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Protein

Host cell factor 2

Gene

HCFC2

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

Functioni

GO - Molecular functioni

  1. transcription coactivator activity Source: ProtInc

GO - Biological processi

  1. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  2. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  3. viral process Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Host cell factor 2
Short name:
HCF-2
Alternative name(s):
C2 factor
Gene namesi
Name:HCFC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:24972. HCFC2.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: HPA
  3. nucleus Source: ProtInc
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134868925.

Polymorphism and mutation databases

BioMutaiHCFC2.
DMDMi62900381.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 792792Host cell factor 2PRO_0000119072Add
BLAST

Proteomic databases

MaxQBiQ9Y5Z7.
PaxDbiQ9Y5Z7.
PRIDEiQ9Y5Z7.

PTM databases

PhosphoSiteiQ9Y5Z7.

Expressioni

Tissue specificityi

Highly expressed in testis. Detected at lower levels in spleen, thymus, prostate, ovary, small intestine and colon.1 Publication

Gene expression databases

BgeeiQ9Y5Z7.
CleanExiHS_HCFC2.
ExpressionAtlasiQ9Y5Z7. baseline and differential.
GenevestigatoriQ9Y5Z7.

Organism-specific databases

HPAiHPA006227.

Interactioni

Subunit structurei

Binds KMT2A/MLL1. Component of the MLL1/MLL complex, at least composed of KMT2A/MLL1, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and HCFC2.1 Publication

Protein-protein interaction databases

BioGridi118959. 10 interactions.
IntActiQ9Y5Z7. 14 interactions.
STRINGi9606.ENSP00000229330.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5Z7.
SMRiQ9Y5Z7. Positions 354-390, 597-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati34 – 7946Kelch 1Add
BLAST
Repeati83 – 13048Kelch 2Add
BLAST
Repeati207 – 25549Kelch 3Add
BLAST
Repeati257 – 30347Kelch 4Add
BLAST
Domaini359 – 44991Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini583 – 67593Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini677 – 787111Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 4 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000021205.
HOVERGENiHBG051889.
InParanoidiQ9Y5Z7.
KOiK14966.
OMAiDETCALP.
OrthoDBiEOG790G05.
PhylomeDBiQ9Y5Z7.
TreeFamiTF314757.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR011043. Gal_Oxase/kelch_b-propeller.
IPR015916. Gal_Oxidase_b-propeller.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF50965. SSF50965. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y5Z7-1) [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
MAAPSLLNWR RVSSFTGPVP RARHGHRAVA IRELMIIFGG GNEGIADELH
60 70 80 90 100
VYNTATNQWF LPAVRGDIPP GCAAHGFVCD GTRILVFGGM VEYGRYSNEL
110 120 130 140 150
YELQASRWLW KKVKPHPPPS GLPPCPRLGH SFSLYGNKCY LFGGLANESE
160 170 180 190 200
DSNNNVPRYL NDFYELELQH GSGVVGWSIP VTKGVVPSPR ESHTAVIYCK
210 220 230 240 250
KDSGSPKMYV FGGMCGARLD DLWQLDLETM SWSKPETKGT VPLPRSLHTA
260 270 280 290 300
SVIGNKMYIF GGWVPHKGEN TETSPHDCEW RCTSSFSYLN LDTTEWTTLV
310 320 330 340 350
SDSQEDKKNS RPRPRAGHCA VAIGTRLYFW SGRDGYKKAL NSQVCCKDLW
360 370 380 390 400
YLDTEKPPAP SQVQLIKATT NSFHVKWDEV STVEGYLLQL STDLPYQAAS
410 420 430 440 450
SDSSAAPNMQ GVRMDPHRQG SNNIVPNSIN DTINSTKTEQ PATKETSMKN
460 470 480 490 500
KPDFKALTDS NAILYPSLAS NASNHNSHVV DMLRKNEGPH TSANVGVLSS
510 520 530 540 550
CLDVRTVIPE TSVSSTVSST QTMVTQQTIK TESSSTNGAV VKDETSLTTF
560 570 580 590 600
STKSEVDETY ALPATKISRV ETHATATPFS KETPSNPVAT VKAGERQWCD
610 620 630 640 650
VGIFKNNTAL VSQFYLLPKG KQSISKVGNA DVPDYSLLKK QDLVPGTGYR
660 670 680 690 700
FRVAAINGCG IGPFSKISEF KTCIPGFPGA PSAVRISKNV EGIHLSWEPP
710 720 730 740 750
TSPSGNILEY SAYLAIRTAQ IQDNPSQLVF MRIYCGLKTS CIVTAGQLAN
760 770 780 790
AHIDYTSRPA IVFRISAKNE KGYGPATQVR WLQGNNKKAP LN
Length:792
Mass (Da):86,779
Last modified:November 1, 1999 - v1
Checksum:iEADF5FF25F70856C
GO
Isoform 2 (identifier: Q9Y5Z7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     411-412: GV → DQ
     413-792: Missing.

Note: No experimental confirmation available.

Show »
Length:412
Mass (Da):45,828
Checksum:i2EA7A06A247B3BCC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461A → S.
Corresponds to variant rs2700500 [ dbSNP | Ensembl ].
VAR_050044
Natural varianti268 – 2681G → A.
Corresponds to variant rs17035206 [ dbSNP | Ensembl ].
VAR_033984

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei411 – 4122GV → DQ in isoform 2. 1 PublicationVSP_057024
Alternative sequencei413 – 792380Missing in isoform 2. 1 PublicationVSP_057025Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117210 mRNA. Translation: AAD27814.1.
AK313466 mRNA. Translation: BAG36252.1.
AC078819 Genomic DNA. No translation available.
AC084359 Genomic DNA. No translation available.
AC089983 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97736.1.
CH471054 Genomic DNA. Translation: EAW97737.1.
BC006558 mRNA. Translation: AAH06558.1.
BC033799 mRNA. Translation: AAH33799.1.
CCDSiCCDS9097.1. [Q9Y5Z7-1]
RefSeqiNP_037452.1. NM_013320.2. [Q9Y5Z7-1]
UniGeneiHs.506558.

Genome annotation databases

EnsembliENST00000229330; ENSP00000229330; ENSG00000111727. [Q9Y5Z7-1]
ENST00000544223; ENSP00000442942; ENSG00000111727. [Q9Y5Z7-2]
GeneIDi29915.
KEGGihsa:29915.
UCSCiuc001tkj.4. human. [Q9Y5Z7-1]

Polymorphism and mutation databases

BioMutaiHCFC2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117210 mRNA. Translation: AAD27814.1.
AK313466 mRNA. Translation: BAG36252.1.
AC078819 Genomic DNA. No translation available.
AC084359 Genomic DNA. No translation available.
AC089983 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97736.1.
CH471054 Genomic DNA. Translation: EAW97737.1.
BC006558 mRNA. Translation: AAH06558.1.
BC033799 mRNA. Translation: AAH33799.1.
CCDSiCCDS9097.1. [Q9Y5Z7-1]
RefSeqiNP_037452.1. NM_013320.2. [Q9Y5Z7-1]
UniGeneiHs.506558.

3D structure databases

ProteinModelPortaliQ9Y5Z7.
SMRiQ9Y5Z7. Positions 354-390, 597-790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118959. 10 interactions.
IntActiQ9Y5Z7. 14 interactions.
STRINGi9606.ENSP00000229330.

PTM databases

PhosphoSiteiQ9Y5Z7.

Polymorphism and mutation databases

BioMutaiHCFC2.
DMDMi62900381.

Proteomic databases

MaxQBiQ9Y5Z7.
PaxDbiQ9Y5Z7.
PRIDEiQ9Y5Z7.

Protocols and materials databases

DNASUi29915.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229330; ENSP00000229330; ENSG00000111727. [Q9Y5Z7-1]
ENST00000544223; ENSP00000442942; ENSG00000111727. [Q9Y5Z7-2]
GeneIDi29915.
KEGGihsa:29915.
UCSCiuc001tkj.4. human. [Q9Y5Z7-1]

Organism-specific databases

CTDi29915.
GeneCardsiGC12P104458.
HGNCiHGNC:24972. HCFC2.
HPAiHPA006227.
MIMi607926. gene.
neXtProtiNX_Q9Y5Z7.
PharmGKBiPA134868925.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000021205.
HOVERGENiHBG051889.
InParanoidiQ9Y5Z7.
KOiK14966.
OMAiDETCALP.
OrthoDBiEOG790G05.
PhylomeDBiQ9Y5Z7.
TreeFamiTF314757.

Miscellaneous databases

ChiTaRSiHCFC2. human.
GenomeRNAii29915.
NextBioi35482244.
PROiQ9Y5Z7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5Z7.
CleanExiHS_HCFC2.
ExpressionAtlasiQ9Y5Z7. baseline and differential.
GenevestigatoriQ9Y5Z7.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
2.130.10.80. 1 hit.
2.60.40.10. 3 hits.
InterProiIPR003961. FN3_dom.
IPR011043. Gal_Oxase/kelch_b-propeller.
IPR015916. Gal_Oxidase_b-propeller.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF50965. SSF50965. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2."
    Johnson K.M., Mahajan S.S., Wilson A.C.
    J. Virol. 73:3930-3940(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "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 1).
    Tissue: Hippocampus.
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Lung.
  6. "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
    Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
    Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH KMT2A.

Entry informationi

Entry nameiHCFC2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Z7
Secondary accession number(s): B2R8Q5, C0H5X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: April 29, 2015
This is version 119 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

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. 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.