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Protein

Protein FAM216A

Gene

FAM216A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM216A
Gene namesi
Name:FAM216A
Synonyms:C12orf24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30180. FAM216A.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128395781.

Polymorphism and mutation databases

BioMutaiFAM216A.
DMDMi74730685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Protein FAM216APRO_0000288861Add
BLAST

Proteomic databases

MaxQBiQ8WUB2.
PaxDbiQ8WUB2.
PRIDEiQ8WUB2.

PTM databases

PhosphoSiteiQ8WUB2.

Expressioni

Gene expression databases

BgeeiQ8WUB2.
CleanExiHS_C12orf24.
ExpressionAtlasiQ8WUB2. baseline and differential.
GenevisibleiQ8WUB2. HS.

Organism-specific databases

HPAiHPA038286.
HPA038287.

Interactioni

Protein-protein interaction databases

BioGridi118951. 2 interactions.
STRINGi9606.ENSP00000366901.

Structurei

3D structure databases

ProteinModelPortaliQ8WUB2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAM216 family.Curated

Phylogenomic databases

eggNOGiNOG47451.
GeneTreeiENSGT00390000012966.
HOGENOMiHOG000111755.
HOVERGENiHBG102671.
InParanoidiQ8WUB2.
OMAiHYPCTTW.
OrthoDBiEOG7DC257.
PhylomeDBiQ8WUB2.
TreeFamiTF337546.

Family and domain databases

InterProiIPR029373. FAM216.
[Graphical view]
PfamiPF15107. FAM216B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WUB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGQLLPHTA RGLGAAEMPG QGPGSDWTER SSSAEPPAVA GTEGGGGGSA
60 70 80 90 100
GYSCYQNSKG SDRIKDGYKV NSHIAKLQEL WKTPQNQTIH LSKSMMEASF
110 120 130 140 150
FKHPDLTTGQ KRYLCSIAKI YNANYLKMLM KRQYMHVLQH SSQKPGVLTH
160 170 180 190 200
HRSRLSSRYS QKQHYPCTTW RHQLEREDSG SSDIAAASAP EMLIQHSLWR
210 220 230 240 250
PVRNKEGIKT GYASKTRCKS LKIFRRPRKL FMQTVSSDDS ESHMSEEKKE
260 270
EDLLNNFMQS MSIEEQGEHL MLT
Length:273
Mass (Da):30,792
Last modified:March 1, 2002 - v1
Checksum:iB06EF30057AB8586
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001R → W in AAB50215 (PubMed:9110174).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti225 – 2251R → G.
Corresponds to variant rs17188964 [ dbSNP | Ensembl ].
VAR_032513

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79274 mRNA. Translation: AAB50215.1.
CR457001 mRNA. Translation: CAG33282.1.
AC002350 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97917.1.
BC020967 mRNA. Translation: AAH20967.1.
CCDSiCCDS31899.1.
RefSeqiNP_037432.2. NM_013300.2.
UniGeneiHs.436618.

Genome annotation databases

EnsembliENST00000377673; ENSP00000366901; ENSG00000204856.
GeneIDi29902.
KEGGihsa:29902.
UCSCiuc001tqu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79274 mRNA. Translation: AAB50215.1.
CR457001 mRNA. Translation: CAG33282.1.
AC002350 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97917.1.
BC020967 mRNA. Translation: AAH20967.1.
CCDSiCCDS31899.1.
RefSeqiNP_037432.2. NM_013300.2.
UniGeneiHs.436618.

3D structure databases

ProteinModelPortaliQ8WUB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118951. 2 interactions.
STRINGi9606.ENSP00000366901.

PTM databases

PhosphoSiteiQ8WUB2.

Polymorphism and mutation databases

BioMutaiFAM216A.
DMDMi74730685.

Proteomic databases

MaxQBiQ8WUB2.
PaxDbiQ8WUB2.
PRIDEiQ8WUB2.

Protocols and materials databases

DNASUi29902.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377673; ENSP00000366901; ENSG00000204856.
GeneIDi29902.
KEGGihsa:29902.
UCSCiuc001tqu.4. human.

Organism-specific databases

CTDi29902.
GeneCardsiGC12P110907.
HGNCiHGNC:30180. FAM216A.
HPAiHPA038286.
HPA038287.
neXtProtiNX_Q8WUB2.
PharmGKBiPA128395781.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47451.
GeneTreeiENSGT00390000012966.
HOGENOMiHOG000111755.
HOVERGENiHBG102671.
InParanoidiQ8WUB2.
OMAiHYPCTTW.
OrthoDBiEOG7DC257.
PhylomeDBiQ8WUB2.
TreeFamiTF337546.

Miscellaneous databases

GenomeRNAii29902.
NextBioi52470.
PROiQ8WUB2.

Gene expression databases

BgeeiQ8WUB2.
CleanExiHS_C12orf24.
ExpressionAtlasiQ8WUB2. baseline and differential.
GenevisibleiQ8WUB2. HS.

Family and domain databases

InterProiIPR029373. FAM216.
[Graphical view]
PfamiPF15107. FAM216B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Colon.

Entry informationi

Entry nameiF216A_HUMAN
AccessioniPrimary (citable) accession number: Q8WUB2
Secondary accession number(s): A6NH30, Q99776
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 80 of the entry and version 1 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

Caution

It is uncertain whether Met-1 or Met-18 is the initiator.Curated

Keywords - Technical termi

Complete proteome, 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. 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.