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Protein

A-kinase anchor protein 3

Gene

AKAP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function as a regulator of both motility- and head-associated functions such as capacitation and the acrosome reaction.

GO - Molecular functioni

  1. protein kinase A binding Source: ProtInc

GO - Biological processi

  1. acrosome reaction Source: ProtInc
  2. movement of cell or subcellular component Source: ProtInc
  3. protein localization Source: Ensembl
  4. regulation of protein kinase A signaling Source: GO_Central
  5. single fertilization Source: ProtInc
  6. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 3
Short name:
AKAP-3
Alternative name(s):
A-kinase anchor protein 110 kDa
Short name:
AKAP 110
Cancer/testis antigen 82
Short name:
CT82
Fibrous sheath protein of 95 kDa
Short name:
FSP95
Fibrousheathin I
Fibrousheathin-1
Protein kinase A-anchoring protein 3
Short name:
PRKA3
Sperm oocyte-binding protein
Gene namesi
Name:AKAP3
Synonyms:AKAP110, SOB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:373. AKAP3.

Subcellular locationi

Cytoplasmic vesiclesecretory vesicleacrosome By similarity
Note: Ribs of the fibrous sheath in the principal piece of the sperm tail. Dorsal margin of the acrosomal segment.

GO - Cellular componenti

  1. acrosomal vesicle Source: UniProtKB-SubCell
  2. cytoplasm Source: GO_Central
  3. nucleus Source: UniProtKB
  4. sperm fibrous sheath Source: GO_Central
  5. sperm principal piece Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311L → P: Abolishes interaction with ROPN1. 1 Publication

Organism-specific databases

PharmGKBiPA24667.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 853853A-kinase anchor protein 3PRO_0000064526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei208 – 2081Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei404 – 4041Phosphotyrosine1 Publication
Modified residuei635 – 6351Phosphoserine1 Publication
Modified residuei636 – 6361Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO75969.
PRIDEiO75969.

PTM databases

PhosphoSiteiO75969.

Expressioni

Tissue specificityi

Testis specific; only expressed in spermatids.

Gene expression databases

BgeeiO75969.
CleanExiHS_AKAP3.
ExpressionAtlasiO75969. baseline and differential.
GenevestigatoriO75969.

Organism-specific databases

HPAiHPA039765.

Interactioni

Subunit structurei

Interacts with ROPN1 AND ROPN1L.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKAR2AP138612EBI-9033101,EBI-2556122
ROPN1BQ9BZX42EBI-9033101,EBI-9033148

Protein-protein interaction databases

BioGridi115817. 8 interactions.
IntActiO75969. 3 interactions.
STRINGi9606.ENSP00000228850.

Structurei

3D structure databases

ProteinModelPortaliO75969.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 13714PKA-RII subunit binding domainAdd
BLAST

Domaini

RII-binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.

Sequence similaritiesi

Belongs to the AKAP110 family.Curated

Phylogenomic databases

eggNOGiNOG42108.
HOGENOMiHOG000220883.
HOVERGENiHBG050478.
InParanoidiO75969.
KOiK16520.
OMAiQYHLAQG.
OrthoDBiEOG7327N3.
PhylomeDBiO75969.
TreeFamiTF105403.

Family and domain databases

InterProiIPR020799. AKAP_110.
IPR018292. AKAP_110_C.
IPR018459. RII_binding_1.
IPR008382. SPHK1-interactor_AKAP_110.
[Graphical view]
PANTHERiPTHR10226. PTHR10226. 1 hit.
PfamiPF05716. AKAP_110. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTiSM00807. AKAP_110. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKVDWLQS QNGVCKVDVY SPGDNQAQDW KMDTSTDPVR VLSWLRRDLE
60 70 80 90 100
KSTAEFQDVR FKPGESFGGE TSNSGDPHKG FSVDYYNTTT KGTPERLHFE
110 120 130 140 150
MTHKEIPCQG PRAQLGNGSS VDEVSFYANR LTNLVIAMAR KEINEKIDGS
160 170 180 190 200
ENKCVYQSLY MGNEPTPTKS LSKIASELVN ETVSACSRNA APDKAPGSGD
210 220 230 240 250
RVSGSSQSPP NLKYKSTLKI KESTKERQGP DDKPPSKKSF FYKEVFESRN
260 270 280 290 300
GDYAREGGRF FPRERKRFRG QERPDDFTAS VSEGIMTYAN SVVSDMMVSI
310 320 330 340 350
MKTLKIQVKD TTIATILLKK VLLKHAKEVV SDLIDSFLRN LHSVTGTLMT
360 370 380 390 400
DTQFVSAVKR TVFSHGSQKA TDIMDAMLRK LYNVMFAKKV PEHVRKAQDK
410 420 430 440 450
AESYSLISMK GMGDPKNRNV NFAMKSETKL REKMYSEPKS EEETCAKTLG
460 470 480 490 500
EHIIKEGLTL WHKTQQKECK SLGFQHAAFE APNTQRKPAS DISFEYPEDI
510 520 530 540 550
GNLSLPPYPP EKPENFMYDS DSWAEDLIVS ALLLIQYHLA QGGRRDARSF
560 570 580 590 600
VEAAGTTNFP ANEPPVAPDE SCLKSAPIVG DQEQAEKKDL RSVFFNFIRN
610 620 630 640 650
LLSETIFKRD QSPEPKVPEQ PVKEDRKLCE RPLASSPPRL YEDDETPGAL
660 670 680 690 700
SGLTKMAVSQ IDGHMSGQMV EHLMNSVMKL CVIIAKSCDA SLAELGDDKS
710 720 730 740 750
GDASRLTSAF PDSLYECLPA KGTGSAEAVL QNAYQAIHNE MRGTSGQPPE
760 770 780 790 800
GCAAPTVIVS NHNLTDTVQN KQLQAVLQWV AASELNVPIL YFAGDDEGIQ
810 820 830 840 850
EKLLQLSAAA VDKGCSVGEV LQSVLRYEKE RQLNEAVGNV TPLQLLDWLM

VNL
Length:853
Mass (Da):94,751
Last modified:December 15, 2009 - v2
Checksum:iCFDEA26922B5A86E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2721E → D in AAD21218 (PubMed:10334916).Curated
Sequence conflicti282 – 2821S → G in AAC35854 (PubMed:10529264).Curated
Sequence conflicti402 – 4021E → V in AAC35854 (PubMed:10529264).Curated
Sequence conflicti467 – 4671K → N in AAC35854 (PubMed:10529264).Curated
Sequence conflicti597 – 5971F → S AA sequence (PubMed:10529264).Curated
Sequence conflicti700 – 7001S → L in AAC35854 (PubMed:10529264).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181G → E.4 Publications
Corresponds to variant rs2072355 [ dbSNP | Ensembl ].
VAR_055488
Natural varianti464 – 4641T → S.3 Publications
Corresponds to variant rs11063266 [ dbSNP | Ensembl ].
VAR_060730
Natural varianti500 – 5001I → T.1 Publication
Corresponds to variant rs12366671 [ dbSNP | Ensembl ].
VAR_055489
Natural varianti525 – 5251E → K.3 Publications
Corresponds to variant rs1990312 [ dbSNP | Ensembl ].
VAR_061000
Natural varianti661 – 6611I → T.
Corresponds to variant rs1990313 [ dbSNP | Ensembl ].
VAR_055490
Natural varianti700 – 7001S → F.
Corresponds to variant rs2041291 [ dbSNP | Ensembl ].
VAR_055491
Natural varianti700 – 7001S → P.
Corresponds to variant rs2041290 [ dbSNP | Ensembl ].
VAR_059112
Natural varianti725 – 7251S → L.
Corresponds to variant rs2072357 [ dbSNP | Ensembl ].
VAR_055492
Natural varianti831 – 8311R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036428

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85715 mRNA. Translation: AAD21218.1.
AF087003 mRNA. Translation: AAC35854.1.
AF093408 mRNA. Translation: AAC63371.1.
AK292451 mRNA. Translation: BAF85140.1.
AC005832 Genomic DNA. No translation available.
BC047535 mRNA. Translation: AAH47535.1.
CCDSiCCDS8531.1.
RefSeqiNP_001265238.1. NM_001278309.1.
NP_006413.3. NM_006422.3.
XP_005253721.1. XM_005253664.1.
XP_005253722.1. XM_005253665.2.
XP_006719014.1. XM_006718951.1.
UniGeneiHs.98397.

Genome annotation databases

EnsembliENST00000228850; ENSP00000228850; ENSG00000111254.
ENST00000545990; ENSP00000440994; ENSG00000111254.
GeneIDi10566.
KEGGihsa:10566.
UCSCiuc001qnb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85715 mRNA. Translation: AAD21218.1.
AF087003 mRNA. Translation: AAC35854.1.
AF093408 mRNA. Translation: AAC63371.1.
AK292451 mRNA. Translation: BAF85140.1.
AC005832 Genomic DNA. No translation available.
BC047535 mRNA. Translation: AAH47535.1.
CCDSiCCDS8531.1.
RefSeqiNP_001265238.1. NM_001278309.1.
NP_006413.3. NM_006422.3.
XP_005253721.1. XM_005253664.1.
XP_005253722.1. XM_005253665.2.
XP_006719014.1. XM_006718951.1.
UniGeneiHs.98397.

3D structure databases

ProteinModelPortaliO75969.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115817. 8 interactions.
IntActiO75969. 3 interactions.
STRINGi9606.ENSP00000228850.

PTM databases

PhosphoSiteiO75969.

Proteomic databases

PaxDbiO75969.
PRIDEiO75969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228850; ENSP00000228850; ENSG00000111254.
ENST00000545990; ENSP00000440994; ENSG00000111254.
GeneIDi10566.
KEGGihsa:10566.
UCSCiuc001qnb.4. human.

Organism-specific databases

CTDi10566.
GeneCardsiGC12M004724.
H-InvDBHIX0026339.
HGNCiHGNC:373. AKAP3.
HPAiHPA039765.
MIMi604689. gene.
neXtProtiNX_O75969.
PharmGKBiPA24667.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42108.
HOGENOMiHOG000220883.
HOVERGENiHBG050478.
InParanoidiO75969.
KOiK16520.
OMAiQYHLAQG.
OrthoDBiEOG7327N3.
PhylomeDBiO75969.
TreeFamiTF105403.

Miscellaneous databases

ChiTaRSiAKAP3. human.
GeneWikiiAKAP3.
GenomeRNAii10566.
NextBioi40101.
PROiO75969.
SOURCEiSearch...

Gene expression databases

BgeeiO75969.
CleanExiHS_AKAP3.
ExpressionAtlasiO75969. baseline and differential.
GenevestigatoriO75969.

Family and domain databases

InterProiIPR020799. AKAP_110.
IPR018292. AKAP_110_C.
IPR018459. RII_binding_1.
IPR008382. SPHK1-interactor_AKAP_110.
[Graphical view]
PANTHERiPTHR10226. PTHR10226. 1 hit.
PfamiPF05716. AKAP_110. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTiSM00807. AKAP_110. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of SOB1, a new testis-specific cDNA encoding a human sperm protein probably involved in oocyte recognition."
    Lefevre A., Duquenne C., Rousseau-Merck M.-F., Rogier E., Finaz C.
    Biochem. Biophys. Res. Commun. 259:60-66(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS GLU-118; SER-464 AND LYS-525.
    Tissue: Testis.
  2. "FSP95, a testis-specific 95-kilodalton fibrous sheath antigen that undergoes tyrosine phosphorylation in capacitated human spermatozoa."
    Mandal A., Naaby-Hansen S., Wolkowicz M.J., Klotz K., Shetty J., Retief J.D., Coonrod S.A., Kinter M., Sherman N., Cesar F., Flickinger C.J., Herr J.C.
    Biol. Reprod. 61:1184-1197(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS GLU-118; SER-464; THR-500 AND LYS-525.
    Tissue: Testis.
  3. "Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein."
    Vijayaraghavan S., Liberty G.A., Mohan J., Winfrey V.P., Olson G.E., Carr D.W.
    Mol. Endocrinol. 13:705-717(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-464 AND LYS-525.
    Tissue: Testis.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-118.
    Tissue: Testis.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-118.
    Tissue: Testis.
  7. "Identification of sperm-specific proteins that interact with A-kinase anchoring proteins in a manner similar to the type II regulatory subunit of PKA."
    Carr D.W., Fujita A., Stentz C.L., Liberty G.A., Olson G.E., Narumiya S.
    J. Biol. Chem. 276:17332-17338(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROPN1 AND ROPN1L, MUTAGENESIS OF LEU-131.
  8. "Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation."
    Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.
    J. Biol. Chem. 278:11579-11589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208; SER-403; TYR-404; SER-635 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Sperm.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-831.

Entry informationi

Entry nameiAKAP3_HUMAN
AccessioniPrimary (citable) accession number: O75969
Secondary accession number(s): O75945, Q86X01, Q9UM61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: December 15, 2009
Last modified: April 1, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.