Q9C026 (TRIM9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase TRIM9
EC=6.3.2.-

Alternative name(s):
RING finger protein 91
Tripartite motif-containing protein 9

Gene names

Name:	TRIM9
Synonyms:	KIAA0282, RNF91

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	710 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SNAP25 By similarity.
Subcellular location	Cytoplasm. Cell projection › dendrite. Cytoplasmic vesicle › secretory vesicle › synaptic vesicle By similarity. Cell junction › synapse By similarity. Cytoplasm › cytoskeleton By similarity. Note: Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle-associated form. Associated with the cytoskeleton By similarity. Found in proximal dendrites of pyramidal neurons in the cerebral cortex and hippocampus, and Purkinje cells in the cerebellum. Ref.7
Tissue specificity	Brain. Highly expressed in the cerebral cortex (at protein level). Severely decreased in the affected brain areas in Parkinson disease and dementia with Lewy bodies. Ref.7
Domain	The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25 By similarity.
Post-translational modification	Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro.
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 2 B box-type zinc fingers. Contains 1 B30.2/SPRY domain. Contains 1 COS domain. Contains 1 fibronectin type-III domain. Contains 1 RING-type zinc finger.
Sequence caution	The sequence AAG53490.1 differs from that shown. Reason: Frameshift at position 660. The sequence AAG53492.1 differs from that shown. Reason: Frameshift at position 655. The sequence BAA13398.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA13398.2 differs from that shown. Reason: Frameshift at position 660.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell junction Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of SNARE complex assembly Inferred from electronic annotation. Source: Compara negative regulation of calcium ion-dependent exocytosis Inferred from electronic annotation. Source: Compara proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.7. Source: UniProtKB synaptic vesicle exocytosis Inferred from electronic annotation. Source: Compara
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from direct assay Ref.1Ref.7. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from direct assay Ref.7. Source: UniProtKB synaptic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9C026-1)

Also known as: Beta;

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 4 (identifier: Q9C026-4)

The sequence of this isoform differs from the canonical sequence as follows:
     436-439: Missing.
     534-534: E → EDTDSEEQTL...QLVDIKKLLA
     692-710: TLHTGLPVPDFYSSRASIA → STLPLRLNSCCWLPVQRLPRAVQSNRREGS

Note: May be due to a competing donor splice site, to exon inclusion and to intron retention.

Isoform 5 (identifier: Q9C026-5)

The sequence of this isoform differs from the canonical sequence as follows:
     535-550: VAWFAFDPGSAHSDII → GKALQQYPSERELRGI
     551-710: Missing.

Note: May be due to intron retention.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 710

710

E3 ubiquitin-protein ligase TRIM9

PRO_0000056208

Regions

Domain

374 – 432

59

COS

Domain

439 – 532

94

Fibronectin type-III

Domain

533 – 702

170

B30.2/SPRY

Zinc finger

10 – 50

41

RING-type

Zinc finger

163 – 212

50

B box-type 1

Zinc finger

224 – 266

43

B box-type 2

Coiled coil

273 – 340

68

Potential

Natural variations

Alternative sequence

436 – 439

4

Missing in isoform 4.

VSP_007922

Alternative sequence

534

1

E → EDTDSEEQTLPFPVPSERLP LRRMSPFSSTLNLQPSFPGR SYFDFRSSPHQLSLHSSLQS LNAPGCNFETQSAPYSQLVD IKKLLA in isoform 4.

VSP_007923

Alternative sequence

535 – 550

16

VAWFA…HSDII → GKALQQYPSERELRGI in isoform 5.

VSP_007925

Alternative sequence

551 – 710

160

Missing in isoform 5.

VSP_007926

Alternative sequence

692 – 710

19

TLHTG…RASIA → STLPLRLNSCCWLPVQRLPR AVQSNRREGS in isoform 4.

VSP_007924

Natural variant

653

1

L → F. Ref.1 Ref.2 Ref.6
Corresponds to variant rs2275462 [ dbSNP | Ensembl ].

VAR_016202

Experimental info

Sequence conflict

314

1

A → V in BAB70913. Ref.2

Sequence conflict

384

1

Q → R in BAB70913. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

710

Helix Strand Turn

Details...

Beta strand

454 – 460

7

Beta strand

473 – 479

7

Beta strand

482 – 485

4

Beta strand

488 – 494

7

Beta strand

498 – 501

4

Beta strand

505 – 507

3

Beta strand

510 – 516

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Beta) [UniParc]. Last modified June 1, 2001. Version 1. Checksum: AEAB24807C89D0E2	FASTA	710	79,177
	10 20 30 40 50 60 MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY 70 80 90 100 110 120 DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV 130 140 150 160 170 180 PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 190 200 210 220 230 240 MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 250 260 270 280 290 300 CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 310 320 330 340 350 360 MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 370 380 390 400 410 420 RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 430 440 450 460 470 480 PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD 490 500 510 520 530 540 DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF 550 560 570 580 590 600 DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR 610 620 630 640 650 660 MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF 670 680 690 700 710 FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA
	Isoform 4 [UniParc]. Checksum: 38ABF6696A12C84C	FASTA	802	89,762
	10 20 30 40 50 60 MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY 70 80 90 100 110 120 DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV 130 140 150 160 170 180 PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 190 200 210 220 230 240 MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 250 260 270 280 290 300 CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 310 320 330 340 350 360 MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 370 380 390 400 410 420 RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 430 440 450 460 470 480 PLLQSIHQLD FVQVKVPATP ILQLEECCTH NNSATLSWKQ PPLSTVPADG YILELDDGNG 490 500 510 520 530 540 GQFREVYVGK ETMCTVDGLH FNSTYNARVK AFNKTGVSPY SKTLVLQTSE DTDSEEQTLP 550 560 570 580 590 600 FPVPSERLPL RRMSPFSSTL NLQPSFPGRS YFDFRSSPHQ LSLHSSLQSL NAPGCNFETQ 610 620 630 640 650 660 SAPYSQLVDI KKLLAVAWFA FDPGSAHSDI ILSNDNLTVT CSSYDDRVVL GKTGFSKGIH 670 680 690 700 710 720 YWELTVDRYD NHPDPAFGVA RMDVMKDVML GKDDKAWAMY VDNNRSWFMH NNSHTNRTEG 730 740 750 760 770 780 GITKGATIGV LLDLNRKNLT FFINDEQQGP IAFDNVEGLF FPAVSLNRNV QVSTLPLRLN 790 800 SCCWLPVQRL PRAVQSNRRE GS
	Isoform 5 [UniParc]. Checksum: 47ACD9147C1BE651	FASTA	550	61,346
	10 20 30 40 50 60 MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY 70 80 90 100 110 120 DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV 130 140 150 160 170 180 PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 190 200 210 220 230 240 MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 250 260 270 280 290 300 CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 310 320 330 340 350 360 MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 370 380 390 400 410 420 RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 430 440 450 460 470 480 PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD 490 500 510 520 530 540 DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEGKALQQ 550 YPSERELRGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The tripartite motif family identifies cell compartments." Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A. EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-653.
[2]	"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins." Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N. DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-653. Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[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] (ISOFORM 4). Tissue: Fetal brain.
[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 (SEP-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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), VARIANT PHE-653. Tissue: Brain and Uterus.
[7]	"TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the brain of Parkinson's disease and dementia with Lewy bodies." Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K. Neurobiol. Dis. 38:210-218(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, TISSUE SPECIFICITY.
[8]	"Solution structures of the FN3 domain of human tripartite motif protein 9." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 437-534.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF220036 mRNA. Translation: AAG53490.1. Frameshift.
AF220037 mRNA. Translation: AAG53491.1.
AF220038 mRNA. Translation: AAG53492.1. Frameshift.
D87458 mRNA. Translation: BAA13398.2. Sequence problems.
AK055388 mRNA. Translation: BAB70913.1.
CH471078 Genomic DNA. Translation: EAW65680.1.
CH471078 Genomic DNA. Translation: EAW65681.1.
CH471078 Genomic DNA. Translation: EAW65682.1.
CH471078 Genomic DNA. Translation: EAW65684.1.
BC013414 mRNA. Translation: AAH13414.1.
BC063872 mRNA. Translation: AAH63872.1.

IPI

IPI00026828.
IPI00102679.
IPI00337362.

RefSeq

NP_055978.4. NM_015163.5.
NP_443210.1. NM_052978.4.

UniGene

Hs.654750.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DB8	NMR	-	A	439-534	[»]

ProteinModelPortal

Q9C026.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9C026. 15 interactions.

MINT

MINT-1478450.

STRING

9606.ENSP00000298355.

PTM databases

PhosphoSite

Q9C026.

Polymorphism databases

DMDM

33516964.

2D gel databases

REPRODUCTION-2DPAGE

Q9C026.

Proteomic databases

PaxDb

Q9C026.

PRIDE

Q9C026.

Protocols and materials databases

DNASU

114088.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000298355; ENSP00000298355; ENSG00000100505.
ENST00000338969; ENSP00000342970; ENSG00000100505.
ENST00000360392; ENSP00000353561; ENSG00000100505.

GeneID

114088.

KEGG

hsa:114088.

UCSC

uc001wyx.4. human.
uc001wyy.2. human.
uc001wyz.4. human.

Organism-specific databases

CTD

114088.

GeneCards

GC14M051441.

HGNC

HGNC:16288. TRIM9.

MIM

606555. gene.

neXtProt

NX_Q9C026.

PharmGKB

PA38116.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260378.

HOVERGEN

HBG062305.

KO

K10649.

OMA

LDLDKMS.

OrthoDB

EOG46HG97.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

Bgee

Q9C026.

CleanEx

HS_TRIM9.

Genevestigator

Q9C026.

GermOnline

ENSG00000100505. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.

InterPro

IPR001870. B30.2/SPRY.
IPR003649. Bbox_C.
IPR008985. ConA-like_lec_gl_sf.
IPR017903. COS_domain.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Pfam

PF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]

SMART

SM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF49265. FN_III-like. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
PS51262. COS. 1 hit.
PS50853. FN3. 1 hit.
PS50119. ZF_BBOX. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9C026.

GenomeRNAi

114088.

NextBio

78980.

SOURCE

Search...

Entry information

Entry name

TRIM9_HUMAN

Accession

Primary (citable) accession number: Q9C026
Secondary accession number(s): D3DSB7 , D3DSB8, Q92557, Q96D24, Q96NI4, Q9C025, Q9C027

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 4, 2003
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 124 of the entry and version 1 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.