Reviewed, UniProtKB/Swiss-Prot P08133 (ANXA6_HUMAN)

Names and origin

Protein names

Recommended name:
    Annexin A6
Alternative name(s):
    Annexin-6
    Annexin VI
    Lipocortin VI
    p68
    p70
    Protein III
    Chromobindin-20
    67 kDa calelectrin
    Calphobindin-II
      Short name=CPB-II

Gene names

Name:	ANXA6
Synonyms:	ANX6

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	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.
Induction	By 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. Ref.9
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
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

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.6

Modified residue

30

1

Phosphotyrosine Ref.9

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

299

1

N6-acetyllysine Ref.12

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

607

1

N6-acetyllysine Ref.12

Modified residue

620

1

N6-acetyllysine Ref.12

Experimental info

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

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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)
	P08133-1 [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

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: 3258820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2963335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 2528541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[5]	"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: Uterus.
[6]	"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: 2139657] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-673.
[7]	"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: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 485-499. Tissue: Adipocyte.
[8]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"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-30, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-68; LYS-75; LYS-81; LYS-299; LYS-306; LYS-370; LYS-418; LYS-483; LYS-607 AND LYS-620, MASS SPECTROMETRY.
[13]	"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: 8709144] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00097 mRNA. Translation: CAA68286.1.
J03578 mRNA. Translation: AAA35656.1.
D00510 mRNA. Translation: BAA00400.1.
AK126836 mRNA. Translation: BAC86715.1. Sequence problems.
BC017046 mRNA. Translation: AAH17046.1.

IPI

IPI00221226.

PIR

AQHU68. JU0032.

RefSeq

NP_001146.2.
NP_004024.2.

UniGene

Hs.412117

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P08133. 4 interactions.

STRING

P08133.

Protein family/group databases

TCDB

1.A.31.1.2. annexin family.

PTM databases

PhosphoSite

P08133.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00221226.

Proteomic databases

PRIDE

P08133.

Genome annotation databases

Ensembl

ENST00000354546; ENSP00000346550; ENSG00000197043; Homo sapiens. [Genome view]

GeneID

309.

KEGG

hsa:309.

UCSC

uc003ltl.1. human.

Organism-specific databases

CTD

309.

GeneCards

GC05M150460.

H-InvDB

HIX0005325.

HGNC

HGNC:544. ANXA6.

MIM

114070. gene.

PharmGKB

PA24834.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P08133.

HOVERGEN

P08133.

OMA

REIFRTK

Gene expression databases

ArrayExpress

P08133.

Bgee

P08133.

CleanEx

HS_ANXA6.

Genevestigator

P08133.

GermOnline

ENSG00000197043. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.10.220.10. Annexin. 8 hits.

PANTHER

PTHR10502. Annexin. 1 hit.

Pfam

PF00191. Annexin. 8 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00202. ANNEXINVI.

SMART

SM00335. ANX. 8 hits.
[Graphical view]

PROSITE

PS00223. ANNEXIN. 8 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1247.

SOURCE

Search...

Entry information

Entry name

ANXA6_HUMAN

Accession

Primary (citable) accession number: P08133
Secondary accession number(s): Q6ZT79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 118 of the entry and version 3 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.