable author statement. Source: ProtInc nucleoplasm Ref.7 Inferred from Experiment. Source: Reactome
Molecular function	nuclear localization sequence binding Ref.2 Traceable author statement. Source: ProtInc protein domain specific binding Inferred from physical interaction. Source: UniProtKB zinc ion binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMN1	Q16637-3	2	EBI-286758,EBI-395447
SMNDC1	O75940	1	EBI-286758,EBI-1052641

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 876

876

Importin subunit beta-1

PRO_0000120745

Regions

Domain

21 – 101

81

Importin N-terminal

Repeat

124 – 163

40

HEAT 1

Repeat

168 – 207

40

HEAT 2

Repeat

213 – 250

38

HEAT 3

Repeat

317 – 357

41

HEAT 4

Repeat

362 – 399

38

HEAT 5

Repeat

404 – 441

38

HEAT 6

Repeat

602 – 641

40

HEAT 7

Repeat

687 – 726

40

HEAT 8

Region

329 – 342

14

IAB-binding

Region

334 – 419

86

Ran-GTP binding

Compositional bias

337 – 341

5

Poly-Asp

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.5

Modified residue

12

1

Phosphoserine Ref.22 Ref.23

Modified residue

211

1

N6-acetyllysine Ref.25

Modified residue

835

1

N6-acetyllysine Ref.25

Modified residue

867

1

N6-acetyllysine Ref.25

Cross-link

206

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Cross-link

211

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.21

Experimental info

Mutagenesis

178

1

I → A: Largely reduced binding to FxFG repeats and reduced nuclear import. Ref.27

Mutagenesis

178

1

I → F or D: Loss of binding to FxFG repeats and reduced nuclear import. Ref.27

Sequence conflict

97

1

Q → H in AAA82869. Ref.1

Sequence conflict

200

1

N → NA AA sequence Ref.4

Sequence conflict

863

1

T → R in AAA82869. Ref.1

Secondary structure

1

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876

Helix Strand Turn

Details...

Helix

3 – 9

7

Helix

15 – 45

31

Helix

51 – 65

15

Helix

70 – 81

12

Helix

85 – 98

14

Beta strand

104 – 106

3

Helix

109 – 120

12

Helix

121 – 123

3

Helix

129 – 138

10

Helix

144 – 160

17

Helix

163 – 165

3

Helix

167 – 169

3

Helix

170 – 181

12

Helix

188 – 201

14

Turn

202 – 205

4

Helix

206 – 209

4

Helix

212 – 225

14

Helix

231 – 247

17

Helix

249 – 251

3

Turn

253 – 259

7

Helix

260 – 269

10

Helix

273 – 297

25

Beta strand

303 – 305

3

Helix

314 – 329

16

Helix

344 – 358

15

Turn

359 – 362

4

Helix

363 – 374

12

Helix

380 – 392

13

Beta strand

394 – 397

4

Turn

399 – 402

4

Turn

404 – 408

5

Helix

409 – 415

7

Helix

416 – 418

3

Helix

422 – 438

17

Helix

439 – 442

4

Turn

446 – 448

3

Helix

449 – 457

9

Helix

464 – 483

20

Turn

500 – 502

3

Helix

503 – 513

11

Helix

524 – 537

14

Helix

544 – 562

19

Turn

563 – 566

4

Helix

573 – 592

20

Helix

597 – 601

5

Helix

604 – 614

11

Helix

623 – 639

17

Helix

640 – 646

7

Helix

647 – 660

14

Helix

664 – 681

18

Helix

682 – 685

4

Helix

686 – 700

15

Helix

707 – 709

3

Helix

710 – 724

15

Helix

725 – 731

7

Helix

732 – 743

12

Helix

752 – 777

26

Beta strand

779 – 782

4

Helix

785 – 789

5

Helix

791 – 793

3

Helix

794 – 805

12

Helix

812 – 829

18

Helix

832 – 838

7

Helix

841 – 852

12

Helix

856 – 873

18

Sequences

	Sequence		Length	Mass (Da)
	Q14974-1 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: F3BB8B73E7E51639	FASTA	876	97,170
	10 20 30 40 50 60 MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ 70 80 90 100 110 120 IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG TETYRPSSAS QCVAGIACAE 130 140 150 160 170 180 IPVNQWPELI PQLVANVTNP NSTEHMKEST LEAIGYICQD IDPEQLQDKS NEILTAIIQG 190 200 210 220 230 240 MRKEEPSNNV KLAATNALLN SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN 250 260 270 280 290 300 LVKIMSLYYQ YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA 310 320 330 340 350 360 AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV CLMLLATCCE 370 380 390 400 410 420 DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GCILEGPEPS QLKPLVIQAM PTLIELMKDP 430 440 450 460 470 480 SVVVRDTAAW TVGRICELLP EAAINDVYLA PLLQCLIEGL SAEPRVASNV CWAFSSLAEA 490 500 510 520 530 540 AYEAADVADD QEEPATYCLS SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA 550 560 570 580 590 600 KDCYPAVQKT TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA 610 620 630 640 650 660 LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF KPFLGIGLKN 670 680 690 700 710 720 YAEYQVCLAA VGLVGDLCRA LQSNIIPFCD EVMQLLLENL GNENVHRSVK PQILSVFGDI 730 740 750 760 770 780 ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS DYDMVDYLNE LRESCLEAYT GIVQGLKGDQ 790 800 810 820 830 840 ENVHPDVMLV QPRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR 850 860 870 PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and characterization of cytoplasmic nuclear protein import factor p97." Chi N.C., Adam E.J.H., Adam S.A. J. Cell Biol. 130:265-274(1995) [PubMed: 7615630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Tissue: Brain.
[2]	"Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope." Goerlich D., Kostka S., Kraft R., Dingwall C., Laskey R.A., Hartmann E., Prehn S. Curr. Biol. 5:383-392(1995) [PubMed: 7627554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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]. Tissue: Brain and Eye.
[4]	"The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import." Weis K., Ryder U., Lamond A.I. EMBO J. 15:1818-1825(1996) [PubMed: 8617227] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH AN IMPORTIN ALPHA SUBUNIT.
[5]	Bienvenut W.V. Submitted (MAY-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-9; 55-62 AND 192-206, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[6]	"Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta." Moroianu J., Blobel G., Radu A. Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996) [PubMed: 8692944] [Abstract] Cited for: RAN-GTP AND ALPHA SUBUNIT BINDING SITES.
[7]	"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta." Henderson B.R., Percipalle P. J. Mol. Biol. 274:693-707(1997) [PubMed: 9405152] [Abstract] Cited for: INTERACTION WITH HIV-1 REV AND TAT.
[8]	"Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure." Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M., Luehrmann R. EMBO J. 17:4114-4126(1998) [PubMed: 9670026] [Abstract] Cited for: INTERACTION WITH SNUPN.
[9]	"Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells." Jaekel S., Goerlich D. EMBO J. 17:4491-4502(1998) [PubMed: 9687515] [Abstract] Cited for: FUNCTION, INTERACTION WITH RPL23A; RPS7; RPL5 AND IPO7.
[10]	"The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1." Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Goerlich D. EMBO J. 18:2411-2423(1999) [PubMed: 10228156] [Abstract] Cited for: FUNCTION, INTERACTION WITH H1 HISTONE AND IPO7.
[11]	"CRM1-mediated recycling of snurportin 1 to the cytoplasm." Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luehrmann R., Goerlich D. J. Cell Biol. 145:255-264(1999) [PubMed: 10209022] [Abstract] Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; SNUPN AND XPO1.
[12]	"The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals." Truant R., Cullen B.R. Mol. Cell. Biol. 19:1210-1217(1999) [PubMed: 9891055] [Abstract] Cited for: INTERACTION WITH HIV-1 REV.
[13]	"Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha." Palmeri D., Malim M.H. Mol. Cell. Biol. 19:1218-1225(1999) [PubMed: 9891056] [Abstract] Cited for: INTERACTION WITH HTLV-1 REX.
[14]	"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta." Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G. Hum. Mol. Genet. 11:1785-1795(2002) [PubMed: 12095920] [Abstract] Cited for: IDENTIFICATION IN AN IMPORT SNRNP COMPLEX.
[15]	"Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C." White W.O., Seibenhener M.L., Wooten M.W. J. Cell. Biochem. 85:42-53(2002) [PubMed: 11891849] [Abstract] Cited for: INTERACTION WITH PRKCI, FUNCTION, SUBCELLULAR LOCATION.
[16]	"Defective importin beta recognition and nuclear import of the sex-determining factor SRY are associated with XY sex-reversing mutations." Harley V.R., Layfield S., Mitchell C.L., Forwood J.K., John A.P., Briggs L.J., McDowall S.G., Jans D.A. Proc. Natl. Acad. Sci. U.S.A. 100:7045-7050(2003) [PubMed: 12764225] [Abstract] Cited for: INTERACTION WITH SRY.
[17]	"Regulation of human SRY subcellular distribution by its acetylation/deacetylation." Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B. EMBO J. 23:3336-3345(2004) [PubMed: 15297880] [Abstract] Cited for: INTERACTION WITH SRY.
[18]	"Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha." Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P., Bardin P.G., Jans D.A. Biochemistry 44:12887-12895(2005) [PubMed: 16171404] [Abstract] Cited for: INTERACTION WITH HRSV PROTEIN M.
[19]	"Respiratory syncytial virus M2-1 protein induces the activation of nuclear factor kappa B." Reimers K., Buchholz K., Werchau H. Virology 331:260-268(2005) [PubMed: 15629770] [Abstract] Cited for: INTERACTION WITH HRSV PROTEIN M2-1.
[20]	"Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1." Arnold M., Nath A., Hauber J., Kehlenbach R.H. J. Biol. Chem. 281:20883-20890(2006) [PubMed: 16704975] [Abstract] Cited for: INTERACTION WITH HIV-1 REV.
[21]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-211, MASS SPECTROMETRY.
[22]	"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-12, MASS SPECTROMETRY.
[23]	"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-12, MASS SPECTROMETRY.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211; LYS-835 AND LYS-867, MASS SPECTROMETRY.
[26]	"Structural view of the Ran-Importin beta interaction at 2.3 A resolution." Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A. Cell 97:635-646(1999) [PubMed: 10367892] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-459.
[27]	"Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking." Bayliss R., Littlewood T., Stewart M. Cell 102:99-108(2000) [PubMed: 10929717] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 3-442, MUTAGENESIS OF ILE-178.
[28]	"Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta." Cingolani G., Bednenko J., Gillespie M.T., Gerace L. Mol. Cell 10:1345-1353(2002) [PubMed: 12504010] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-485.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L39793 Genomic DNA. Translation: AAA82869.1.
L38951 mRNA. Translation: AAC41763.1.
BC003572 mRNA. Translation: AAH03572.1.
BC024045 mRNA. Translation: AAH24045.1.
BC036703 mRNA. Translation: AAH36703.1.

IPI

IPI00001639.

PIR

I52907.

RefSeq

NP_002256.2.

UniGene

Hs.532793

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F59	X-ray	2.80	A/B	1-442	[»]
1IBR	X-ray	2.30	B/D	1-462	[»]
1M5N	X-ray	2.90	S	1-485	[»]
1O6O	X-ray	2.80	A/B/C	1-442	[»]
1O6P	X-ray	2.80	A/B	1-442	[»]
1QGK	X-ray	2.50	A	1-876	[»]
1QGR	X-ray	2.30	A	1-876	[»]
2P8Q	X-ray	2.35	A	1-876	[»]
2Q5D	X-ray	3.20	A/B	1-876	[»]
2QNA	X-ray	2.84	A	127-875	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6204N.

IntAct

Q14974. 19 interactions.

STRING

Q14974.

PTM databases

PhosphoSite

Q14974.

Proteomic databases

PeptideAtlas

Q14974.

PRIDE

Q14974.

Genome annotation databases

Ensembl

ENST00000290158; ENSP00000290158; ENSG00000108424; Homo sapiens. [Genome view]

GeneID

3837.

KEGG

hsa:3837.

UCSC

uc002ilt.1. human.

Organism-specific databases

CTD

3837.

GeneCards

GC17P043082.

H-InvDB

HIX0013923.

HGNC

HGNC:6400. KPNB1.

MIM

602738. gene.

PharmGKB

PA30191.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q14974.

HOVERGEN

Q14974.

OMA

DTARWAR.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_578. Apoptosis.
REACT_6167. Influenza Infection.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

Q14974.

Bgee

Q14974.

CleanEx

HS_KPNB1.

Genevestigator

Q14974.

GermOnline

ENSG00000108424. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR000225. Armadillo.
IPR000357. HEAT.
IPR001494. Importin-b_N.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF00514. Arm. 1 hit.
PF02985. HEAT. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]

PROSITE

PS50077. HEAT_REPEAT. 1 hit.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

15083.

SOURCE

Search...

Entry information

Entry name

IMB1_HUMAN

Accession

Primary (citable) accession number: Q14974
Secondary accession number(s): Q14637, Q96J27

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 15, 2002
Last modified:	November 3, 2009
This is version 108 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.