Q8IUH5 (ZDH17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Palmitoyltransferase ZDHHC17
EC=2.3.1.-

Alternative name(s):
Huntingtin yeast partner H
Huntingtin-interacting protein 14
Short name=HIP-14
Huntingtin-interacting protein 3
Short name=HIP-3
Huntingtin-interacting protein H
Putative MAPK-activating protein PM11
Putative NF-kappa-B-activating protein 205
Zinc finger DHHC domain-containing protein 17
Short name=DHHC-17

Gene names

Name:	ZDHHC17
Synonyms:	HIP14, HIP3, HYPH, KIAA0946
ORF Names:	HSPC294

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

General annotation (Comments)

Function	Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg2+ transport. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11
Catalytic activity	Palmitoyl-CoA + protein-cysteine = S-palmitoyl protein + CoA.
Subunit structure	Interacts (via ANK repeats) with HD. This interaction is inversely correlated to the length of the polyglutamine tract added to the huntingtin protein in Huntington disease. Ref.1 Ref.6
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note: Low extracellular Mg2+ induces increase in Golgi and in post-Golgi membrane vesicles. Ref.8 Ref.10
Tissue specificity	Expressed in all brain regions. Expression is highest in the cortex, cerebellum, occipital lobe and caudate and lowest in the spinal cord. Expression is also seen in testis, pancreas, heart and kidney. ZDHHC17 is the only palmitoyltransferase in erythrocytes. Ref.1 Ref.11
Domain	The DHHC domain is required for palmitoyltransferase activity.
Post-translational modification	Autopalmitoylated. Autopalmitoylation has a regulatory role in ZDHHC17-mediated Mg2+ transport. Ref.8
Miscellaneous	The early and prominent pathology of HD is observed in the medium spiny neurons that project into the globus.
Sequence similarities	Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily. Contains 5 ANK repeats. Contains 1 DHHC-type zinc finger.
Biophysicochemical properties	Kinetic parameters: KM=0.87 mM for for magnesium ions
Sequence caution	The sequence AAF28972.1 differs from that shown. Reason: Frameshift at positions 183 and 191. The sequence AAH30990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA76790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAC77366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAC77388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cytoplasmic vesicle Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	ANK repeat Repeat Transmembrane Transmembrane helix Zinc-finger
Ligand	Magnesium Metal-binding Zinc
Molecular function	Acyltransferase Transferase
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipoprotein transport Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype Ref.3. Source: UniProtKB protein palmitoylation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi-associated vesicle membrane Inferred from direct assay Ref.10. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion transmembrane transporter activity Inferred from direct assay Ref.10. Source: UniProtKB protein-cysteine S-palmitoleyltransferase activity Inferred from direct assay Ref.8. Source: UniProtKB signal transducer activity Inferred from mutant phenotype Ref.3. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HTT	P42858	2	EBI-524753,EBI-466029
SNAP25	P60880	3	EBI-524753,EBI-524785

Alternative products

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

Isoform 1 (identifier: Q8IUH5-1)

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: Q8IUH5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
     51-66: THIDDYSTWDIVKATQ → MSTIPKRAVCPFSTQR
     258-266: GESALDLAK → AILRCHMAL
     267-632: Missing.

Isoform 3 (identifier: Q8IUH5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     204-632: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 632

632

Palmitoyltransferase ZDHHC17

PRO_0000212900

Regions

Topological domain

1 – 304

304

Cytoplasmic Potential

Transmembrane

305 – 325

21

Helical; Potential

Transmembrane

326 – 346

21

Helical; Potential

Topological domain

347 – 357

11

Cytoplasmic Potential

Transmembrane

358 – 378

21

Helical; Potential

Topological domain

379 – 381

3

Lumenal Potential

Transmembrane

382 – 402

21

Helical; Potential

Topological domain

403 – 480

78

Cytoplasmic Potential

Transmembrane

481 – 501

21

Helical; Potential

Topological domain

502 – 529

28

Lumenal Potential

Transmembrane

530 – 550

21

Helical; Potential

Topological domain

551 – 632

82

Cytoplasmic Potential

Repeat

89 – 118

30

ANK 1

Repeat

123 – 155

33

ANK 2

Repeat

156 – 188

33

ANK 3

Repeat

189 – 219

31

ANK 4

Repeat

224 – 253

30

ANK 5

Zinc finger

437 – 487

51

DHHC-type

Sites

Active site

467

1

S-palmitoyl cysteine intermediate Probable

Amino acid modifications

Modified residue

70

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 50

50

Missing in isoform 2.

VSP_010021

Alternative sequence

51 – 66

16

THIDD…VKATQ → MSTIPKRAVCPFSTQR in isoform 2.

VSP_010022

Alternative sequence

204 – 632

429

Missing in isoform 3.

VSP_010023

Alternative sequence

258 – 266

9

GESALDLAK → AILRCHMAL in isoform 2.

VSP_010024

Alternative sequence

267 – 632

366

Missing in isoform 2.

VSP_010025

Natural variant

383

1

N → S.
Corresponds to variant rs33996476 [ dbSNP | Ensembl ].

VAR_052978

Experimental info

Mutagenesis

467

1

C → S: Abolishes palmitoyltransferase activity. Ref.9

Sequence conflict

3

1

R → G in AAF28972. Ref.7

Sequence conflict

39

1

Y → F in BAC22089. Ref.1

Sequence conflict

173

1

V → VV in BAC22089. Ref.1

Sequence conflict

182

1

D → E in AAF28972. Ref.7

Secondary structure

1

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632

Helix Strand Turn

Details...

Helix

56 – 58

3

Helix

61 – 66

6

Helix

70 – 78

9

Helix

93 – 99

7

Helix

103 – 111

9

Turn

121 – 124

4

Helix

127 – 134

8

Helix

137 – 145

9

Helix

160 – 166

7

Helix

170 – 178

9

Helix

193 – 200

8

Helix

207 – 212

6

Turn

222 – 224

3

Helix

228 – 235

8

Helix

238 – 247

10

Helix

261 – 267

7

Helix

271 – 280

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 3FD5FD592F2C617F	FASTA	632	72,640
	10 20 30 40 50 60 MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK THIDDYSTWD 70 80 90 100 110 120 IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG 130 140 150 160 170 180 GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG 190 200 210 220 230 240 QDVDMMDQNG MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV 250 260 270 280 290 300 ISLLLEAGAN VDAQNIKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE 310 320 330 340 350 360 FRQKVMLGTP FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF DHSMHSALPL 370 380 390 400 410 420 GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY NFGKSWKSDP GIIKATEEQK 430 440 450 460 470 480 KKTIVELAET GSLDLSIFCS TCLIRKPVRS KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR 490 500 510 520 530 540 YFMGYLFFLL FMICWMIYGC ISYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF 550 560 570 580 590 600 HFMWVAVLLM CQMYQISCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF 610 620 630 RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV
	Isoform 2 [UniParc]. Checksum: A07B4620B70A6593	FASTA	216	23,941
	10 20 30 40 50 60 MSTIPKRAVC PFSTQRYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI 70 80 90 100 110 120 SKGAIVDQLG GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT 130 140 150 160 170 180 SIVAYLIAKG QDVDMMDQNG MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH 190 200 210 WAVLAGNTTV ISLLLEAGAN VDAQNIKAIL RCHMAL
	Isoform 3 [UniParc]. Checksum: F37602D7183923C5	FASTA	203	22,845
	10 20 30 40 50 60 MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK THIDDYSTWD 70 80 90 100 110 120 IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG 130 140 150 160 170 180 GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG 190 200 QDVDMMDQNG MTPLMWAAYR THS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis." Singaraja R.R., Hadano S., Metzler M., Givan S., Wellington C.L., Warby S., Yanai A., Gutekunst C.-A., Leavitt B.R., Yi H., Fichter K., Gan L., McGutcheon K., Chopra V., Michel J., Hersch S.M., Ikeda J.E., Hayden M.R. Hum. Mol. Genet. 11:2815-2828(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HD, TISSUE SPECIFICITY, FUNCTION. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways." Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S. Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung fibroblast.
[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 2).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Bone marrow and Testis.
[6]	"Huntingtin interacts with a family of WW domain proteins." Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E. Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-182, INTERACTION WITH HD. Tissue: Testis.
[7]	"Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 3). Tissue: Umbilical cord blood.
[8]	"Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins." Huang K., Yanai A., Kang R., Arstikaitis P., Singaraja R.R., Metzler M., Mullard A., Haigh B., Gauthier-Campbell C., Gutekunst C.-A., Hayden M.R., El-Husseini A. Neuron 44:977-986(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPALMITOYLATION.
[9]	"Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase." Ducker C.E., Stettler E.M., French K.J., Upson J.J., Smith C.D. Oncogene 23:9230-9237(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-467.
[10]	"Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions, palmitoyl acyltransferase and Mg2+ transport." Goytain A., Hines R.M., Quamme G.A. J. Biol. Chem. 283:33365-33374(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells." Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J., Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J., Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F. J. Biol. Chem. 287:18974-18984(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]	"The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding." Gao T., Collins R.E., Horton J.R., Zhang X., Zhang R., Dhayalan A., Tamas R., Jeltsch A., Cheng X. Proteins 76:772-777(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 51-288.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB024494 mRNA. Translation: BAC22089.1.
AB023163 mRNA. Translation: BAA76790.1. Different initiation.
AB097013 mRNA. Translation: BAC77366.1. Different initiation.
AB097035 mRNA. Translation: BAC77388.1. Different initiation.
AK299089 mRNA. Translation: BAG61151.1.
BC030990 mRNA. Translation: AAH30990.1. Different initiation.
BC050324 mRNA. Translation: AAH50324.1.
AF049612 mRNA. Translation: AAC26848.1.
AF161412 mRNA. Translation: AAF28972.1. Frameshift.

IPI

IPI00216753.
IPI00410687.
IPI00410688.

RefSeq

NP_056151.2. NM_015336.2.

UniGene

Hs.4014.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EU9	X-ray	1.99	A/B/C	51-288	[»]

ProteinModelPortal

Q8IUH5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IUH5. 9 interactions.

STRING

9606.ENSP00000403397.

Protein family/group databases

TCDB

9.B.37.1.1. huntington-interacting protein 14 (HIP14) family.

PTM databases

PhosphoSite

Q8IUH5.

Polymorphism databases

DMDM

46395885.

Proteomic databases

PaxDb

Q8IUH5.

PRIDE

Q8IUH5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334822; ENSP00000334868; ENSG00000186908.
ENST00000359019; ENSP00000351913; ENSG00000186908.
ENST00000426126; ENSP00000403397; ENSG00000186908.

GeneID

23390.

KEGG

hsa:23390.

UCSC

uc001syk.1. human.

Organism-specific databases

CTD

23390.

GeneCards

GC12P077157.

HGNC

HGNC:18412. ZDHHC17.

HPA

HPA016807.

MIM

607799. gene.

neXtProt

NX_Q8IUH5.

PharmGKB

PA134991292.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOVERGEN

HBG051907.

InParanoid

Q8IUH5.

OMA

QAKGYDS.

OrthoDB

EOG44J2HH.

PhylomeDB

Q8IUH5.

Gene expression databases

ArrayExpress

Q8IUH5.

Bgee

Q8IUH5.

CleanEx

HS_ZDHHC17.

Genevestigator

Q8IUH5.

GermOnline

ENSG00000186908. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]

Pfam

PF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
PF01529. zf-DHHC. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 5 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50216. ZF_DHHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8IUH5.

GenomeRNAi

23390.

NextBio

45515.

SOURCE

Search...

Entry information

Entry name

ZDH17_HUMAN

Accession

Primary (citable) accession number: Q8IUH5
Secondary accession number(s): B4DR39 , O75407, Q7Z2I0, Q86W89, Q86YK0, Q9P088, Q9UPZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 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.