P08133 (ANXA6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Annexin A6

Alternative name(s):
67 kDa calelectrin
Annexin VI
Annexin-6
Calphobindin-II
Short name=CPB-II
Chromobindin-20
Lipocortin VI
Protein III
p68
p70

Gene names

Name:	ANXA6
Synonyms:	ANX6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May associate with CD21. May regulate the release of Ca2+ from intracellular stores.
Subcellular location	Cytoplasm By similarity. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10
Induction	By Epstein-Barr virus (EBV).
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Post-translational modification	Phosphorylated in response to growth factor stimulation.
Miscellaneous	Seems to bind one calcium ion with high affinity.
Sequence similarities	Belongs to the annexin family. Contains 8 annexin repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion transport Inferred from electronic annotation. Source: Compara regulation of muscle contraction Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent phospholipid binding Inferred from direct assay PubMed 2138016. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P08133-1)

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: P08133-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 673

672

Annexin A6

PRO_0000067494

Regions

Repeat

29 – 89

61

Annexin 1

Repeat

101 – 161

61

Annexin 2

Repeat

185 – 245

61

Annexin 3

Repeat

260 – 320

61

Annexin 4

Repeat

372 – 432

61

Annexin 5

Repeat

444 – 504

61

Annexin 6

Repeat

533 – 593

61

Annexin 7

Repeat

608 – 668

61

Annexin 8

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

30

1

Phosphotyrosine Ref.11

Modified residue

63

1

N6-acetyllysine Ref.12

Modified residue

68

1

N6-acetyllysine Ref.12

Modified residue

75

1

N6-acetyllysine Ref.12

Modified residue

81

1

N6-acetyllysine Ref.12

Modified residue

201

1

Phosphotyrosine By similarity

Modified residue

306

1

N6-acetyllysine Ref.12

Modified residue

370

1

N6-acetyllysine Ref.12

Modified residue

418

1

N6-acetyllysine Ref.12

Modified residue

483

1

N6-acetyllysine Ref.12

Modified residue

620

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

1 – 32

32

Missing in isoform 2.

VSP_045480

Experimental info

Sequence conflict

221

1

T → A in BAH13893. Ref.4

Sequence conflict

226 – 227

2

IE → MK in AAA35656. Ref.2

Sequence conflict

248

1

C → R in BAC86715. Ref.4

Sequence conflict

555

1

S → T in AAA35656. Ref.2

Sequence conflict

619

1

E → D in CAA68286. Ref.1

Secondary structure

1

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673

Helix Strand Turn

Details...

Helix

22 – 32

11

Beta strand

34 – 37

4

Helix

40 – 47

8

Helix

52 – 66

15

Helix

70 – 77

8

Helix

80 – 90

11

Helix

93 – 105

13

Beta strand

106 – 109

4

Helix

112 – 121

10

Helix

124 – 137

14

Helix

142 – 149

8

Helix

152 – 163

12

Helix

174 – 187

14

Turn

188 – 190

3

Beta strand

191 – 193

3

Helix

196 – 205

10

Helix

208 – 221

14

Beta strand

222 – 224

3

Helix

226 – 230

5

Turn

231 – 233

3

Helix

236 – 262

27

Beta strand

264 – 268

5

Helix

271 – 280

10

Turn

281 – 285

5

Helix

286 – 296

11

Beta strand

297 – 299

3

Helix

301 – 306

6

Helix

311 – 321

11

Helix

333 – 348

16

Helix

365 – 376

12

Beta strand

377 – 380

4

Helix

383 – 391

9

Helix

395 – 409

15

Helix

413 – 420

8

Helix

424 – 433

10

Helix

436 – 448

13

Beta strand

449 – 452

4

Helix

455 – 464

10

Helix

467 – 481

15

Helix

485 – 492

8

Helix

495 – 504

10

Helix

516 – 530

15

Helix

535 – 537

3

Helix

546 – 553

8

Helix

556 – 568

13

Beta strand

569 – 572

4

Helix

574 – 581

8

Helix

584 – 611

28

Beta strand

613 – 616

4

Helix

619 – 628

10

Turn

630 – 633

4

Helix

634 – 645

12

Helix

649 – 656

8

Helix

659 – 668

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 90F47474F7F6D7B6	FASTA	673	75,873
	10 20 30 40 50 60 MAKPAQGAKY RGSIHDFPGF DPNQDAEALY TAMKGFGSDK EAILDIITSR SNRQRQEVCQ 70 80 90 100 110 120 SYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYCDAKE IKDAISGIGT DEKCLIEILA 130 140 150 160 170 180 SRTNEQMHQL VAAYKDAYER DLEADIIGDT SGHFQKMLVV LLQGTREEDD VVSEDLVQQD 190 200 210 220 230 240 VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK 250 260 270 280 290 300 LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 310 320 330 340 350 360 LYSMIKNDTS GEYKKTLLKL SGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA 370 380 390 400 410 420 NDFNPDADAK ALRKAMKGLG TDEDTIIDII THRSNVQRQQ IRQTFKSHFG RDLMTDLKSE 430 440 450 460 470 480 ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI RAINEAYKED 490 500 510 520 530 540 YHKSLEDALS SDTSGHFRRI LISLATGHRE EGGENLDQAR EDAQVAAEIL EIADTPSGDK 550 560 570 580 590 600 TSLETRFMTI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDAF VAIVQSVKNK 610 620 630 640 650 660 PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD 670 FLKALLALCG GED
	Isoform 2 [UniParc]. Checksum: 61E3E5CAF66A51E3	FASTA	641	72,423
	10 20 30 40 50 60 MKGFGSDKEA ILDIITSRSN RQRQEVCQSY KSLYGKDLIA DLKYELTGKF ERLIVGLMRP 70 80 90 100 110 120 PAYCDAKEIK DAISGIGTDE KCLIEILASR TNEQMHQLVA AYKDAYERDL EADIIGDTSG 130 140 150 160 170 180 HFQKMLVVLL QGTREEDDVV SEDLVQQDVQ DLYEAGELKW GTDEAQFIYI LGNRSKQHLR 190 200 210 220 230 240 LVFDEYLKTT GKPIEASIRG ELSGDFEKLM LAVVKCIRST PEYFAERLFK AMKGLGTRDN 250 260 270 280 290 300 TLIRIMVSRS ELDMLDIREI FRTKYEKSLY SMIKNDTSGE YKKTLLKLSG GDDDAAGQFF 310 320 330 340 350 360 PEAAQVAYQM WELSAVARVE LKGTVRPAND FNPDADAKAL RKAMKGLGTD EDTIIDIITH 370 380 390 400 410 420 RSNVQRQQIR QTFKSHFGRD LMTDLKSEIS GDLARLILGL MMPPAHYDAK QLKKAMEGAG 430 440 450 460 470 480 TDEKALIEIL ATRTNAEIRA INEAYKEDYH KSLEDALSSD TSGHFRRILI SLATGHREEG 490 500 510 520 530 540 GENLDQARED AQVAAEILEI ADTPSGDKTS LETRFMTILC TRSYPHLRRV FQEFIKMTNY 550 560 570 580 590 600 DVEHTIKKEM SGDVRDAFVA IVQSVKNKPL FFADKLYKSM KGAGTDEKTL TRIMVSRSEI 610 620 630 640 DLLNIRREFI EKYDKSLHQA IEGDTSGDFL KALLALCGGE D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the human, membrane-associated Ca2+-binding protein p68 a novel member of a protein family." Crompton M.R., Owens R.J., Totty N.F., Moss S.E., Waterfield M.D., Crumpton M.J. EMBO J. 7:21-27(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Human 67-kDa calelectrin contains a duplication of four repeats found in 35-kDa lipocortins." Suedhof T.C., Slaughter C.A., Leznicki I., Barjon P., Reynolds G.A. Proc. Natl. Acad. Sci. U.S.A. 85:664-668(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[3]	"Structure and expression of cDNA for calphobindin II, a human placental coagulation inhibitor." Iwasaki A., Suda M., Watanabe M., Nakao H., Hattori Y., Nagoya T., Saino Y., Shidara Y., Maki M. J. Biochem. 106:43-49(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Amygdala and Thymus.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[8]	"Structure and properties of calphobindin II, an anticoagulant protein from human placenta." Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y., Maki M. J. Biochem. 107:43-50(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-673.
[9]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 485-499. Tissue: Adipocyte.
[10]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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-63; LYS-68; LYS-75; LYS-81; LYS-306; LYS-370; LYS-418; LYS-483 AND LYS-620, MASS SPECTROMETRY.
[13]	"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].
[14]	"The structure of recombinant human annexin VI in crystals and membrane-bound." Benz J., Bergner A., Hofmann A., Demange P., Goettig P., Liemann S., Huber R., Voges D. J. Mol. Biol. 260:638-643(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00097 mRNA. Translation: CAA68286.1.
J03578 mRNA. Translation: AAA35656.1.
D00510 mRNA. Translation: BAA00400.1.
AK126836 mRNA. Translation: BAC86715.1. Sequence problems.
AK303078 mRNA. Translation: BAH13893.1.
AC008641 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61684.1.
CH471062 Genomic DNA. Translation: EAW61686.1.
BC017046 mRNA. Translation: AAH17046.1.

IPI

IPI00221226.
IPI01011319.

PIR

AQHU68. JU0032.

RefSeq

NP_001146.2. NM_001155.4.
NP_001180473.1. NM_001193544.1.

UniGene

Hs.412117.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M9I	X-ray	2.65	A	2-672	[»]

ProteinModelPortal

P08133.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08133. 8 interactions.

MINT

MINT-4999263.

STRING

9606.ENSP00000346550.

Protein family/group databases

TCDB

1.A.31.1.2. annexin family.

PTM databases

PhosphoSite

P08133.

Polymorphism databases

DMDM

113962.

2D gel databases

REPRODUCTION-2DPAGE

IPI00221226.

UCD-2DPAGE

P08133.

Proteomic databases

PaxDb

P08133.

PRIDE

P08133.

Protocols and materials databases

DNASU

309.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354546; ENSP00000346550; ENSG00000197043.
ENST00000523714; ENSP00000430517; ENSG00000197043.

GeneID

309.

KEGG

hsa:309.

UCSC

uc003ltl.2. human.

Organism-specific databases

CTD

309.

GeneCards

GC05M150460.

HGNC

HGNC:544. ANXA6.

HPA

CAB005077.
HPA002462.
HPA009650.

MIM

114070. gene.

neXtProt

NX_P08133.

PharmGKB

PA24834.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG267770.

HOGENOM

HOG000158803.

HOVERGEN

HBG061815.

InParanoid

P08133.

OMA

EKSLYSM.

OrthoDB

EOG4PVNZ6.

Gene expression databases

ArrayExpress

P08133.

Bgee

P08133.

CleanEx

HS_ANXA6.

Genevestigator

P08133.

GermOnline

ENSG00000197043. Homo sapiens.

Family and domain databases

Gene3D

1.10.220.10. 8 hits.

InterPro

IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002393. AnnexinVI.
[Graphical view]

PANTHER

PTHR10502. PTHR10502. 1 hit.

Pfam

PF00191. Annexin. 8 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00202. ANNEXINVI.

SMART

SM00335. ANX. 8 hits.
[Graphical view]

SUPFAM

SSF47874. Annexin. 2 hits.

PROSITE

PS00223. ANNEXIN. 8 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ANXA6. human.

EvolutionaryTrace

P08133.

GenomeRNAi

309.

NextBio

1247.

SOURCE

Search...

Entry information

Entry name

ANXA6_HUMAN

Accession

Primary (citable) accession number: P08133
Secondary accession number(s): B7Z8A7 , D3DQH4, E9PGK1, Q6ZT79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.