Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q3B820

- F161A_HUMAN

UniProt

Q3B820 - F161A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein FAM161A

Gene

FAM161A

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

Functioni

Involved in ciliogenesis.1 Publication

GO - Biological processi

  1. cilium assembly Source: UniProtKB
  2. response to stimulus Source: UniProtKB-KW
  3. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM161A
Gene namesi
Name:FAM161A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:25808. FAM161A.

Subcellular locationi

Cytoplasmcytoskeletoncilium basal body 1 Publication. Cell projectioncilium 1 Publication
Note: Localized to the region between the outer and inner photoreceptor segments, corresponding to the photoreceptor connecting cilium.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. ciliary basal body Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. photoreceptor connecting cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 28 (RP28) [MIM:606068]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Ciliopathy, Retinitis pigmentosa

Organism-specific databases

MIMi606068. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA162386876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Protein FAM161APRO_0000329052Add
BLAST

Proteomic databases

MaxQBiQ3B820.
PaxDbiQ3B820.
PRIDEiQ3B820.

PTM databases

PhosphoSiteiQ3B820.

Expressioni

Tissue specificityi

Isoform 1 and isoform 3 are widely expressed with highest levels in retina and testis, with isoform 1 being the most abundant in all tissues tested.2 Publications

Gene expression databases

BgeeiQ3B820.
CleanExiHS_FAM161A.
ExpressionAtlasiQ3B820. baseline and differential.
GenevestigatoriQ3B820.

Organism-specific databases

HPAiHPA032119.

Interactioni

Subunit structurei

Interacts (via C-terminus) with microtubules. Interacts with LCA5, CEP290 and SDCCAG8. Interacts with FAM161B.2 Publications

Protein-protein interaction databases

BioGridi123909. 2 interactions.
IntActiQ3B820. 1 interaction.
STRINGi9606.ENSP00000385893.

Structurei

3D structure databases

ProteinModelPortaliQ3B820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili93 – 12028Sequence AnalysisAdd
BLAST
Coiled coili296 – 32025Sequence AnalysisAdd
BLAST
Coiled coili522 – 55231Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Glu
Compositional biasi609 – 65850Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the FAM161 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG80167.
GeneTreeiENSGT00530000063901.
HOGENOMiHOG000049209.
HOVERGENiHBG107870.
InParanoidiQ3B820.
KOiK16772.
OMAiAEKHYSN.
PhylomeDBiQ3B820.
TreeFamiTF321199.

Family and domain databases

InterProiIPR019579. UPF0564.
[Graphical view]
PfamiPF10595. UPF0564. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3B820) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATSHRVAKL VASSLQTPVN PITGARVAQY EREDPLKALA AAEAILEDEE
60 70 80 90 100
EEKVAQPAGA SADLNTSFSG VDEHAPISYE DFVNFPDIHH SNEEYFKKVE
110 120 130 140 150
ELKAAHIETM AKLEKMYQDK LHLKEVQPVV IREDSLSDSS RSVSEKNSYH
160 170 180 190 200
PVSLMTSFSE PDLGQSSSLY VSSSEEELPN LEKEYPRKNR MMTYAKELIN
210 220 230 240 250
NMWTDFCVED YIRCKDTGFH AAEKRRKKRK EWVPTITVPE PFQMMIREQK
260 270 280 290 300
KKEESMKSKS DIEMVHKALK KQEEDPEYKK KFRANPVPAS VFLPLYHDLV
310 320 330 340 350
KQKEERRRSL KEKSKEALLA SQKPFKFIAR EEQKRAAREK QLRDFLKYKK
360 370 380 390 400
KTNRFKARPI PRSTYGSTTN DKLKEEELYR NLRTQLRAQE HLQNSSPLPC
410 420 430 440 450
RSACGCRNPR CPEQAVKLKC KHKVRCPTPD FEDLPERYQK HLSEHKSPKL
460 470 480 490 500
LTVCKPFDLH ASPHASIKRE KILADIEADE ENLKETRWPY LSPRRKSPVR
510 520 530 540 550
CAGVNPVPCN CNPPVPTVSS RGREQAVRKS EKERMREYQR ELEEREEKLK
560 570 580 590 600
KRPLLFERVA QKNARMAAEK HYSNTLKALG ISDEFVSKKG QSGKVLEYFN
610 620 630 640 650
NQETKSVTED KESFNEEEKI EERENGEENY FIDTNSQDSY KEKDEANEES
660
EEEKSVEESH
Length:660
Mass (Da):76,752
Last modified:April 8, 2008 - v2
Checksum:iE2C0D443C1A0DAA5
GO
Isoform 2 (identifier: Q3B820-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.

Note: No experimental confirmation available.

Show »
Length:551
Mass (Da):64,836
Checksum:iF31A08F7C2AB938E
GO
Isoform 3 (identifier: Q3B820-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-527: V → VRRSLEEKKMLEEERNRILTKQKQRMKELQKLLTTRAKAYDSHQSLAQISKSRVKCL

Show »
Length:716
Mass (Da):83,492
Checksum:iC2346158DFD127CD
GO

Sequence cautioni

The sequence BAG58969.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451E → G in BX648834. (PubMed:17974005)Curated
Sequence conflicti167 – 1671S → F in BAB14544. (PubMed:14702039)Curated
Sequence conflicti534 – 5341R → M in BAG58969. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071I → M.1 Publication
Corresponds to variant rs11125895 [ dbSNP | Ensembl ].
VAR_060180
Natural varianti236 – 2361I → V.
Corresponds to variant rs17513722 [ dbSNP | Ensembl ].
VAR_042630
Natural varianti273 – 2731E → K.
Corresponds to variant rs6733774 [ dbSNP | Ensembl ].
VAR_042631

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 109109Missing in isoform 2. 1 PublicationVSP_032935Add
BLAST
Alternative sequencei527 – 5271V → VRRSLEEKKMLEEERNRILT KQKQRMKELQKLLTTRAKAY DSHQSLAQISKSRVKCL in isoform 3. 1 PublicationVSP_039126

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX648834 mRNA. No translation available.
BX649029 mRNA. No translation available.
AC107081 Genomic DNA. No translation available.
AK023367 mRNA. Translation: BAB14544.1.
AK296255 mRNA. Translation: BAG58969.1. Different initiation.
BC107162 mRNA. No translation available.
BC107163 mRNA. No translation available.
CCDSiCCDS42687.2. [Q3B820-1]
CCDS56120.1. [Q3B820-3]
RefSeqiNP_001188472.1. NM_001201543.1. [Q3B820-3]
NP_115556.2. NM_032180.2. [Q3B820-1]
XP_006712177.1. XM_006712114.1. [Q3B820-2]
UniGeneiHs.440466.

Genome annotation databases

EnsembliENST00000404929; ENSP00000385158; ENSG00000170264. [Q3B820-3]
ENST00000405894; ENSP00000385893; ENSG00000170264. [Q3B820-1]
GeneIDi84140.
KEGGihsa:84140.
UCSCiuc002sbm.4. human. [Q3B820-3]
uc002sbn.4. human. [Q3B820-1]

Polymorphism databases

DMDMi182705173.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX648834 mRNA. No translation available.
BX649029 mRNA. No translation available.
AC107081 Genomic DNA. No translation available.
AK023367 mRNA. Translation: BAB14544.1 .
AK296255 mRNA. Translation: BAG58969.1 . Different initiation.
BC107162 mRNA. No translation available.
BC107163 mRNA. No translation available.
CCDSi CCDS42687.2. [Q3B820-1 ]
CCDS56120.1. [Q3B820-3 ]
RefSeqi NP_001188472.1. NM_001201543.1. [Q3B820-3 ]
NP_115556.2. NM_032180.2. [Q3B820-1 ]
XP_006712177.1. XM_006712114.1. [Q3B820-2 ]
UniGenei Hs.440466.

3D structure databases

ProteinModelPortali Q3B820.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123909. 2 interactions.
IntActi Q3B820. 1 interaction.
STRINGi 9606.ENSP00000385893.

PTM databases

PhosphoSitei Q3B820.

Polymorphism databases

DMDMi 182705173.

Proteomic databases

MaxQBi Q3B820.
PaxDbi Q3B820.
PRIDEi Q3B820.

Protocols and materials databases

DNASUi 84140.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000404929 ; ENSP00000385158 ; ENSG00000170264 . [Q3B820-3 ]
ENST00000405894 ; ENSP00000385893 ; ENSG00000170264 . [Q3B820-1 ]
GeneIDi 84140.
KEGGi hsa:84140.
UCSCi uc002sbm.4. human. [Q3B820-3 ]
uc002sbn.4. human. [Q3B820-1 ]

Organism-specific databases

CTDi 84140.
GeneCardsi GC02M062051.
GeneReviewsi FAM161A.
H-InvDB HIX0002084.
HGNCi HGNC:25808. FAM161A.
HPAi HPA032119.
MIMi 606068. phenotype.
613596. gene.
neXtProti NX_Q3B820.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA162386876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80167.
GeneTreei ENSGT00530000063901.
HOGENOMi HOG000049209.
HOVERGENi HBG107870.
InParanoidi Q3B820.
KOi K16772.
OMAi AEKHYSN.
PhylomeDBi Q3B820.
TreeFami TF321199.

Miscellaneous databases

GenomeRNAii 84140.
NextBioi 73449.
PROi Q3B820.
SOURCEi Search...

Gene expression databases

Bgeei Q3B820.
CleanExi HS_FAM161A.
ExpressionAtlasi Q3B820. baseline and differential.
Genevestigatori Q3B820.

Family and domain databases

InterProi IPR019579. UPF0564.
[Graphical view ]
Pfami PF10595. UPF0564. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT MET-107.
    Tissue: Colon endothelium and Retina.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-660 (ISOFORMS 1/2).
    Tissue: Ovary and Thalamus.
  4. "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] OF 43-660 (ISOFORM 1).
  5. Cited for: INVOLVEMENT IN RP28, TISSUE SPECIFICITY.
  6. "Homozygosity mapping reveals null mutations in FAM161A as a cause of autosomal-recessive retinitis pigmentosa."
    Bandah-Rozenfeld D., Mizrahi-Meissonnier L., Farhy C., Obolensky A., Chowers I., Pe'er J., Merin S., Ben-Yosef T., Ashery-Padan R., Banin E., Sharon D.
    Am. J. Hum. Genet. 87:382-391(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RP28, TISSUE SPECIFICITY.
  7. "FAM161A, associated with retinitis pigmentosa, is a component of the cilia-basal body complex and interacts with proteins involved in ciliopathies."
    Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D., Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.
    Hum. Mol. Genet. 21:5174-5184(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LCA5; CEP290 AND SDCCAG8.
  8. "The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein involved in intermolecular protein interaction and microtubule association."
    Zach F., Grassmann F., Langmann T., Sorusch N., Wolfrum U., Stohr H.
    Hum. Mol. Genet. 21:4573-4586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES AND FAM161B.

Entry informationi

Entry nameiF161A_HUMAN
AccessioniPrimary (citable) accession number: Q3B820
Secondary accession number(s): B4DJV7, Q9H8R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: October 29, 2014
This is version 75 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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