Q00536 (CDK16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 16
EC=2.7.11.22

Alternative name(s):
Cell division protein kinase 16
PCTAIRE-motif protein kinase 1
Serine/threonine-protein kinase PCTAIRE-1

Gene names

Name:	CDK16
Synonyms:	PCTK1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in signal transduction cascades in terminally differentiated cells.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEC23A	Q15436	3	EBI-726261,EBI-81088

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 496

496

Cyclin-dependent kinase 16

PRO_0000086484

Regions

Domain

165 – 446

282

Protein kinase

Nucleotide binding

171 – 179

9

ATP By similarity

Sites

Active site

286

1

Proton acceptor By similarity

Binding site

194

1

ATP By similarity

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.10 Ref.13

Modified residue

14

1

Phosphothreonine Ref.13

Modified residue

36

1

Phosphoserine Ref.10 Ref.13

Modified residue

42

1

Phosphoserine Ref.10 Ref.13

Modified residue

65

1

Phosphoserine Ref.10 Ref.13

Modified residue

78

1

Phosphoserine Ref.10 Ref.13

Modified residue

82

1

Phosphoserine Ref.10 Ref.13

Modified residue

86

1

Phosphoserine Ref.13

Modified residue

88

1

Phosphothreonine Ref.13

Modified residue

89

1

Phosphoserine Ref.13

Modified residue

90

1

Phosphoserine Ref.13

Modified residue

95

1

Phosphoserine Ref.10 Ref.13

Modified residue

110

1

Phosphoserine Ref.10 Ref.13

Modified residue

119

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.13

Modified residue

135

1

Phosphothreonine Ref.13

Modified residue

138

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Modified residue

153

1

Phosphoserine Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Modified residue

155

1

Phosphoserine Ref.11 Ref.13

Modified residue

175

1

Phosphothreonine Ref.14

Modified residue

176

1

Phosphotyrosine Ref.8

Modified residue

478

1

Phosphoserine Ref.13

Modified residue

480

1

Phosphoserine Ref.10 Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

496

Helix Strand Turn

Details...

Beta strand

177 – 180

4

Turn

185 – 187

3

Beta strand

191 – 196

6

Helix

212 – 215

4

Beta strand

226 – 231

6

Beta strand

236 – 241

6

Beta strand

244 – 246

3

Helix

247 – 253

7

Helix

260 – 271

12

Helix

275 – 279

5

Helix

289 – 291

3

Beta strand

292 – 294

3

Beta strand

300 – 302

3

Helix

325 – 327

3

Helix

330 – 333

4

Helix

342 – 345

4

Helix

351 – 356

6

Helix

367 – 377

11

Turn

383 – 385

3

Helix

393 – 397

5

Helix

408 – 411

4

Helix

421 – 426

6

Helix

437 – 440

4

Helix

444 – 446

3

Beta strand

454 – 456

3

Helix

462 – 464

3

Sequences

	Sequence		Length	Mass (Da)
	Q00536 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 9A5DDD34A5E5CBBB	FASTA	496	55,716
	10 20 30 40 50 60 MDRMKKIKRQ LSMTLRGGRG IDKTNGAPEQ IGLDESGGGG GSDPGEAPTR AAPGELRSAR 70 80 90 100 110 120 GPLSSAPEIV HEDLKMGSDG ESDQASATSS DEVQSPVRVR MRNHPPRKIS TEDINKRLSL 130 140 150 160 170 180 PADIRLPEGY LEKLTLNSPI FDKPLSRRLR RVSLSEIGFG KLETYIKLDK LGEGTYATVY 190 200 210 220 230 240 KGKSKLTDNL VALKEIRLEH EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF 250 260 270 280 290 300 EYLDKDLKQY LDDCGNIINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL 310 320 330 340 350 360 KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC IFYEMATGRP 370 380 390 400 410 420 LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFKTYNY PKYRAEALLS HAPRLDSDGA 430 440 450 460 470 480 DLLTKLLQFE GRNRISAEDA MKHPFFLSLG ERIHKLPDTT SIFALKEIQL QKEASLRSSS 490 MPDSGRPAFR VVDTEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of human cdc2-related protein kinases." Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H. EMBO J. 11:2909-2917(1992) [PubMed: 1639063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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: Thalamus.
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Placenta.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-153, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-176, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[9]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-138 AND SER-153, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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; SER-36; SER-42; SER-65; SER-78; SER-82; SER-95; SER-110; SER-119; SER-138; SER-153 AND SER-480, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-138; SER-153 AND SER-155, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-14; SER-36; SER-42; SER-65; SER-78; SER-82; SER-86; THR-88; SER-89; SER-90; SER-95; SER-110; SER-119; THR-135; SER-138; SER-153; SER-155; SER-478 AND SER-480, MASS SPECTROMETRY.
[14]	"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 THR-175, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66363 mRNA. Translation: CAA47006.1.
BT006827 mRNA. Translation: AAP35473.1.
AK290145 mRNA. Translation: BAF82834.1.
AL096791 Genomic DNA. Translation: CAD20055.1.
CH471164 Genomic DNA. Translation: EAW59297.1.
BC001048 mRNA. Translation: AAH01048.1.
BC015607 mRNA. Translation: AAH15607.1.

IPI

IPI00549858.

PIR

S23385.

RefSeq

NP_001163931.1. NM_001170460.1.
NP_006192.1. NM_006201.4.
NP_148978.2. NM_033018.3.

UniGene

Hs.496068.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MTL	X-ray	2.40	A	163-478	[»]

ProteinModelPortal

Q00536.

SMR

Q00536. Positions 162-472.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00536. 3 interactions.

STRING

Q00536.

PTM databases

PhosphoSite

Q00536.

Polymorphism databases

DMDM

266425.

Proteomic databases

PRIDE

Q00536.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276052; ENSP00000276052; ENSG00000102225.
ENST00000357227; ENSP00000349762; ENSG00000102225.
ENST00000457458; ENSP00000405798; ENSG00000102225.

GeneID

5127.

KEGG

hsa:5127.

UCSC

uc004dhn.1. human.

Organism-specific databases

CTD

5127.

GeneCards

GC0XP047078.

H-InvDB

HIX0016760.

HGNC

HGNC:8749. CDK16.

HPA

CAB016535.
HPA001366.

MIM

311550. gene.

neXtProt

NX_Q00536.

PharmGKB

PA33095.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13693.

HOVERGEN

HBG014652.

InParanoid

Q00536.

OrthoDB

EOG44BB24.

PhylomeDB

Q00536.

Enzyme and pathway databases

BRENDA

2.7.11.22. 2681.

Gene expression databases

ArrayExpress

Q00536.

Bgee

Q00536.

CleanEx

HS_PCTK1.

Genevestigator

Q00536.

GermOnline

ENSG00000102225. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K08820.

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

19762.

SOURCE

Search...

Entry information

Entry name

CDK16_HUMAN

Accession

Primary (citable) accession number: Q00536
Secondary accession number(s): A8K280

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	January 25, 2012
This is version 122 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.